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Conserved domains on  [gi|10862703|ref|NP_066124|]
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proto-oncogene tyrosine-protein kinase receptor Ret isoform a precursor [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
723-1012 0e+00

Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. RET is a receptor PTK (RTK) containing an extracellular region with four cadherin-like repeats, a calcium-binding site, and a cysteine-rich domain, a transmembrane segment, and an intracellular catalytic domain. It is part of a multisubunit complex that binds glial-derived neurotropic factor (GDNF) family ligands (GFLs) including GDNF, neurturin, artemin, and persephin. GFLs bind RET along with four GPI-anchored coreceptors, bringing two RET molecules together, leading to autophosphorylation, activation, and intracellular signaling. RET is essential for the development of the sympathetic, parasympathetic and enteric nervous systems, and the kidney. RET disruption by germline mutations causes diseases in humans including congenital aganglionosis of the gastrointestinal tract (Hirschsprung's disease) and three related inherited cancers: multiple endocrine neoplasia type 2A (MEN2A), MEN2B, and familial medullary thyroid carcinoma. The RET subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


:

Pssm-ID: 173631 [Multi-domain]  Cd Length: 290  Bit Score: 602.72  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  723 NLVLGKTLGEGEFGKVVKATAFHLKGRAGYTTVAVKMLKENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLL 802
Cdd:cd05045    1 NLVLGKTLGEGEFGKVVKATAFRLKGRAGYTTVAVKMLKENASSSELRDLLSEFNLLKQVNHPHVIKLYGACSQDGPLLL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  803 IVEYAKYGSLRGFLRESRKVGPGYLGSGGSRNSSSLDHPDERALTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNILV 882
Cdd:cd05045   81 IVEYAKYGSLRSFLRESRKVGPSYLGSDGNRNSSYLDNPDERALTMGDLISFAWQISRGMQYLAEMKLVHRDLAARNVLV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  883 AEGRKMKISDFGLSRDVYEEDSYVKRSQGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLGGNPYPGIPPERLFN 962
Cdd:cd05045  161 AEGRKMKISDFGLSRDVYEEDSYVKRSKGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLGGNPYPGIAPERLFN 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 10862703  963 LLKTGHRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADISKDLEKMMVKR 1012
Cdd:cd05045  241 LLKTGYRMERPENCSEEMYNLMLTCWKQEPDKRPTFADISKELEKMMVKS 290
RET_CLD1 pfam17756
RET Cadherin like domain 1; RET is a single transmembrane-spanning receptor tyrosine kinase ...
29-154 1.19e-66

RET Cadherin like domain 1; RET is a single transmembrane-spanning receptor tyrosine kinase (RTK) that plays critical roles in the development of vertebrates. Structural analysis indicate that RET contains four consecutive cadherin-like domains (CLD). This entry relates to the first CLD at the N-terminal. Several regions within RET-CLD1 have been shown to be important for ligand-coreceptor binding. CLD1 and CLD2 have a distinctive clamshell shape and CLD1 is essential for CLD2 folding. CLD1 contains 2 sites for GDNF receptor alpha 1 binding.


:

Pssm-ID: 465485  Cd Length: 124  Bit Score: 219.87  E-value: 1.19e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703     29 LYFSRDAYWEKLYVDQAAGTPLLYVHALRDAPEEVPSFRLGQHLyGTYRTRLHENNWICIQEDTGLLYLNRSLDHSSWEK 108
Cdd:pfam17756    1 LYFPQKEYSENVYVGQPAGTPLLQVHALRDSPSEVPHFYLCQHL-GIYRRRPHYNSWFHIDEDTGLLYLNKTLDRSDFES 79
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 10862703    109 LSVRNRGfPLLTVYLKVFLSPTSLREGECQWPGCARVYFSFFNTSF 154
Cdd:pfam17756   80 LSSGNWG-PLKKLTLQVFLSSTPFREKECHSPTCARVYLSFINATA 124
RET_CLD4 pfam17813
RET Cadherin like domain 4; RET is a single transmembrane-spanning receptor tyrosine kinase ...
404-506 8.61e-60

RET Cadherin like domain 4; RET is a single transmembrane-spanning receptor tyrosine kinase (RTK) that plays critical roles in the development of vertebrates. Structural analysis indicate that the ligand-binding RET ectodomain (RET-ECD) contains four consecutive cadherin-like domains (CLD1-CLD4) followed by a membrane-proximal cysteine-rich domain (CRD). This entry relates to CLD4 which is required for CRD folding.


:

Pssm-ID: 465517  Cd Length: 104  Bit Score: 199.48  E-value: 8.61e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703    404 LPS-TYSLSVSRRARRFAQIGKVCVENCQAFSGINVQYKLHSSGANCSTLGVVTSAEDTSGILFVNDTKALRRPKCAELH 482
Cdd:pfam17813    1 FPNvTYSFTVSRRARRYAQIGKVCVENCQEFSGIRVQYRLQPSDTNCYALGVATSPEDTSGTLYVNDTEALRRPECQELQ 80
                           90       100
                   ....*....|....*....|....
gi 10862703    483 YMVVATDQQTSRQAQAQLLVTVEG 506
Cdd:pfam17813   81 YTVVAQEQQTQLQAQTQLLVTVEG 104
RET_CLD3 pfam17812
RET Cadherin like domain 3; RET is a single transmembrane-spanning receptor tyrosine kinase ...
265-379 2.26e-58

RET Cadherin like domain 3; RET is a single transmembrane-spanning receptor tyrosine kinase (RTK) that plays critical roles in the development of vertebrates. Structural analysis indicate that RET contains four consecutive cadherin-like domains (CLD). This entry relates to CLD3. Classical cadherin calcium-coordinating motifs can be found between CLD2 and CLD3.


:

Pssm-ID: 465516  Cd Length: 114  Bit Score: 196.07  E-value: 2.26e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703    265 EDDSAPTFpAGVDTASAVVEFKRKEDTVVATLRVFDADVVPA--SGELVRRYTSTLLPGDTWAQQTFRVEHWPNETSVQA 342
Cdd:pfam17812    1 EDDSAPYV-NGTDTADAVVEFNRKEGTVFGTLRVFDRDTTPIypKDQSHNKYVGTLLTNDPWIKETFRIEHSFNETKAIF 79
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 10862703    343 NGsfVRATVHDYRLVLNRNLSISENRTMQLAVLVNDS 379
Cdd:pfam17812   80 GN--VRGTVHEYKLVLNRNLPITENRSLQLDYLVNDT 114
Cadherin pfam00028
Cadherin domain;
172-261 4.10e-16

Cadherin domain;


:

Pssm-ID: 394985 [Multi-domain]  Cd Length: 92  Bit Score: 74.64  E-value: 4.10e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703    172 PSFRIRENRPPGTF-HQFRLLPVQfLCPNISVAYRLLEG-EGLPFRCAPDSLEVSTRWALDREQREKYELVAVCTVHAG- 248
Cdd:pfam00028    1 YSASVPENAPVGTEvLTVTATDPD-LGPNGRIFYSILGGgPGGNFRIDPDTGDISTTKPLDRESIGEYELTVEATDSGGp 79
                           90
                   ....*....|...
gi 10862703    249 AREEVVMVPFPVT 261
Cdd:pfam00028   80 PLSSTATVTITVL 92
 
Name Accession Description Interval E-value
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
723-1012 0e+00

Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. RET is a receptor PTK (RTK) containing an extracellular region with four cadherin-like repeats, a calcium-binding site, and a cysteine-rich domain, a transmembrane segment, and an intracellular catalytic domain. It is part of a multisubunit complex that binds glial-derived neurotropic factor (GDNF) family ligands (GFLs) including GDNF, neurturin, artemin, and persephin. GFLs bind RET along with four GPI-anchored coreceptors, bringing two RET molecules together, leading to autophosphorylation, activation, and intracellular signaling. RET is essential for the development of the sympathetic, parasympathetic and enteric nervous systems, and the kidney. RET disruption by germline mutations causes diseases in humans including congenital aganglionosis of the gastrointestinal tract (Hirschsprung's disease) and three related inherited cancers: multiple endocrine neoplasia type 2A (MEN2A), MEN2B, and familial medullary thyroid carcinoma. The RET subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173631 [Multi-domain]  Cd Length: 290  Bit Score: 602.72  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  723 NLVLGKTLGEGEFGKVVKATAFHLKGRAGYTTVAVKMLKENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLL 802
Cdd:cd05045    1 NLVLGKTLGEGEFGKVVKATAFRLKGRAGYTTVAVKMLKENASSSELRDLLSEFNLLKQVNHPHVIKLYGACSQDGPLLL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  803 IVEYAKYGSLRGFLRESRKVGPGYLGSGGSRNSSSLDHPDERALTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNILV 882
Cdd:cd05045   81 IVEYAKYGSLRSFLRESRKVGPSYLGSDGNRNSSYLDNPDERALTMGDLISFAWQISRGMQYLAEMKLVHRDLAARNVLV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  883 AEGRKMKISDFGLSRDVYEEDSYVKRSQGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLGGNPYPGIPPERLFN 962
Cdd:cd05045  161 AEGRKMKISDFGLSRDVYEEDSYVKRSKGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLGGNPYPGIAPERLFN 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 10862703  963 LLKTGHRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADISKDLEKMMVKR 1012
Cdd:cd05045  241 LLKTGYRMERPENCSEEMYNLMLTCWKQEPDKRPTFADISKELEKMMVKS 290
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
724-1005 9.00e-134

Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. Protein kinases catalyze the transfer of the gamma phosphate from nucleotide triphosphates (often ATP) to one or more amino acid residues in a protein substrate side chain, resulting in a conformational change affecting protein function. Phosphoprotein phosphatases catalyze the reverse process. Protein kinases fall into three broad classes, characterized with respect to substrate specificity; Serine/threonine-protein kinases, tyrosine-protein kinases, and dual specificity protein kinases (e.g. MEK - phosphorylates both Thr and Tyr on target proteins). This entry represents the catalytic domain found in a number of serine/threonine- and tyrosine-protein kinases. It does not include the catalytic domain of dual specificity kinases.


Pssm-ID: 462242 [Multi-domain]  Cd Length: 258  Bit Score: 405.73  E-value: 9.00e-134
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703    724 LVLGKTLGEGEFGKVVKATAFHLKGRAGyTTVAVKMLKENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLI 803
Cdd:pfam07714    1 LTLGEKLGEGAFGEVYKGTLKGEGENTK-IKVAVKTLKEGADEEEREDFLEEASIMKKLDHPNIVKLLGVCTQGEPLYIV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703    804 VEYAKYGSLRGFLRESRkvgpgylgsggsrnsssldhpdeRALTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNILVA 883
Cdd:pfam07714   80 TEYMPGGDLLDFLRKHK-----------------------RKLTLKDLLSMALQIAKGMEYLESKNFVHRDLAARNCLVS 136
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703    884 EGRKMKISDFGLSRDVYEEDSYVKRSQGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLGGNPYPGIPPERLFNL 963
Cdd:pfam07714  137 ENLVVKISDFGLSRDIYDDDYYRKRGGGKLPIKWMAPESLKDGKFTSKSDVWSFGVLLWEIFTLGEQPYPGMSNEEVLEF 216
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 10862703    964 LKTGHRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADISKDL 1005
Cdd:pfam07714  217 LEDGYRLPQPENCPDELYDLMKQCWAYDPEDRPTFSELVEDL 258
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
724-1005 3.57e-131

Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class of kinases can not be predicted. Possible dual-specificity Ser/Thr/Tyr kinase.


Pssm-ID: 214568 [Multi-domain]  Cd Length: 258  Bit Score: 398.85  E-value: 3.57e-131
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703     724 LVLGKTLGEGEFGKVVKATAFHLKGrAGYTTVAVKMLKENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLI 803
Cdd:smart00221    1 LTLGKKLGEGAFGEVYKGTLKGKGD-GKEVEVAVKTLKEDASEQQIEEFLREARIMRKLDHPNIVKLLGVCTEEEPLMIV 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703     804 VEYAKYGSLRGFLRESRkvgpgylgsggsrnsssldhpdERALTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNILVA 883
Cdd:smart00221   80 MEYMPGGDLLDYLRKNR----------------------PKELSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVG 137
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703     884 EGRKMKISDFGLSRDVYEEDsYVKRSQGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLGGNPYPGIPPERLFNL 963
Cdd:smart00221  138 ENLVVKISDFGLSRDLYDDD-YYKVKGGKLPIRWMAPESLKEGKFTSKSDVWSFGVLLWEIFTLGEEPYPGMSNAEVLEY 216
                           250       260       270       280
                    ....*....|....*....|....*....|....*....|..
gi 10862703     964 LKTGHRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADISKDL 1005
Cdd:smart00221  217 LKKGYRLPKPPNCPPELYKLMLQCWAEDPEDRPTFSELVEIL 258
RET_CLD1 pfam17756
RET Cadherin like domain 1; RET is a single transmembrane-spanning receptor tyrosine kinase ...
29-154 1.19e-66

RET Cadherin like domain 1; RET is a single transmembrane-spanning receptor tyrosine kinase (RTK) that plays critical roles in the development of vertebrates. Structural analysis indicate that RET contains four consecutive cadherin-like domains (CLD). This entry relates to the first CLD at the N-terminal. Several regions within RET-CLD1 have been shown to be important for ligand-coreceptor binding. CLD1 and CLD2 have a distinctive clamshell shape and CLD1 is essential for CLD2 folding. CLD1 contains 2 sites for GDNF receptor alpha 1 binding.


Pssm-ID: 465485  Cd Length: 124  Bit Score: 219.87  E-value: 1.19e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703     29 LYFSRDAYWEKLYVDQAAGTPLLYVHALRDAPEEVPSFRLGQHLyGTYRTRLHENNWICIQEDTGLLYLNRSLDHSSWEK 108
Cdd:pfam17756    1 LYFPQKEYSENVYVGQPAGTPLLQVHALRDSPSEVPHFYLCQHL-GIYRRRPHYNSWFHIDEDTGLLYLNKTLDRSDFES 79
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 10862703    109 LSVRNRGfPLLTVYLKVFLSPTSLREGECQWPGCARVYFSFFNTSF 154
Cdd:pfam17756   80 LSSGNWG-PLKKLTLQVFLSSTPFREKECHSPTCARVYLSFINATA 124
RET_CLD4 pfam17813
RET Cadherin like domain 4; RET is a single transmembrane-spanning receptor tyrosine kinase ...
404-506 8.61e-60

RET Cadherin like domain 4; RET is a single transmembrane-spanning receptor tyrosine kinase (RTK) that plays critical roles in the development of vertebrates. Structural analysis indicate that the ligand-binding RET ectodomain (RET-ECD) contains four consecutive cadherin-like domains (CLD1-CLD4) followed by a membrane-proximal cysteine-rich domain (CRD). This entry relates to CLD4 which is required for CRD folding.


Pssm-ID: 465517  Cd Length: 104  Bit Score: 199.48  E-value: 8.61e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703    404 LPS-TYSLSVSRRARRFAQIGKVCVENCQAFSGINVQYKLHSSGANCSTLGVVTSAEDTSGILFVNDTKALRRPKCAELH 482
Cdd:pfam17813    1 FPNvTYSFTVSRRARRYAQIGKVCVENCQEFSGIRVQYRLQPSDTNCYALGVATSPEDTSGTLYVNDTEALRRPECQELQ 80
                           90       100
                   ....*....|....*....|....
gi 10862703    483 YMVVATDQQTSRQAQAQLLVTVEG 506
Cdd:pfam17813   81 YTVVAQEQQTQLQAQTQLLVTVEG 104
RET_CLD3 pfam17812
RET Cadherin like domain 3; RET is a single transmembrane-spanning receptor tyrosine kinase ...
265-379 2.26e-58

RET Cadherin like domain 3; RET is a single transmembrane-spanning receptor tyrosine kinase (RTK) that plays critical roles in the development of vertebrates. Structural analysis indicate that RET contains four consecutive cadherin-like domains (CLD). This entry relates to CLD3. Classical cadherin calcium-coordinating motifs can be found between CLD2 and CLD3.


Pssm-ID: 465516  Cd Length: 114  Bit Score: 196.07  E-value: 2.26e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703    265 EDDSAPTFpAGVDTASAVVEFKRKEDTVVATLRVFDADVVPA--SGELVRRYTSTLLPGDTWAQQTFRVEHWPNETSVQA 342
Cdd:pfam17812    1 EDDSAPYV-NGTDTADAVVEFNRKEGTVFGTLRVFDRDTTPIypKDQSHNKYVGTLLTNDPWIKETFRIEHSFNETKAIF 79
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 10862703    343 NGsfVRATVHDYRLVLNRNLSISENRTMQLAVLVNDS 379
Cdd:pfam17812   80 GN--VRGTVHEYKLVLNRNLPITENRSLQLDYLVNDT 114
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
725-996 2.93e-27

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 117.04  E-value: 2.93e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  725 VLGKTLGEGEFGKVVKATAFHLkGRagytTVAVKMLKEN--ASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLL 802
Cdd:COG0515   10 RILRLLGRGGMGVVYLARDLRL-GR----PVALKVLRPElaADPEARERFRREARALARLNHPNIVRVYDVGEEDGRPYL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  803 IVEYAKYGSLRGFLREsrkvgpgylgsggsrnsssldhpdERALTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNILV 882
Cdd:COG0515   85 VMEYVEGESLADLLRR------------------------RGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILL 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  883 AEGRKMKISDFGLSRDVyeEDSYVKRSQGRI-PVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTlGGNPYPGIPPERLF 961
Cdd:COG0515  141 TPDGRVKLIDFGIARAL--GGATLTQTGTVVgTPGYMAPEQARGEPVDPRSDVYSLGVTLYELLT-GRPPFDGDSPAELL 217
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 10862703  962 nllkTGHRMERP-------DNCSEEMYRLMLQCWKQEPDKRP 996
Cdd:COG0515  218 ----RAHLREPPpppselrPDLPPALDAIVLRALAKDPEERY 255
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
677-996 2.20e-16

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 82.18  E-value: 2.20e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703   677 RRPAQAFPV----SYSSSGARRPSLDSMENQVSVDAFKILEdpkwefpRKNLVlgktlGEGEFGKVVKATaFHLKGRagy 752
Cdd:PLN00034   37 RDPSLAVPLplppPSSSSSSSSSSSASGSAPSAAKSLSELE-------RVNRI-----GSGAGGTVYKVI-HRPTGR--- 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703   753 tTVAVKMLKENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVEYAKYGSLRGflresRKVGpgylgsggs 832
Cdd:PLN00034  101 -LYALKVIYGNHEDTVRRQICREIEILRDVNHPNVVKCHDMFDHNGEIQVLLEFMDGGSLEG-----THIA--------- 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703   833 rnsssldhpDERALTmgDLisfAWQISQGMQYLAEMKLVHRDLAARNILVAEGRKMKISDFGLSRDVYEEDSYVKRSQGR 912
Cdd:PLN00034  166 ---------DEQFLA--DV---ARQILSGIAYLHRRHIVHRDIKPSNLLINSAKNVKIADFGVSRILAQTMDPCNSSVGT 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703   913 IpvKWMAIE----SLFDHIYTTQS-DVWSFGVLLWEIVtLGGNPYpGIPPERLFNLLKTGHRM----ERPDNCSEEMYRL 983
Cdd:PLN00034  232 I--AYMSPErintDLNHGAYDGYAgDIWSLGVSILEFY-LGRFPF-GVGRQGDWASLMCAICMsqppEAPATASREFRHF 307
                         330
                  ....*....|...
gi 10862703   984 MLQCWKQEPDKRP 996
Cdd:PLN00034  308 ISCCLQREPAKRW 320
Cadherin pfam00028
Cadherin domain;
172-261 4.10e-16

Cadherin domain;


Pssm-ID: 394985 [Multi-domain]  Cd Length: 92  Bit Score: 74.64  E-value: 4.10e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703    172 PSFRIRENRPPGTF-HQFRLLPVQfLCPNISVAYRLLEG-EGLPFRCAPDSLEVSTRWALDREQREKYELVAVCTVHAG- 248
Cdd:pfam00028    1 YSASVPENAPVGTEvLTVTATDPD-LGPNGRIFYSILGGgPGGNFRIDPDTGDISTTKPLDRESIGEYELTVEATDSGGp 79
                           90
                   ....*....|...
gi 10862703    249 AREEVVMVPFPVT 261
Cdd:pfam00028   80 PLSSTATVTITVL 92
CA smart00112
Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. ...
198-270 1.35e-06

Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. Cadherin domains occur as repeats in the extracellular regions which are thought to mediate cell-cell contact when bound to calcium.


Pssm-ID: 214520 [Multi-domain]  Cd Length: 81  Bit Score: 47.34  E-value: 1.35e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 10862703     198 PNISVAYRLLEG-EGLPFRCAPDSLEVSTRWALDREQREKYELVAVCTVHaGAREEVVMVPFPVTVYDEDDSAP 270
Cdd:smart00112    9 ENGKVTYSILSGnDDGLFSIDPETGEITTTKPLDREEQPEYTLTVEATDG-GGPPLSSTATVTITVLDVNDNAP 81
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
726-954 1.37e-06

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 52.49  E-value: 1.37e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703   726 LGKTLGEGEFGKVVKATAfHLKGRagytTVAVKMLKenaspSEL-RDllSEFnVLK---------QVNHPHVIKLY--Ga 793
Cdd:NF033483   11 IGERIGRGGMAEVYLAKD-TRLDR----DVAVKVLR-----PDLaRD--PEF-VARfrreaqsaaSLSHPNIVSVYdvG- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703   794 csQDGPLLLIV-EYAKYGSLRGFLRESRKVGPgylgsggsrnsssldhpdERALTMGDlisfawQISQGMQYLAEMKLVH 872
Cdd:NF033483   77 --EDGGIPYIVmEYVDGRTLKDYIREHGPLSP------------------EEAVEIMI------QILSALEHAHRNGIVH 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703   873 RDLAARNILVAEGRKMKISDFGLSRDVYEED-----------SYVKRSQGR-IPVkwmaieslfdhiyTTQSDVWSFGVL 940
Cdd:NF033483  131 RDIKPQNILITKDGRVKVTDFGIARALSSTTmtqtnsvlgtvHYLSPEQARgGTV-------------DARSDIYSLGIV 197
                         250
                  ....*....|....
gi 10862703   941 LWEIVTlGGNPYPG 954
Cdd:NF033483  198 LYEMLT-GRPPFDG 210
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
173-267 1.41e-06

Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. The cadherin repeat domains occur as tandem repeats in the extracellular regions, which are thought to mediate cell-cell contact when bound to calcium. They play numerous roles in cell fate, signalling, proliferation, differentiation, and migration; members include E-, N-, P-, T-, VE-, CNR-, proto-, and FAT-family cadherin, desmocollin, and desmoglein, a large variety of domain architectures with varying repeat copy numbers. Cadherin-repeat containing proteins exist as monomers, homodimers, or heterodimers.


Pssm-ID: 206637 [Multi-domain]  Cd Length: 98  Bit Score: 47.69  E-value: 1.41e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  173 SFRIRENRPPGTfhqfrllPVQFLC-------PNISVAYRLLEG-EGLPFRCAPDSLEVSTRWALDREQREKYELVAVCT 244
Cdd:cd11304    3 EVSVPENAPPGT-------VVLTVSatdpdsgENGEVTYSIVSGnEDGLFSIDPSTGEITTAKPLDREEQSSYTLTVTAT 75
                         90       100
                 ....*....|....*....|...
gi 10862703  245 VHAGAREEVVmVPFPVTVYDEDD 267
Cdd:cd11304   76 DGGGPPLSST-ATVTITVLDVND 97
 
Name Accession Description Interval E-value
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
723-1012 0e+00

Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. RET is a receptor PTK (RTK) containing an extracellular region with four cadherin-like repeats, a calcium-binding site, and a cysteine-rich domain, a transmembrane segment, and an intracellular catalytic domain. It is part of a multisubunit complex that binds glial-derived neurotropic factor (GDNF) family ligands (GFLs) including GDNF, neurturin, artemin, and persephin. GFLs bind RET along with four GPI-anchored coreceptors, bringing two RET molecules together, leading to autophosphorylation, activation, and intracellular signaling. RET is essential for the development of the sympathetic, parasympathetic and enteric nervous systems, and the kidney. RET disruption by germline mutations causes diseases in humans including congenital aganglionosis of the gastrointestinal tract (Hirschsprung's disease) and three related inherited cancers: multiple endocrine neoplasia type 2A (MEN2A), MEN2B, and familial medullary thyroid carcinoma. The RET subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173631 [Multi-domain]  Cd Length: 290  Bit Score: 602.72  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  723 NLVLGKTLGEGEFGKVVKATAFHLKGRAGYTTVAVKMLKENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLL 802
Cdd:cd05045    1 NLVLGKTLGEGEFGKVVKATAFRLKGRAGYTTVAVKMLKENASSSELRDLLSEFNLLKQVNHPHVIKLYGACSQDGPLLL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  803 IVEYAKYGSLRGFLRESRKVGPGYLGSGGSRNSSSLDHPDERALTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNILV 882
Cdd:cd05045   81 IVEYAKYGSLRSFLRESRKVGPSYLGSDGNRNSSYLDNPDERALTMGDLISFAWQISRGMQYLAEMKLVHRDLAARNVLV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  883 AEGRKMKISDFGLSRDVYEEDSYVKRSQGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLGGNPYPGIPPERLFN 962
Cdd:cd05045  161 AEGRKMKISDFGLSRDVYEEDSYVKRSKGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLGGNPYPGIAPERLFN 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 10862703  963 LLKTGHRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADISKDLEKMMVKR 1012
Cdd:cd05045  241 LLKTGYRMERPENCSEEMYNLMLTCWKQEPDKRPTFADISKELEKMMVKS 290
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
711-1009 9.51e-145

Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The FGFR subfamily consists of FGFR1, FGFR2, FGFR3, FGFR4, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, and to heparin/heparan sulfate (HS) results in the formation of a ternary complex, which leads to receptor dimerization and activation, and intracellular signaling. There are at least 23 FGFs and four types of FGFRs. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. FGF/FGFR signaling is important in the regulation of embryonic development, homeostasis, and regenerative processes. Depending on the cell type and stage, FGFR signaling produces diverse cellular responses including proliferation, growth arrest, differentiation, and apoptosis. Aberrant signaling leads to many human diseases such as skeletal, olfactory, and metabolic disorders, as well as cancer. The FGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase .


Pssm-ID: 270646 [Multi-domain]  Cd Length: 294  Bit Score: 436.08  E-value: 9.51e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  711 ILEDPKWEFPRKNLVLGKTLGEGEFGKVVKATAFHL-KGRAGYTTVAVKMLKENASPSELRDLLSEFNVLKQV-NHPHVI 788
Cdd:cd05053    1 LPLDPEWELPRDRLTLGKPLGEGAFGQVVKAEAVGLdNKPNEVVTVAVKMLKDDATEKDLSDLVSEMEMMKMIgKHKNII 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  789 KLYGACSQDGPLLLIVEYAKYGSLRGFLRESRKVGPGYlgsggsrnSSSLDHPDERALTMGDLISFAWQISQGMQYLAEM 868
Cdd:cd05053   81 NLLGACTQDGPLYVVVEYASKGNLREFLRARRPPGEEA--------SPDDPRVPEEQLTQKDLVSFAYQVARGMEYLASK 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  869 KLVHRDLAARNILVAEGRKMKISDFGLSRDVYEEDSYVKRSQGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLG 948
Cdd:cd05053  153 KCIHRDLAARNVLVTEDNVMKIADFGLARDIHHIDYYRKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLG 232
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 10862703  949 GNPYPGIPPERLFNLLKTGHRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADISKDLEKMM 1009
Cdd:cd05053  233 GSPYPGIPVEELFKLLKEGHRMEKPQNCTQELYMLMRDCWHEVPSQRPTFKQLVEDLDRIL 293
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
728-1006 6.27e-140

Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. They can be classified into receptor and non-receptor tyr kinases. PTKs play important roles in many cellular processes including, lymphocyte activation, epithelium growth and maintenance, metabolism control, organogenesis regulation, survival, proliferation, differentiation, migration, adhesion, motility, and morphogenesis. Receptor tyr kinases (RTKs) are integral membrane proteins which contain an extracellular ligand-binding region, a transmembrane segment, and an intracellular tyr kinase domain. RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain, leading to intracellular signaling. Some RTKs are orphan receptors with no known ligands. Non-receptor (or cytoplasmic) tyr kinases are distributed in different intracellular compartments and are usually multi-domain proteins containing a catalytic tyr kinase domain as well as various regulatory domains such as SH3 and SH2. PTKs are usually autoinhibited and require a mechanism for activation. In many PTKs, the phosphorylation of tyr residues in the activation loop is essential for optimal activity. Aberrant expression of PTKs is associated with many development abnormalities and cancers.The PTK family is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270623 [Multi-domain]  Cd Length: 262  Bit Score: 421.95  E-value: 6.27e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  728 KTLGEGEFGKVVKATAFHLKGRAgyTTVAVKMLKENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVEYA 807
Cdd:cd00192    1 KKLGEGAFGEVYKGKLKGGDGKT--VDVAVKTLKEDASESERKDFLKEARVMKKLGHPNVVRLLGVCTEEEPLYLVMEYM 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  808 KYGSLRGFLRESRKVGPgylgsggsrnsssldHPDERALTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNILVAEGRK 887
Cdd:cd00192   79 EGGDLLDFLRKSRPVFP---------------SPEPSTLSLKDLLSFAIQIAKGMEYLASKKFVHRDLAARNCLVGEDLV 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  888 MKISDFGLSRDVYEEDSYVKRSQGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLGGNPYPGIPPERLFNLLKTG 967
Cdd:cd00192  144 VKISDFGLSRDIYDDDYYRKKTGGKLPIRWMAPESLKDGIFTSKSDVWSFGVLLWEIFTLGATPYPGLSNEEVLEYLRKG 223
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 10862703  968 HRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADISKDLE 1006
Cdd:cd00192  224 YRLPKPENCPDELYELMLSCWQLDPEDRPTFSELVERLE 262
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
724-1005 9.00e-134

Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. Protein kinases catalyze the transfer of the gamma phosphate from nucleotide triphosphates (often ATP) to one or more amino acid residues in a protein substrate side chain, resulting in a conformational change affecting protein function. Phosphoprotein phosphatases catalyze the reverse process. Protein kinases fall into three broad classes, characterized with respect to substrate specificity; Serine/threonine-protein kinases, tyrosine-protein kinases, and dual specificity protein kinases (e.g. MEK - phosphorylates both Thr and Tyr on target proteins). This entry represents the catalytic domain found in a number of serine/threonine- and tyrosine-protein kinases. It does not include the catalytic domain of dual specificity kinases.


Pssm-ID: 462242 [Multi-domain]  Cd Length: 258  Bit Score: 405.73  E-value: 9.00e-134
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703    724 LVLGKTLGEGEFGKVVKATAFHLKGRAGyTTVAVKMLKENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLI 803
Cdd:pfam07714    1 LTLGEKLGEGAFGEVYKGTLKGEGENTK-IKVAVKTLKEGADEEEREDFLEEASIMKKLDHPNIVKLLGVCTQGEPLYIV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703    804 VEYAKYGSLRGFLRESRkvgpgylgsggsrnsssldhpdeRALTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNILVA 883
Cdd:pfam07714   80 TEYMPGGDLLDFLRKHK-----------------------RKLTLKDLLSMALQIAKGMEYLESKNFVHRDLAARNCLVS 136
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703    884 EGRKMKISDFGLSRDVYEEDSYVKRSQGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLGGNPYPGIPPERLFNL 963
Cdd:pfam07714  137 ENLVVKISDFGLSRDIYDDDYYRKRGGGKLPIKWMAPESLKDGKFTSKSDVWSFGVLLWEIFTLGEQPYPGMSNEEVLEF 216
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 10862703    964 LKTGHRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADISKDL 1005
Cdd:pfam07714  217 LEDGYRLPQPENCPDELYDLMKQCWAYDPEDRPTFSELVEDL 258
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
724-1005 3.57e-131

Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class of kinases can not be predicted. Possible dual-specificity Ser/Thr/Tyr kinase.


Pssm-ID: 214568 [Multi-domain]  Cd Length: 258  Bit Score: 398.85  E-value: 3.57e-131
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703     724 LVLGKTLGEGEFGKVVKATAFHLKGrAGYTTVAVKMLKENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLI 803
Cdd:smart00221    1 LTLGKKLGEGAFGEVYKGTLKGKGD-GKEVEVAVKTLKEDASEQQIEEFLREARIMRKLDHPNIVKLLGVCTEEEPLMIV 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703     804 VEYAKYGSLRGFLRESRkvgpgylgsggsrnsssldhpdERALTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNILVA 883
Cdd:smart00221   80 MEYMPGGDLLDYLRKNR----------------------PKELSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVG 137
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703     884 EGRKMKISDFGLSRDVYEEDsYVKRSQGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLGGNPYPGIPPERLFNL 963
Cdd:smart00221  138 ENLVVKISDFGLSRDLYDDD-YYKVKGGKLPIRWMAPESLKEGKFTSKSDVWSFGVLLWEIFTLGEEPYPGMSNAEVLEY 216
                           250       260       270       280
                    ....*....|....*....|....*....|....*....|..
gi 10862703     964 LKTGHRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADISKDL 1005
Cdd:smart00221  217 LKKGYRLPKPPNCPPELYKLMLQCWAEDPEDRPTFSELVEIL 258
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
724-1005 5.44e-131

Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 398.44  E-value: 5.44e-131
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703     724 LVLGKTLGEGEFGKVVKATAFHLKGrAGYTTVAVKMLKENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLI 803
Cdd:smart00219    1 LTLGKKLGEGAFGEVYKGKLKGKGG-KKKVEVAVKTLKEDASEQQIEEFLREARIMRKLDHPNVVKLLGVCTEEEPLYIV 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703     804 VEYAKYGSLRGFLRESRKvgpgylgsggsrnsssldhpderALTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNILVA 883
Cdd:smart00219   80 MEYMEGGDLLSYLRKNRP-----------------------KLSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVG 136
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703     884 EGRKMKISDFGLSRDVYEEDSYVKRSqGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLGGNPYPGIPPERLFNL 963
Cdd:smart00219  137 ENLVVKISDFGLSRDLYDDDYYRKRG-GKLPIRWMAPESLKEGKFTSKSDVWSFGVLLWEIFTLGEQPYPGMSNEEVLEY 215
                           250       260       270       280
                    ....*....|....*....|....*....|....*....|..
gi 10862703     964 LKTGHRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADISKDL 1005
Cdd:smart00219  216 LKNGYRLPQPPNCPPELYDLMLQCWAEDPEDRPTFSELVEIL 257
PTKc_FGFR4 cd05099
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs ...
714-1023 9.70e-123

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Unlike other FGFRs, there is only one splice form of FGFR4. It binds FGF1, FGF2, FGF6, FGF19, and FGF23. FGF19 is a selective ligand for FGFR4. Although disruption of FGFR4 in mice causes no obvious phenotype, in vivo inhibition of FGFR4 in cultured skeletal muscle cells resulted in an arrest of muscle progenitor differentiation. FGF6 and FGFR4 are uniquely expressed in myofibers and satellite cells. FGF6/FGFR4 signaling appears to play a key role in the regulation of muscle regeneration. A polymorphism in FGFR4 is found in head and neck squamous cell carcinoma. FGFR4 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR4 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133230 [Multi-domain]  Cd Length: 314  Bit Score: 379.31  E-value: 9.70e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  714 DPKWEFPRKNLVLGKTLGEGEFGKVVKATAFHL-KGRAGYT-TVAVKMLKENASPSELRDLLSEFNVLKQVN-HPHVIKL 790
Cdd:cd05099    4 DPKWEFPRDRLVLGKPLGEGCFGQVVRAEAYGIdKSRPDQTvTVAVKMLKDNATDKDLADLISEMELMKLIGkHKNIINL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  791 YGACSQDGPLLLIVEYAKYGSLRGFLRESRKVGPGYlgsggsrnssSLDHPD--ERALTMGDLISFAWQISQGMQYLAEM 868
Cdd:cd05099   84 LGVCTQEGPLYVIVEYAAKGNLREFLRARRPPGPDY----------TFDITKvpEEQLSFKDLVSCAYQVARGMEYLESR 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  869 KLVHRDLAARNILVAEGRKMKISDFGLSRDVYEEDSYVKRSQGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLG 948
Cdd:cd05099  154 RCIHRDLAARNVLVTEDNVMKIADFGLARGVHDIDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILMWEIFTLG 233
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 10862703  949 GNPYPGIPPERLFNLLKTGHRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADISKDLEKMMVK-RRDYLDLaaSTP 1023
Cdd:cd05099  234 GSPYPGIPVEELFKLLREGHRMDKPSNCTHELYMLMRECWHAVPTQRPTFKQLVEALDKVLAAvSEEYLDL--SMP 307
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
706-1009 9.72e-112

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. There are many splice variants of FGFR2 which show differential expression and binding to FGF ligands. Disruption of either FGFR2 or FGFR2b is lethal in mice, due to defects in the placenta or severe impairment of tissue development including lung, limb, and thyroid, respectively. Disruption of FGFR2c in mice results in defective bone and skull development. Genetic alterations of FGFR2 are associated with many human skeletal disorders including Apert syndrome, Crouzon syndrome, Jackson-Weiss syndrome, and Pfeiffer syndrome. FGFR2 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270679 [Multi-domain]  Cd Length: 313  Bit Score: 350.08  E-value: 9.72e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  706 VDAFKILEDPKWEFPRKNLVLGKTLGEGEFGKVVKATAFHL-KGRAGYT-TVAVKMLKENASPSELRDLLSEFNVLKQV- 782
Cdd:cd05101    8 VSEYELPEDPKWEFPRDKLTLGKPLGEGCFGQVVMAEAVGIdKDKPKEAvTVAVKMLKDDATEKDLSDLVSEMEMMKMIg 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  783 NHPHVIKLYGACSQDGPLLLIVEYAKYGSLRGFLRESRKVGPGYLGSGGSRnsssldhPDERaLTMGDLISFAWQISQGM 862
Cdd:cd05101   88 KHKNIINLLGACTQDGPLYVIVEYASKGNLREYLRARRPPGMEYSYDINRV-------PEEQ-MTFKDLVSCTYQLARGM 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  863 QYLAEMKLVHRDLAARNILVAEGRKMKISDFGLSRDVYEEDSYVKRSQGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLW 942
Cdd:cd05101  160 EYLASQKCIHRDLAARNVLVTENNVMKIADFGLARDINNIDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLMW 239
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 10862703  943 EIVTLGGNPYPGIPPERLFNLLKTGHRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADISKDLEKMM 1009
Cdd:cd05101  240 EIFTLGGSPYPGIPVEELFKLLKEGHRMDKPANCTNELYMMMRDCWHAVPSQRPTFKQLVEDLDRIL 306
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
713-1009 1.59e-111

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Alternative splicing of FGFR1 transcripts produces a variety of isoforms, which are differentially expressed in cells. FGFR1 binds the ligands, FGF1 and FGF2, with high affinity and has also been reported to bind FGF4, FGF6, and FGF9. FGFR1 signaling is critical in the control of cell migration during embryo development. It promotes cell proliferation in fibroblasts. Nuclear FGFR1 plays a role in the regulation of transcription. Mutations, insertions or deletions of FGFR1 have been identified in patients with Kallman's syndrome (KS), an inherited disorder characterized by hypogonadotropic hypogonadism and loss of olfaction. Aberrant FGFR1 expression has been found in some human cancers including 8P11 myeloproliferative syndrome (EMS), breast cancer, and pancreatic adenocarcinoma. FGFR1 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270678 [Multi-domain]  Cd Length: 302  Bit Score: 348.93  E-value: 1.59e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  713 EDPKWEFPRKNLVLGKTLGEGEFGKVVKATAFHLKGRA--GYTTVAVKMLKENASPSELRDLLSEFNVLKQV-NHPHVIK 789
Cdd:cd05098    4 EDPRWELPRDRLVLGKPLGEGCFGQVVLAEAIGLDKDKpnRVTKVAVKMLKSDATEKDLSDLISEMEMMKMIgKHKNIIN 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  790 LYGACSQDGPLLLIVEYAKYGSLRGFLRESRKVGPGYLGSGgsrnssslDHPDERALTMGDLISFAWQISQGMQYLAEMK 869
Cdd:cd05098   84 LLGACTQDGPLYVIVEYASKGNLREYLQARRPPGMEYCYNP--------SHNPEEQLSSKDLVSCAYQVARGMEYLASKK 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  870 LVHRDLAARNILVAEGRKMKISDFGLSRDVYEEDSYVKRSQGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLGG 949
Cdd:cd05098  156 CIHRDLAARNVLVTEDNVMKIADFGLARDIHHIDYYKKTTNGRLPVKWMAPEALFDRIYTHQSDVWSFGVLLWEIFTLGG 235
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  950 NPYPGIPPERLFNLLKTGHRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADISKDLEKMM 1009
Cdd:cd05098  236 SPYPGVPVEELFKLLKEGHRMDKPSNCTNELYMMMRDCWHAVPSQRPTFKQLVEDLDRIV 295
PTKc_FGFR3 cd05100
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs ...
714-1019 1.87e-108

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Many FGFR3 splice variants have been reported with the IIIb and IIIc isoforms being the predominant forms. FGFR3 IIIc is the isoform expressed in chondrocytes, the cells affected in dwarfism, while IIIb is expressed in epithelial cells. FGFR3 ligands include FGF1, FGF2, FGF4, FGF8, FGF9, and FGF23. It is a negative regulator of long bone growth. In the cochlear duct and in the lens, FGFR3 is involved in differentiation while it appears to have a role in cell proliferation in epithelial cells. Germline mutations in FGFR3 are associated with skeletal disorders including several forms of dwarfism. Some missense mutations are associated with multiple myeloma and carcinomas of the bladder and cervix. Overexpression of FGFR3 is found in thyroid carcinoma. FGFR3 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR3 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173652 [Multi-domain]  Cd Length: 334  Bit Score: 342.00  E-value: 1.87e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  714 DPKWEFPRKNLVLGKTLGEGEFGKVVKATAFHLKGR--AGYTTVAVKMLKENASPSELRDLLSEFNVLKQV-NHPHVIKL 790
Cdd:cd05100    4 DPKWELSRTRLTLGKPLGEGCFGQVVMAEAIGIDKDkpNKPVTVAVKMLKDDATDKDLSDLVSEMEMMKMIgKHKNIINL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  791 YGACSQDGPLLLIVEYAKYGSLRGFLRESRKVGPGYlgsggsrNSSSLDHPDERaLTMGDLISFAWQISQGMQYLAEMKL 870
Cdd:cd05100   84 LGACTQDGPLYVLVEYASKGNLREYLRARRPPGMDY-------SFDTCKLPEEQ-LTFKDLVSCAYQVARGMEYLASQKC 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  871 VHRDLAARNILVAEGRKMKISDFGLSRDVYEEDSYVKRSQGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLGGN 950
Cdd:cd05100  156 IHRDLAARNVLVTEDNVMKIADFGLARDVHNIDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGS 235
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 10862703  951 PYPGIPPERLFNLLKTGHRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADISKDLEKM--MVKRRDYLDLA 1019
Cdd:cd05100  236 PYPGIPVEELFKLLKEGHRMDKPANCTHELYMIMRECWHAVPSQRPTFKQLVEDLDRVltVTSTDEYLDLS 306
PTKc_VEGFR cd05054
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
716-1005 7.16e-108

Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The VEGFR subfamily consists of VEGFR1 (Flt1), VEGFR2 (Flk1), VEGFR3 (Flt4), and similar proteins. VEGFR subfamily members are receptor PTKss (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. In VEGFR3, the fifth Ig-like domain is replaced by a disulfide bridge. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. There are five VEGF ligands in mammals, which bind, in an overlapping pattern to the three VEGFRs, which can form homo or heterodimers. VEGFRs regulate the cardiovascular system. They are critical for vascular development during embryogenesis and blood vessel formation in adults. They induce cellular functions common to other growth factor receptors such as cell migration, survival, and proliferation. The VEGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270647 [Multi-domain]  Cd Length: 298  Bit Score: 339.08  E-value: 7.16e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  716 KWEFPRKNLVLGKTLGEGEFGKVVKATAFHLKGRAGYTTVAVKMLKENASPSELRDLLSEFNVLKQV-NHPHVIKLYGAC 794
Cdd:cd05054    1 KWEFPRDRLKLGKPLGRGAFGKVIQASAFGIDKSATCRTVAVKMLKEGATASEHKALMTELKILIHIgHHLNVVNLLGAC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  795 S-QDGPLLLIVEYAKYGSLRGFLRESRKVGPGYLGSGGSRNSSSLDHPD--ERALTMGDLISFAWQISQGMQYLAEMKLV 871
Cdd:cd05054   81 TkPGGPLMVIVEFCKFGNLSNYLRSKREEFVPYRDKGARDVEEEEDDDElyKEPLTLEDLICYSFQVARGMEFLASRKCI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  872 HRDLAARNILVAEGRKMKISDFGLSRDVYEEDSYVKRSQGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLGGNP 951
Cdd:cd05054  161 HRDLAARNILLSENNVVKICDFGLARDIYKDPDYVRKGDARLPLKWMAPESIFDKVYTTQSDVWSFGVLLWEIFSLGASP 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 10862703  952 YPGIP-PERLFNLLKTGHRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADISKDL 1005
Cdd:cd05054  241 YPGVQmDEEFCRRLKEGTRMRAPEYTTPEIYQIMLDCWHGEPKERPTFSELVEKL 295
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
702-1009 2.08e-105

Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The PDGFR subfamily consists of PDGFR alpha, PDGFR beta, KIT, CSF-1R, the mammalian FLT3, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. PDGFR kinase domains are autoinhibited by their juxtamembrane regions containing tyr residues. The binding to their ligands leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. PDGFR subfamily receptors are important in the development of a variety of cells. PDGFRs are expressed in a many cells including fibroblasts, neurons, endometrial cells, mammary epithelial cells, and vascular smooth muscle cells. PDGFR signaling is critical in normal embryonic development, angiogenesis, and wound healing. Kit is important in the development of melanocytes, germ cells, mast cells, hematopoietic stem cells, the interstitial cells of Cajal, and the pacemaker cells of the GI tract. CSF-1R signaling is critical in the regulation of macrophages and osteoclasts. Mammalian FLT3 plays an important role in the survival, proliferation, and differentiation of stem cells. The PDGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase .


Pssm-ID: 133186 [Multi-domain]  Cd Length: 302  Bit Score: 332.91  E-value: 2.08e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  702 NQVSVDAFKILEDPKWEFPRKNLVLGKTLGEGEFGKVVKATAFHLKGRAGYTTVAVKMLKENASPSELRDLLSEFNVLKQ 781
Cdd:cd05055   15 EYVYIDPTQLPYDLKWEFPRNNLSFGKTLGAGAFGKVVEATAYGLSKSDAVMKVAVKMLKPTAHSSEREALMSELKIMSH 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  782 V-NHPHVIKLYGACSQDGPLLLIVEYAKYGSLRGFLRESRkvgpgylgsggsrnsssldhpdERALTMGDLISFAWQISQ 860
Cdd:cd05055   95 LgNHENIVNLLGACTIGGPILVITEYCCYGDLLNFLRRKR----------------------ESFLTLEDLLSFSYQVAK 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  861 GMQYLAEMKLVHRDLAARNILVAEGRKMKISDFGLSRDVYEEDSYVKRSQGRIPVKWMAIESLFDHIYTTQSDVWSFGVL 940
Cdd:cd05055  153 GMAFLASKNCIHRDLAARNVLLTHGKIVKICDFGLARDIMNDSNYVVKGNARLPVKWMAPESIFNCVYTFESDVWSYGIL 232
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  941 LWEIVTLGGNPYPGIPPERLF-NLLKTGHRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADISKDLEKMM 1009
Cdd:cd05055  233 LWEIFSLGSNPYPGMPVDSKFyKLIKEGYRMAQPEHAPAEIYDIMKTCWDADPLKRPTFKQIVQLIGKQL 302
PTKc_VEGFR1 cd14207
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
716-1005 3.17e-99

Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. VEGFR1 (or Flt1) binds VEGFA, VEGFB, and placenta growth factor (PLGF). It regulates monocyte and macrophage migration, vascular permeability, haematopoiesis, and the recruitment of haematopietic progenitor cells from the bone marrow. VEGFR1 is a member of the VEGFR subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. The VEGFR1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271109 [Multi-domain]  Cd Length: 340  Bit Score: 317.71  E-value: 3.17e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  716 KWEFPRKNLVLGKTLGEGEFGKVVKATAFHLKGRAGYTTVAVKMLKENASPSELRDLLSEFNVLKQV-NHPHVIKLYGAC 794
Cdd:cd14207    1 KWEFARERLKLGKSLGRGAFGKVVQASAFGIKKSPTCRVVAVKMLKEGATASEYKALMTELKILIHIgHHLNVVNLLGAC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  795 S-QDGPLLLIVEYAKYGSLRGFLRESR------------------KVGPGYLGSGGSRNSSSLDHPD------------- 842
Cdd:cd14207   81 TkSGGPLMVIVEYCKYGNLSNYLKSKRdffvtnkdtslqeelikeKKEAEPTGGKKKRLESVTSSESfassgfqedksls 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  843 -------------ERALTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNILVAEGRKMKISDFGLSRDVYEEDSYVKRS 909
Cdd:cd14207  161 dveeeeedsgdfyKRPLTMEDLISYSFQVARGMEFLSSRKCIHRDLAARNILLSENNVVKICDFGLARDIYKNPDYVRKG 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  910 QGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLGGNPYPGIP-PERLFNLLKTGHRMERPDNCSEEMYRLMLQCW 988
Cdd:cd14207  241 DARLPLKWMAPESIFDKIYSTKSDVWSYGVLLWEIFSLGASPYPGVQiDEDFCSKLKEGIRMRAPEFATSEIYQIMLDCW 320
                        330
                 ....*....|....*..
gi 10862703  989 KQEPDKRPVFADISKDL 1005
Cdd:cd14207  321 QGDPNERPRFSELVERL 337
PTKc_VEGFR3 cd05102
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; ...
716-1012 3.76e-98

Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. VEGFR3 (or Flt4) preferentially binds the ligands VEGFC and VEGFD. VEGFR3 is essential for lymphatic endothelial cell (EC) development and function. It has been shown to regulate adaptive immunity during corneal transplantation. VEGFR3 is upregulated on blood vascular ECs in pathological conditions such as vascular tumors and the periphery of solid tumors. It plays a role in cancer progression and lymph node metastasis. Missense mutations in the VEGFR3 gene are associated with primary human lymphedema. VEGFR3 is a member of the VEGFR subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. In VEGFR3, the fifth Ig-like domain is replaced by a disulfide bridge. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. The VEGFR3 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270680 [Multi-domain]  Cd Length: 336  Bit Score: 314.61  E-value: 3.76e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  716 KWEFPRKNLVLGKTLGEGEFGKVVKATAFHLKGRAGYTTVAVKMLKENASPSELRDLLSEFNVLKQV-NHPHVIKLYGAC 794
Cdd:cd05102    1 QWEFPRDRLRLGKVLGHGAFGKVVEASAFGIDKSSSCETVAVKMLKEGATASEHKALMSELKILIHIgNHLNVVNLLGAC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  795 SQ-DGPLLLIVEYAKYGSLRGFLR-----------------------------ESRKVGPGYLGSGGSRNSSSLDHPDER 844
Cdd:cd05102   81 TKpNGPLMVIVEFCKYGNLSNFLRakregfspyrersprtrsqvrsmveavraDRRSRQGSDRVASFTESTSSTNQPRQE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  845 A-------LTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNILVAEGRKMKISDFGLSRDVYEEDSYVKRSQGRIPVKW 917
Cdd:cd05102  161 VddlwqspLTMEDLICYSFQVARGMEFLASRKCIHRDLAARNILLSENNVVKICDFGLARDIYKDPDYVRKGSARLPLKW 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  918 MAIESLFDHIYTTQSDVWSFGVLLWEIVTLGGNPYPGIP-PERLFNLLKTGHRMERPDNCSEEMYRLMLQCWKQEPDKRP 996
Cdd:cd05102  241 MAPESIFDKVYTTQSDVWSFGVLLWEIFSLGASPYPGVQiNEEFCQRLKDGTRMRAPEYATPEIYRIMLSCWHGDPKERP 320
                        330
                 ....*....|....*.
gi 10862703  997 VFADISKDLEKMMVKR 1012
Cdd:cd05102  321 TFSDLVEILGDLLQEN 336
PTKc_VEGFR2 cd05103
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; ...
716-1009 2.95e-97

Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. VEGFR2 (or Flk1) binds the ligands VEGFA, VEGFC, VEGFD and VEGFE. VEGFR2 signaling is implicated in all aspects of normal and pathological vascular endothelial cell biology. It induces a variety of cellular effects including migration, survival, and proliferation. It is critical in regulating embryonic vascular development and angiogenesis. VEGFR2 is the major signal transducer in pathological angiogenesis including cancer and diabetic retinopathy, and is a target for inhibition in cancer therapy. The carboxyl terminus of VEGFR2 plays an important role in its autophosphorylation and activation. VEGFR2 is a member of the VEGFR subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. The VEGFR2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270681 [Multi-domain]  Cd Length: 343  Bit Score: 312.69  E-value: 2.95e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  716 KWEFPRKNLVLGKTLGEGEFGKVVKATAFHLKGRAGYTTVAVKMLKENASPSELRDLLSEFNVLKQV-NHPHVIKLYGAC 794
Cdd:cd05103    1 KWEFPRDRLKLGKPLGRGAFGQVIEADAFGIDKTATCRTVAVKMLKEGATHSEHRALMSELKILIHIgHHLNVVNLLGAC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  795 SQ-DGPLLLIVEYAKYGSLRGFLRESR---------------------------------------KVGPGYLGSGGSRN 834
Cdd:cd05103   81 TKpGGPLMVIVEFCKFGNLSAYLRSKRsefvpyktkgarfrqgkdyvgdisvdlkrrldsitssqsSASSGFVEEKSLSD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  835 SSSLDHPDE----RALTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNILVAEGRKMKISDFGLSRDVYEEDSYVKRSQ 910
Cdd:cd05103  161 VEEEEAGQEdlykDFLTLEDLICYSFQVAKGMEFLASRKCIHRDLAARNILLSENNVVKICDFGLARDIYKDPDYVRKGD 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  911 GRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLGGNPYPGIPPERLF-NLLKTGHRMERPDNCSEEMYRLMLQCWK 989
Cdd:cd05103  241 ARLPLKWMAPETIFDRVYTIQSDVWSFGVLLWEIFSLGASPYPGVKIDEEFcRRLKEGTRMRAPDYTTPEMYQTMLDCWH 320
                        330       340
                 ....*....|....*....|
gi 10862703  990 QEPDKRPVFADISKDLEKMM 1009
Cdd:cd05103  321 GEPSQRPTFSELVEHLGNLL 340
PTKc_CSF-1R cd05106
Catalytic domain of the Protein Tyrosine Kinase, Colony-Stimulating Factor-1 Receptor; PTKs ...
702-1009 3.43e-96

Catalytic domain of the Protein Tyrosine Kinase, Colony-Stimulating Factor-1 Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. CSF-1R, also called c-Fms, is a member of the Platelet Derived Growth Factor Receptor (PDGFR) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of CSF-1R to its ligand, CSF-1, leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. CSF-1R signaling is critical in the regulation of macrophages and osteoclasts. It leads to increases in gene transcription and protein translation, and induces cytoskeletal remodeling. CSF-1R signaling leads to a variety of cellular responses including survival, proliferation, and differentiation of target cells. It plays an important role in innate immunity, tissue development and function, and the pathogenesis of some diseases including atherosclerosis and cancer. CSF-1R signaling is also implicated in mammary gland development during pregnancy and lactation. Aberrant CSF-1/CSF-1R expression correlates with tumor cell invasiveness, poor clinical prognosis, and bone metastasis in breast cancer. Although the structure of the human CSF-1R catalytic domain is known, it is excluded from this specific alignment model because it contains a deletion in its sequence. The CSF-1R subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133237 [Multi-domain]  Cd Length: 374  Bit Score: 310.62  E-value: 3.43e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  702 NQVSVDAFKILEDPKWEFPRKNLVLGKTLGEGEFGKVVKATAFHLKGRAGYTTVAVKMLKENASPSELRDLLSEFNVLKQ 781
Cdd:cd05106   18 NYTFIDPTQLPYNEKWEFPRDNLQFGKTLGAGAFGKVVEATAFGLGKEDNVLRVAVKMLKASAHTDEREALMSELKILSH 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  782 V-NHPHVIKLYGACSQDGPLLLIVEYAKYGSLRGFLRE--------------------------------------SRKV 822
Cdd:cd05106   98 LgQHKNIVNLLGACTHGGPVLVITEYCCYGDLLNFLRKkaetflnfvmalpeisetssdyknitlekkyirsdsgfSSQG 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  823 GPGYL--------GSGGSRNSSSLDHPDERALTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNILVAEGRKMKISDFG 894
Cdd:cd05106  178 SDTYVemrpvsssSSQSSDSKDEEDTEDSWPLDLDDLLRFSSQVAQGMDFLASKNCIHRDVAARNVLLTDGRVAKICDFG 257
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  895 LSRDVYEEDSYVKRSQGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLGGNPYPGIPPERLF-NLLKTGHRMERP 973
Cdd:cd05106  258 LARDIMNDSNYVVKGNARLPVKWMAPESIFDCVYTVQSDVWSYGILLWEIFSLGKSPYPGILVNSKFyKMVKRGYQMSRP 337
                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 10862703  974 DNCSEEMYRLMLQCWKQEPDKRPVFADISKDLEKMM 1009
Cdd:cd05106  338 DFAPPEIYSIMKMCWNLEPTERPTFSQISQLIQRQL 373
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
717-1001 3.23e-95

Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The InsR subfamily is composed of InsR, Insulin-like Growth Factor-1 Receptor (IGF-1R), and similar proteins. InsR and IGF-1R are receptor PTKs (RTKs) composed of two alphabeta heterodimers. Binding of the ligand (insulin, IGF-1, or IGF-2) to the extracellular alpha subunit activates the intracellular tyr kinase domain of the transmembrane beta subunit. Receptor activation leads to autophosphorylation, stimulating downstream kinase activities, which initiate signaling cascades and biological function. InsR and IGF-1R, which share 84% sequence identity in their kinase domains, display physiologically distinct yet overlapping functions in cell growth, differentiation, and metabolism. InsR activation leads primarily to metabolic effects while IGF-1R activation stimulates mitogenic pathways. In cells expressing both receptors, InsR/IGF-1R hybrids are found together with classical receptors. Both receptors can interact with common adaptor molecules such as IRS-1 and IRS-2. The InsR-like subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173625 [Multi-domain]  Cd Length: 277  Bit Score: 304.27  E-value: 3.23e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  717 WEFPRKNLVLGKTLGEGEFGKVVKATAFHLKGRAGYTTVAVKMLKENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQ 796
Cdd:cd05032    1 WELPREKITLIRELGQGSFGMVYEGLAKGVVKGEPETRVAIKTVNENASMRERIEFLNEASVMKEFNCHHVVRLLGVVST 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  797 DGPLLLIVEYAKYGSLRGFLRESRkvgpgylgsggsrnsssldhPDER------ALTMGDLISFAWQISQGMQYLAEMKL 870
Cdd:cd05032   81 GQPTLVVMELMAKGDLKSYLRSRR--------------------PEAEnnpglgPPTLQKFIQMAAEIADGMAYLAAKKF 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  871 VHRDLAARNILVAEGRKMKISDFGLSRDVYEEDSYVKRSQGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLGGN 950
Cdd:cd05032  141 VHRDLAARNCMVAEDLTVKIGDFGMTRDIYETDYYRKGGKGLLPVRWMAPESLKDGVFTTKSDVWSFGVVLWEMATLAEQ 220
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 10862703  951 PYPGIPPERLFNLLKTGHRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADI 1001
Cdd:cd05032  221 PYQGLSNEEVLKFVIDGGHLDLPENCPDKLLELMRMCWQYNPKMRPTFLEI 271
PTKc_Kit cd05104
Catalytic domain of the Protein Tyrosine Kinase, Kit; PTKs catalyze the transfer of the ...
702-1009 6.72e-90

Catalytic domain of the Protein Tyrosine Kinase, Kit; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Kit is important in the development of melanocytes, germ cells, mast cells, hematopoietic stem cells, the interstitial cells of Cajal, and the pacemaker cells of the GI tract. Kit signaling is involved in major cellular functions including cell survival, proliferation, differentiation, adhesion, and chemotaxis. Mutations in Kit, which result in constitutive ligand-independent activation, are found in human cancers such as gastrointestinal stromal tumor (GIST) and testicular germ cell tumor (TGCT). The aberrant expression of Kit and/or SCF is associated with other tumor types such as systemic mastocytosis and cancers of the breast, neurons, lung, prostate, colon, and rectum. Although the structure of the human Kit catalytic domain is known, it is excluded from this specific alignment model because it contains a deletion in its sequence. Kit is a member of the Platelet Derived Growth Factor Receptor (PDGFR) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of Kit to its ligand, the stem-cell factor (SCF), leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. The Kit subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270682 [Multi-domain]  Cd Length: 375  Bit Score: 293.73  E-value: 6.72e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  702 NQVSVDAFKILEDPKWEFPRKNLVLGKTLGEGEFGKVVKATAFHLKGRAGYTTVAVKMLKENASPSELRDLLSEFNVLKQ 781
Cdd:cd05104   15 NYVYIDPTQLPYDHKWEFPRDRLRFGKTLGAGAFGKVVEATAYGLAKADSAMTVAVKMLKPSAHSTEREALMSELKVLSY 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  782 V-NHPHVIKLYGACSQDGPLLLIVEYAKYGSLRGFLRESR-------------------------------------KVG 823
Cdd:cd05104   95 LgNHINIVNLLGACTVGGPTLVITEYCCYGDLLNFLRRKRdsficpkfedlaeaalyrnllhqremacdslneymdmKPS 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  824 PGYLGSGGSR--------------NSSSLDHPDERALTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNILVAEGRKMK 889
Cdd:cd05104  175 VSYVVPTKADkrrgvrsgsyvdqdVTSEILEEDELALDTEDLLSFSYQVAKGMEFLASKNCIHRDLAARNILLTHGRITK 254
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  890 ISDFGLSRDVYEEDSYVKRSQGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLGGNPYPGIPPE-RLFNLLKTGH 968
Cdd:cd05104  255 ICDFGLARDIRNDSNYVVKGNARLPVKWMAPESIFECVYTFESDVWSYGILLWEIFSLGSSPYPGMPVDsKFYKMIKEGY 334
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 10862703  969 RMERPDNCSEEMYRLMLQCWKQEPDKRPVFADISKDLEKMM 1009
Cdd:cd05104  335 RMDSPEFAPSEMYDIMRSCWDADPLKRPTFKQIVQLIEQQL 375
PTKc_PDGFR_alpha cd05105
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor alpha; ...
704-1009 6.36e-87

Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor alpha; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. PDGFR alpha is a receptor PTK (RTK) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding to its ligands, the PDGFs, leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. PDGFR alpha forms homodimers or heterodimers with PDGFR beta, depending on the nature of the PDGF ligand. PDGF-AA, PDGF-AB, and PDGF-CC induce PDGFR alpha homodimerization. PDGFR signaling plays many roles in normal embryonic development and adult physiology. PDGFR alpha signaling is important in the formation of lung alveoli, intestinal villi, mesenchymal dermis, and hair follicles, as well as in the development of oligodendrocytes, retinal astrocytes, neural crest cells, and testicular cells. Aberrant PDGFR alpha expression is associated with some human cancers. Mutations in PDGFR alpha have been found within a subset of gastrointestinal stromal tumors (GISTs). An active fusion protein FIP1L1-PDGFR alpha, derived from interstitial deletion, is associated with idiopathic hypereosinophilic syndrome and chronic eosinophilic leukemia. The PDGFR alpha subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173653 [Multi-domain]  Cd Length: 400  Bit Score: 286.54  E-value: 6.36e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  704 VSVDAFKILEDPKWEFPRKNLVLGKTLGEGEFGKVVKATAFHLKGRAGYTTVAVKMLKENASPSELRDLLSEFNVLKQVN 783
Cdd:cd05105   19 IYVDPMQLPYDSRWEFPRDGLVLGRILGSGAFGKVVEGTAYGLSRSQPVMKVAVKMLKPTARSSEKQALMSELKIMTHLG 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  784 -HPHVIKLYGACSQDGPLLLIVEYAKYGSLRGFLRESRK------------------VGPG-----------------YL 827
Cdd:cd05105   99 pHLNIVNLLGACTKSGPIYIITEYCFYGDLVNYLHKNRDnflsrhpekpkkdldifgINPAdestrsyvilsfenkgdYM 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  828 GSGGSRNSSSL-------------------DHPDE------------------RALTMGDLISFAWQISQGMQYLAEMKL 870
Cdd:cd05105  179 DMKQADTTQYVpmleikeaskysdiqrsnyDRPASykgsndsevknllsddgsEGLTTLDLLSFTYQVARGMEFLASKNC 258
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  871 VHRDLAARNILVAEGRKMKISDFGLSRDVYEEDSYVKRSQGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLGGN 950
Cdd:cd05105  259 VHRDLAARNVLLAQGKIVKICDFGLARDIMHDSNYVSKGSTFLPVKWMAPESIFDNLYTTLSDVWSYGILLWEIFSLGGT 338
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  951 PYPG-IPPERLFNLLKTGHRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADISKDLEKMM 1009
Cdd:cd05105  339 PYPGmIVDSTFYNKIKSGYRMAKPDHATQEVYDIMVKCWNSEPEKRPSFLHLSDIVESLL 398
PTKc_c-ros cd05044
Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the ...
728-1006 8.04e-85

Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily contains c-ros, Sevenless, and similar proteins. The proto-oncogene c-ros encodes an orphan receptor PTK (RTK) with an unknown ligand. RTKs contain an extracellular ligand-binding domain, a transmembrane region, and an intracellular tyr kinase domain. RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. C-ros is expressed in embryonic cells of the kidney, intestine and lung, but disappears soon after birth. It persists only in the adult epididymis. Male mice bearing inactive mutations of c-ros lack the initial segment of the epididymis and are infertile. The Drosophila protein, Sevenless, is required for the specification of the R7 photoreceptor cell during eye development. The c-ros subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270640 [Multi-domain]  Cd Length: 268  Bit Score: 275.83  E-value: 8.04e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  728 KTLGEGEFGKVVKATAFHLKGRA-GYTTVAVKMLKENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVEY 806
Cdd:cd05044    1 KFLGSGAFGEVFEGTAKDILGDGsGETKVAVKTLRKGATDQEKAEFLKEAHLMSNFKHPNILKLLGVCLDNDPQYIILEL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  807 AKYGSLRGFLRESRKVGPGylgsggsrnsssldhpdERALTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNILVAEG- 885
Cdd:cd05044   81 MEGGDLLSYLRAARPTAFT-----------------PPLLTLKDLLSICVDVAKGCVYLEDMHFVHRDLAARNCLVSSKd 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  886 ---RKMKISDFGLSRDVYEEDSYVKRSQGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLGGNPYPGIPPERLFN 962
Cdd:cd05044  144 yreRVVKIGDFGLARDIYKNDYYRKEGEGLLPVRWMAPESLVDGVFTTQSDVWAFGVLMWEILTLGQQPYPARNNLEVLH 223
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 10862703  963 LLKTGHRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADISKDLE 1006
Cdd:cd05044  224 FVRAGGRLDQPDNCPDDLYELMLRCWSTDPEERPSFARILEQLQ 267
PTKc_PDGFR_beta cd05107
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor beta; ...
704-1010 1.13e-84

Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor beta; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. PDGFR beta is a receptor PTK (RTK) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding to its ligands, the PDGFs, leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. PDGFR beta forms homodimers or heterodimers with PDGFR alpha, depending on the nature of the PDGF ligand. PDGF-BB and PDGF-DD induce PDGFR beta homodimerization. PDGFR signaling plays many roles in normal embryonic development and adult physiology. PDGFR beta signaling leads to a variety of cellular effects including the stimulation of cell growth and chemotaxis, as well as the inhibition of apoptosis and GAP junctional communication. It is critical in normal angiogenesis as it is involved in the recruitment of pericytes and smooth muscle cells essential for vessel stability. Aberrant PDGFR beta expression is associated with some human cancers. The continuously-active fusion proteins of PDGFR beta with COL1A1 and TEL are associated with dermatofibrosarcoma protuberans (DFSP) and a subset of chronic myelomonocytic leukemia (CMML), respectively. The PDGFR beta subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133238 [Multi-domain]  Cd Length: 401  Bit Score: 280.36  E-value: 1.13e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  704 VSVDAFKILEDPKWEFPRKNLVLGKTLGEGEFGKVVKATAFHLKGRAGYTTVAVKMLKENASPSELRDLLSEFNVLKQVN 783
Cdd:cd05107   19 IYVDPMQLPYDSAWEMPRDNLVLGRTLGSGAFGRVVEATAHGLSHSQSTMKVAVKMLKSTARSSEKQALMSELKIMSHLG 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  784 -HPHVIKLYGACSQDGPLLLIVEYAKYGSLRGFLRESRKV-------------------------GPGYLGSGGSRNSSS 837
Cdd:cd05107   99 pHLNIVNLLGACTKGGPIYIITEYCRYGDLVDYLHRNKHTflqyyldknrddgslisggstplsqRKSHVSLGSESDGGY 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  838 LDHP-------------------------------------------------DERALTMGDLISFAWQISQGMQYLAEM 868
Cdd:cd05107  179 MDMSkdesadyvpmqdmkgtvkyadiessnyespydqylpsapertrrdtlinESPALSYMDLVGFSYQVANGMEFLASK 258
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  869 KLVHRDLAARNILVAEGRKMKISDFGLSRDVYEEDSYVKRSQGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLG 948
Cdd:cd05107  259 NCVHRDLAARNVLICEGKLVKICDFGLARDIMRDSNYISKGSTFLPLKWMAPESIFNNLYTTLSDVWSFGILLWEIFTLG 338
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 10862703  949 GNPYPGIP-PERLFNLLKTGHRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADISKDLEKMMV 1010
Cdd:cd05107  339 GTPYPELPmNEQFYNAIKRGYRMAKPAHASDEIYEIMQKCWEEKFEIRPDFSQLVHLVGDLLT 401
PTKc_Tie1 cd05089
Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; ...
730-1019 1.31e-84

Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; Tie1; catalytic (c) domain. The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K). PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tie1 is a receptor tyr kinase (RTK) containing an extracellular region, a transmembrane segment, and an intracellular catalytic domain. The extracellular region contains an immunoglobulin (Ig)-like domain, three epidermal growth factor (EGF)-like domains, a second Ig-like domain, and three fibronectin type III repeats. Tie receptors are specifically expressed in endothelial cells and hematopoietic stem cells. No specific ligand has been identified for Tie1, although the angiopoietin, Ang-1, binds to Tie1 through integrins at high concentrations. In vivo studies of Tie1 show that it is critical in vascular development.


Pssm-ID: 270671 [Multi-domain]  Cd Length: 297  Bit Score: 276.49  E-value: 1.31e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  730 LGEGEFGKVVKATafhLKGRAGYTTVAVKMLKENASPSELRDLLSEFNVL-KQVNHPHVIKLYGACSQDGPLLLIVEYAK 808
Cdd:cd05089   10 IGEGNFGQVIKAM---IKKDGLKMNAAIKMLKEFASENDHRDFAGELEVLcKLGHHPNIINLLGACENRGYLYIAIEYAP 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  809 YGSLRGFLRESR--KVGPGYLGsggsrnssslDHPDERALTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNILVAEGR 886
Cdd:cd05089   87 YGNLLDFLRKSRvlETDPAFAK----------EHGTASTLTSQQLLQFASDVAKGMQYLSEKQFIHRDLAARNVLVGENL 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  887 KMKISDFGLSRDvyeEDSYVKRSQGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLGGNPYPGIPPERLFNLLKT 966
Cdd:cd05089  157 VSKIADFGLSRG---EEVYVKKTMGRLPVRWMAIESLNYSVYTTKSDVWSFGVLLWEIVSLGGTPYCGMTCAELYEKLPQ 233
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 10862703  967 GHRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADISKDLEKMMVKRRDYLDLA 1019
Cdd:cd05089  234 GYRMEKPRNCDDEVYELMRQCWRDRPYERPPFSQISVQLSRMLEARKAYVNMA 286
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
728-999 1.32e-84

Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Src subfamily members include Src, Lck, Hck, Blk, Lyn, Fgr, Fyn, Yrk, and Yes. Src (or c-Src) proteins are cytoplasmic (or non-receptor) PTKs which are anchored to the plasma membrane. They contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. They were identified as the first proto-oncogene products, and they regulate cell adhesion, invasion, and motility in cancer cells and tumor vasculature, contributing to cancer progression and metastasis. Src kinases are overexpressed in a variety of human cancers, making them attractive targets for therapy. They are also implicated in acute inflammatory responses and osteoclast function. Src, Fyn, Yes, and Yrk are widely expressed, while Blk, Lck, Hck, Fgr, and Lyn show a limited expression pattern. The Src-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270630 [Multi-domain]  Cd Length: 248  Bit Score: 274.54  E-value: 1.32e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  728 KTLGEGEFGKVVKATAfhlkgrAGYTTVAVKMLKENA-SPSelrDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVEY 806
Cdd:cd05034    1 KKLGAGQFGEVWMGVW------NGTTKVAVKTLKPGTmSPE---AFLQEAQIMKKLRHDKLVQLYAVCSDEEPIYIVTEL 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  807 AKYGSLRGFLResrkvgpgylgsggsrnsssldHPDERALTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNILVAEGR 886
Cdd:cd05034   72 MSKGSLLDYLR----------------------TGEGRALRLPQLIDMAAQIASGMAYLESRNYIHRDLAARNILVGENN 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  887 KMKISDFGLSRdVYEEDSYVKRSQGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLGGNPYPGIPPERLFNLLKT 966
Cdd:cd05034  130 VCKVADFGLAR-LIEDDEYTAREGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLYEIVTYGRVPYPGMTNREVLEQVER 208
                        250       260       270
                 ....*....|....*....|....*....|...
gi 10862703  967 GHRMERPDNCSEEMYRLMLQCWKQEPDKRPVFA 999
Cdd:cd05034  209 GYRMPKPPGCPDELYDIMLQCWKKEPEERPTFE 241
PTKc_Tie cd05047
Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
730-1009 2.71e-83

Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tie proteins, consisting of Tie1 and Tie2, are receptor PTKs (RTKs) containing an extracellular region, a transmembrane segment, and an intracellular catalytic domain. The extracellular region contains an immunoglobulin (Ig)-like domain, three epidermal growth factor (EGF)-like domains, a second Ig-like domain, and three fibronectin type III repeats. Tie receptors are specifically expressed in endothelial cells and hematopoietic stem cells. The angiopoietins (Ang-1 to Ang-4) serve as ligands for Tie2, while no specific ligand has been identified for Tie1. The binding of Ang-1 to Tie2 leads to receptor autophosphorylation and activation, promoting cell migration and survival. In contrast, Ang-2 binding to Tie2 does not result in the same response, suggesting that Ang-2 may function as an antagonist. In vivo studies of Tie1 show that it is critical in vascular development. The Tie subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270641 [Multi-domain]  Cd Length: 270  Bit Score: 271.91  E-value: 2.71e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  730 LGEGEFGKVVKAtafHLKGRAGYTTVAVKMLKENASPSELRDLLSEFNVL-KQVNHPHVIKLYGACSQDGPLLLIVEYAK 808
Cdd:cd05047    3 IGEGNFGQVLKA---RIKKDGLRMDAAIKRMKEYASKDDHRDFAGELEVLcKLGHHPNIINLLGACEHRGYLYLAIEYAP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  809 YGSLRGFLRESR--KVGPGYlgsggsrnssSLDHPDERALTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNILVAEGR 886
Cdd:cd05047   80 HGNLLDFLRKSRvlETDPAF----------AIANSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENY 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  887 KMKISDFGLSRDvyeEDSYVKRSQGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLGGNPYPGIPPERLFNLLKT 966
Cdd:cd05047  150 VAKIADFGLSRG---QEVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAELYEKLPQ 226
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 10862703  967 GHRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADISKDLEKMM 1009
Cdd:cd05047  227 GYRLEKPLNCDDEVYDLMRQCWREKPYERPSFAQILVSLNRML 269
PTKc_ALK_LTK cd05036
Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte ...
718-1001 8.19e-79

Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte Tyrosine Kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyr residues in protein substrates. ALK and LTK are orphan receptor PTKs (RTKs) whose ligands are not yet well-defined. ALK appears to play an important role in mammalian neural development as well as visceral muscle differentiation in Drosophila. ALK is aberrantly expressed as fusion proteins, due to chromosomal translocations, in about 60% of anaplastic large cell lymphomas (ALCLs). ALK fusion proteins are also found in rare cases of diffuse large B cell lymphomas (DLBCLs). LTK is mainly expressed in B lymphocytes and neuronal tissues. It is important in cell proliferation and survival. Transgenic mice expressing TLK display retarded growth and high mortality rate. In addition, a polymorphism in mouse and human LTK is implicated in the pathogenesis of systemic lupus erythematosus. RTKs contain an extracellular ligand-binding domain, a transmembrane region, and an intracellular tyr kinase domain. They are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. The ALK/LTK subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270632 [Multi-domain]  Cd Length: 277  Bit Score: 259.63  E-value: 8.19e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  718 EFPRKNLVLGKTLGEGEFGKVVKATAFHLKGRAGYTTVAVKMLKENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQD 797
Cdd:cd05036    2 EVPRKNLTLIRALGQGAFGEVYEGTVSGMPGDPSPLQVAVKTLPELCSEQDEMDFLMEALIMSKFNHPNIVRCIGVCFQR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  798 GPLLLIVEYAKYGSLRGFLRESRKvgpgylgsggsrnssSLDHPDerALTMGDLISFAWQISQGMQYLAEMKLVHRDLAA 877
Cdd:cd05036   82 LPRFILLELMAGGDLKSFLRENRP---------------RPEQPS--SLTMLDLLQLAQDVAKGCRYLEENHFIHRDIAA 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  878 RNILVA---EGRKMKISDFGLSRDVYEEDSYVKRSQGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLGGNPYPG 954
Cdd:cd05036  145 RNCLLTckgPGRVAKIGDFGMARDIYRADYYRKGGKAMLPVKWMPPEAFLDGIFTSKTDVWSFGVLLWEIFSLGYMPYPG 224
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 10862703  955 IPPERLFNLLKTGHRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADI 1001
Cdd:cd05036  225 KSNQEVMEFVTSGGRMDPPKNCPGPVYRIMTQCWQHIPEDRPNFSTI 271
PTKc_Ror cd05048
Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan ...
718-1005 3.51e-77

Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Ror subfamily consists of Ror1, Ror2, and similar proteins. Ror proteins are orphan receptor PTKs (RTKs) containing an extracellular region with immunoglobulin-like, cysteine-rich, and kringle domains, a transmembrane segment, and an intracellular catalytic domain. Ror RTKs are unrelated to the nuclear receptor subfamily called retinoid-related orphan receptors (RORs). RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. Ror kinases are expressed in many tissues during development. They play important roles in bone and heart formation. Mutations in human Ror2 result in two different bone development genetic disorders, recessive Robinow syndrome and brachydactyly type B. Drosophila Ror is expressed only in the developing nervous system during neurite outgrowth and neuronal differentiation, suggesting a role for Drosophila Ror in neural development. More recently, mouse Ror1 and Ror2 have also been found to play an important role in regulating neurite growth in central neurons. Ror1 and Ror2 are believed to have some overlapping and redundant functions. The Ror subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270642 [Multi-domain]  Cd Length: 283  Bit Score: 255.38  E-value: 3.51e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  718 EFPRKNLVLGKTLGEGEFGKVVKATAFHLKGRAGYTTVAVKMLKENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQD 797
Cdd:cd05048    1 EIPLSAVRFLEELGEGAFGKVYKGELLGPSSEESAISVAIKTLKENASPKTQQDFRREAELMSDLQHPNIVCLLGVCTKE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  798 GPLLLIVEYAKYGSLRGFL-RESRKVGPGyLGSGGSRNSSSLDHPDeraltmgdLISFAWQISQGMQYLAEMKLVHRDLA 876
Cdd:cd05048   81 QPQCMLFEYMAHGDLHEFLvRHSPHSDVG-VSSDDDGTASSLDQSD--------FLHIAIQIAAGMEYLSSHHYVHRDLA 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  877 ARNILVAEGRKMKISDFGLSRDVYEEDSYVKRSQGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLGGNPYPGIP 956
Cdd:cd05048  152 ARNCLVGDGLTVKISDFGLSRDIYSSDYYRVQSKSLLPVRWMPPEAILYGKFTTESDVWSFGVVLWEIFSYGLQPYYGYS 231
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 10862703  957 PERLFNLLKTGHRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADISKDL 1005
Cdd:cd05048  232 NQEVIEMIRSRQLLPCPEDCPARVYSLMVECWHEIPSRRPRFKEIHTRL 280
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
716-1006 2.72e-76

Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Frk and Srk are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Frk, also known as Rak, is specifically expressed in liver, lung, kidney, intestine, mammary glands, and the islets of Langerhans. Rodent homologs were previously referred to as GTK (gastrointestinal tyr kinase), BSK (beta-cell Src-like kinase), or IYK (intestinal tyr kinase). Studies in mice reveal that Frk is not essential for viability. It plays a role in the signaling that leads to cytokine-induced beta-cell death in Type I diabetes. It also regulates beta-cell number during embryogenesis and early in life. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Frk-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270653 [Multi-domain]  Cd Length: 267  Bit Score: 252.33  E-value: 2.72e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  716 KWEFPRKNLVLGKTLGEGEFGKVvkatafhLKGRAGYTT-VAVKMLKE-NASPSelrDLLSEFNVLKQVNHPHVIKLYGA 793
Cdd:cd05068    2 QWEIDRKSLKLLRKLGSGQFGEV-------WEGLWNNTTpVAVKTLKPgTMDPE---DFLREAQIMKKLRHPKLIQLYAV 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  794 CSQDGPLLLIVEYAKYGSLRGFLresrkvgpgylgsggsrnsssldHPDERALTMGDLISFAWQISQGMQYLAEMKLVHR 873
Cdd:cd05068   72 CTLEEPIYIITELMKHGSLLEYL-----------------------QGKGRSLQLPQLIDMAAQVASGMAYLESQNYIHR 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  874 DLAARNILVAEGRKMKISDFGLSRDVYEEDSYVKRSQGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLGGNPYP 953
Cdd:cd05068  129 DLAARNVLVGENNICKVADFGLARVIKVEDEYEAREGAKFPIKWTAPEAANYNRFSIKSDVWSFGILLTEIVTYGRIPYP 208
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 10862703  954 GIPPERLFNLLKTGHRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADISKDLE 1006
Cdd:cd05068  209 GMTNAEVLQQVERGYRMPCPPNCPPQLYDIMLECWKADPMERPTFETLQWKLE 261
PTKc_TAM cd05035
Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer ...
724-1009 3.58e-76

Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The TAM subfamily consists of Tyro3 (or Sky), Axl, Mer (or Mertk), and similar proteins. TAM subfamily members are receptor tyr kinases (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. TAM proteins are implicated in a variety of cellular effects including survival, proliferation, migration, and phagocytosis. They are also associated with several types of cancer as well as inflammatory, autoimmune, vascular, and kidney diseases. The TAM subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270631 [Multi-domain]  Cd Length: 273  Bit Score: 252.46  E-value: 3.58e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  724 LVLGKTLGEGEFGKVVKATafhLKGRAG-YTTVAVKMLK-ENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPL- 800
Cdd:cd05035    1 LKLGKILGEGEFGSVMEAQ---LKQDDGsQLKVAVKTMKvDIHTYSEIEEFLSEAACMKDFDHPNVMRLIGVCFTASDLn 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  801 -----LLIVEYAKYGSLRGFLRESR-KVGPGYLgsggsrnsssldhpderalTMGDLISFAWQISQGMQYLAEMKLVHRD 874
Cdd:cd05035   78 kppspMVILPFMKHGDLHSYLLYSRlGGLPEKL-------------------PLQTLLKFMVDIAKGMEYLSNRNFIHRD 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  875 LAARNILVAEGRKMKISDFGLSRDVYEEDSYvkrSQGRI---PVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLGGNP 951
Cdd:cd05035  139 LAARNCMLDENMTVCVADFGLSRKIYSGDYY---RQGRIskmPVKWIALESLADNVYTSKSDVWSFGVTMWEIATRGQTP 215
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 10862703  952 YPGIPPERLFNLLKTGHRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADISKDLEKMM 1009
Cdd:cd05035  216 YPGVENHEIYDYLRNGNRLKQPEDCLDEVYFLMYFCWTVDPKDRPTFTKLREVLENIL 273
PTKc_Musk cd05050
Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the ...
718-1007 4.33e-76

Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Musk is a receptor PTK (RTK) containing an extracellular region with four immunoglobulin-like domains and a cysteine-rich cluster, a transmembrane segment, and an intracellular catalytic domain. Musk is expressed and concentrated in the postsynaptic membrane in skeletal muscle. It is essential for the establishment of the neuromuscular junction (NMJ), a peripheral synapse that conveys signals from motor neurons to muscle cells. Agrin, a large proteoglycan released from motor neurons, stimulates Musk autophosphorylation and activation, leading to the clustering of acetylcholine receptors (AChRs). To date, there is no evidence to suggest that agrin binds directly to Musk. Mutations in AChR, Musk and other partners are responsible for diseases of the NMJ, such as the autoimmune syndrome myasthenia gravis. The Musk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133181 [Multi-domain]  Cd Length: 288  Bit Score: 252.83  E-value: 4.33e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  718 EFPRKNLVLGKTLGEGEFGKVVKATAFHLKGRAGYTTVAVKMLKENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQD 797
Cdd:cd05050    1 EYPRNNIEYVRDIGQGAFGRVFQARAPGLLPYEPFTMVAVKMLKEEASADMQADFQREAALMAEFDHPNIVKLLGVCAVG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  798 GPLLLIVEYAKYGSLRGFLRE-SRKVGPGYLGSGGSRNSSSLDHPDeraLTMGDLISFAWQISQGMQYLAEMKLVHRDLA 876
Cdd:cd05050   81 KPMCLLFEYMAYGDLNEFLRHrSPRAQCSLSHSTSSARKCGLNPLP---LSCTEQLCIAKQVAAGMAYLSERKFVHRDLA 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  877 ARNILVAEGRKMKISDFGLSRDVYEEDSYVKRSQGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLGGNPYPGIP 956
Cdd:cd05050  158 TRNCLVGENMVVKIADFGLSRNIYSADYYKASENDAIPIRWMPPESIFYNRYTTESDVWAYGVVLWEIFSYGMQPYYGMA 237
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 10862703  957 PERLFNLLKTGHRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADISKDLEK 1007
Cdd:cd05050  238 HEEVIYYVRDGNVLSCPDNCPLELYNLMRLCWSKLPSDRPSFASINRILQR 288
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
717-1006 6.38e-76

Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of Csk, Chk, and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. They negatively regulate the activity of Src kinases that are anchored to the plasma membrane. To inhibit Src kinases, Csk and Chk are translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. Csk catalyzes the tyr phosphorylation of the regulatory C-terminal tail of Src kinases, resulting in their inactivation. Chk inhibit Src kinases using a noncatalytic mechanism by simply binding to them. As negative regulators of Src kinases, Csk and Chk play important roles in cell proliferation, survival, and differentiation, and consequently, in cancer development and progression. The Csk-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270635 [Multi-domain]  Cd Length: 256  Bit Score: 251.12  E-value: 6.38e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  717 WEFPRKNLVLGKTLGEGEFGKVVKATafhLKGRagytTVAVKMLKENASPSElrDLLSEFNVLKQVNHPHVIKLYGACSQ 796
Cdd:cd05039    1 WAINKKDLKLGELIGKGEFGDVMLGD---YRGQ----KVAVKCLKDDSTAAQ--AFLAEASVMTTLRHPNLVQLLGVVLE 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  797 DGPLLLIVEYAKYGSLRGFLReSRkvgpgylgsggsrnsssldhpdERA-LTMGDLISFAWQISQGMQYLAEMKLVHRDL 875
Cdd:cd05039   72 GNGLYIVTEYMAKGSLVDYLR-SR----------------------GRAvITRKDQLGFALDVCEGMEYLESKKFVHRDL 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  876 AARNILVAEGRKMKISDFGLSRDV-YEEDSyvkrsqGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLGGNPYPG 954
Cdd:cd05039  129 AARNVLVSEDNVAKVSDFGLAKEAsSNQDG------GKLPIKWTAPEALREKKFSTKSDVWSFGILLWEIYSFGRVPYPR 202
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 10862703  955 IPPERLFNLLKTGHRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADISKDLE 1006
Cdd:cd05039  203 IPLKDVVPHVEKGYRMEAPEGCPPEVYKVMKNCWELDPAKRPTFKQLREKLE 254
PTKc_Trk cd05049
Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze ...
718-1007 6.73e-75

Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Trk subfamily consists of TrkA, TrkB, TrkC, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, the nerve growth factor (NGF) family of neutrotrophins, leads to Trk receptor oligomerization and activation of the catalytic domain. Trk receptors are mainly expressed in the peripheral and central nervous systems. They play important roles in cell fate determination, neuronal survival and differentiation, as well as in the regulation of synaptic plasticity. Altered expression of Trk receptors is associated with many human diseases. The Trk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270643 [Multi-domain]  Cd Length: 280  Bit Score: 248.92  E-value: 6.73e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  718 EFPRKNLVLGKTLGEGEFGKVVKATAFHLKGRAGYTTVAVKMLKENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQD 797
Cdd:cd05049    1 HIKRDTIVLKRELGEGAFGKVFLGECYNLEPEQDKMLVAVKTLKDASSPDARKDFEREAELLTNLQHENIVKFYGVCTEG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  798 GPLLLIVEYAKYGSLRGFLRESrkvGPGYLGSGGSRNsssldhpDERALTMGDLISFAWQISQGMQYLAEMKLVHRDLAA 877
Cdd:cd05049   81 DPLLMVFEYMEHGDLNKFLRSH---GPDAAFLASEDS-------APGELTLSQLLHIAVQIASGMVYLASQHFVHRDLAT 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  878 RNILVAEGRKMKISDFGLSRDVYEEDSYvkRSQGR--IPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLGGNPYPGI 955
Cdd:cd05049  151 RNCLVGTNLVVKIGDFGMSRDIYSTDYY--RVGGHtmLPIRWMPPESILYRKFTTESDVWSFGVVLWEIFTYGKQPWFQL 228
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 10862703  956 PPERLFNLLKTGHRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADISKDLEK 1007
Cdd:cd05049  229 SNTEVIECITQGRLLQRPRTCPSEVYAVMLGCWKREPQQRLNIKDIHKRLQE 280
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
728-1015 4.27e-74

Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Syk-like subfamily is composed of Syk, ZAP-70, Shark, and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing two Src homology 2 (SH2) domains N-terminal to the catalytic tyr kinase domain. They are involved in the signaling downstream of activated receptors (including B-cell, T-cell, and Fc receptors) that contain ITAMs (immunoreceptor tyr activation motifs), leading to processes such as cell proliferation, differentiation, survival, adhesion, migration, and phagocytosis. Syk is important in B-cell receptor signaling, while Zap-70 is primarily expressed in T-cells and NK cells, and is a crucial component in T-cell receptor signaling. Syk also plays a central role in Fc receptor-mediated phagocytosis in the adaptive immune system. Shark is exclusively expressed in ectodermally derived epithelia, and is localized preferentially to the apical surface of the epithelial cells, it may play a role in a signaling pathway for epithelial cell polarity. The Syk-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270650 [Multi-domain]  Cd Length: 257  Bit Score: 245.72  E-value: 4.27e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  728 KTLGEGEFGKVVKATAFHLKGRAgyTTVAVKMLKENASPSELRDLLSEFNVLKQVNHPHVIKLYGACsQDGPLLLIVEYA 807
Cdd:cd05060    1 KELGHGNFGSVRKGVYLMKSGKE--VEVAVKTLKQEHEKAGKKEFLREASVMAQLDHPCIVRLIGVC-KGEPLMLVMELA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  808 KYGSLRGFLResrkvgpgylgsggsrnsssldhpDERALTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNILVAEGRK 887
Cdd:cd05060   78 PLGPLLKYLK------------------------KRREIPVSDLKELAHQVAMGMAYLESKHFVHRDLAARNVLLVNRHQ 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  888 MKISDFGLSRDVYEEDSYVK-RSQGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLGGNPYPGIPPERLFNLLKT 966
Cdd:cd05060  134 AKISDFGMSRALGAGSDYYRaTTAGRWPLKWYAPECINYGKFSSKSDVWSYGVTLWEAFSYGAKPYGEMKGPEVIAMLES 213
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 10862703  967 GHRMERPDNCSEEMYRLMLQCWKQEPDKRPVFAdiskDLEKMMvkRRDY 1015
Cdd:cd05060  214 GERLPRPEECPQEIYSIMLSCWKYRPEDRPTFS----ELESTF--RRDP 256
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
717-1005 1.32e-73

Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal regulatory tyrosine and N-terminal myristylation sites (Srm) and Breast tumor kinase (Brk); PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Srm and Brk (also called protein tyrosine kinase 6) are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Brk has been found to be overexpressed in a majority of breast tumors. Src kinases in general contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr; they are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). Srm and Brk however, lack the N-terminal myristylation sites. Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. The Srm/Brk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133248 [Multi-domain]  Cd Length: 261  Bit Score: 244.65  E-value: 1.32e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  717 WEFPRKNLVLGKTLGEGEFGKVvkatafhLKGR-AGYTTVAVKMLKeNASPSELRDLLSEFNVLKQVNHPHVIKLYGACS 795
Cdd:cd05148    1 WERPREEFTLERKLGSGYFGEV-------WEGLwKNRVRVAIKILK-SDDLLKQQDFQKEVQALKRLRHKHLISLFAVCS 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  796 QDGPLLLIVEYAKYGSLRGFLREsrkvgpgylgsggsrnsssldhPDERALTMGDLISFAWQISQGMQYLAEMKLVHRDL 875
Cdd:cd05148   73 VGEPVYIITELMEKGSLLAFLRS----------------------PEGQVLPVASLIDMACQVAEGMAYLEEQNSIHRDL 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  876 AARNILVAEGRKMKISDFGLSRdVYEEDSYVKRSQgRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLGGNPYPGI 955
Cdd:cd05148  131 AARNILVGEDLVCKVADFGLAR-LIKEDVYLSSDK-KIPYKWTAPEAASHGTFSTKSDVWSFGILLYEMFTYGQVPYPGM 208
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 10862703  956 PPERLFNLLKTGHRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADISKDL 1005
Cdd:cd05148  209 NNHEVYDQITAGYRMPCPAKCPQEIYKIMLECWAAEPEDRPSFKALREEL 258
PTKc_DDR cd05051
Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze ...
718-1001 1.79e-73

Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The DDR subfamily consists of homologs of mammalian DDR1, DDR2, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDRs results in a slow but sustained receptor activation. DDRs regulate cell adhesion, proliferation, and extracellular matrix remodeling. They have been linked to a variety of human cancers including breast, colon, ovarian, brain, and lung. There is no evidence showing that DDRs act as transforming oncogenes. They are more likely to play a role in the regulation of tumor growth and metastasis. The DDR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270644 [Multi-domain]  Cd Length: 297  Bit Score: 245.71  E-value: 1.79e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  718 EFPRKNLVLGKTLGEGEFGKVV--KATAFHLKGRAGYTT---------VAVKMLKENASPSELRDLLSEFNVLKQVNHPH 786
Cdd:cd05051    1 EFPREKLEFVEKLGEGQFGEVHlcEANGLSDLTSDDFIGndnkdepvlVAVKMLRPDASKNAREDFLKEVKIMSQLKDPN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  787 VIKLYGACSQDGPLLLIVEYAKYGSLRGFLRESRKVGPGYLGSGGSRnsssldhpderaLTMGDLISFAWQISQGMQYLA 866
Cdd:cd05051   81 IVRLLGVCTRDEPLCMIVEYMENGDLNQFLQKHEAETQGASATNSKT------------LSYGTLLYMATQIASGMKYLE 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  867 EMKLVHRDLAARNILVAEGRKMKISDFGLSRDVYEEDSYvkRSQGR--IPVKWMAIESLFDHIYTTQSDVWSFGVLLWEI 944
Cdd:cd05051  149 SLNFVHRDLATRNCLVGPNYTIKIADFGMSRNLYSGDYY--RIEGRavLPIRWMAWESILLGKFTTKSDVWAFGVTLWEI 226
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 10862703  945 VTLGG-NPYPGIPPE-------RLFNLLKTGHRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADI 1001
Cdd:cd05051  227 LTLCKeQPYEHLTDEqvienagEFFRDDGMEVYLSRPPNCPKEIYELMLECWRRDEEDRPTFREI 291
PTKc_Mer cd14204
Catalytic Domain of the Protein Tyrosine Kinase, Mer; PTKs catalyze the transfer of the ...
721-1011 4.51e-73

Catalytic Domain of the Protein Tyrosine Kinase, Mer; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Mer (or Mertk) is named after its original reported expression pattern (monocytes, epithelial, and reproductive tissues). It is required for the ingestion of apoptotic cells by phagocytes such as macrophages, retinal pigment epithelial cells, and dendritic cells. Mer is also important in maintaining immune homeostasis. Mer is a member of the TAM subfamily, composed of receptor PTKs (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. The Mer subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271106 [Multi-domain]  Cd Length: 284  Bit Score: 244.07  E-value: 4.51e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  721 RKNLVLGKTLGEGEFGKVVKAtafHLKGRAGYT-TVAVKMLK-ENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDG 798
Cdd:cd14204    6 RNLLSLGKVLGEGEFGSVMEG---ELQQPDGTNhKVAVKTMKlDNFSQREIEEFLSEAACMKDFNHPNVIRLLGVCLEVG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  799 PL-----LLIVEYAKYGSLRGFLRESR-KVGPGYLgsggsrnsssldhpderalTMGDLISFAWQISQGMQYLAEMKLVH 872
Cdd:cd14204   83 SQripkpMVILPFMKYGDLHSFLLRSRlGSGPQHV-------------------PLQTLLKFMIDIALGMEYLSSRNFLH 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  873 RDLAARNILVAEGRKMKISDFGLSRDVYEEDSYvkrSQGRI---PVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLGG 949
Cdd:cd14204  144 RDLAARNCMLRDDMTVCVADFGLSKKIYSGDYY---RQGRIakmPVKWIAVESLADRVYTVKSDVWAFGVTMWEIATRGM 220
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 10862703  950 NPYPGIPPERLFNLLKTGHRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADISKDLEKMMVK 1011
Cdd:cd14204  221 TPYPGVQNHEIYDYLLHGHRLKQPEDCLDELYDIMYSCWRSDPTDRPTFTQLRENLEKLLES 282
PTKc_InsR cd05061
Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer ...
717-1001 1.57e-72

Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. InsR is a receptor PTK (RTK) that is composed of two alphabeta heterodimers. Binding of the insulin ligand to the extracellular alpha subunit activates the intracellular tyr kinase domain of the transmembrane beta subunit. Receptor activation leads to autophosphorylation, stimulating downstream kinase activities, which initiate signaling cascades and biological function. InsR signaling plays an important role in many cellular processes including glucose homeostasis, glycogen synthesis, lipid and protein metabolism, ion and amino acid transport, cell cycle and proliferation, cell differentiation, gene transcription, and nitric oxide synthesis. Insulin resistance, caused by abnormalities in InsR signaling, has been described in diabetes, hypertension, cardiovascular disease, metabolic syndrome, heart failure, and female infertility. The InsR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133192 [Multi-domain]  Cd Length: 288  Bit Score: 242.95  E-value: 1.57e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  717 WEFPRKNLVLGKTLGEGEFGKVVKATAFHL-KGRAGyTTVAVKMLKENASPSELRDLLSEFNVLKQVNHPHVIKLYGACS 795
Cdd:cd05061    1 WEVSREKITLLRELGQGSFGMVYEGNARDIiKGEAE-TRVAVKTVNESASLRERIEFLNEASVMKGFTCHHVVRLLGVVS 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  796 QDGPLLLIVEYAKYGSLRGFLRESRKVGPgylgsggsrnssslDHPDERALTMGDLISFAWQISQGMQYLAEMKLVHRDL 875
Cdd:cd05061   80 KGQPTLVVMELMAHGDLKSYLRSLRPEAE--------------NNPGRPPPTLQEMIQMAAEIADGMAYLNAKKFVHRDL 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  876 AARNILVAEGRKMKISDFGLSRDVYEEDSYVKRSQGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLGGNPYPGI 955
Cdd:cd05061  146 AARNCMVAHDFTVKIGDFGMTRDIYETDYYRKGGKGLLPVRWMAPESLKDGVFTTSSDMWSFGVVLWEITSLAEQPYQGL 225
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 10862703  956 PPERLFNLLKTGHRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADI 1001
Cdd:cd05061  226 SNEQVLKFVMDGGYLDQPDNCPERVTDLMRMCWQFNPKMRPTFLEI 271
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
717-1006 2.51e-72

Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. FAK is a cytoplasmic (or nonreceptor) PTK that contains an autophosphorylation site and a FERM domain at the N-terminus, a central tyr kinase domain, proline-rich regions, and a C-terminal FAT (focal adhesion targeting) domain. FAK activity is dependent on integrin-mediated cell adhesion, which facilitates N-terminal autophosphorylation. Full activation is achieved by the phosphorylation of its two adjacent A-loop tyrosines. FAK is important in mediating signaling initiated at sites of cell adhesions and at growth factor receptors. Through diverse molecular interactions, FAK functions as a biosensor or integrator to control cell motility. It is a key regulator of cell survival, proliferation, migration and invasion, and thus plays an important role in the development and progression of cancer. Src binds to autophosphorylated FAK forming the FAK-Src dual kinase complex, which is activated in a wide variety of tumor cells and generates signals promoting growth and metastasis. FAK is being developed as a target for cancer therapy. The FAK subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133187 [Multi-domain]  Cd Length: 270  Bit Score: 241.56  E-value: 2.51e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  717 WEFPRKNLVLGKTLGEGEFGKVVKATAFHLKGRAgyTTVAVKMLKENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSq 796
Cdd:cd05056    1 YEIQREDITLGRCIGEGQFGDVYQGVYMSPENEK--IAVAVKTCKNCTSPSVREKFLQEAYIMRQFDHPHIVKLIGVIT- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  797 DGPLLLIVEYAKYGSLRGFLRESRKvgpgylgsggsrnsssldhpderALTMGDLISFAWQISQGMQYLAEMKLVHRDLA 876
Cdd:cd05056   78 ENPVWIVMELAPLGELRSYLQVNKY-----------------------SLDLASLILYAYQLSTALAYLESKRFVHRDIA 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  877 ARNILVAEGRKMKISDFGLSRDVyEEDSYVKRSQGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLGGNPYPGIP 956
Cdd:cd05056  135 ARNVLVSSPDCVKLGDFGLSRYM-EDESYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMLGVKPFQGVK 213
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 10862703  957 PERLFNLLKTGHRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADISKDLE 1006
Cdd:cd05056  214 NNDVIGRIENGERLPMPPNCPPTLYSLMTKCWAYDPSKRPRFTELKAQLS 263
PTKc_Tie2 cd05088
Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the ...
730-1017 2.86e-72

Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tie2 is a receptor PTK (RTK) containing an extracellular region, a transmembrane segment, and an intracellular catalytic domain. The extracellular region contains an immunoglobulin (Ig)-like domain, three epidermal growth factor (EGF)-like domains, a second Ig-like domain, and three fibronectin type III repeats. Tie2 is expressed mainly in endothelial cells and hematopoietic stem cells. It is also found in a subset of tumor-associated monocytes and eosinophils. The angiopoietins (Ang-1 to Ang-4) serve as ligands for Tie2. The binding of Ang-1 to Tie2 leads to receptor autophosphorylation and activation, promoting cell migration and survival. In contrast, Ang-2 binding to Tie2 does not result in the same response, suggesting that Ang-2 may function as an antagonist. Tie2 signaling plays key regulatory roles in vascular integrity and quiescence, and in inflammation. The Tie2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133219 [Multi-domain]  Cd Length: 303  Bit Score: 242.60  E-value: 2.86e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  730 LGEGEFGKVVKAtafHLKGRAGYTTVAVKMLKENASPSELRDLLSEFNVLKQVN-HPHVIKLYGACSQDGPLLLIVEYAK 808
Cdd:cd05088   15 IGEGNFGQVLKA---RIKKDGLRMDAAIKRMKEYASKDDHRDFAGELEVLCKLGhHPNIINLLGACEHRGYLYLAIEYAP 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  809 YGSLRGFLRESR--KVGPGYlgsggsrnssSLDHPDERALTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNILVAEGR 886
Cdd:cd05088   92 HGNLLDFLRKSRvlETDPAF----------AIANSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENY 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  887 KMKISDFGLSRDvyeEDSYVKRSQGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLGGNPYPGIPPERLFNLLKT 966
Cdd:cd05088  162 VAKIADFGLSRG---QEVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAELYEKLPQ 238
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 10862703  967 GHRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADISKDLEKMMVKRRDYLD 1017
Cdd:cd05088  239 GYRLEKPLNCDDEVYDLMRQCWREKPYERPSFAQILVSLNRMLEERKTYVN 289
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
730-1005 1.15e-71

Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; Fes subfamily; catalytic (c) domain. Fes subfamily members include Fes (or Fps), Fer, and similar proteins. The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K). PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fes subfamily proteins are cytoplasmic (or nonreceptor) tyr kinases containing an N-terminal region with FCH (Fes/Fer/CIP4 homology) and coiled-coil domains, followed by a SH2 domain, and a C-terminal catalytic domain. The genes for Fes (feline sarcoma) and Fps (Fujinami poultry sarcoma) were first isolated from tumor-causing retroviruses. The viral oncogenes encode chimeric Fes proteins consisting of Gag sequences at the N-termini, resulting in unregulated tyr kinase activity. Fes and Fer kinases play roles in haematopoiesis, inflammation and immunity, growth factor signaling, cytoskeletal regulation, cell migration and adhesion, and the regulation of cell-cell interactions. Fes and Fer show redundancy in their biological functions.


Pssm-ID: 270637 [Multi-domain]  Cd Length: 251  Bit Score: 238.88  E-value: 1.15e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  730 LGEGEFGKVVKATafhLKGRAgyTTVAVKMLKENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVEYAKY 809
Cdd:cd05041    3 IGRGNFGDVYRGV---LKPDN--TEVAVKTCRETLPPDLKRKFLQEARILKQYDHPNIVKLIGVCVQKQPIMIVMELVPG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  810 GSLRGFLRESRKvgpgylgsggsrnsssldhpderALTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNILVAEGRKMK 889
Cdd:cd05041   78 GSLLTFLRKKGA-----------------------RLTVKQLLQMCLDAAAGMEYLESKNCIHRDLAARNCLVGENNVLK 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  890 ISDFGLSRDvyEEDSYVKRSQGR--IPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLGGNPYPGIPPERLFNLLKTG 967
Cdd:cd05041  135 ISDFGMSRE--EEDGEYTVSDGLkqIPIKWTAPEALNYGRYTSESDVWSFGILLWEIFSLGATPYPGMSNQQTREQIESG 212
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 10862703  968 HRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADISKDL 1005
Cdd:cd05041  213 YRMPAPELCPEAVYRLMLQCWAYDPENRPSFSEIYNEL 250
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
722-1008 4.17e-71

Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EphRs comprise the largest subfamily of receptor PTKs (RTKs). They can be classified into two classes (EphA and EphB), according to their extracellular sequences, which largely correspond to binding preferences for either GPI-anchored ephrin-A ligands or transmembrane ephrin-B ligands. Vertebrates have ten EphA and six EphB receptors, which display promiscuous ligand interactions within each class. EphRs contain an ephrin binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. This allows ephrin/EphR dimers to form, leading to the activation of the intracellular tyr kinase domain. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). The main effect of ephrin/EphR interaction is cell-cell repulsion or adhesion. Ephrin/EphR signaling is important in neural development and plasticity, cell morphogenesis and proliferation, cell-fate determination, embryonic development, tissue patterning, and angiogenesis.The EphR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270629 [Multi-domain]  Cd Length: 266  Bit Score: 238.04  E-value: 4.17e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  722 KNLVLGKTLGEGEFGKVVKAtAFHLKGRAgYTTVAVKMLKENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLL 801
Cdd:cd05033    4 SYVTIEKVIGGGEFGEVCSG-SLKLPGKK-EIDVAIKTLKSGYSDKQRLDFLTEASIMGQFDHPNVIRLEGVVTKSRPVM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  802 LIVEYAKYGSLRGFLResrkvgpgylgsggsrnsssldHPDERaLTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNIL 881
Cdd:cd05033   82 IVTEYMENGSLDKFLR----------------------ENDGK-FTVTQLVGMLRGIASGMKYLSEMNYVHRDLAARNIL 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  882 VAEGRKMKISDFGLSRDVYEEDSYVKRSQGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLGGNPYPGIPPERLF 961
Cdd:cd05033  139 VNSDLVCKVSDFGLSRRLEDSEATYTTKGGKIPIRWTAPEAIAYRKFTSASDVWSFGIVMWEVMSYGERPYWDMSNQDVI 218
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 10862703  962 NLLKTGHRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADISKDLEKM 1008
Cdd:cd05033  219 KAVEDGYRLPPPMDCPSALYQLMLDCWQKDRNERPTFSQIVSTLDKM 265
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
717-1008 7.05e-71

Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Abl (or c-Abl) is a ubiquitously-expressed cytoplasmic (or nonreceptor) PTK that contains SH3, SH2, and tyr kinase domains in its N-terminal region, as well as nuclear localization motifs, a putative DNA-binding domain, and F- and G-actin binding domains in its C-terminal tail. It also contains a short autoinhibitory cap region in its N-terminus. Abl function depends on its subcellular localization. In the cytoplasm, Abl plays a role in cell proliferation and survival. In response to DNA damage or oxidative stress, Abl is transported to the nucleus where it induces apoptosis. In chronic myelogenous leukemia (CML) patients, an aberrant translocation results in the replacement of the first exon of Abl with the BCR (breakpoint cluster region) gene. The resulting BCR-Abl fusion protein is constitutively active and associates into tetramers, resulting in a hyperactive kinase sending a continuous signal. This leads to uncontrolled proliferation, morphological transformation and anti-apoptotic effects. BCR-Abl is the target of selective inhibitors, such as imatinib (Gleevec), used in the treatment of CML. Abl2, also known as ARG (Abelson-related gene), is thought to play a cooperative role with Abl in the proper development of the nervous system. The Tel-ARG fusion protein, resulting from reciprocal translocation between chromosomes 1 and 12, is associated with acute myeloid leukemia (AML). The TEL gene is a frequent fusion partner of other tyr kinase oncogenes, including Tel/Abl, Tel/PDGFRbeta, and Tel/Jak2, found in patients with leukemia and myeloproliferative disorders. The Abl subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270645 [Multi-domain]  Cd Length: 263  Bit Score: 237.32  E-value: 7.05e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  717 WEFPRKNLVLGKTLGEGEFGKVVKATafhlkGRAGYTTVAVKMLKENASpsELRDLLSEFNVLKQVNHPHVIKLYGACSQ 796
Cdd:cd05052    1 WEIERTDITMKHKLGGGQYGEVYEGV-----WKKYNLTVAVKTLKEDTM--EVEEFLKEAAVMKEIKHPNLVQLLGVCTR 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  797 DGPLLLIVEYAKYGSLRGFLREsrkvgpgylgsggsrnsssldhPDERALTMGDLISFAWQISQGMQYLAEMKLVHRDLA 876
Cdd:cd05052   74 EPPFYIITEFMPYGNLLDYLRE----------------------CNREELNAVVLLYMATQIASAMEYLEKKNFIHRDLA 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  877 ARNILVAEGRKMKISDFGLSRdVYEEDSYVKRSQGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLGGNPYPGIP 956
Cdd:cd05052  132 ARNCLVGENHLVKVADFGLSR-LMTGDTYTAHAGAKFPIKWTAPESLAYNKFSIKSDVWAFGVLLWEIATYGMSPYPGID 210
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 10862703  957 PERLFNLLKTGHRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADISKDLEKM 1008
Cdd:cd05052  211 LSQVYELLEKGYRMERPEGCPPKVYELMRACWQWNPSDRPSFAEIHQALETM 262
PTKc_Tyro3 cd05074
Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the ...
720-1006 8.31e-70

Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tyro3 (or Sky) is predominantly expressed in the central nervous system and the brain, and functions as a neurotrophic factor. It is also expressed in osteoclasts and has a role in bone resorption. Tyro3 is a member of the TAM subfamily, composed of receptor PTKs (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. The Tyro3 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270659 [Multi-domain]  Cd Length: 284  Bit Score: 235.20  E-value: 8.31e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  720 PRKNLVLGKTLGEGEFGKVVKAtafHLKGRAG-YTTVAVKMLKENA-SPSELRDLLSEFNVLKQVNHPHVIKLYGACSQD 797
Cdd:cd05074    7 QEQQFTLGRMLGKGEFGSVREA---QLKSEDGsFQKVAVKMLKADIfSSSDIEEFLREAACMKEFDHPNVIKLIGVSLRS 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  798 GPL------LLIVEYAKYGSLRGFLRESRkVGpgylgsggsrnssslDHPdeRALTMGDLISFAWQISQGMQYLAEMKLV 871
Cdd:cd05074   84 RAKgrlpipMVILPFMKHGDLHTFLLMSR-IG---------------EEP--FTLPLQTLVRFMIDIASGMEYLSSKNFI 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  872 HRDLAARNILVAEGRKMKISDFGLSRDVYEEDSYVKRSQGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLGGNP 951
Cdd:cd05074  146 HRDLAARNCMLNENMTVCVADFGLSKKIYSGDYYRQGCASKLPVKWLALESLADNVYTTHSDVWAFGVTMWEIMTRGQTP 225
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 10862703  952 YPGIPPERLFNLLKTGHRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADISKDLE 1006
Cdd:cd05074  226 YAGVENSEIYNYLIKGNRLKQPPDCLEDVYELMCQCWSPEPKCRPSFQHLRDQLE 280
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
718-1008 1.06e-69

Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EGFR (HER, ErbB) subfamily members include EGFR (HER1, ErbB1), HER2 (ErbB2), HER3 (ErbB3), HER4 (ErbB4), and similar proteins. They are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, resulting in the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. Collectively, they can recognize a variety of ligands including EGF, TGFalpha, and neuregulins, among others. All four subfamily members can form homo- or heterodimers. HER3 contains an impaired kinase domain and depends on its heterodimerization partner for activation. EGFR subfamily members are involved in signaling pathways leading to a broad range of cellular responses including cell proliferation, differentiation, migration, growth inhibition, and apoptosis. Gain of function alterations, through their overexpression, deletions, or point mutations in their kinase domains, have been implicated in various cancers. These receptors are targets of many small molecule inhibitors and monoclonal antibodies used in cancer therapy. The EGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270648 [Multi-domain]  Cd Length: 279  Bit Score: 234.62  E-value: 1.06e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  718 EFPRKNLVLGKTLGEGEFGKVVKATAFHLKGRAGYTtVAVKMLKENASPSELRDLLSEFNVLKQVNHPHVIKLYGAC--S 795
Cdd:cd05057    3 IVKETELEKGKVLGSGAFGTVYKGVWIPEGEKVKIP-VAIKVLREETGPKANEEILDEAYVMASVDHPHLVRLLGIClsS 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  796 QdgpLLLIVEYAKYGSLRGFLRESR-KVGPGYLgsggsrnsssldhpderaltmgdlISFAWQISQGMQYLAEMKLVHRD 874
Cdd:cd05057   82 Q---VQLITQLMPLGCLLDYVRNHRdNIGSQLL------------------------LNWCVQIAKGMSYLEEKRLVHRD 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  875 LAARNILVAEGRKMKISDFGLSRDVYEEDSYVKRSQGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLGGNPYPG 954
Cdd:cd05057  135 LAARNVLVKTPNHVKITDFGLAKLLDVDEKEYHAEGGKVPIKWMALESIQYRIYTHKSDVWSYGVTVWELMTFGAKPYEG 214
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 10862703  955 IPPERLFNLLKTGHRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADISKDLEKM 1008
Cdd:cd05057  215 IPAVEIPDLLEKGERLPQPPICTIDVYMVLVKCWMIDAESRPTFKELANEFSKM 268
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
719-1009 1.78e-69

Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily is composed of Jak1, Jak2, Jak3, TYK2, and similar proteins. They are PTKs, catalyzing the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jaks are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase catalytic domain. Most Jaks are expressed in a wide variety of tissues, except for Jak3, which is expressed only in hematopoietic cells. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). Jaks are also involved in regulating the surface expression of some cytokine receptors. The Jak-STAT pathway is involved in many biological processes including hematopoiesis, immunoregulation, host defense, fertility, lactation, growth, and embryogenesis. The Jak subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270634 [Multi-domain]  Cd Length: 284  Bit Score: 234.20  E-value: 1.78e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  719 FPRKNLVLGKTLGEGEFGKVVKATAFHLKGRAGyTTVAVKMLKENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDG 798
Cdd:cd05038    1 FEERHLKFIKQLGEGHFGSVELCRYDPLGDNTG-EQVAVKSLQPSGEEQHMSDFKREIEILRTLDHEYIVKYKGVCESPG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  799 P--LLLIVEYAKYGSLRGFLRESRkvgpgylgsggsrnsSSLDHPDeraltmgdLISFAWQISQGMQYLAEMKLVHRDLA 876
Cdd:cd05038   80 RrsLRLIMEYLPSGSLRDYLQRHR---------------DQIDLKR--------LLLFASQICKGMEYLGSQRYIHRDLA 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  877 ARNILVAEGRKMKISDFGLSRDVYEE-DSYVKRSQGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLG------- 948
Cdd:cd05038  137 ARNILVESEDLVKISDFGLAKVLPEDkEYYYVKEPGESPIFWYAPECLRESRFSSASDVWSFGVTLYELFTYGdpsqspp 216
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 10862703  949 GNPYPGIPP-------ERLFNLLKTGHRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADISKDLEKMM 1009
Cdd:cd05038  217 ALFLRMIGIaqgqmivTRLLELLKSGERLPRPPSCPDEVYDLMKECWEYEPQDRPSFSDLILIIDRLR 284
PTKc_Axl cd05075
Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the ...
724-1009 2.12e-69

Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Axl is widely expressed in a variety of organs and cells including epithelial, mesenchymal, hematopoietic, as well as non-transformed cells. It is important in many cellular functions such as survival, anti-apoptosis, proliferation, migration, and adhesion. Axl was originally isolated from patients with chronic myelogenous leukemia and a chronic myeloproliferative disorder. It is overexpressed in many human cancers including colon, squamous cell, thyroid, breast, and lung carcinomas. Axl is a member of the TAM subfamily, composed of receptor PTKs (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to its ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. The Axl subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270660 [Multi-domain]  Cd Length: 277  Bit Score: 233.75  E-value: 2.12e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  724 LVLGKTLGEGEFGKVVKAtafHLKGRAGYTTVAVKMLK-ENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQD----- 797
Cdd:cd05075    2 LALGKTLGEGEFGSVMEG---QLNQDDSVLKVAVKTMKiAICTRSEMEDFLSEAVCMKEFDHPNVMRLIGVCLQNteseg 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  798 --GPLLlIVEYAKYGSLRGFLRESRkVG--PGYLgsggsrnsssldhPDERaltmgdLISFAWQISQGMQYLAEMKLVHR 873
Cdd:cd05075   79 ypSPVV-ILPFMKHGDLHSFLLYSR-LGdcPVYL-------------PTQM------LVKFMTDIASGMEYLSSKNFIHR 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  874 DLAARNILVAEGRKMKISDFGLSRDVYEEDSYvkrSQGRI---PVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLGGN 950
Cdd:cd05075  138 DLAARNCMLNENMNVCVADFGLSKKIYNGDYY---RQGRIskmPVKWIAIESLADRVYTTKSDVWSFGVTMWEIATRGQT 214
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 10862703  951 PYPGIPPERLFNLLKTGHRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADISKDLEKMM 1009
Cdd:cd05075  215 PYPGVENSEIYDYLRQGNRLKQPPDCLDGLYELMSSCWLLNPKDRPSFETLRCELEKIL 273
PTKc_TrkA cd05092
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze ...
721-1007 4.29e-69

Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. TrkA is a receptor PTK (RTK) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding of TrkA to its ligand, nerve growth factor (NGF), results in receptor oligomerization and activation of the catalytic domain. TrkA is expressed mainly in neural-crest-derived sensory and sympathetic neurons of the peripheral nervous system, and in basal forebrain cholinergic neurons of the central nervous system. It is critical for neuronal growth, differentiation and survival. Alternative TrkA splicing has been implicated as a pivotal regulator of neuroblastoma (NB) behavior. Normal TrkA expression is associated with better NB prognosis, while the hypoxia-regulated TrkAIII splice variant promotes NB pathogenesis and progression. Aberrant TrkA expression has also been demonstrated in non-neural tumors including prostate, breast, lung, and pancreatic cancers. The TrkA subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270674 [Multi-domain]  Cd Length: 280  Bit Score: 232.93  E-value: 4.29e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  721 RKNLVLGKTLGEGEFGKVVKATAFHLKGRAGYTTVAVKMLKEnASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPL 800
Cdd:cd05092    4 RRDIVLKWELGEGAFGKVFLAECHNLLPEQDKMLVAVKALKE-ATESARQDFQREAELLTVLQHQHIVRFYGVCTEGEPL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  801 LLIVEYAKYGSLRGFLRESrkvGPgylgsggsrNSSSLDHPDERA---LTMGDLISFAWQISQGMQYLAEMKLVHRDLAA 877
Cdd:cd05092   83 IMVFEYMRHGDLNRFLRSH---GP---------DAKILDGGEGQApgqLTLGQMLQIASQIASGMVYLASLHFVHRDLAT 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  878 RNILVAEGRKMKISDFGLSRDVYEEDSYvkRSQGR--IPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLGGNPYPGI 955
Cdd:cd05092  151 RNCLVGQGLVVKIGDFGMSRDIYSTDYY--RVGGRtmLPIRWMPPESILYRKFTTESDIWSFGVVLWEIFTYGKQPWYQL 228
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 10862703  956 PPERLFNLLKTGHRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADISKDLEK 1007
Cdd:cd05092  229 SNTEAIECITQGRELERPRTCPPEVYAIMQGCWQREPQQRHSIKDIHSRLQA 280
PTK_CCK4 cd05046
Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also ...
719-1007 2.91e-68

Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also called protein tyrosine kinase 7 (PTK7), is an orphan receptor PTK (RTK) containing an extracellular region with seven immunoglobulin domains, a transmembrane segment, and an intracellular inactive pseudokinase domain, which shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. Studies in mice reveal that CCK4 is essential for neural development. Mouse embryos containing a truncated CCK4 die perinatally and display craniorachischisis, a severe form of neural tube defect. The mechanism of action of the CCK4 pseudokinase is still unknown. Other pseudokinases such as HER3 rely on the activity of partner RTKs. The CCK4 subfamily is part of a larger superfamily that includes other pseudokinases and the catalytic domains of active kinases including PTKs, protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133178 [Multi-domain]  Cd Length: 275  Bit Score: 230.43  E-value: 2.91e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  719 FPRKNLVLGKTLGEGEFGKVVKATAFHLKGRAGYTTVAVKML---KENASPSELRdllSEFNVLKQVNHPHVIKLYGACS 795
Cdd:cd05046    2 FPRSNLQEITTLGRGEFGEVFLAKAKGIEEEGGETLVLVKALqktKDENLQSEFR---RELDMFRKLSHKNVVRLLGLCR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  796 QDGPLLLIVEYAKYGSLRGFLRESRKvgpgylgsggsrnssSLDHPDERALTMGDLISFAWQISQGMQYLAEMKLVHRDL 875
Cdd:cd05046   79 EAEPHYMILEYTDLGDLKQFLRATKS---------------KDEKLKPPPLSTKQKVALCTQIALGMDHLSNARFVHRDL 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  876 AARNILVAEGRKMKISDFGLSRDVYEEDsYVKRSQGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLGGNPYPGI 955
Cdd:cd05046  144 AARNCLVSSQREVKVSLLSLSKDVYNSE-YYKLRNALIPLRWLAPEAVQEDDFSTKSDVWSFGVLMWEVFTQGELPFYGL 222
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 10862703  956 PPERLFNLLKTGH-RMERPDNCSEEMYRLMLQCWKQEPDKRPVFADISKDLEK 1007
Cdd:cd05046  223 SDEEVLNRLQAGKlELPVPEGCPSRLYKLMTRCWAVNPKDRPSFSELVSALGE 275
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
716-1006 7.88e-68

Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Lck and Blk are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Lck is expressed in T-cells and natural killer cells. It plays a critical role in T-cell maturation, activation, and T-cell receptor (TCR) signaling. Lck phosphorylates ITAM (immunoreceptor tyr activation motif) sequences on several subunits of TCRs, leading to the activation of different second messenger cascades. Phosphorylated ITAMs serve as binding sites for other signaling factor such as Syk and ZAP-70, leading to their activation and propagation of downstream events. In addition, Lck regulates drug-induced apoptosis by interfering with the mitochondrial death pathway. The apototic role of Lck is independent of its primary function in T-cell signaling. Blk is expressed specifically in B-cells. It is involved in pre-BCR (B-cell receptor) signaling. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Lck/Blk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270652 [Multi-domain]  Cd Length: 264  Bit Score: 228.62  E-value: 7.88e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  716 KWEFPRKNLVLGKTLGEGEFGKVvkATAFHlkgrAGYTTVAVKMLKENA-SPSELrdlLSEFNVLKQVNHPHVIKLYGAC 794
Cdd:cd05067    1 EWEVPRETLKLVERLGAGQFGEV--WMGYY----NGHTKVAIKSLKQGSmSPDAF---LAEANLMKQLQHQRLVRLYAVV 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  795 SQDgPLLLIVEYAKYGSLRGFLREsrkvgpgylgsggsrnsssldhPDERALTMGDLISFAWQISQGMQYLAEMKLVHRD 874
Cdd:cd05067   72 TQE-PIYIITEYMENGSLVDFLKT----------------------PSGIKLTINKLLDMAAQIAEGMAFIEERNYIHRD 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  875 LAARNILVAEGRKMKISDFGLSRdVYEEDSYVKRSQGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLGGNPYPG 954
Cdd:cd05067  129 LRAANILVSDTLSCKIADFGLAR-LIEDNEYTAREGAKFPIKWTAPEAINYGTFTIKSDVWSFGILLTEIVTHGRIPYPG 207
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 10862703  955 IP-PERLFNlLKTGHRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADISKDLE 1006
Cdd:cd05067  208 MTnPEVIQN-LERGYRMPRPDNCPEELYQLMRLCWKERPEDRPTFEYLRSVLE 259
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
730-1005 1.13e-66

Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed mainly of MAP3Ks and similar proteins, including TGF-beta Activated Kinase-1 (TAK1, also called MAP3K7), MAP3K12, MAP3K13, Mixed lineage kinase (MLK), MLK-Like mitogen-activated protein Triple Kinase (MLTK), and Raf (Rapidly Accelerated Fibrosarcoma) kinases. MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Also included in this subfamily is the pseudokinase Kinase Suppressor of Ras (KSR), which is a scaffold protein that functions downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway.


Pssm-ID: 270901 [Multi-domain]  Cd Length: 245  Bit Score: 224.72  E-value: 1.13e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  730 LGEGEFGKVVKATafhLKGragyTTVAVKMLK-ENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVEYAK 808
Cdd:cd13999    1 IGSGSFGEVYKGK---WRG----TDVAIKKLKvEDDNDELLKEFRREVSILSKLRHPNIVQFIGACLSPPPLCIVTEYMP 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  809 YGSLRGFLRESRKVgpgylgsggsrnsssldhpderaLTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNILVAEGRKM 888
Cdd:cd13999   74 GGSLYDLLHKKKIP-----------------------LSWSLRLKIALDIARGMNYLHSPPIIHRDLKSLNILLDENFTV 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  889 KISDFGLSRdvYEEDSYVKRSQGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTlGGNPYPGIPPERLFNLLKTGH 968
Cdd:cd13999  131 KIADFGLSR--IKNSTTEKMTGVVGTPRWMAPEVLRGEPYTEKADVYSFGIVLWELLT-GEVPFKELSPIQIAAAVVQKG 207
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 10862703  969 RM-ERPDNCSEEMYRLMLQCWKQEPDKRPVFADISKDL 1005
Cdd:cd13999  208 LRpPIPPDCPPELSKLIKRCWNEDPEKRPSFSEIVKRL 245
RET_CLD1 pfam17756
RET Cadherin like domain 1; RET is a single transmembrane-spanning receptor tyrosine kinase ...
29-154 1.19e-66

RET Cadherin like domain 1; RET is a single transmembrane-spanning receptor tyrosine kinase (RTK) that plays critical roles in the development of vertebrates. Structural analysis indicate that RET contains four consecutive cadherin-like domains (CLD). This entry relates to the first CLD at the N-terminal. Several regions within RET-CLD1 have been shown to be important for ligand-coreceptor binding. CLD1 and CLD2 have a distinctive clamshell shape and CLD1 is essential for CLD2 folding. CLD1 contains 2 sites for GDNF receptor alpha 1 binding.


Pssm-ID: 465485  Cd Length: 124  Bit Score: 219.87  E-value: 1.19e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703     29 LYFSRDAYWEKLYVDQAAGTPLLYVHALRDAPEEVPSFRLGQHLyGTYRTRLHENNWICIQEDTGLLYLNRSLDHSSWEK 108
Cdd:pfam17756    1 LYFPQKEYSENVYVGQPAGTPLLQVHALRDSPSEVPHFYLCQHL-GIYRRRPHYNSWFHIDEDTGLLYLNKTLDRSDFES 79
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 10862703    109 LSVRNRGfPLLTVYLKVFLSPTSLREGECQWPGCARVYFSFFNTSF 154
Cdd:pfam17756   80 LSSGNWG-PLKKLTLQVFLSSTPFREKECHSPTCARVYLSFINATA 124
PTKc_Met_Ron cd05058
Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of ...
730-1006 1.23e-66

Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Met and Ron are receptor PTKs (RTKs) composed of an alpha-beta heterodimer. The extracellular alpha chain is disulfide linked to the beta chain, which contains an extracellular ligand-binding region with a sema domain, a PSI domain and four IPT repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. Met binds to the ligand, hepatocyte growth factor/scatter factor (HGF/SF), and is also called the HGF receptor. HGF/Met signaling plays a role in growth, transformation, cell motility, invasion, metastasis, angiogenesis, wound healing, and tissue regeneration. Aberrant expression of Met through mutations or gene amplification is associated with many human cancers including hereditary papillary renal and gastric carcinomas. The ligand for Ron is macrophage stimulating protein (MSP). Ron signaling is important in regulating cell motility, adhesion, proliferation, and apoptosis. Aberrant Ron expression is implicated in tumorigenesis and metastasis. The Met/Ron subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270649 [Multi-domain]  Cd Length: 262  Bit Score: 225.43  E-value: 1.23e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  730 LGEGEFGKVVKATAFHLKGRAgyTTVAVKMLKENASPSELRDLLSEFNVLKQVNHPHVIKLYGAC-SQDGPLLLIVEYAK 808
Cdd:cd05058    3 IGKGHFGCVYHGTLIDSDGQK--IHCAVKSLNRITDIEEVEQFLKEGIIMKDFSHPNVLSLLGIClPSEGSPLVVLPYMK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  809 YGSLRGFLREsrkvgpgylgsggsrnsssldhpDERALTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNILVAEGRKM 888
Cdd:cd05058   81 HGDLRNFIRS-----------------------ETHNPTVKDLIGFGLQVAKGMEYLASKKFVHRDLAARNCMLDESFTV 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  889 KISDFGLSRDVYEEDSYV--KRSQGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLGGNPYPGIPPERLFNLLKT 966
Cdd:cd05058  138 KVADFGLARDIYDKEYYSvhNHTGAKLPVKWMALESLQTQKFTTKSDVWSFGVLLWELMTRGAPPYPDVDSFDITVYLLQ 217
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 10862703  967 GHRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADISKDLE 1006
Cdd:cd05058  218 GRRLLQPEYCPDPLYEVMLSCWHPKPEMRPTFSELVSRIS 257
PTKc_IGF-1R cd05062
Catalytic domain of the Protein Tyrosine Kinase, Insulin-like Growth Factor-1 Receptor; PTKs ...
717-1001 1.40e-66

Catalytic domain of the Protein Tyrosine Kinase, Insulin-like Growth Factor-1 Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. IGF-1R is a receptor PTK (RTK) that is composed of two alphabeta heterodimers. Binding of the ligand (IGF-1 or IGF-2) to the extracellular alpha subunit activates the intracellular tyr kinase domain of the transmembrane beta subunit. Receptor activation leads to autophosphorylation, which stimulates downstream kinase activities and biological function. IGF-1R signaling is important in the differentiation, growth, and survival of normal cells. In cancer cells, where it is frequently overexpressed, IGF-1R is implicated in proliferation, the suppression of apoptosis, invasion, and metastasis. IGF-1R is being developed as a therapeutic target in cancer treatment. The IGF-1R subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133193 [Multi-domain]  Cd Length: 277  Bit Score: 225.68  E-value: 1.40e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  717 WEFPRKNLVLGKTLGEGEFGKVVKATAFHLKGRAGYTTVAVKMLKENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQ 796
Cdd:cd05062    1 WEVAREKITMSRELGQGSFGMVYEGIAKGVVKDEPETRVAIKTVNEAASMRERIEFLNEASVMKEFNCHHVVRLLGVVSQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  797 DGPLLLIVEYAKYGSLRGFLRESRKVGPGylgsggsrnsssldHPDERALTMGDLISFAWQISQGMQYLAEMKLVHRDLA 876
Cdd:cd05062   81 GQPTLVIMELMTRGDLKSYLRSLRPEMEN--------------NPVQAPPSLKKMIQMAGEIADGMAYLNANKFVHRDLA 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  877 ARNILVAEGRKMKISDFGLSRDVYEEDSYVKRSQGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLGGNPYPGIP 956
Cdd:cd05062  147 ARNCMVAEDFTVKIGDFGMTRDIYETDYYRKGGKGLLPVRWMSPESLKDGVFTTYSDVWSFGVVLWEIATLAEQPYQGMS 226
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 10862703  957 PERLFNLLKTGHRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADI 1001
Cdd:cd05062  227 NEQVLRFVMEGGLLDKPDNCPDMLFELMRMCWQYNPKMRPSFLEI 271
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
727-1005 3.66e-66

Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fes (or Fps) is a cytoplasmic (or nonreceptor) PTK containing an N-terminal region with FCH (Fes/Fer/CIP4 homology) and coiled-coil domains, followed by a SH2 domain, and a C-terminal catalytic domain. The genes for Fes (feline sarcoma) and Fps (Fujinami poultry sarcoma) were first isolated from tumor-causing retroviruses. The viral oncogenes encode chimeric Fes proteins consisting of Gag sequences at the N-termini, resulting in unregulated PTK activity. Fes kinase is expressed in myeloid, vascular endothelial, epithelial, and neuronal cells. It plays important roles in cell growth and differentiation, angiogenesis, inflammation and immunity, and cytoskeletal regulation. A recent study implicates Fes kinase as a tumor suppressor in colorectal cancer. The Fes subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270667 [Multi-domain]  Cd Length: 252  Bit Score: 223.65  E-value: 3.66e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  727 GKTLGEGEFGKVvkataFHLKGRAGYTTVAVKMLKENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVEY 806
Cdd:cd05084    1 GERIGRGNFGEV-----FSGRLRADNTPVAVKSCRETLPPDLKAKFLQEARILKQYSHPNIVRLIGVCTQKQPIYIVMEL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  807 AKYGSLRGFLRESrkvGPgylgsggsrnsssldhpderALTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNILVAEGR 886
Cdd:cd05084   76 VQGGDFLTFLRTE---GP--------------------RLKVKELIRMVENAAAGMEYLESKHCIHRDLAARNCLVTEKN 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  887 KMKISDFGLSRDvyEEDSYVKRSQG--RIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLGGNPYPGIPPERLFNLL 964
Cdd:cd05084  133 VLKISDFGMSRE--EEDGVYAATGGmkQIPVKWTAPEALNYGRYSSESDVWSFGILLWETFSLGAVPYANLSNQQTREAV 210
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 10862703  965 KTGHRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADISKDL 1005
Cdd:cd05084  211 EQGVRLPCPENCPDEVYRLMEQCWEYDPRKRPSFSTVHQDL 251
PTK_Ryk cd05043
Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase ...
732-998 5.83e-66

Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase (RTK) containing an extracellular region with two leucine-rich motifs, a transmembrane segment, and an intracellular inactive pseudokinase domain, which shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. The extracellular region of Ryk shows homology to the N-terminal domain of Wnt inhibitory factor-1 (WIF) and serves as the ligand (Wnt) binding domain of Ryk. Ryk is expressed in many different tissues both during development and in adults, suggesting a widespread function. It acts as a chemorepulsive axon guidance receptor of Wnt glycoproteins and is responsible for the establishment of axon tracts during the development of the central nervous system. In addition, studies in mice reveal that Ryk is essential in skeletal, craniofacial, and cardiac development. Thus, it appears Ryk is involved in signal transduction despite its lack of kinase activity. Ryk may function as an accessory protein that modulates the signals coming from catalytically active partner RTKs such as the Eph receptors. The Ryk subfamily is part of a larger superfamily that includes other pseudokinases and the catalytic domains of active kinases including PTKs, protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270639 [Multi-domain]  Cd Length: 279  Bit Score: 223.87  E-value: 5.83e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  732 EGEFGKVVKATAFHLKGRAgyTTVAVKMLKENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQD-GPLLLIVEYAKYG 810
Cdd:cd05043   16 EGTFGRIFHGILRDEKGKE--EEVLVKTVKDHASEIQVTMLLQESSLLYGLSHQNLLPILHVCIEDgEKPMVLYPYMNWG 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  811 SLRGFLRESRKVGPGylgsggsrnsssldhpDERALTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNILVAEGRKMKI 890
Cdd:cd05043   94 NLKLFLQQCRLSEAN----------------NPQALSTQQLVHMALQIACGMSYLHRRGVIHKDIAARNCVIDDELQVKI 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  891 SDFGLSRDVYEEDSYVKRSQGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLGGNPYPGIPPERLFNLLKTGHRM 970
Cdd:cd05043  158 TDNALSRDLFPMDYHCLGDNENRPIKWMSLESLVNKEYSSASDVWSFGVLLWELMTLGQTPYVEIDPFEMAAYLKDGYRL 237
                        250       260
                 ....*....|....*....|....*...
gi 10862703  971 ERPDNCSEEMYRLMLQCWKQEPDKRPVF 998
Cdd:cd05043  238 AQPINCPDELFAVMACCWALDPEERPSF 265
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
727-1005 6.14e-66

Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; Fer kinase; catalytic (c) domain. The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K). PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fer kinase is a member of the Fes subfamily of proteins which are cytoplasmic (or nonreceptor) tyr kinases containing an N-terminal region with FCH (Fes/Fer/CIP4 homology) and coiled-coil domains, followed by a SH2 domain, and a C-terminal catalytic domain. Fer kinase is expressed in a wide variety of tissues, and is found to reside in both the cytoplasm and the nucleus. It plays important roles in neuronal polarization and neurite development, cytoskeletal reorganization, cell migration, growth factor signaling, and the regulation of cell-cell interactions mediated by adherens junctions and focal adhesions. Fer kinase also regulates cell cycle progression in malignant cells.


Pssm-ID: 270668 [Multi-domain]  Cd Length: 251  Bit Score: 222.96  E-value: 6.14e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  727 GKTLGEGEFGKVVKATafhLKGRagyTTVAVKMLKENAsPSELR-DLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVE 805
Cdd:cd05085    1 GELLGKGNFGEVYKGT---LKDK---TPVAVKTCKEDL-PQELKiKFLSEARILKQYDHPNIVKLIGVCTQRQPIYIVME 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  806 YAKYGSLRGFLRESRkvgpgylgsggsrnsssldhpDEraLTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNILVAEG 885
Cdd:cd05085   74 LVPGGDFLSFLRKKK---------------------DE--LKTKQLVKFSLDAAAGMAYLESKNCIHRDLAARNCLVGEN 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  886 RKMKISDFGLSRdvyEEDSYVKRSQG--RIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLGGNPYPGIPPERLFNL 963
Cdd:cd05085  131 NALKISDFGMSR---QEDDGVYSSSGlkQIPIKWTAPEALNYGRYSSESDVWSFGILLWETFSLGVCPYPGMTNQQAREQ 207
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 10862703  964 LKTGHRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADISKDL 1005
Cdd:cd05085  208 VEKGYRMSAPQRCPEDIYKIMQRCWDYNPENRPKFSELQKEL 249
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
722-1005 3.19e-65

Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Tec-like subfamily is composed of Tec, Btk, Bmx (Etk), Itk (Tsk, Emt), Rlk (Txk), and similar proteins. They are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, some members contain the Tec homology (TH) domain, which contains proline-rich and zinc-binding regions. Tec kinases form the second largest subfamily of nonreceptor PTKs and are expressed mainly by haematopoietic cells, although Tec and Bmx are also found in endothelial cells. B-cells express Btk and Tec, while T-cells express Itk, Txk, and Tec. Collectively, Tec kinases are expressed in a variety of myeloid cells such as mast cells, platelets, macrophages, and dendritic cells. Each Tec kinase shows a distinct cell-type pattern of expression. Tec kinases play important roles in the development, differentiation, maturation, regulation, survival, and function of B-cells and T-cells. Mutations in Btk cause the severe B-cell immunodeficiency, X-linked agammaglobulinaemia (XLA). The Tec-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173637 [Multi-domain]  Cd Length: 256  Bit Score: 221.17  E-value: 3.19e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  722 KNLVLGKTLGEGEFGKVvkatafHLKGRAGYTTVAVKMLKENASPSElrDLLSEFNVLKQVNHPHVIKLYGACSQDGPLL 801
Cdd:cd05059    4 SELTFLKELGSGQFGVV------HLGKWRGKIDVAIKMIKEGSMSED--DFIEEAKVMMKLSHPKLVQLYGVCTKQRPIF 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  802 LIVEYAKYGSLRGFLRESRKVgpgylgsggsrnsssldhpderaLTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNIL 881
Cdd:cd05059   76 IVTEYMANGCLLNYLRERRGK-----------------------FQTEQLLEMCKDVCEAMEYLESNGFIHRDLAARNCL 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  882 VAEGRKMKISDFGLSRDVYEeDSYVKRSQGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLGGNPYPGIPPERLF 961
Cdd:cd05059  133 VGEQNVVKVSDFGLARYVLD-DEYTSSVGTKFPVKWSPPEVFMYSKFSSKSDVWSFGVLMWEVFSEGKMPYERFSNSEVV 211
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 10862703  962 NLLKTGHRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADISKDL 1005
Cdd:cd05059  212 EHISQGYRLYRPHLAPTEVYTIMYSCWHEKPEERPTFKILLSQL 255
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
728-1005 6.41e-65

Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily includes Ack1, thirty-eight-negative kinase 1 (Tnk1), and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing an N-terminal catalytic domain, an SH3 domain, a Cdc42-binding CRIB domain, and a proline-rich region. They are mainly expressed in brain and skeletal tissues and are involved in the regulation of cell adhesion and growth, receptor degradation, and axonal guidance. Ack1 is also associated with androgen-independent prostate cancer progression. Tnk1 regulates TNFalpha signaling and may play an important role in cell death. The Ack-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270636 [Multi-domain]  Cd Length: 258  Bit Score: 220.29  E-value: 6.41e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  728 KTLGEGEFGkVVKatafhlkgRAGYTT-------VAVKMLKEN--ASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDg 798
Cdd:cd05040    1 EKLGDGSFG-VVR--------RGEWTTpsgkviqVAVKCLKSDvlSQPNAMDDFLKEVNAMHSLDHPNLIRLYGVVLSS- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  799 PLLLIVEYAKYGSLRGFLRESRkvgpgylgsggsrnsssldhpdeRALTMGDLISFAWQISQGMQYLAEMKLVHRDLAAR 878
Cdd:cd05040   71 PLMMVTELAPLGSLLDRLRKDQ-----------------------GHFLISTLCDYAVQIANGMAYLESKRFIHRDLAAR 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  879 NILVAEGRKMKISDFGLSRDV-YEEDSYVKRSQGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLGGNPYPGIPP 957
Cdd:cd05040  128 NILLASKDKVKIGDFGLMRALpQNEDHYVMQEHRKVPFAWCAPESLKTRKFSHASDVWMFGVTLWEMFTYGEEPWLGLNG 207
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 10862703  958 ER-LFNLLKTGHRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADISKDL 1005
Cdd:cd05040  208 SQiLEKIDKEGERLERPDDCPQDIYNVMLQCWAHKPADRPTFVALRDFL 256
PTKc_EGFR cd05108
Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs ...
728-1024 3.65e-63

Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EGFR (HER1, ErbB1) is a receptor PTK (RTK) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. Ligands for EGFR include EGF, heparin binding EGF-like growth factor (HBEGF), epiregulin, amphiregulin, TGFalpha, and betacellulin. Upon ligand binding, EGFR can form homo- or heterodimers with other EGFR subfamily members. The EGFR signaling pathway is one of the most important pathways regulating cell proliferation, differentiation, survival, and growth. Overexpression and mutation in the kinase domain of EGFR have been implicated in the development and progression of a variety of cancers. A number of monoclonal antibodies and small molecule inhibitors have been developed that target EGFR, including the antibodies Cetuximab and Panitumumab, which are used in combination with other therapies for the treatment of colorectal cancer and non-small cell lung carcinoma (NSCLC). The small molecule inhibitors Gefitinib (Iressa) and Erlotinib (Tarceva), already used for NSCLC, are undergoing clinical trials for other types of cancer including gastrointestinal, breast, head and neck, and bladder. The EGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270683 [Multi-domain]  Cd Length: 313  Bit Score: 217.58  E-value: 3.65e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  728 KTLGEGEFGKVVKATaFHLKGRAGYTTVAVKMLKENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGpLLLIVEYA 807
Cdd:cd05108   13 KVLGSGAFGTVYKGL-WIPEGEKVKIPVAIKELREATSPKANKEILDEAYVMASVDNPHVCRLLGICLTST-VQLITQLM 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  808 KYGSLRGFLRESR-KVGPGYLgsggsrnsssldhpderaltmgdlISFAWQISQGMQYLAEMKLVHRDLAARNILVAEGR 886
Cdd:cd05108   91 PFGCLLDYVREHKdNIGSQYL------------------------LNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQ 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  887 KMKISDFGLSRDVYEEDSYVKRSQGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLGGNPYPGIPPERLFNLLKT 966
Cdd:cd05108  147 HVKITDFGLAKLLGAEEKEYHAEGGKVPIKWMALESILHRIYTHQSDVWSYGVTVWELMTFGSKPYDGIPASEISSILEK 226
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 10862703  967 GHRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADISKDLEKMMVKRRDYLDLAASTPS 1024
Cdd:cd05108  227 GERLPQPPICTIDVYMIMVKCWMIDADSRPKFRELIIEFSKMARDPQRYLVIQGDERM 284
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
717-998 4.17e-63

Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Lyn is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Lyn is expressed in B lymphocytes and myeloid cells. It exhibits both positive and negative regulatory roles in B cell receptor (BCR) signaling. Lyn, as well as Fyn and Blk, promotes B cell activation by phosphorylating ITAMs (immunoreceptor tyr activation motifs) in CD19 and in Ig components of BCR. It negatively regulates signaling by its unique ability to phosphorylate ITIMs (immunoreceptor tyr inhibition motifs) in cell surface receptors like CD22 and CD5. Lyn also plays an important role in G-CSF receptor signaling by phosphorylating a variety of adaptor molecules. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Lyn subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270657 [Multi-domain]  Cd Length: 272  Bit Score: 215.68  E-value: 4.17e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  717 WEFPRKNLVLGKTLGEGEFGKVvkATAFHlkgrAGYTTVAVKMLKENASpsELRDLLSEFNVLKQVNHPHVIKLYGACSQ 796
Cdd:cd05072    2 WEIPRESIKLVKKLGAGQFGEV--WMGYY----NNSTKVAVKTLKPGTM--SVQAFLEEANLMKTLQHDKLVRLYAVVTK 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  797 DGPLLLIVEYAKYGSLRGFLREsrkvgpgylgsggsrnsssldhpDERA-LTMGDLISFAWQISQGMQYLAEMKLVHRDL 875
Cdd:cd05072   74 EEPIYIITEYMAKGSLLDFLKS-----------------------DEGGkVLLPKLIDFSAQIAEGMAYIERKNYIHRDL 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  876 AARNILVAEGRKMKISDFGLSRdVYEEDSYVKRSQGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLGGNPYPGI 955
Cdd:cd05072  131 RAANVLVSESLMCKIADFGLAR-VIEDNEYTAREGAKFPIKWTAPEAINFGSFTIKSDVWSFGILLYEIVTYGKIPYPGM 209
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 10862703  956 PPERLFNLLKTGHRMERPDNCSEEMYRLMLQCWKQEPDKRPVF 998
Cdd:cd05072  210 SNSDVMSALQRGYRMPRMENCPDELYDIMKTCWKEKAEERPTF 252
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the ...
728-999 4.41e-62

Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Syk is a cytoplasmic (or nonreceptor) PTK containing two Src homology 2 (SH2) domains N-terminal to the catalytic tyr kinase domain. Syk was first cloned from the spleen, and its function in hematopoietic cells is well-established. It is involved in the signaling downstream of activated receptors (including B-cell and Fc receptors) that contain ITAMs (immunoreceptor tyr activation motifs), leading to processes such as cell proliferation, differentiation, survival, adhesion, migration, and phagocytosis. More recently, Syk expression has been detected in other cell types (including epithelial cells, vascular endothelial cells, neurons, hepatocytes, and melanocytes), suggesting a variety of biological functions in non-immune cells. Syk plays a critical role in maintaining vascular integrity and in wound healing during embryogenesis. It also regulates Vav3, which is important in osteoclast function including bone development. In breast epithelial cells, where Syk acts as a negative regulator for EGFR signaling, loss of Syk expression is associated with abnormal proliferation during cancer development suggesting a potential role as a tumor suppressor. In mice, Syk has been shown to inhibit malignant transformation of mammary epithelial cells induced with murine mammary tumor virus (MMTV). The Syk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133247 [Multi-domain]  Cd Length: 257  Bit Score: 212.13  E-value: 4.41e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  728 KTLGEGEFGKVVKAtafHLKGRAGYTTVAVKMLKENASPSELRD-LLSEFNVLKQVNHPHVIKLYGACSQDGpLLLIVEY 806
Cdd:cd05116    1 GELGSGNFGTVKKG---YYQMKKVVKTVAVKILKNEANDPALKDeLLREANVMQQLDNPYIVRMIGICEAES-WMLVMEM 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  807 AKYGSLRGFLRESRKVgpgylgsggsrnsssldhpderalTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNILVAEGR 886
Cdd:cd05116   77 AELGPLNKFLQKNRHV------------------------TEKNITELVHQVSMGMKYLEESNFVHRDLAARNVLLVTQH 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  887 KMKISDFGLSRDVYEEDSYVK-RSQGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLGGNPYPGIPPERLFNLLK 965
Cdd:cd05116  133 YAKISDFGLSKALRADENYYKaQTHGKWPVKWYAPECMNYYKFSSKSDVWSFGVLMWEAFSYGQKPYKGMKGNEVTQMIE 212
                        250       260       270
                 ....*....|....*....|....*....|....
gi 10862703  966 TGHRMERPDNCSEEMYRLMLQCWKQEPDKRPVFA 999
Cdd:cd05116  213 KGERMECPAGCPPEMYDLMKLCWTYDVDERPGFA 246
PTKc_HER2 cd05109
Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the ...
728-1008 1.93e-61

Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. HER2 (ErbB2, HER2/neu) is a member of the EGFR (HER, ErbB) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. HER2 does not bind to any known EGFR subfamily ligands, but contributes to the kinase activity of all possible heterodimers. It acts as the preferred partner of other ligand-bound EGFR proteins and functions as a signal amplifier, with the HER2-HER3 heterodimer being the most potent pair in mitogenic signaling. HER2 plays an important role in cell development, proliferation, survival and motility. Overexpression of HER2 results in its activation and downstream signaling, even in the absence of ligand. HER2 overexpression, mainly due to gene amplification, has been shown in a variety of human cancers. Its role in breast cancer is especially well-documented. HER2 is up-regulated in about 25% of breast tumors and is associated with increases in tumor aggressiveness, recurrence and mortality. HER2 is a target for monoclonal antibodies and small molecule inhibitors, which are being developed as treatments for cancer. The first humanized antibody approved for clinical use is Trastuzumab (Herceptin), which is being used in combination with other therapies to improve the survival rates of patients with HER2-overexpressing breast cancer. The HER2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270684 [Multi-domain]  Cd Length: 279  Bit Score: 211.42  E-value: 1.93e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  728 KTLGEGEFGKVVKATaFHLKGRAGYTTVAVKMLKENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDgPLLLIVEYA 807
Cdd:cd05109   13 KVLGSGAFGTVYKGI-WIPDGENVKIPVAIKVLRENTSPKANKEILDEAYVMAGVGSPYVCRLLGICLTS-TVQLVTQLM 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  808 KYGSLRGFLRESR-KVGPGylgsggsrnsssldhpderaltmgDLISFAWQISQGMQYLAEMKLVHRDLAARNILVAEGR 886
Cdd:cd05109   91 PYGCLLDYVRENKdRIGSQ------------------------DLLNWCVQIAKGMSYLEEVRLVHRDLAARNVLVKSPN 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  887 KMKISDFGLSRDVYEEDSYVKRSQGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLGGNPYPGIPPERLFNLLKT 966
Cdd:cd05109  147 HVKITDFGLARLLDIDETEYHADGGKVPIKWMALESILHRRFTHQSDVWSYGVTVWELMTFGAKPYDGIPAREIPDLLEK 226
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 10862703  967 GHRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADISKDLEKM 1008
Cdd:cd05109  227 GERLPQPPICTIDVYMIMVKCWMIDSECRPRFRELVDEFSRM 268
PTKc_TrkB cd05093
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze ...
721-1017 2.12e-61

Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. TrkB is a receptor PTK (RTK) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding of TrkB to its ligands, brain-derived neurotrophic factor (BDNF) or neurotrophin 4 (NT4), results in receptor oligomerization and activation of the catalytic domain. TrkB is broadly expressed in the nervous system and in some non-neural tissues. It plays important roles in cell proliferation, differentiation, and survival. BDNF/Trk signaling plays a key role in regulating activity-dependent synaptic plasticity. TrkB also contributes to protection against gp120-induced neuronal cell death. TrkB overexpression is associated with poor prognosis in neuroblastoma (NB) and other human cancers. It acts as a suppressor of anoikis (detachment-induced apoptosis) and contributes to tumor metastasis. The TrkB subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270675 [Multi-domain]  Cd Length: 288  Bit Score: 211.44  E-value: 2.12e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  721 RKNLVLGKTLGEGEFGKVVKATAFHLKGRAGYTTVAVKMLKEnASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPL 800
Cdd:cd05093    4 RHNIVLKRELGEGAFGKVFLAECYNLCPEQDKILVAVKTLKD-ASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  801 LLIVEYAKYGSLRGFLRESrkvGPGYLGSGGSRNSSSLDHPDeraltmgdLISFAWQISQGMQYLAEMKLVHRDLAARNI 880
Cdd:cd05093   83 IMVFEYMKHGDLNKFLRAH---GPDAVLMAEGNRPAELTQSQ--------MLHIAQQIAAGMVYLASQHFVHRDLATRNC 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  881 LVAEGRKMKISDFGLSRDVYEEDSYVKRSQGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLGGNPYPGIPPERL 960
Cdd:cd05093  152 LVGENLLVKIGDFGMSRDVYSTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNEV 231
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 10862703  961 FNLLKTGHRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADISKDLEKMMVKRRDYLD 1017
Cdd:cd05093  232 IECITQGRVLQRPRTCPKEVYDLMLGCWQREPHMRLNIKEIHSLLQNLAKASPVYLD 288
PTKc_DDR2 cd05095
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze ...
718-1007 3.33e-61

Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. DDR2 is a receptor PTK (RTK) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDR2 results in a slow but sustained receptor activation. DDR2 binds mostly to fibrillar collagens as well as collagen X. DDR2 is widely expressed in many tissues with the highest levels found in skeletal muscle, skin, kidney and lung. It is important in cell proliferation and development. Mice, with a deletion of DDR2, suffer from dwarfism and delayed healing of epidermal wounds. DDR2 also contributes to collagen (type I) regulation by inhibiting fibrillogenesis and altering the morphology of collagen fibers. It is also expressed in immature dendritic cells (DCs), where it plays a role in DC activation and function. The DDR2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270677 [Multi-domain]  Cd Length: 297  Bit Score: 211.39  E-value: 3.33e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  718 EFPRKNLVLGKTLGEGEFGKV----------VKATAFHLKGRAGYTT-VAVKMLKENASPSELRDLLSEFNVLKQVNHPH 786
Cdd:cd05095    1 EFPRKLLTFKEKLGEGQFGEVhlceaegmekFMDKDFALEVSENQPVlVAVKMLRADANKNARNDFLKEIKIMSRLKDPN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  787 VIKLYGACSQDGPLLLIVEYAKYGSLRGFLreSRKVGPGYLGSGgsrnsssldhPDERALTMGDLISFAWQISQGMQYLA 866
Cdd:cd05095   81 IIRLLAVCITDDPLCMITEYMENGDLNQFL--SRQQPEGQLALP----------SNALTVSYSDLRFMAAQIASGMKYLS 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  867 EMKLVHRDLAARNILVAEGRKMKISDFGLSRDVYEEDSYvkRSQGR--IPVKWMAIESLFDHIYTTQSDVWSFGVLLWEI 944
Cdd:cd05095  149 SLNFVHRDLATRNCLVGKNYTIKIADFGMSRNLYSGDYY--RIQGRavLPIRWMSWESILLGKFTTASDVWAFGVTLWET 226
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 10862703  945 VTL-GGNPYPGIPPERLFNllKTGH---------RMERPDNCSEEMYRLMLQCWKQEPDKRPVFADISKDLEK 1007
Cdd:cd05095  227 LTFcREQPYSQLSDEQVIE--NTGEffrdqgrqtYLPQPALCPDSVYKLMLSCWRRDTKDRPSFQEIHTLLQE 297
PTKc_DDR1 cd05096
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 1; PTKs catalyze ...
718-1001 5.56e-61

Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. DDR1 is a receptor PTK (RTK) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDR1 results in a slow but sustained receptor activation. DDR1 binds to all collagens tested to date (types I-IV). It is widely expressed in many tissues. It is abundant in the brain and is also found in keratinocytes, colonic mucosa epithelium, lung epithelium, thyroid follicles, and the islets of Langerhans. During embryonic development, it is found in the developing neuroectoderm. DDR1 is a key regulator of cell morphogenesis, differentiation and proliferation. It is important in the development of the mammary gland, the vasculator and the kidney. DDR1 is also found in human leukocytes, where it facilitates cell adhesion, migration, maturation, and cytokine production. The DDR1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133227 [Multi-domain]  Cd Length: 304  Bit Score: 210.95  E-value: 5.56e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  718 EFPRKNLVLGKTLGEGEFGKV----------VKATAFHLKGRAGYTT-VAVKMLKENASPSELRDLLSEFNVLKQVNHPH 786
Cdd:cd05096    1 KFPRGHLLFKEKLGEGQFGEVhlcevvnpqdLPTLQFPFNVRKGRPLlVAVKILRPDANKNARNDFLKEVKILSRLKDPN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  787 VIKLYGACSQDGPLLLIVEYAKYGSLRGFLRESR---KVGPGYLGSGGSRNSSSLDHPDeraltmgdLISFAWQISQGMQ 863
Cdd:cd05096   81 IIRLLGVCVDEDPLCMITEYMENGDLNQFLSSHHlddKEENGNDAVPPAHCLPAISYSS--------LLHVALQIASGMK 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  864 YLAEMKLVHRDLAARNILVAEGRKMKISDFGLSRDVYEEDSYvkRSQGR--IPVKWMAIESLFDHIYTTQSDVWSFGVLL 941
Cdd:cd05096  153 YLSSLNFVHRDLATRNCLVGENLTIKIADFGMSRNLYAGDYY--RIQGRavLPIRWMAWECILMGKFTTASDVWAFGVTL 230
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 10862703  942 WEIVTL-GGNPYPGIPPER-------LFNLLKTGHRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADI 1001
Cdd:cd05096  231 WEILMLcKEQPYGELTDEQvienageFFRDQGRQVYLFRPPPCPQGLYELMLQCWSRDCRERPSFSDI 298
PTKc_TrkC cd05094
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze ...
721-1008 1.03e-60

Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. TrkC is a receptor PTK (RTK) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding of TrkC to its ligand, neurotrophin 3 (NT3), results in receptor oligomerization and activation of the catalytic domain. TrkC is broadly expressed in the nervous system and in some non-neural tissues including the developing heart. NT3/TrkC signaling plays an important role in the innervation of the cardiac conducting system and the development of smooth muscle cells. Mice deficient with NT3 and TrkC have multiple heart defects. NT3/TrkC signaling is also critical for the development and maintenance of enteric neurons that are important for the control of gut peristalsis. The TrkC subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270676 [Multi-domain]  Cd Length: 287  Bit Score: 209.48  E-value: 1.03e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  721 RKNLVLGKTLGEGEFGKVVKATAFHLKGRAGYTTVAVKMLKEnASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPL 800
Cdd:cd05094    4 RRDIVLKRELGEGAFGKVFLAECYNLSPTKDKMLVAVKTLKD-PTLAARKDFQREAELLTNLQHDHIVKFYGVCGDGDPL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  801 LLIVEYAKYGSLRGFLRESrkvGPGYLGSGGSRNSSSldhpdERALTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNI 880
Cdd:cd05094   83 IMVFEYMKHGDLNKFLRAH---GPDAMILVDGQPRQA-----KGELGLSQMLHIATQIASGMVYLASQHFVHRDLATRNC 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  881 LVAEGRKMKISDFGLSRDVYEEDSYVKRSQGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLGGNPYPGIPPERL 960
Cdd:cd05094  155 LVGANLLVKIGDFGMSRDVYSTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSFGVILWEIFTYGKQPWFQLSNTEV 234
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 10862703  961 FNLLKTGHRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADISKDLEKM 1008
Cdd:cd05094  235 IECITQGRVLERPRVCPKEVYDIMLGCWQREPQQRLNIKEIYKILHAL 282
RET_CLD4 pfam17813
RET Cadherin like domain 4; RET is a single transmembrane-spanning receptor tyrosine kinase ...
404-506 8.61e-60

RET Cadherin like domain 4; RET is a single transmembrane-spanning receptor tyrosine kinase (RTK) that plays critical roles in the development of vertebrates. Structural analysis indicate that the ligand-binding RET ectodomain (RET-ECD) contains four consecutive cadherin-like domains (CLD1-CLD4) followed by a membrane-proximal cysteine-rich domain (CRD). This entry relates to CLD4 which is required for CRD folding.


Pssm-ID: 465517  Cd Length: 104  Bit Score: 199.48  E-value: 8.61e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703    404 LPS-TYSLSVSRRARRFAQIGKVCVENCQAFSGINVQYKLHSSGANCSTLGVVTSAEDTSGILFVNDTKALRRPKCAELH 482
Cdd:pfam17813    1 FPNvTYSFTVSRRARRYAQIGKVCVENCQEFSGIRVQYRLQPSDTNCYALGVATSPEDTSGTLYVNDTEALRRPECQELQ 80
                           90       100
                   ....*....|....*....|....
gi 10862703    483 YMVVATDQQTSRQAQAQLLVTVEG 506
Cdd:pfam17813   81 YTVVAQEQQTQLQAQTQLLVTVEG 104
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
713-1006 2.20e-59

Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Hck is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Hck is present in myeloid and lymphoid cells that play a role in the development of cancer. It may be important in the oncogenic signaling of the protein Tel-Abl, which induces a chronic myelogenous leukemia (CML)-like disease. Hck also acts as a negative regulator of G-CSF-induced proliferation of granulocytic precursors, suggesting a possible role in the development of acute myeloid leukemia (AML). In addition, Hck is essential in regulating the degranulation of polymorphonuclear leukocytes. Genetic polymorphisms affect the expression level of Hck, which affects PMN mediator release and influences the development of chronic obstructive pulmonary disease (COPD). Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Hck subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270658 [Multi-domain]  Cd Length: 265  Bit Score: 204.87  E-value: 2.20e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  713 EDPKWEFPRKNLVLGKTLGEGEFGKVVKATafhlkgRAGYTTVAVKMLKENASPSELrdLLSEFNVLKQVNHPHVIKLYG 792
Cdd:cd05073    2 EKDAWEIPRESLKLEKKLGAGQFGEVWMAT------YNKHTKVAVKTMKPGSMSVEA--FLAEANVMKTLQHDKLVKLHA 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  793 ACSQDgPLLLIVEYAKYGSLRGFLRESrkvgpgylgsggsrnsssldhpDERALTMGDLISFAWQISQGMQYLAEMKLVH 872
Cdd:cd05073   74 VVTKE-PIYIITEFMAKGSLLDFLKSD----------------------EGSKQPLPKLIDFSAQIAEGMAFIEQRNYIH 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  873 RDLAARNILVAEGRKMKISDFGLSRdVYEEDSYVKRSQGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLGGNPY 952
Cdd:cd05073  131 RDLRAANILVSASLVCKIADFGLAR-VIEDNEYTAREGAKFPIKWTAPEAINFGSFTIKSDVWSFGILLMEIVTYGRIPY 209
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 10862703  953 PGIPPERLFNLLKTGHRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADISKDLE 1006
Cdd:cd05073  210 PGMSNPEVIRALERGYRMPRPENCPEELYNIMMRCWKNRPEERPTFEYIQSVLD 263
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
728-1009 3.84e-59

Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The EphA2 receptor is overexpressed in tumor cells and tumor blood vessels in a variety of cancers including breast, prostate, lung, and colon. As a result, it is an attractive target for drug design since its inhibition could affect several aspects of tumor progression. EphRs comprise the largest subfamily of receptor PTKs (RTKs). Class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. EphRs contain an ephrin binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion, making it important in neural development and plasticity, cell morphogenesis, cell-fate determination, embryonic development, tissue patterning, and angiogenesis. The EphA2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 133194 [Multi-domain]  Cd Length: 268  Bit Score: 204.44  E-value: 3.84e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  728 KTLGEGEFGKVVKATaFHLKGRAgYTTVAVKMLKENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVEYA 807
Cdd:cd05063   11 KVIGAGEFGEVFRGI-LKMPGRK-EVAVAIKTLKPGYTEKQRQDFLSEASIMGQFSHHNIIRLEGVVTKFKPAMIITEYM 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  808 KYGSLRGFLResrkvgpgylgsggsrnssslDHPDEraLTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNILVAEGRK 887
Cdd:cd05063   89 ENGALDKYLR---------------------DHDGE--FSSYQLVGMLRGIAAGMKYLSDMNYVHRDLAARNILVNSNLE 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  888 MKISDFGLSRdVYEED---SYVKrSQGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLGGNPYPGIPPERLFNLL 964
Cdd:cd05063  146 CKVSDFGLSR-VLEDDpegTYTT-SGGKIPIRWTAPEAIAYRKFTSASDVWSFGIVMWEVMSFGERPYWDMSNHEVMKAI 223
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 10862703  965 KTGHRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADISKDLEKMM 1009
Cdd:cd05063  224 NDGFRLPAPMDCPSAVYQLMLQCWQQDRARRPRFVDIVNLLDKLL 268
RET_CLD3 pfam17812
RET Cadherin like domain 3; RET is a single transmembrane-spanning receptor tyrosine kinase ...
265-379 2.26e-58

RET Cadherin like domain 3; RET is a single transmembrane-spanning receptor tyrosine kinase (RTK) that plays critical roles in the development of vertebrates. Structural analysis indicate that RET contains four consecutive cadherin-like domains (CLD). This entry relates to CLD3. Classical cadherin calcium-coordinating motifs can be found between CLD2 and CLD3.


Pssm-ID: 465516  Cd Length: 114  Bit Score: 196.07  E-value: 2.26e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703    265 EDDSAPTFpAGVDTASAVVEFKRKEDTVVATLRVFDADVVPA--SGELVRRYTSTLLPGDTWAQQTFRVEHWPNETSVQA 342
Cdd:pfam17812    1 EDDSAPYV-NGTDTADAVVEFNRKEGTVFGTLRVFDRDTTPIypKDQSHNKYVGTLLTNDPWIKETFRIEHSFNETKAIF 79
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 10862703    343 NGsfVRATVHDYRLVLNRNLSISENRTMQLAVLVNDS 379
Cdd:pfam17812   80 GN--VRGTVHEYKLVLNRNLPITENRSLQLDYLVNDT 114
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
717-1006 3.10e-58

Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Csk catalyzes the tyr phosphorylation of the regulatory C-terminal tail of Src kinases, resulting in their inactivation. Csk is expressed in a wide variety of tissues. As a negative regulator of Src, Csk plays a role in cell proliferation, survival, and differentiation, and consequently, in cancer development and progression. Csk is a cytoplasmic (or nonreceptor) PTK containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. To inhibit Src kinases, Csk is translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. In addition, Csk also shows Src-independent functions. It is a critical component in G-protein signaling, and plays a role in cytoskeletal reorganization and cell migration. The Csk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133213 [Multi-domain]  Cd Length: 256  Bit Score: 201.36  E-value: 3.10e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  717 WEFPRKNLVLGKTLGEGEFGKVvkatafhLKGRAGYTTVAVKMLKENASPselRDLLSEFNVLKQVNHPHVIKLYGACSQ 796
Cdd:cd05082    1 WALNMKELKLLQTIGKGEFGDV-------MLGDYRGNKVAVKCIKNDATA---QAFLAEASVMTQLRHSNLVQLLGVIVE 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  797 D-GPLLLIVEYAKYGSLRGFLReSRKvgpgylgsggsrnsssldhpdeRALTMGD-LISFAWQISQGMQYLAEMKLVHRD 874
Cdd:cd05082   71 EkGGLYIVTEYMAKGSLVDYLR-SRG----------------------RSVLGGDcLLKFSLDVCEAMEYLEGNNFVHRD 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  875 LAARNILVAEGRKMKISDFGLSRDVYEedsyvKRSQGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLGGNPYPG 954
Cdd:cd05082  128 LAARNVLVSEDNVAKVSDFGLTKEASS-----TQDTGKLPVKWTAPEALREKKFSTKSDVWSFGILLWEIYSFGRVPYPR 202
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 10862703  955 IPPERLFNLLKTGHRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADISKDLE 1006
Cdd:cd05082  203 IPLKDVVPRVEKGYKMDAPDGCPPAVYDVMKNCWHLDAAMRPSFLQLREQLE 254
PTKc_Ror1 cd05090
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
718-1001 4.57e-58

Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Ror kinases are expressed in many tissues during development. Avian Ror1 was found to be involved in late limb development. Studies in mice reveal that Ror1 is important in the regulation of neurite growth in central neurons, as well as in respiratory development. Loss of Ror1 also enhances the heart and skeletal abnormalities found in Ror2-deficient mice. Ror proteins are orphan receptor PTKs (RTKs) containing an extracellular region with immunoglobulin-like, cysteine-rich, and kringle domains, a transmembrane segment, and an intracellular catalytic domain. Ror RTKs are unrelated to the nuclear receptor subfamily called retinoid-related orphan receptors (RORs). RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. The Ror1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270672 [Multi-domain]  Cd Length: 283  Bit Score: 201.78  E-value: 4.57e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  718 EFPRKNLVLGKTLGEGEFGKVVKAtAFHLKGRAGYTTVAVKMLKENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQD 797
Cdd:cd05090    1 ELPLSAVRFMEELGECAFGKIYKG-HLYLPGMDHAQLVAIKTLKDYNNPQQWNEFQQEASLMTELHHPNIVCLLGVVTQE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  798 GPLLLIVEYAKYGSLRGFL-RESRKVGPGYLGSGGSRNSSSLDHpderaltmGDLISFAWQISQGMQYLAEMKLVHRDLA 876
Cdd:cd05090   80 QPVCMLFEFMNQGDLHEFLiMRSPHSDVGCSSDEDGTVKSSLDH--------GDFLHIAIQIAAGMEYLSSHFFVHKDLA 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  877 ARNILVAEGRKMKISDFGLSRDVYEEDSYVKRSQGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLGGNPYPGIP 956
Cdd:cd05090  152 ARNILVGEQLHVKISDLGLSREIYSSDYYRVQNKSLLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFGLQPYYGFS 231
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 10862703  957 PERLFNLLKTGHRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADI 1001
Cdd:cd05090  232 NQEVIEMVRKRQLLPCSEDCPPRMYSLMTECWQEIPSRRPRFKDI 276
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
717-1008 6.21e-58

Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Chk is also referred to as megakaryocyte-associated tyrosine kinase (Matk). Chk inhibits Src kinases using a noncatalytic mechanism by simply binding to them. As a negative regulator of Src kinases, Chk may play important roles in cell proliferation, survival, and differentiation, and consequently, in cancer development and progression. Chk is expressed in brain and hematopoietic cells. Like Csk, it is a cytoplasmic (or nonreceptor) tyr kinase containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. To inhibit Src kinases that are anchored to the plasma membrane, Chk is translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. Studies in mice reveal that Chk is not functionally redundant with Csk and that it plays an important role as a regulator of immune responses. Chk also plays a role in neural differentiation in a manner independent of Src by enhancing Mapk activation via Ras-mediated signaling. The Chk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270666 [Multi-domain]  Cd Length: 254  Bit Score: 200.48  E-value: 6.21e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  717 WEFPRKNLVLGKTLGEGEFGKVvkatafhLKGRAGYTTVAVKMLKENASPselRDLLSEFNVLKQVNHPHVIKLYGACSQ 796
Cdd:cd05083    1 WLLNLQKLTLGEIIGEGEFGAV-------LQGEYMGQKVAVKNIKCDVTA---QAFLEETAVMTKLQHKNLVRLLGVILH 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  797 DGpLLLIVEYAKYGSLRGFLRESRKVgpgylgsggsrnsssldhpderALTMGDLISFAWQISQGMQYLAEMKLVHRDLA 876
Cdd:cd05083   71 NG-LYIVMELMSKGNLVNFLRSRGRA----------------------LVPVIQLLQFSLDVAEGMEYLESKKLVHRDLA 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  877 ARNILVAEGRKMKISDFGLSRDVYEEDSyvkrsQGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLGGNPYPGIP 956
Cdd:cd05083  128 ARNILVSEDGVAKISDFGLAKVGSMGVD-----NSRLPVKWTAPEALKNKKFSSKSDVWSYGVLLWEVFSYGRAPYPKMS 202
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 10862703  957 PERLFNLLKTGHRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADISKDLEKM 1008
Cdd:cd05083  203 VKEVKEAVEKGYRMEPPEGCPPDVYSIMTSCWEAEPGKRPSFKKLREKLEKE 254
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
728-1006 1.09e-57

Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily includes a subset of Src-like PTKs including Src, Fyn, Yrk, and Yes, which are all widely expressed. Yrk has been detected only in chickens. It is primarily found in neuronal and epithelial cells and in macrophages. It may play a role in inflammation and in response to injury. Src (or c-Src) proteins are cytoplasmic (or non-receptor) PTKs which are anchored to the plasma membrane. They contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. They were identified as the first proto-oncogene products, and they regulate cell adhesion, invasion, and motility in cancer cells and tumor vasculature, contributing to cancer progression and metastasis. They are also implicated in acute inflammatory responses and osteoclast function. The Src/Fyn-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271105 [Multi-domain]  Cd Length: 248  Bit Score: 199.37  E-value: 1.09e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  728 KTLGEGEFGKVVKATAfhlkgrAGYTTVAVKMLKENASPSElrDLLSEFNVLKQVNHPHVIKLYGACSQDgPLLLIVEYA 807
Cdd:cd14203    1 VKLGQGCFGEVWMGTW------NGTTKVAIKTLKPGTMSPE--AFLEEAQIMKKLRHDKLVQLYAVVSEE-PIYIVTEFM 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  808 KYGSLRGFLREsrkvgpgylgsggsrnsssldhPDERALTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNILVAEGRK 887
Cdd:cd14203   72 SKGSLLDFLKD----------------------GEGKYLKLPQLVDMAAQIASGMAYIERMNYIHRDLRAANILVGDNLV 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  888 MKISDFGLSRdVYEEDSYVKRSQGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLGGNPYPGIPPERLFNLLKTG 967
Cdd:cd14203  130 CKIADFGLAR-LIEDNEYTARQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELVTKGRVPYPGMNNREVLEQVERG 208
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 10862703  968 HRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADISKDLE 1006
Cdd:cd14203  209 YRMPCPPGCPESLHELMCQCWRKDPEERPTFEYLQSFLE 247
PTKc_DDR_like cd05097
Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the ...
718-1005 3.32e-57

Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. DDR-like proteins are members of the DDR subfamily, which are receptor PTKs (RTKs) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDRs results in a slow but sustained receptor activation. DDRs regulate cell adhesion, proliferation, and extracellular matrix remodeling. They have been linked to a variety of human cancers including breast, colon, ovarian, brain, and lung. There is no evidence showing that DDRs act as transforming oncogenes. They are more likely to play a role in the regulation of tumor growth and metastasis. The DDR-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133228 [Multi-domain]  Cd Length: 295  Bit Score: 199.82  E-value: 3.32e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  718 EFPRKNLVLGKTLGEGEFGKVVKATAFHLKGRAGYTT---------VAVKMLKENASPSELRDLLSEFNVLKQVNHPHVI 788
Cdd:cd05097    1 EFPRQQLRLKEKLGEGQFGEVHLCEAEGLAEFLGEGApefdgqpvlVAVKMLRADVTKTARNDFLKEIKIMSRLKNPNII 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  789 KLYGACSQDGPLLLIVEYAKYGSLRGFLREsRKVgpgylgsggsrnSSSLDHPDE-RALTMGDLISFAWQISQGMQYLAE 867
Cdd:cd05097   81 RLLGVCVSDDPLCMITEYMENGDLNQFLSQ-REI------------ESTFTHANNiPSVSIANLLYMAVQIASGMKYLAS 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  868 MKLVHRDLAARNILVAEGRKMKISDFGLSRDVYEEDSYvkRSQGR--IPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIV 945
Cdd:cd05097  148 LNFVHRDLATRNCLVGNHYTIKIADFGMSRNLYSGDYY--RIQGRavLPIRWMAWESILLGKFTTASDVWAFGVTLWEMF 225
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  946 TL-GGNPYPGIPPERLFNllKTGH---------RMERPDNCSEEMYRLMLQCWKQEPDKRPVFADISKDL 1005
Cdd:cd05097  226 TLcKEQPYSLLSDEQVIE--NTGEffrnqgrqiYLSQTPLCPSPVFKLMMRCWSRDIKDRPTFNKIHHFL 293
PTKc_EphR_B cd05065
Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze ...
728-1009 6.65e-57

Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Class EphB receptors bind to transmembrane ephrin-B ligands. There are six vertebrate EphB receptors (EphB1-6), which display promiscuous interactions with three ephrin-B ligands. One exception is EphB2, which also interacts with ephrin A5. EphB receptors play important roles in synapse formation and plasticity, spine morphogenesis, axon guidance, and angiogenesis. In the intestinal epithelium, EphBs are Wnt signaling target genes that control cell compartmentalization. They function as suppressors of colon cancer progression. EphRs comprise the largest subfamily of receptor PTKs (RTKs). They contain an ephrin-binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion. The EphB subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173638 [Multi-domain]  Cd Length: 269  Bit Score: 197.78  E-value: 6.65e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  728 KTLGEGEFGKVVKAtafHLK--GRAGYTtVAVKMLKENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVE 805
Cdd:cd05065   10 EVIGAGEFGEVCRG---RLKlpGKREIF-VAIKTLKSGYTEKQRRDFLSEASIMGQFDHPNIIHLEGVVTKSRPVMIITE 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  806 YAKYGSLRGFLREsrkvgpgylgsggsrnsssldhpDERALTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNILVAEG 885
Cdd:cd05065   86 FMENGALDSFLRQ-----------------------NDGQFTVIQLVGMLRGIAAGMKYLSEMNYVHRDLAARNILVNSN 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  886 RKMKISDFGLSRDVYEEDS---YVKRSQGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLGGNPYPGIPPERLFN 962
Cdd:cd05065  143 LVCKVSDFGLSRFLEDDTSdptYTSSLGGKIPIRWTAPEAIAYRKFTSASDVWSYGIVMWEVMSYGERPYWDMSNQDVIN 222
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 10862703  963 LLKTGHRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADISKDLEKMM 1009
Cdd:cd05065  223 AIEQDYRLPPPMDCPTALHQLMLDCWQKDRNLRPKFGQIVNTLDKMI 269
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
717-1006 8.47e-56

Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Yes (or c-Yes) is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. c-Yes kinase is the cellular homolog of the oncogenic protein (v-Yes) encoded by the Yamaguchi 73 and Esh sarcoma viruses. It displays functional overlap with other Src subfamily members, particularly Src. It also shows some unique functions such as binding to occludins, transmembrane proteins that regulate extracellular interactions in tight junctions. Yes also associates with a number of proteins in different cell types that Src does not interact with, like JAK2 and gp130 in pre-adipocytes, and Pyk2 in treated pulmonary vein endothelial cells. Although the biological function of Yes remains unclear, it appears to have a role in regulating cell-cell interactions and vesicle trafficking in polarized cells. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Yes subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270654 [Multi-domain]  Cd Length: 279  Bit Score: 195.29  E-value: 8.47e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  717 WEFPRKNLVLGKTLGEGEFGKVVKATAfhlkgrAGYTTVAVKMLKENASPSELrdLLSEFNVLKQVNHPHVIKLYGACSQ 796
Cdd:cd05069    7 WEIPRESLRLDVKLGQGCFGEVWMGTW------NGTTKVAIKTLKPGTMMPEA--FLQEAQIMKKLRHDKLVPLYAVVSE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  797 DgPLLLIVEYAKYGSLRGFLRESrkvgpgylgsggsrnsssldhpDERALTMGDLISFAWQISQGMQYLAEMKLVHRDLA 876
Cdd:cd05069   79 E-PIYIVTEFMGKGSLLDFLKEG----------------------DGKYLKLPQLVDMAAQIADGMAYIERMNYIHRDLR 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  877 ARNILVAEGRKMKISDFGLSRdVYEEDSYVKRSQGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLGGNPYPGIP 956
Cdd:cd05069  136 AANILVGDNLVCKIADFGLAR-LIEDNEYTARQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELVTKGRVPYPGMV 214
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 10862703  957 PERLFNLLKTGHRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADISKDLE 1006
Cdd:cd05069  215 NREVLEQVERGYRMPCPQGCPESLHELMKLCWKKDPDERPTFEYIQSFLE 264
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
726-1004 1.04e-55

Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or threonine-specific kinase subfamily.


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 193.90  E-value: 1.04e-55
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703     726 LGKTLGEGEFGKVVKATafHLK-GRagytTVAVKMLKENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIV 804
Cdd:smart00220    3 ILEKLGEGSFGKVYLAR--DKKtGK----LVAIKVIKKKKIKKDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVM 76
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703     805 EYAKYGSLRGFLRESRKvgpgylgsggsrnsssldhpderaLTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNILVAE 884
Cdd:smart00220   77 EYCEGGDLFDLLKKRGR------------------------LSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDE 132
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703     885 GRKMKISDFGLSRdVYEEDSYVKRSQGRIPvkWMAIESLFDHIYTTQSDVWSFGVLLWEIVTlGGNPYPGI-PPERLFNL 963
Cdd:smart00220  133 DGHVKLADFGLAR-QLDPGEKLTTFVGTPE--YMAPEVLLGKGYGKAVDIWSLGVILYELLT-GKPPFPGDdQLLELFKK 208
                           250       260       270       280
                    ....*....|....*....|....*....|....*....|...
gi 10862703     964 LKTGHR--MERPDNCSEEMYRLMLQCWKQEPDKRPVFADISKD 1004
Cdd:smart00220  209 IGKPKPpfPPPEWDISPEAKDLIRKLLVKDPEKRLTAEEALQH 251
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
717-1006 1.63e-55

Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fyn and Yrk are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Fyn, together with Lck, plays a critical role in T-cell signal transduction by phosphorylating ITAM (immunoreceptor tyr activation motif) sequences on T-cell receptors, ultimately leading to the proliferation and differentiation of T-cells. In addition, Fyn is involved in the myelination of neurons, and is implicated in Alzheimer's and Parkinson's diseases. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Fyn/Yrk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase.


Pssm-ID: 270655 [Multi-domain]  Cd Length: 274  Bit Score: 194.13  E-value: 1.63e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  717 WEFPRKNLVLGKTLGEGEFGKVVKATAfhlkgrAGYTTVAVKMLKENASPSElrDLLSEFNVLKQVNHPHVIKLYGACSQ 796
Cdd:cd05070    4 WEIPRESLQLIKRLGNGQFGEVWMGTW------NGNTKVAIKTLKPGTMSPE--SFLEEAQIMKKLKHDKLVQLYAVVSE 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  797 DgPLLLIVEYAKYGSLRGFLREsrkvGPGylgsggsrnsssldhpdeRALTMGDLISFAWQISQGMQYLAEMKLVHRDLA 876
Cdd:cd05070   76 E-PIYIVTEYMSKGSLLDFLKD----GEG------------------RALKLPNLVDMAAQVAAGMAYIERMNYIHRDLR 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  877 ARNILVAEGRKMKISDFGLSRdVYEEDSYVKRSQGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLGGNPYPGIP 956
Cdd:cd05070  133 SANILVGNGLICKIADFGLAR-LIEDNEYTARQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELVTKGRVPYPGMN 211
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 10862703  957 PERLFNLLKTGHRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADISKDLE 1006
Cdd:cd05070  212 NREVLEQVERGYRMPCPQDCPISLHELMIHCWKKDPEERPTFEYLQGFLE 261
PTKc_HER4 cd05110
Catalytic domain of the Protein Tyrosine Kinase, HER4; PTKs catalyze the transfer of the ...
728-1037 2.92e-55

Catalytic domain of the Protein Tyrosine Kinase, HER4; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. HER4 (ErbB4) is a member of the EGFR (HER, ErbB) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. Ligands that bind HER4 fall into two groups, the neuregulins (or heregulins) and some EGFR (HER1) ligands including betacellulin, HBEGF, and epiregulin. All four neuregulins (NRG1-4) interact with HER4. Upon ligand binding, HER4 forms homo- or heterodimers with other HER proteins. HER4 is essential in embryonic development. It is implicated in mammary gland, cardiac, and neural development. As a postsynaptic receptor of NRG1, HER4 plays an important role in synaptic plasticity and maturation. The impairment of NRG1/HER4 signaling may contribute to schizophrenia. The HER4 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173655 [Multi-domain]  Cd Length: 303  Bit Score: 194.51  E-value: 2.92e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  728 KTLGEGEFGKVVKATaFHLKGRAGYTTVAVKMLKENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDgPLLLIVEYA 807
Cdd:cd05110   13 KVLGSGAFGTVYKGI-WVPEGETVKIPVAIKILNETTGPKANVEFMDEALIMASMDHPHLVRLLGVCLSP-TIQLVTQLM 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  808 KYGSLRGFLREsrkvgpgylgsggsrnsssldHPDERALTMgdLISFAWQISQGMQYLAEMKLVHRDLAARNILVAEGRK 887
Cdd:cd05110   91 PHGCLLDYVHE---------------------HKDNIGSQL--LLNWCVQIAKGMMYLEERRLVHRDLAARNVLVKSPNH 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  888 MKISDFGLSRDVYEEDSYVKRSQGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLGGNPYPGIPPERLFNLLKTG 967
Cdd:cd05110  148 VKITDFGLARLLEGDEKEYNADGGKMPIKWMALECIHYRKFTHQSDVWSYGVTIWELMTFGGKPYDGIPTREIPDLLEKG 227
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 10862703  968 HRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADISKDLEKMMVKRRDYLDLAAS------TPSDSLIYDDGLSEEE 1037
Cdd:cd05110  228 ERLPQPPICTIDVYMVMVKCWMIDADSRPKFKELAAEFSRMARDPQRYLVIQGDdrmklpSPNDSKFFQNLLDEED 303
PTKc_EphR_A cd05066
Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze ...
728-1009 4.38e-55

Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of most class EphA receptors including EphA3, EphA4, EphA5, and EphA7, but excluding EphA1, EphA2 and EphA10. Class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. One exception is EphA4, which also binds ephrins-B2/B3. EphA receptors and ephrin-A ligands are expressed in multiple areas of the developing brain, especially in the retina and tectum. They are part of a system controlling retinotectal mapping. EphRs comprise the largest subfamily of receptor PTKs (RTKs). EphRs contain an ephrin-binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion, making it important in neural development and plasticity, cell morphogenesis, cell-fate determination, embryonic development, tissue patterning, and angiogenesis. The EphA subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270651 [Multi-domain]  Cd Length: 267  Bit Score: 192.77  E-value: 4.38e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  728 KTLGEGEFGKVVKATaFHLKGRAGYTtVAVKMLKENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVEYA 807
Cdd:cd05066   10 KVIGAGEFGEVCSGR-LKLPGKREIP-VAIKTLKAGYTEKQRRDFLSEASIMGQFDHPNIIHLEGVVTRSKPVMIVTEYM 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  808 KYGSLRGFLREsrkvgpgylgsggsrnsssldhpDERALTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNILVAEGRK 887
Cdd:cd05066   88 ENGSLDAFLRK-----------------------HDGQFTVIQLVGMLRGIASGMKYLSDMGYVHRDLAARNILVNSNLV 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  888 MKISDFGLSRdVYEED---SYVKRSqGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLGGNPYPGIPPERLFNLL 964
Cdd:cd05066  145 CKVSDFGLSR-VLEDDpeaAYTTRG-GKIPIRWTAPEAIAYRKFTSASDVWSYGIVMWEVMSYGERPYWEMSNQDVIKAI 222
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 10862703  965 KTGHRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADISKDLEKMM 1009
Cdd:cd05066  223 EEGYRLPAPMDCPAALHQLMLDCWQKDRNERPKFEQIVSILDKLI 267
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
721-998 1.02e-54

Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow kinase on the X chromosome; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Btk and Bmx (also named Etk) are members of the Tec-like subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, Btk contains the Tec homology (TH) domain with proline-rich and zinc-binding regions. Btk is expressed in B-cells, and a variety of myeloid cells including mast cells, platelets, neutrophils, and dendrictic cells. It interacts with a variety of partners, from cytosolic proteins to nuclear transcription factors, suggesting a diversity of functions. Stimulation of a diverse array of cell surface receptors, including antigen engagement of the B-cell receptor, leads to PH-mediated membrane translocation of Btk and subsequent phosphorylation by Src kinase and activation. Btk plays an important role in the life cycle of B-cells including their development, differentiation, proliferation, survival, and apoptosis. Mutations in Btk cause the primary immunodeficiency disease, X-linked agammaglobulinaemia (XLA) in humans. Bmx is primarily expressed in bone marrow and the arterial endothelium, and plays an important role in ischemia-induced angiogenesis. It facilitates arterial growth, capillary formation, vessel maturation, and bone marrow-derived endothelial progenitor cell mobilization. The Btk/Bmx subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173657 [Multi-domain]  Cd Length: 256  Bit Score: 191.25  E-value: 1.02e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  721 RKNLVLGKTLGEGEFGkVVKatafHLKGRAGYTtVAVKMLKEnASPSElRDLLSEFNVLKQVNHPHVIKLYGACSQDGPL 800
Cdd:cd05113    3 PKDLTFLKELGTGQFG-VVK----YGKWRGQYD-VAIKMIKE-GSMSE-DEFIEEAKVMMNLSHEKLVQLYGVCTKQRPI 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  801 LLIVEYAKYGSLRGFLRESRKvgpgylgsggsrnsssldhpderALTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNI 880
Cdd:cd05113   75 FIITEYMANGCLLNYLREMRK-----------------------RFQTQQLLEMCKDVCEAMEYLESKQFLHRDLAARNC 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  881 LVAEGRKMKISDFGLSRDVYEeDSYVKRSQGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLGGNPYPGIPPERL 960
Cdd:cd05113  132 LVNDQGVVKVSDFGLSRYVLD-DEYTSSVGSKFPVRWSPPEVLMYSKFSSKSDVWAFGVLMWEVYSLGKMPYERFTNSET 210
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 10862703  961 FNLLKTGHRMERPDNCSEEMYRLMLQCWKQEPDKRPVF 998
Cdd:cd05113  211 VEHVSQGLRLYRPHLASEKVYTIMYSCWHEKADERPTF 248
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
724-999 2.34e-54

Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Itk, also known as Tsk or Emt, is a member of the Tec-like subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, Itk contains the Tec homology (TH) domain containing one proline-rich region and a zinc-binding region. Itk is expressed in T-cells and mast cells, and is important in their development and differentiation. Of the three Tec kinases expressed in T-cells, Itk plays the predominant role in T-cell receptor (TCR) signaling. It is activated by phosphorylation upon TCR crosslinking and is involved in the pathway resulting in phospholipase C-gamma1 activation and actin polymerization. It also plays a role in the downstream signaling of the T-cell costimulatory receptor CD28, the T-cell surface receptor CD2, and the chemokine receptor CXCR4. In addition, Itk is crucial for the development of T-helper(Th)2 effector responses. The Itk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133243 [Multi-domain]  Cd Length: 256  Bit Score: 190.16  E-value: 2.34e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  724 LVLGKTLGEGEFGKVvkatafHLKGRAGYTTVAVKMLKENASPSElrDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLI 803
Cdd:cd05112    6 LTFVQEIGSGQFGLV------HLGYWLNKDKVAIKTIREGAMSEE--DFIEEAEVMMKLSHPKLVQLYGVCLEQAPICLV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  804 VEYAKYGSLRGFLRESRKvgpgylgsggsrnsssldhpderALTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNILVA 883
Cdd:cd05112   78 FEFMEHGCLSDYLRTQRG-----------------------LFSAETLLGMCLDVCEGMAYLEEASVIHRDLAARNCLVG 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  884 EGRKMKISDFGLSRDVYeEDSYVKRSQGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLGGNPYPGIPPERLFNL 963
Cdd:cd05112  135 ENQVVKVSDFGMTRFVL-DDQYTSSTGTKFPVKWSSPEVFSFSRYSSKSDVWSFGVLMWEVFSEGKIPYENRSNSEVVED 213
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 10862703  964 LKTGHRMERPDNCSEEMYRLMLQCWKQEPDKRPVFA 999
Cdd:cd05112  214 INAGFRLYKPRLASTHVYEIMNHCWKERPEDRPSFS 249
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
730-1005 3.02e-54

Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. PKs make up a large family of serine/threonine kinases (STKs), protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins. Majority of protein phosphorylation occurs on serine residues while only 1% occurs on tyrosine residues. Protein phosphorylation is a mechanism by which a wide variety of cellular proteins, such as enzymes and membrane channels, are reversibly regulated in response to certain stimuli. PKs often function as components of signal transduction pathways in which one kinase activates a second kinase, which in turn, may act on other kinases; this sequential action transmits a signal from the cell surface to target proteins, which results in cellular responses. The PK family is one of the largest known protein families with more than 100 homologous yeast enzymes and more than 500 human proteins. A fraction of PK family members are pseudokinases that lack crucial residues for catalytic activity. The mutiplicity of kinases allows for specific regulation according to substrate, tissue distribution, and cellular localization. PKs regulate many cellular processes including proliferation, division, differentiation, motility, survival, metabolism, cell-cycle progression, cytoskeletal rearrangement, immunity, and neuronal functions. Many kinases are implicated in the development of various human diseases including different types of cancer. The PK family is part of a larger superfamily that includes the catalytic domains of RIO kinases, aminoglycoside phosphotransferase, choline kinase, phosphoinositide 3-kinase (PI3K), and actin-fragmin kinase.


Pssm-ID: 270622 [Multi-domain]  Cd Length: 215  Bit Score: 188.25  E-value: 3.02e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  730 LGEGEFGKVVKATAFHLKGRagyttVAVKMLKENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVEYAKY 809
Cdd:cd00180    1 LGKGSFGKVYKARDKETGKK-----VAVKVIPKEKLKKLLEELLREIEILKKLNHPNIVKLYDVFETENFLYLVMEYCEG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  810 GSLRGFLRESRKVgpgylgsggsrnsssldhpderaLTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNILVAEGRKMK 889
Cdd:cd00180   76 GSLKDLLKENKGP-----------------------LSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDSDGTVK 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  890 ISDFGLSRDVYEEDSYVKRSQGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIvtlggnpypgipperlfnllktghr 969
Cdd:cd00180  133 LADFGLAKDLDSDDSLLKTTGGTTPPYYAPPELLGGRYYGPKVDIWSLGVILYEL------------------------- 187
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 10862703  970 merpdncsEEMYRLMLQCWKQEPDKRPVFADISKDL 1005
Cdd:cd00180  188 --------EELKDLIRRMLQYDPKKRPSAKELLEHL 215
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
719-1008 6.72e-54

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jak2 is widely expressed in many tissues and is essential for the signaling of hormone-like cytokines such as growth hormone, erythropoietin, thrombopoietin, and prolactin, as well as some IFNs and cytokines that signal through the IL-3 and gp130 receptors. Disruption of Jak2 in mice results in an embryonic lethal phenotype with multiple defects including erythropoietic and cardiac abnormalities. It is the only Jak gene that results in a lethal phenotype when disrupted in mice. A mutation in the pseudokinase domain of Jak2, V617F, is present in many myeloproliferative diseases, including almost all patients with polycythemia vera, and 50% of patients with essential thrombocytosis and myelofibrosis. Jak2 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal catalytic tyr kinase domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271107 [Multi-domain]  Cd Length: 284  Bit Score: 189.84  E-value: 6.72e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  719 FPRKNLVLGKTLGEGEFGKVVKATAFHLKGRAGyTTVAVKMLkENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDG 798
Cdd:cd14205    1 FEERHLKFLQQLGKGNFGSVEMCRYDPLQDNTG-EVVAVKKL-QHSTEEHLRDFEREIEILKSLQHDNIVKYKGVCYSAG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  799 --PLLLIVEYAKYGSLRGFLRESRKvgpgylgsggsrnssSLDHPDeraltmgdLISFAWQISQGMQYLAEMKLVHRDLA 876
Cdd:cd14205   79 rrNLRLIMEYLPYGSLRDYLQKHKE---------------RIDHIK--------LLQYTSQICKGMEYLGTKRYIHRDLA 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  877 ARNILVAEGRKMKISDFGLSRDVYEEDSYVK-RSQGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVT--------- 946
Cdd:cd14205  136 TRNILVENENRVKIGDFGLTKVLPQDKEYYKvKEPGESPIFWYAPESLTESKFSVASDVWSFGVVLYELFTyiekskspp 215
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 10862703  947 ------LGGNPYPGIPPERLFNLLKTGHRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADISKDLEKM 1008
Cdd:cd14205  216 aefmrmIGNDKQGQMIVFHLIELLKNNGRLPRPDGCPDEIYMIMTECWNNNVNQRPSFRDLALRVDQI 283
PTKc_Zap-70 cd05115
Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs ...
721-1001 7.21e-54

Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Zap-70 is a cytoplasmic (or nonreceptor) PTK containing two Src homology 2 (SH2) domains N-terminal to the catalytic tyr kinase domain. Zap-70 is primarily expressed in T-cells and NK cells, and is a crucial component in T-cell receptor (TCR) signaling. Zap-70 binds the phosphorylated ITAM (immunoreceptor tyr activation motif) sequences of the activated TCR zeta-chain through its SH2 domains, leading to its phosphorylation and activation. It then phosphorylates target proteins, which propagate the signals to downstream pathways. Zap-70 is hardly detected in normal peripheral B-cells, but is present in some B-cell malignancies. It is used as a diagnostic marker for chronic lymphocytic leukemia (CLL) as it is associated with the more aggressive subtype of the disease. The Zap-70 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270686 [Multi-domain]  Cd Length: 269  Bit Score: 189.39  E-value: 7.21e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  721 RKNLVLGKT-LGEGEFGKVVKATafhLKGRAGYTTVAVKMLKENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGp 799
Cdd:cd05115    2 RDNLLIDEVeLGSGNFGCVKKGV---YKMRKKQIDVAIKVLKQGNEKAVRDEMMREAQIMHQLDNPYIVRMIGVCEAEA- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  800 LLLIVEYAKYGSLRGFLRESRkvgpgylgsggsrnsssldhpDEraLTMGDLISFAWQISQGMQYLAEMKLVHRDLAARN 879
Cdd:cd05115   78 LMLVMEMASGGPLNKFLSGKK---------------------DE--ITVSNVVELMHQVSMGMKYLEEKNFVHRDLAARN 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  880 ILVAEGRKMKISDFGLSRDVYEEDSYVK-RSQGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLGGNPYPGIPPE 958
Cdd:cd05115  135 VLLVNQHYAKISDFGLSKALGADDSYYKaRSAGKWPLKWYAPECINFRKFSSRSDVWSYGVTMWEAFSYGQKPYKKMKGP 214
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 10862703  959 RLFNLLKTGHRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADI 1001
Cdd:cd05115  215 EVMSFIEQGKRMDCPAECPPEMYALMSDCWIYKWEDRPNFLTV 257
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
717-1006 9.09e-53

Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Src (or c-Src) is a cytoplasmic (or non-receptor) PTK, containing an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region with a conserved tyr. It is activated by autophosphorylation at the tyr kinase domain, and is negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). c-Src is the vertebrate homolog of the oncogenic protein (v-Src) from Rous sarcoma virus. Together with other Src subfamily proteins, it is involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. Src also play a role in regulating cell adhesion, invasion, and motility in cancer cells and tumor vasculature, contributing to cancer progression and metastasis. Elevated levels of Src kinase activity have been reported in a variety of human cancers. Several inhibitors of Src have been developed as anti-cancer drugs. Src is also implicated in acute inflammatory responses and osteoclast function. The Src subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270656 [Multi-domain]  Cd Length: 277  Bit Score: 186.43  E-value: 9.09e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  717 WEFPRKNLVLGKTLGEGEFGKVVKATAfhlkgrAGYTTVAVKMLKENASPSELrdLLSEFNVLKQVNHPHVIKLYGACSQ 796
Cdd:cd05071    4 WEIPRESLRLEVKLGQGCFGEVWMGTW------NGTTRVAIKTLKPGTMSPEA--FLQEAQVMKKLRHEKLVQLYAVVSE 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  797 DgPLLLIVEYAKYGSLRGFLRESRKvgpgylgsggsrnsssldhpdeRALTMGDLISFAWQISQGMQYLAEMKLVHRDLA 876
Cdd:cd05071   76 E-PIYIVTEYMSKGSLLDFLKGEMG----------------------KYLRLPQLVDMAAQIASGMAYVERMNYVHRDLR 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  877 ARNILVAEGRKMKISDFGLSRdVYEEDSYVKRSQGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLGGNPYPGIP 956
Cdd:cd05071  133 AANILVGENLVCKVADFGLAR-LIEDNEYTARQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELTTKGRVPYPGMV 211
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 10862703  957 PERLFNLLKTGHRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADISKDLE 1006
Cdd:cd05071  212 NREVLDQVERGYRMPCPPECPESLHDLMCQCWRKEPEERPTFEYLQAFLE 261
PTKc_Ror2 cd05091
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
730-1005 2.05e-51

Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Ror2 plays important roles in skeletal and heart formation. Ror2-deficient mice show widespread bone abnormalities, ventricular defects in the heart, and respiratory dysfunction. Mutations in human Ror2 result in two different bone development genetic disorders, recessive Robinow syndrome and brachydactyly type B. Ror2 is also implicated in neural development. Ror proteins are orphan receptor PTKs (RTKs) containing an extracellular region with immunoglobulin-like, cysteine-rich, and kringle domains, a transmembrane segment, and an intracellular catalytic domain. Ror RTKs are unrelated to the nuclear receptor subfamily called retinoid-related orphan receptors (RORs). RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. The Ror2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270673 [Multi-domain]  Cd Length: 284  Bit Score: 182.91  E-value: 2.05e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  730 LGEGEFGKVVKAtafHLKGRA-GYTT--VAVKMLKENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVEY 806
Cdd:cd05091   14 LGEDRFGKVYKG---HLFGTApGEQTqaVAIKTLKDKAEGPLREEFRHEAMLRSRLQHPNIVCLLGVVTKEQPMSMIFSY 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  807 AKYGSLRGFL---RESRKVGpgylgsggsrnSSSLDHPDERALTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNILVA 883
Cdd:cd05091   91 CSHGDLHEFLvmrSPHSDVG-----------STDDDKTVKSTLEPADFLHIVTQIAAGMEYLSSHHVVHKDLATRNVLVF 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  884 EGRKMKISDFGLSRDVYEEDSYVKRSQGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLGGNPYPGIPPERLFNL 963
Cdd:cd05091  160 DKLNVKISDLGLFREVYAADYYKLMGNSLLPIRWMSPEAIMYGKFSIDSDIWSYGVVLWEVFSYGLQPYCGYSNQDVIEM 239
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 10862703  964 LKTGHRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADISKDL 1005
Cdd:cd05091  240 IRNRQVLPCPDDCPAWVYTLMLECWNEFPSRRPRFKDIHSRL 281
PTKc_EphR_A10 cd05064
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A10; PTKs catalyze the ...
718-1009 3.30e-51

Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A10; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EphA10, which contains an inactive tyr kinase domain, may function to attenuate signals of co-clustered active receptors. EphA10 is mainly expressed in the testis. Ephrin/EphR interaction results in cell-cell repulsion or adhesion, making it important in neural development and plasticity, cell morphogenesis, cell-fate determination, embryonic development, tissue patterning, and angiogenesis. EphRs comprise the largest subfamily of receptor tyr kinases (RTKs). In general, class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. EphRs contain an ephrin binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). The EphA10 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133195 [Multi-domain]  Cd Length: 266  Bit Score: 181.66  E-value: 3.30e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  718 EFPRKNLVLGKTLGEGEFGKVVKAtAFHLKGRAGYTtVAVKMLKENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQD 797
Cdd:cd05064    1 ELDNKSIKIERILGTGRFGELCRG-CLKLPSKRELP-VAIHTLRAGCSDKQRRGFLAEALTLGQFDHSNIVRLEGVITRG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  798 GPLLLIVEYAKYGSLRGFLRESrkvgpgylgsggsrnsssldhpdERALTMGDLISFAWQISQGMQYLAEMKLVHRDLAA 877
Cdd:cd05064   79 NTMMIVTEYMSNGALDSFLRKH-----------------------EGQLVAGQLMGMLPGLASGMKYLSEMGYVHKGLAA 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  878 RNILVAEGRKMKISDFG-LSRDVYEedSYVKRSQGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLGGNPYPGIP 956
Cdd:cd05064  136 HKVLVNSDLVCKISGFRrLQEDKSE--AIYTTMSGKSPVLWAAPEAIQYHHFSSASDVWSFGIVMWEVMSYGERPYWDMS 213
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 10862703  957 PERLFNLLKTGHRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADISKDLEKMM 1009
Cdd:cd05064  214 GQDVIKAVEDGFRLPAPRNCPNLLHQLMLDCWQKERGERPRFSQIHSILSKMV 266
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
719-1008 3.42e-51

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jak3 is expressed only in hematopoietic cells. It binds the shared receptor subunit common gamma chain and thus, is essential in the signaling of cytokines that use it such as IL-2, IL-4, IL-7, IL-9, IL-15, and IL-21. Jak3 is important in lymphoid development and myeloid cell differentiation. Inactivating mutations in Jak3 have been reported in humans with severe combined immunodeficiency (SCID). Jak3 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal catalytic tyr kinase domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270665 [Multi-domain]  Cd Length: 283  Bit Score: 182.02  E-value: 3.42e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  719 FPRKNLVLGKTLGEGEFGKVVKATAFHLKGRAGyTTVAVKMLKENaSPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDG 798
Cdd:cd05081    1 FEERHLKYISQLGKGNFGSVELCRYDPLGDNTG-ALVAVKQLQHS-GPDQQRDFQREIQILKALHSDFIVKYRGVSYGPG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  799 --PLLLIVEYAKYGSLRGFLRESRKVgpgylgsggsrnsssLDHpderaltmGDLISFAWQISQGMQYLAEMKLVHRDLA 876
Cdd:cd05081   79 rrSLRLVMEYLPSGCLRDFLQRHRAR---------------LDA--------SRLLLYSSQICKGMEYLGSRRCVHRDLA 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  877 ARNILVAEGRKMKISDFGLSRDV-YEEDSYVKRSQGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLGGNPYPgi 955
Cdd:cd05081  136 ARNILVESEAHVKIADFGLAKLLpLDKDYYVVREPGQSPIFWYAPESLSDNIFSRQSDVWSFGVVLYELFTYCDKSCS-- 213
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 10862703  956 PPE----------------RLFNLLKTGHRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADISKDLEKM 1008
Cdd:cd05081  214 PSAeflrmmgcerdvpalcRLLELLEEGQRLPAPPACPAEVHELMKLCWAPSPQDRPSFSALGPQLDML 282
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
719-1008 3.93e-51

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tyk2 is widely expressed in many tissues. It is involved in signaling via the cytokine receptors IFN-alphabeta, IL-6, IL-10, IL-12, IL-13, and IL-23. It mediates cell surface urokinase receptor (uPAR) signaling and plays a role in modulating vascular smooth muscle cell (VSMC) functional behavior in response to injury. Tyk2 is also important in dendritic cell function and T helper (Th)1 cell differentiation. A homozygous mutation of Tyk2 was found in a patient with hyper-IgE syndrome (HIES), a primary immunodeficiency characterized by recurrent skin abscesses, pneumonia, and elevated serum IgE. This suggests that Tyk2 may play important roles in multiple cytokine signaling involved in innate and adaptive immunity. Tyk2 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase catalytic domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The Tyk2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270664 [Multi-domain]  Cd Length: 283  Bit Score: 182.02  E-value: 3.93e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  719 FPRKNLVLGKTLGEGEFGKVVKATAFHLKGRAGyTTVAVKMLKENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDG 798
Cdd:cd05080    1 FHKRYLKKIRDLGEGHFGKVSLYCYDPTNDGTG-EMVAVKALKADCGPQHRSGWKQEIDILKTLYHENIVKYKGCCSEQG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  799 P--LLLIVEYAKYGSLRGFLRESRkvgpgylgsggsrnsssldhpderaLTMGDLISFAWQISQGMQYLAEMKLVHRDLA 876
Cdd:cd05080   80 GksLQLIMEYVPLGSLRDYLPKHS-------------------------IGLAQLLLFAQQICEGMAYLHSQHYIHRDLA 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  877 ARNILVAEGRKMKISDFGLSRDVYEEDSYVK-RSQGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTlGGNPYPGI 955
Cdd:cd05080  135 ARNVLLDNDRLVKIGDFGLAKAVPEGHEYYRvREDGDSPVFWYAPECLKEYKFYYASDVWSFGVTLYELLT-HCDSSQSP 213
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 10862703  956 PPE---------------RLFNLLKTGHRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADISKDLEKM 1008
Cdd:cd05080  214 PTKflemigiaqgqmtvvRLIELLERGERLPCPDKCPQEVYHLMKNCWETEASFRPTFENLIPILKTV 281
PTK_HER3 cd05111
Pseudokinase domain of the Protein Tyrosine Kinase, HER3; HER3 (ErbB3) is a member of the EGFR ...
719-1016 2.38e-50

Pseudokinase domain of the Protein Tyrosine Kinase, HER3; HER3 (ErbB3) is a member of the EGFR (HER, ErbB) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. HER3 contains an impaired tyr kinase domain, which lacks crucial residues for catalytic activity against exogenous substrates but is still able to bind ATP and autophosphorylate. HER3 binds the neuregulin ligands, NRG1 and NRG2, and it relies on its heterodimerization partners for activity following ligand binding. The HER2-HER3 heterodimer constitutes a high affinity co-receptor capable of potent mitogenic signaling. HER3 participates in a signaling pathway involved in the proliferation, survival, adhesion, and motility of tumor cells. The HER3 subfamily is part of a larger superfamily that includes other pseudokinases and the the catalytic domains of active kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173656 [Multi-domain]  Cd Length: 279  Bit Score: 179.38  E-value: 2.38e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  719 FPRKNLVLGKTLGEGEFGKVVKATAFHlKGRAGYTTVAVKMLKENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSqdG 798
Cdd:cd05111    4 FKETELRKLKVLGSGVFGTVHKGIWIP-EGDSIKIPVAIKVIQDRSGRQSFQAVTDHMLAIGSLDHAYIVRLLGICP--G 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  799 P-LLLIVEYAKYGSLRGFLRESRKvgpgylgsggsrnsssldhpderALTMGDLISFAWQISQGMQYLAEMKLVHRDLAA 877
Cdd:cd05111   81 AsLQLVTQLLPLGSLLDHVRQHRG-----------------------SLGPQLLLNWCVQIAKGMYYLEEHRMVHRNLAA 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  878 RNILVAEGRKMKISDFGLSRDVYEEDSYVKRSQGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLGGNPYPGIPP 957
Cdd:cd05111  138 RNVLLKSPSQVQVADFGVADLLYPDDKKYFYSEAKTPIKWMALESIHFGKYTHQSDVWSYGVTVWEMMTFGAEPYAGMRL 217
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 10862703  958 ERLFNLLKTGHRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADISKDLEKMMVKRRDYL 1016
Cdd:cd05111  218 AEVPDLLEKGERLAQPQICTIDVYMVMVKCWMIDENIRPTFKELANEFTRMARDPPRYL 276
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
724-1009 3.62e-50

Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular carcinoma and Resting lymphocyte kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tec and Rlk (also named Txk) are members of the Tec-like subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. Instead of PH, Rlk contains an N-terminal cysteine-rich region. In addition to PH, Tec also contains the Tec homology (TH) domain with proline-rich and zinc-binding regions. Tec kinases are expressed mainly by haematopoietic cells. Tec is more widely-expressed than other Tec-like subfamily kinases. It is found in endothelial cells, both B- and T-cells, and a variety of myeloid cells including mast cells, erythroid cells, platelets, macrophages and neutrophils. Rlk is expressed in T-cells and mast cell lines. Tec and Rlk are both key components of T-cell receptor (TCR) signaling. They are important in TCR-stimulated proliferation, IL-2 production and phopholipase C-gamma1 activation. The Tec/Rlk subfamily is part of a larger superfamily, that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270685 [Multi-domain]  Cd Length: 260  Bit Score: 178.13  E-value: 3.62e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  724 LVLGKTLGEGEFGKVvkatafHL-KGRAGYTtVAVKMLKENASPSElrDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLL 802
Cdd:cd05114    6 LTFMKELGSGLFGVV------RLgKWRAQYK-VAIKAIREGAMSEE--DFIEEAKVMMKLTHPKLVQLYGVCTQQKPIYI 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  803 IVEYAKYGSLRGFLRESRKVgpgylgsggsrnsssldhpderaLTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNILV 882
Cdd:cd05114   77 VTEFMENGCLLNYLRQRRGK-----------------------LSRDMLLSMCQDVCEGMEYLERNNFIHRDLAARNCLV 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  883 AEGRKMKISDFGLSRDVYEeDSYVKRSQGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLGGNPYPGIPPERLFN 962
Cdd:cd05114  134 NDTGVVKVSDFGMTRYVLD-DQYTSSSGAKFPVKWSPPEVFNYSKFSSKSDVWSFGVLMWEVFTEGKMPFESKSNYEVVE 212
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 10862703  963 LLKTGHRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADISKDLEKMM 1009
Cdd:cd05114  213 MVSRGHRLYRPKLASKSVYEVMYSCWHEKPEGRPTFADLLRTITEIA 259
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
719-1009 2.22e-49

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jak1 is widely expressed in many tissues. Many cytokines are dependent on Jak1 for signaling, including those that use the shared receptor subunits common gamma chain (IL-2, IL-4, IL-7, IL-9, IL-15, IL-21) and gp130 (IL-6, IL-11, oncostatin M, G-CSF, and IFNs, among others). The many varied interactions of Jak1 and its ubiquitous expression suggest many biological roles. Jak1 is important in neurological development, as well as in lymphoid development and function. It also plays a role in the pathophysiology of cardiac hypertrophy and heart failure. A mutation in the ATP-binding site of Jak1 was identified in a human uterine leiomyosarcoma cell line, resulting in defective cytokine induction and antigen presentation, thus allowing the tumor to evade the immune system. Jak1 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The Jak1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173644 [Multi-domain]  Cd Length: 284  Bit Score: 177.04  E-value: 2.22e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  719 FPRKNLVLGKTLGEGEFGKVvKATAFHLKGRAGYTTVAVKMLKENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDG 798
Cdd:cd05079    1 FEKRFLKRIRDLGEGHFGKV-ELCRYDPEGDNTGEQVAVKSLKPESGGNHIADLKKEIEILRNLYHENIVKYKGICTEDG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  799 --PLLLIVEYAKYGSLRGFLRESRKvgpgylgsggsrnsssldhpderALTMGDLISFAWQISQGMQYLAEMKLVHRDLA 876
Cdd:cd05079   80 gnGIKLIMEFLPSGSLKEYLPRNKN-----------------------KINLKQQLKYAVQICKGMDYLGSRQYVHRDLA 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  877 ARNILVAEGRKMKISDFGLSRDVY-EEDSYVKRSQGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVT--------- 946
Cdd:cd05079  137 ARNVLVESEHQVKIGDFGLTKAIEtDKEYYTVKDDLDSPVFWYAPECLIQSKFYIASDVWSFGVTLYELLTycdsesspm 216
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 10862703  947 -----LGGNPYPGIPPERLFNLLKTGHRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADISKDLEKMM 1009
Cdd:cd05079  217 tlflkMIGPTHGQMTVTRLVRVLEEGKRLPRPPNCPEEVYQLMRKCWEFQPSKRTTFQNLIEGFEAIL 284
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
730-1009 1.11e-45

Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated Kinase-1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAK1 is also known as mitogen-activated protein kinase kinase kinase 7 (MAPKKK7 or MAP3K7), TAK, or MEKK7. As a MAPKKK, it is an important mediator of cellular responses to extracellular signals. It regulates both the c-Jun N-terminal kinase and p38 MAPK cascades by activating the MAPK kinases, MKK4 and MKK3/6. In addition, TAK1 plays diverse roles in immunity and development, in different biological contexts, through many signaling pathways including TGFbeta/BMP, Wnt/Fz, and NF-kB. It is also implicated in the activation of the tumor suppressor kinase, LKB1. The TAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270960 [Multi-domain]  Cd Length: 253  Bit Score: 165.30  E-value: 1.11e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  730 LGEGEFGKVVKATafhLKGRagytTVAVKMLKenaSPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVEYAKY 809
Cdd:cd14058    1 VGRGSFGVVCKAR---WRNQ----IVAVKIIE---SESEKKAFEVEVRQLSRVDHPNIIKLYGACSNQKPVCLVMEYAEG 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  810 GSLRGFLrESRKVGPGYlgsggsrnsssldhpderalTMGDLISFAWQISQGMQYLAEMK---LVHRDLAARNIL-VAEG 885
Cdd:cd14058   71 GSLYNVL-HGKEPKPIY--------------------TAAHAMSWALQCAKGVAYLHSMKpkaLIHRDLKPPNLLlTNGG 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  886 RKMKISDFGLSRDVYeedSYVKRSQGRIPvkWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLgGNPYPGIPPERlFNLLK 965
Cdd:cd14058  130 TVLKICDFGTACDIS---THMTNNKGSAA--WMAPEVFEGSKYSEKCDVFSWGIILWEVITR-RKPFDHIGGPA-FRIMW 202
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 10862703  966 TGHRMERPD---NCSEEMYRLMLQCWKQEPDKRPVFADISKDLEKMM 1009
Cdd:cd14058  203 AVHNGERPPlikNCPKPIESLMTRCWSKDPEKRPSMKEIVKIMSHLM 249
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
730-1008 1.19e-41

Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLKs act as mitogen-activated protein kinase kinase kinases (MAP3Ks, MKKKs, MAPKKKs), which phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Mammals have four MLKs (MLK1-4), mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. The MLK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270963 [Multi-domain]  Cd Length: 258  Bit Score: 153.70  E-value: 1.19e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  730 LGEGEFGKVVKATafhLKGRagytTVAVKMLK----ENASPSeLRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVE 805
Cdd:cd14061    2 IGVGGFGKVYRGI---WRGE----EVAVKAARqdpdEDISVT-LENVRQEARLFWMLRHPNIIALRGVCLQPPNLCLVME 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  806 YAKYGSLRGFLrESRKVGPGYLgsggsrnsssldhpderaltmgdlISFAWQISQGMQYL---AEMKLVHRDLAARNILV 882
Cdd:cd14061   74 YARGGALNRVL-AGRKIPPHVL------------------------VDWAIQIARGMNYLhneAPVPIIHRDLKSSNILI 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  883 AEG--------RKMKISDFGLSRDVYEEdsyVKRSQGRIpVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTlGGNPYPG 954
Cdd:cd14061  129 LEAienedlenKTLKITDFGLAREWHKT---TRMSAAGT-YAWMAPEVIKSSTFSKASDVWSYGVLLWELLT-GEVPYKG 203
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 10862703  955 IPPERL-----FNLLKtghrMERPDNCSEEMYRLMLQCWKQEPDKRPVFADISKDLEKM 1008
Cdd:cd14061  204 IDGLAVaygvaVNKLT----LPIPSTCPEPFAQLMKDCWQPDPHDRPSFADILKQLENI 258
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
725-996 2.15e-40

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPKKKs (MKKKs or MAP3Ks) are also called MAP/ERK kinase kinases (MEKKs) in some cases. They phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. This subfamily is composed of the Apoptosis Signal-regulating Kinases ASK1 (or MAPKKK5) and ASK2 (or MAPKKK6), MEKK1, MEKK2, MEKK3, MEKK4, as well as plant and fungal MAPKKKs. Also included in this subfamily are the cell division control proteins Schizosaccharomyces pombe Cdc7 and Saccharomyces cerevisiae Cdc15. The MAPKKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270783 [Multi-domain]  Cd Length: 258  Bit Score: 149.98  E-value: 2.15e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  725 VLGKTLGEGEFGKVVKATAfHLKGRagytTVAVKMLK-ENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLI 803
Cdd:cd06606    3 KKGELLGKGSFGSVYLALN-LDTGE----LMAVKEVElSGDSEEELEALEREIRILSSLKHPNIVRYLGTERTENTLNIF 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  804 VEYAKYGSLRGFLResrKVGPgylgsggsrnsssLDHPDERaltmgdliSFAWQISQGMQYLAEMKLVHRDLAARNILVA 883
Cdd:cd06606   78 LEYVPGGSLASLLK---KFGK-------------LPEPVVR--------KYTRQILEGLEYLHSNGIVHRDIKGANILVD 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  884 EGRKMKISDFGLSRDVyEEDSYVKRSQGRI--PVkWMAIESLFDHIYTTQSDVWSFGVLLWEIVTlGGNPYPGI--PPER 959
Cdd:cd06606  134 SDGVVKLADFGCAKRL-AEIATGEGTKSLRgtPY-WMAPEVIRGEGYGRAADIWSLGCTVIEMAT-GKPPWSELgnPVAA 210
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 10862703  960 LFNLLKTGHRMERPDNCSEEMYRLMLQCWKQEPDKRP 996
Cdd:cd06606  211 LFKIGSSGEPPPIPEHLSEEAKDFLRKCLQRDPKKRP 247
PTKc_Aatyk3 cd14206
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 3; PTKs ...
730-1001 2.01e-38

Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Aatyk3, also called lemur tyrosine kinase 3 (Lmtk3) is a receptor kinase containing a transmembrane segment and a long C-terminal cytoplasmic tail with a catalytic domain. The function of Aatyk3 is still unknown. The Aatyk3 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 271108 [Multi-domain]  Cd Length: 276  Bit Score: 145.09  E-value: 2.01e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  730 LGEGEFGKVVKATAFhlkgrAGYTT--VAVKMLKENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVEYA 807
Cdd:cd14206    5 IGNGWFGKVILGEIF-----SDYTPaqVVVKELRVSAGPLEQRKFISEAQPYRSLQHPNILQCLGLCTETIPFLLIMEFC 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  808 KYGSLRGFLRESRKvgPGYLGsggsrnsssldhPDERALTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNILVAEGRK 887
Cdd:cd14206   80 QLGDLKRYLRAQRK--ADGMT------------PDLPTRDLRTLQRMAYEITLGLLHLHKNNYIHSDLALRNCLLTSDLT 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  888 MKISDFGLSRDVYEEDSYVKRSQGRIPVKWMAIEsLFDHIY--------TTQSDVWSFGVLLWEIVTLGGNPYPGIPPER 959
Cdd:cd14206  146 VRIGDYGLSHNNYKEDYYLTPDRLWIPLRWVAPE-LLDELHgnlivvdqSKESNVWSLGVTIWELFEFGAQPYRHLSDEE 224
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 10862703  960 LFNLLKTGHRME--RPD---NCSEEMYRLMLQCWKqEPDKRPVFADI 1001
Cdd:cd14206  225 VLTFVVREQQMKlaKPRlklPYADYWYEIMQSCWL-PPSQRPSVEEL 270
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
730-1006 2.02e-37

Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase Kinases 12 and 13; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP3K12 is also called MAPK upstream kinase (MUK), dual leucine zipper-bearing kinase (DLK) or leucine-zipper protein kinase (ZPK). It is involved in the c-Jun N-terminal kinase (JNK) pathway that directly regulates axonal regulation through the phosphorylation of microtubule-associated protein 1B (MAP1B). It also regulates the differentiation of many cell types including adipocytes and may play a role in adipogenesis. MAP3K13, also called leucine zipper-bearing kinase (LZK), directly phosphorylates and activates MKK7, which in turn activates the JNK pathway. It also activates NF-kB through IKK activation and this activity is enhanced by antioxidant protein-1 (AOP-1). MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAP2Ks (MAPKKs or MKKs), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The MAP3K12/13 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270961 [Multi-domain]  Cd Length: 237  Bit Score: 140.71  E-value: 2.02e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  730 LGEGEFGKVvkatafhLKGRAGYTTVAVKMLKENASpselrdllSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVEYAKY 809
Cdd:cd14059    1 LGSGAQGAV-------FLGKFRGEEVAVKKVRDEKE--------TDIKHLRKLNHPNIIKFKGVCTQAPCYCILMEYCPY 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  810 GSLRGFLRESRKVGPGYLgsggsrnsssldhpderaltmgdlISFAWQISQGMQYLAEMKLVHRDLAARNILVAEGRKMK 889
Cdd:cd14059   66 GQLYEVLRAGREITPSLL------------------------VDWSKQIASGMNYLHLHKIIHRDLKSPNVLVTYNDVLK 121
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  890 ISDFGLSRDVYEEDSYVKRSQgriPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTlGGNPYPGIPPER-LFNLLKTGH 968
Cdd:cd14059  122 ISDFGTSKELSEKSTKMSFAG---TVAWMAPEVIRNEPCSEKVDIWSFGVVLWELLT-GEIPYKDVDSSAiIWGVGSNSL 197
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 10862703  969 RMERPDNCSEEMYRLMLQCWKQEPDKRPVFADISKDLE 1006
Cdd:cd14059  198 QLPVPSTCPDGFKLLMKQCWNSKPRNRPSFRQILMHLD 235
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
730-1005 2.08e-37

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK4 is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The specific function of MLK4 is yet to be determined. Mutations in the kinase domain of MLK4 have been detected in colorectal cancers. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation.The MLK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271048 [Multi-domain]  Cd Length: 268  Bit Score: 141.71  E-value: 2.08e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  730 LGEGEFGKVVKATafhLKGRAgyttVAVKMLKEN------ASPSELRDLLSEFNVLKqvnHPHVIKLYGACSQDGPLLLI 803
Cdd:cd14146    2 IGVGGFGKVYRAT---WKGQE----VAVKAARQDpdedikATAESVRQEAKLFSMLR---HPNIIKLEGVCLEEPNLCLV 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  804 VEYAKYGSL-RGFLRESRKVGPgylgsggsrnsssldhPDERALTMGDLISFAWQISQGMQYLAE---MKLVHRDLAARN 879
Cdd:cd14146   72 MEFARGGTLnRALAAANAAPGP----------------RRARRIPPHILVNWAVQIARGMLYLHEeavVPILHRDLKSSN 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  880 ILVAE-------GRK-MKISDFGLSRDVYEEdsyVKRSQGRIpVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTlGGNP 951
Cdd:cd14146  136 ILLLEkiehddiCNKtLKITDFGLAREWHRT---TKMSAAGT-YAWMAPEVIKSSLFSKGSDIWSYGVLLWELLT-GEVP 210
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 10862703  952 YPGIPPERL-FNLLKTGHRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADISKDL 1005
Cdd:cd14146  211 YRGIDGLAVaYGVAVNKLTLPIPSTCPEPFAKLMKECWEQDPHIRPSFALILEQL 265
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
726-996 1.11e-35

Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily include Schizosaccharomyces pombe Cdc7, Saccharomyces cerevisiae Cdc15, Arabidopsis thaliana mitogen-activated protein kinase kinase kinase (MAPKKK) epsilon, and related proteins. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Fission yeast Cdc7 is essential for cell division by playing a key role in the initiation of septum formation and cytokinesis. Budding yeast Cdc15 functions to coordinate mitotic exit with cytokinesis. Arabidopsis MAPKKK epsilon is required for pollen development in the plasma membrane. The Cdc7-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270797 [Multi-domain]  Cd Length: 254  Bit Score: 136.20  E-value: 1.11e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  726 LGKTLGEGEFGKVVKAtafhLKGRAGYTtVAVKMLK-ENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIV 804
Cdd:cd06627    4 LGDLIGRGAFGSVYKG----LNLNTGEF-VAIKQISlEKIPKSDLKSVMGEIDLLKKLNHPNIVKYIGSVKTKDSLYIIL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  805 EYAKYGSLRGFLResrKVGPgylgsggsrnsssldHPDERAltmgdlISFAWQISQGMQYLAEMKLVHRDLAARNILVAE 884
Cdd:cd06627   79 EYVENGSLASIIK---KFGK---------------FPESLV------AVYIYQVLEGLAYLHEQGVIHRDIKGANILTTK 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  885 GRKMKISDFGLSRDVYEEDSYVKRSQGriPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTlGGNPYPGIPPER-LFNL 963
Cdd:cd06627  135 DGLVKLADFGVATKLNEVEKDENSVVG--TPYWMAPEVIEMSGVTTASDIWSVGCTVIELLT-GNPPYYDLQPMAaLFRI 211
                        250       260       270
                 ....*....|....*....|....*....|...
gi 10862703  964 LKTGHrMERPDNCSEEMYRLMLQCWKQEPDKRP 996
Cdd:cd06627  212 VQDDH-PPLPENISPELRDFLLQCFQKDPTLRP 243
PTKc_Aatyk cd05042
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinases; PTKs ...
728-1005 2.82e-35

Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Aatyk subfamily is also referred to as the lemur tyrosine kinase (Lmtk) subfamily. It consists of Aatyk1 (Lmtk1), Aatyk2 (Lmtk2, Brek), Aatyk3 (Lmtk3), and similar proteins. Aatyk proteins are mostly receptor PTKs (RTKs) containing a transmembrane segment and a long C-terminal cytoplasmic tail with a catalytic domain. Aatyk1 does not contain a transmembrane segment and is a cytoplasmic (or nonreceptor) kinase. Aatyk proteins are classified as PTKs based on overall sequence similarity and the phylogenetic tree. However, analysis of catalytic residues suggests that Aatyk proteins may be multispecific kinases, functioning also as serine/threonine kinases. They are involved in neural differentiation, nerve growth factor (NGF) signaling, apoptosis, and spermatogenesis. The Aatyk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270638 [Multi-domain]  Cd Length: 269  Bit Score: 135.79  E-value: 2.82e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  728 KTLGEGEFGKVVKATAFhlkgrAGYTT--VAVKMLKENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVE 805
Cdd:cd05042    1 QEIGNGWFGKVLLGEIY-----SGTSVaqVVVKELKASANPKEQDTFLKEGQPYRILQHPNILQCLGQCVEAIPYLLVME 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  806 YAKYGSLRGFLRESRkvgpgylgsggsrnSSSLDHPDERALTmgdliSFAWQISQGMQYLAEMKLVHRDLAARNILVAEG 885
Cdd:cd05042   76 FCDLGDLKAYLRSER--------------EHERGDSDTRTLQ-----RMACEVAAGLAHLHKLNFVHSDLALRNCLLTSD 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  886 RKMKISDFGLSRDVYEEDSYVKRSQGRIPVKWMAIEsLFDHIY--------TTQSDVWSFGVLLWEIVTLGGNPYPGIPP 957
Cdd:cd05042  137 LTVKIGDYGLAHSRYKEDYIETDDKLWFPLRWTAPE-LVTEFHdrllvvdqTKYSNIWSLGVTLWELFENGAQPYSNLSD 215
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 10862703  958 ERLFN-LLKTGH-RMERPD---NCSEEMYRLMLQCWKQePDKRPVFADISKDL 1005
Cdd:cd05042  216 LDVLAqVVREQDtKLPKPQlelPYSDRWYEVLQFCWLS-PEQRPAAEDVHLLL 267
PTKc_Aatyk1 cd05087
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 1; PTKs ...
728-996 6.58e-35

Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Aatyk1 (or simply Aatyk) is also called lemur tyrosine kinase 1 (Lmtk1). It is a cytoplasmic (or nonreceptor) kinase containing a long C-terminal region. The expression of Aatyk1 is upregulated during growth arrest and apoptosis in myeloid cells. Aatyk1 has been implicated in neural differentiation, and is a regulator of the Na-K-2Cl cotransporter, a membrane protein involved in cell proliferation and survival, epithelial transport, and blood pressure control. The Aatyk1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270670 [Multi-domain]  Cd Length: 271  Bit Score: 134.73  E-value: 6.58e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  728 KTLGEGEFGKVVKAtafHLKGRAGYTTVAVKMLKENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVEYA 807
Cdd:cd05087    3 KEIGHGWFGKVFLG---EVNSGLSSTQVVVKELKASASVQDQMQFLEEAQPYRALQHTNLLQCLAQCAEVTPYLLVMEFC 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  808 KYGSLRGFLRESRkvgpgylgsggsrnSSSLDHPDERALTmgdliSFAWQISQGMQYLAEMKLVHRDLAARNILVAEGRK 887
Cdd:cd05087   80 PLGDLKGYLRSCR--------------AAESMAPDPLTLQ-----RMACEVACGLLHLHRNNFVHSDLALRNCLLTADLT 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  888 MKISDFGLSRDVYEEDSYVKRSQGRIPVKWMAIEsLFDHIY--------TTQSDVWSFGVLLWEIVTLGGNPYPGIPPER 959
Cdd:cd05087  141 VKIGDYGLSHCKYKEDYFVTADQLWVPLRWIAPE-LVDEVHgnllvvdqTKQSNVWSLGVTIWELFELGNQPYRHYSDRQ 219
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 10862703  960 LFNLLKTGHRMERPD-----NCSEEMYRLMLQCWKQePDKRP 996
Cdd:cd05087  220 VLTYTVREQQLKLPKpqlklSLAERWYEVMQFCWLQ-PEQRP 260
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
726-996 1.55e-34

Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes many bacterial eukaryotic-type STKs including Staphylococcus aureus PknB (also called PrkC or Stk1), Bacillus subtilis PrkC, and Mycobacterium tuberculosis Pkn proteins (PknB, PknD, PknE, PknF, PknL, and PknH), among others. S. aureus PknB is the only eukaryotic-type STK present in this species, although many microorganisms encode for several such proteins. It is important for the survival and pathogenesis of S. aureus as it is involved in the regulation of purine and pyrimidine biosynthesis, cell wall metabolism, autolysis, virulence, and antibiotic resistance. M. tuberculosis PknB is essential for growth and it acts on diverse substrates including proteins involved in peptidoglycan synthesis, cell division, transcription, stress responses, and metabolic regulation. B. subtilis PrkC is located at the inner membrane of endospores and functions to trigger spore germination. Bacterial STKs in this subfamily show varied domain architectures. The well-characterized members such as S. aureus and M. tuberculosis PknB, and B. subtilis PrkC, contain an N-terminal cytosolic kinase domain, a transmembrane (TM) segment, and mutliple C-terminal extracellular PASTA domains. The PknB subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270916 [Multi-domain]  Cd Length: 260  Bit Score: 133.10  E-value: 1.55e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  726 LGKTLGEGEFGKVVKATAFHLkGRagytTVAVKMLKENASPSE--LRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLI 803
Cdd:cd14014    4 LVRLLGRGGMGEVYRARDTLL-GR----PVAIKVLRPELAEDEefRERFLREARALARLSHPNIVRVYDVGEDDGRPYIV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  804 VEYAKYGSLRGFLRESRKVgpgylgsggsrnsssldhPDERALTMGDlisfawQISQGMQYLAEMKLVHRDLAARNILVA 883
Cdd:cd14014   79 MEYVEGGSLADLLRERGPL------------------PPREALRILA------QIADALAAAHRAGIVHRDIKPANILLT 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  884 EGRKMKISDFGLSRDVyeEDSYVKRSQGRI--PVkWMAIESLFDHIYTTQSDVWSFGVLLWEIVTlGGNPYPGIPPER-L 960
Cdd:cd14014  135 EDGRVKLTDFGIARAL--GDSGLTQTGSVLgtPA-YMAPEQARGGPVDPRSDIYSLGVVLYELLT-GRPPFDGDSPAAvL 210
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 10862703  961 FNLLKTGHRMERPDN--CSEEMYRLMLQCWKQEPDKRP 996
Cdd:cd14014  211 AKHLQEAPPPPSPLNpdVPPALDAIILRALAKDPEERP 248
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
730-1006 1.72e-34

Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Raf kinases act as mitogen-activated protein kinase kinase kinases (MAP3Ks, MKKKs, MAPKKKs), which phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. They function in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. Aberrant expression or activation of components in this pathway are associated with tumor initiation, progression, and metastasis. Raf proteins contain a Ras binding domain, a zinc finger cysteine-rich domain, and a catalytic kinase domain. Vertebrates have three Raf isoforms (A-, B-, and C-Raf) with different expression profiles, modes of regulation, and abilities to function in the ERK cascade, depending on cellular context and stimuli. They have essential and non-overlapping roles during embryo- and organogenesis. Knockout of each isoform results in a lethal phenotype or abnormality in most mouse strains. The Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270964 [Multi-domain]  Cd Length: 253  Bit Score: 132.90  E-value: 1.72e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  730 LGEGEFGKVVKAtafHLKGragytTVAVKMLK-ENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGpLLLIVEYAK 808
Cdd:cd14062    1 IGSGSFGTVYKG---RWHG-----DVAVKKLNvTDPTPSQLQAFKNEVAVLRKTRHVNILLFMGYMTKPQ-LAIVTQWCE 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  809 YGSLRGFLresrkvgpgylgsggsrnsssldHPDERALTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNILVAEGRKM 888
Cdd:cd14062   72 GSSLYKHL-----------------------HVLETKFEMLQLIDIARQTAQGMDYLHAKNIIHRDLKSNNIFLHEDLTV 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  889 KISDFGLSRDVYEEDSYVKRSQGRIPVKWMA---IESLFDHIYTTQSDVWSFGVLLWEIVTlGGNPYPGIPPERLFnLLK 965
Cdd:cd14062  129 KIGDFGLATVKTRWSGSQQFEQPTGSILWMApevIRMQDENPYSFQSDVYAFGIVLYELLT-GQLPYSHINNRDQI-LFM 206
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 10862703  966 TGHRMERPD------NCSEEMYRLMLQCWKQEPDKRPVFADISKDLE 1006
Cdd:cd14062  207 VGRGYLRPDlskvrsDTPKALRRLMEDCIKFQRDERPLFPQILASLE 253
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
726-996 3.19e-34

Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. This family is composed of STKs, and some dual-specificity PKs that phosphorylate both threonine and tyrosine residues of target proteins. Most members are kinases involved in mitogen-activated protein kinase (MAPK) signaling cascades, acting as MAPK kinases (MAPKKs), MAPKK kinases (MAPKKKs), or MAPKKK kinases (MAP4Ks). The MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The pathways involve a triple kinase core cascade comprising of the MAPK, which is phosphorylated and activated by a MAPKK, which itself is phosphorylated and activated by a MAPKKK. Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAPKKK to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Other STE family members include p21-activated kinases (PAKs) and class III myosins, among others. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain, which can phosphorylate several cytoskeletal proteins, conventional myosin regulatory light chains, as well as autophosphorylate the C-terminal motor domain. They play an important role in maintaining the structural integrity of photoreceptor cell microvilli. The STE family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270692 [Multi-domain]  Cd Length: 254  Bit Score: 131.94  E-value: 3.19e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  726 LGKTLGEGEFGKVVKAtaFHLKGRagyTTVAVKMLKENaSPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVE 805
Cdd:cd05122    4 ILEKIGKGGFGVVYKA--RHKKTG---QIVAIKKINLE-SKEKKESILNEIAILKKCKHPNIVKYYGSYLKKDELWIVME 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  806 YAKYGSLRGFLRESRKVGPgylgsggsrnsssldhPDERALTMGDLIsfawqisQGMQYLAEMKLVHRDLAARNILVAEG 885
Cdd:cd05122   78 FCSGGSLKDLLKNTNKTLT----------------EQQIAYVCKEVL-------KGLEYLHSHGIIHRDIKAANILLTSD 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  886 RKMKISDFGLSRDvyeedsyVKRSQGRI----PVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTlGGNPYPGIPPERLF 961
Cdd:cd05122  135 GEVKLIDFGLSAQ-------LSDGKTRNtfvgTPYWMAPEVIQGKPYGFKADIWSLGITAIEMAE-GKPPYSELPPMKAL 206
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 10862703  962 NLLKTGHRMERPD--NCSEEMYRLMLQCWKQEPDKRP 996
Cdd:cd05122  207 FLIATNGPPGLRNpkKWSKEFKDFLKKCLQKDPEKRP 243
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
730-1008 3.26e-34

Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases and related STKs; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. Some IRAKs may also play roles in T- and B-cell signaling, and adaptive immunity. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK-1, -2, and -4 are ubiquitously expressed and are active kinases, while IRAK-M is only induced in monocytes and macrophages and is an inactive kinase. Variations in IRAK genes are linked to diverse diseases including infection, sepsis, cancer, and autoimmune diseases. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain (a pseudokinase domain in the case of IRAK3), and a C-terminal domain; IRAK-4 lacks the C-terminal domain. This subfamily includes plant receptor-like kinases (RLKs) including Arabidopsis thaliana BAK1 and CLAVATA1 (CLV1). BAK1 functions in BR (brassinosteroid)-regulated plant development and in pathways involved in plant resistance to pathogen infection and herbivore attack. CLV1, directly binds small signaling peptides, CLAVATA3 (CLV3) and CLAVATA3/EMBRYO SURROUNDING REGI0N (CLE), to restrict stem cell proliferation: the CLV3-CLV1-WUS (WUSCHEL) module influences stem cell maintenance in the shoot apical meristem, and the CLE40 (CLAVATA3/EMBRYO SURROUNDING REGION40) -ACR4 (CRINKLY4) -CLV1- WOX5 (WUSCHEL-RELATED HOMEOBOX5) module at the root apical meristem. The IRAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270968 [Multi-domain]  Cd Length: 272  Bit Score: 132.78  E-value: 3.26e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  730 LGEGEFGKVVKATafhlkgRAGYTTVAVKMLKENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVEYAKY 809
Cdd:cd14066    1 IGSGGFGTVYKGV------LENGTVVAVKRLNEMNCAASKKEFLTELEMLGRLRHPNLVRLLGYCLESDEKLLVYEYMPN 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  810 GSLRGFLRESRKVGPgylgsggsrnsssLDHPdERaltmgdlISFAWQISQGMQYLAE---MKLVHRDLAARNILVAEGR 886
Cdd:cd14066   75 GSLEDRLHCHKGSPP-------------LPWP-QR-------LKIAKGIARGLEYLHEecpPPIIHGDIKSSNILLDEDF 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  887 KMKISDFGLSRDVYEEDSYVKRSQGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTlGGNPYPGIPPERLFNLLKT 966
Cdd:cd14066  134 EPKLTDFGLARLIPPSESVSKTSAVKGTIGYLAPEYIRTGRVSTKSDVYSFGVVLLELLT-GKPAVDENRENASRKDLVE 212
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  967 GHRMERPDNCS------------------EEMYRLMLQCWKQEPDKRPVFADISKDLEKM 1008
Cdd:cd14066  213 WVESKGKEELEdildkrlvdddgveeeevEALLRLALLCTRSDPSLRPSMKEVVQMLEKL 272
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
730-1000 1.19e-33

Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RIP kinases serve as essential sensors of cellular stress. They are involved in regulating NF-kappaB and MAPK signaling, and are implicated in mediating cellular processes such as apoptosis, necroptosis, differentiation, and survival. RIP kinases contain a homologous N-terminal kinase domain and varying C-terminal domains. Higher vertebrates contain multiple RIP kinases, with mammals harboring at least five members. RIP1 and RIP2 harbor C-terminal domains from the Death domain (DD) superfamily while RIP4 contains ankyrin (ANK) repeats. RIP3 contain a RIP homotypic interaction motif (RHIM) that facilitates binding to RIP1. RIP1 and RIP3 are important in apoptosis and necroptosis, while RIP2 and RIP4 play roles in keratinocyte differentiation and inflammatory immune responses. The RIP subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270880 [Multi-domain]  Cd Length: 263  Bit Score: 130.65  E-value: 1.19e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  730 LGEGEFGKVVKAtaFHlkgRAGYTTVAVKMLKENASPSELR-DLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVEYAK 808
Cdd:cd13978    1 LGSGGFGTVSKA--RH---VSWFGMVAIKCLHSSPNCIEERkALLKEAEKMERARHSYVLPLLGVCVERRSLGLVMEYME 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  809 YGSLRGFL-RESRKVGPgylgsggsrnsssldhpderaltmgDL-ISFAWQISQGMQYLAEMK--LVHRDLAARNILVAE 884
Cdd:cd13978   76 NGSLKSLLeREIQDVPW-------------------------SLrFRIIHEIALGMNFLHNMDppLLHHDLKPENILLDN 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  885 GRKMKISDFGLSRdVYEEDSYVKRSQGRIP----VKWMAIESLFDHIY--TTQSDVWSFGVLLWEIVTlGGNPYPG-IPP 957
Cdd:cd13978  131 HFHVKISDFGLSK-LGMKSISANRRRGTENlggtPIYMAPEAFDDFNKkpTSKSDVYSFAIVIWAVLT-RKEPFENaINP 208
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 10862703  958 ERLFNLLKTGHRMERPDNCS-------EEMYRLMLQCWKQEPDKRPVFAD 1000
Cdd:cd13978  209 LLIMQIVSKGDRPSLDDIGRlkqienvQELISLMIRCWDGNPDARPTFLE 258
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
722-1008 1.45e-33

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK3 is a mitogen-activated protein kinase kinase kinases (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MLK3 activates multiple MAPK pathways and plays a role in apoptosis, proliferation, migration, and differentiation, depending on the cellular context. It is highly expressed in breast cancer cells and its signaling through c-Jun N-terminal kinase has been implicated in the migration, invasion, and malignancy of cancer cells. MLK3 also functions as a negative regulator of Inhibitor of Nuclear Factor-KappaB Kinase (IKK) and consequently, it also impacts inflammation and immunity. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation.The MLK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271049 [Multi-domain]  Cd Length: 267  Bit Score: 130.53  E-value: 1.45e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  722 KNLVLGKTLGEGEFGKVVKATafhLKGRagytTVAVKMLKENasPSE-----LRDLLSEFNVLKQVNHPHVIKLYGACSQ 796
Cdd:cd14147    3 QELRLEEVIGIGGFGKVYRGS---WRGE----LVAVKAARQD--PDEdisvtAESVRQEARLFAMLAHPNIIALKAVCLE 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  797 DGPLLLIVEYAKYGSLRGFLrESRKVGPGYlgsggsrnsssldhpderaltmgdLISFAWQISQGMQYL---AEMKLVHR 873
Cdd:cd14147   74 EPNLCLVMEYAAGGPLSRAL-AGRRVPPHV------------------------LVNWAVQIARGMHYLhceALVPVIHR 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  874 DLAARNILVA--------EGRKMKISDFGLSRDVYEedsyVKRSQGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIV 945
Cdd:cd14147  129 DLKSNNILLLqpienddmEHKTLKITDFGLAREWHK----TTQMSAAGTYAWMAPEVIKASTFSKGSDVWSFGVLLWELL 204
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 10862703  946 TlGGNPYPGIPPERL-FNLLKTGHRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADISKDLEKM 1008
Cdd:cd14147  205 T-GEVPYRGIDCLAVaYGVAVNKLTLPIPSTCPEPFAQLMADCWAQDPHRRPDFASILQQLEAL 267
Pkinase pfam00069
Protein kinase domain;
724-1001 1.58e-33

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 128.90  E-value: 1.58e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703    724 LVLGKTLGEGEFGKVVKATAfHLKGRagytTVAVKML-KENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLL 802
Cdd:pfam00069    1 YEVLRKLGSGSFGTVYKAKH-RDTGK----IVAIKKIkKEKIKKKKDKNILREIKILKKLNHPNIVRLYDAFEDKDNLYL 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703    803 IVEYAKYGSLRGFLREsrkvgpgylgsggsrnsssldhpdERALTMGDLISFAWQISQGMQYlaemklvhrdlaarnilv 882
Cdd:pfam00069   76 VLEYVEGGSLFDLLSE------------------------KGAFSEREAKFIMKQILEGLES------------------ 113
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703    883 aegrkmkisdfGLSRDVYEEDSYvkrsqgripvkWMAIESLFDHIYTTQSDVWSFGVLLWEIVTlGGNPYPGIPPERLF- 961
Cdd:pfam00069  114 -----------GSSLTTFVGTPW-----------YMAPEVLGGNPYGPKVDVWSLGCILYELLT-GKPPFPGINGNEIYe 170
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 10862703    962 -NLLKTGHRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADI 1001
Cdd:pfam00069  171 lIIDQPYAFPELPSNLSEEAKDLLKKLLKKDPSKRLTATQA 211
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
730-1005 2.34e-33

Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. Members of this subfamily include LIMK, Testicular or testis-specific protein kinase (TESK), and similar proteins. LIMKs are characterized as serine/threonine kinases (STKs) while TESKs are dual-specificity protein kinases. Both LIMK and TESK phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They are implicated in many cellular functions including cell spreading, motility, morphogenesis, meiosis, mitosis, and spermatogenesis. The LIMK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270967 [Multi-domain]  Cd Length: 252  Bit Score: 129.53  E-value: 2.34e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  730 LGEGEFGKVVKATafHlkgragYTTVAVKMLKENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVEYAKY 809
Cdd:cd14065    1 LGKGFFGEVYKVT--H------RETGKVMVMKELKRFDEQRSFLKEVKLMRRLSHPNILRFIGVCVKDNKLNFITEYVNG 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  810 GSLRGFLREsrkvgpgylgsggsrnsssldhPDErALTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNILVAE---GR 886
Cdd:cd14065   73 GTLEELLKS----------------------MDE-QLPWSQRVSLAKDIASGMAYLHSKNIIHRDLNSKNCLVREanrGR 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  887 KMKISDFGLSRDVYEEDSYVKRSQGRIPV----KWMAIESLFDHIYTTQSDVWSFGVLLWEIVT-LGGNPyPGIPPERLF 961
Cdd:cd14065  130 NAVVADFGLAREMPDEKTKKPDRKKRLTVvgspYWMAPEMLRGESYDEKVDVFSFGIVLCEIIGrVPADP-DYLPRTMDF 208
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 10862703  962 NLLKTGHRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADISKDL 1005
Cdd:cd14065  209 GLDVRAFRTLYVPDCPPSFLPLAIRCCQLDPEKRPSFVELEHHL 252
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
723-1001 6.04e-33

Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The AMPK-like subfamily is composed of AMPK, MARK, BRSK, NUAK, MELK, SNRK, TSSK, and SIK, among others. LKB1 serves as a master upstream kinase that activates AMPK and most AMPK-like kinases. AMPK, also called SNF1 (sucrose non-fermenting1) in yeasts and SnRK1 (SNF1-related kinase1) in plants, is a heterotrimeric enzyme composed of a catalytic alpha subunit and two regulatory subunits, beta and gamma. It is a stress-activated kinase that serves as master regulator of glucose and lipid metabolism by monitoring carbon and energy supplies, via sensing the cell's AMP:ATP ratio. MARKs phosphorylate tau and related microtubule-associated proteins (MAPs), and regulates microtubule-based intracellular transport. They are involved in embryogenesis, epithelial cell polarization, cell signaling, and neuronal differentiation. BRSKs play important roles in establishing neuronal polarity. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. The AMPK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270905 [Multi-domain]  Cd Length: 252  Bit Score: 128.40  E-value: 6.04e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  723 NLVLGKTLGEGEFGKVVKATafHLKGRagyTTVAVKML-KENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLL 801
Cdd:cd14003    1 NYELGKTLGEGSFGKVKLAR--HKLTG---EKVAIKIIdKSKLKEEIEEKIKREIEIMKLLNHPNIIKLYEVIETENKIY 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  802 LIVEYAKYGSLRGFLRESRKvgpgylgsggsrnsssLDHPDERALtmgdlisFaWQISQGMQYLAEMKLVHRDLAARNIL 881
Cdd:cd14003   76 LVMEYASGGELFDYIVNNGR----------------LSEDEARRF-------F-QQLISAVDYCHSNGIVHRDLKLENIL 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  882 VAEGRKMKISDFGLSRdVYEEDSYVKRSQGRIPvkWMAIESLFDHIY-TTQSDVWSFGVLLWEIVTlGGNPYPGIPPERL 960
Cdd:cd14003  132 LDKNGNLKIIDFGLSN-EFRGGSLLKTFCGTPA--YAAPEVLLGRKYdGPKADVWSLGVILYAMLT-GYLPFDDDNDSKL 207
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 10862703  961 FNLLKTGHrMERPDNCSEEMYRLMLQCWKQEPDKRPVFADI 1001
Cdd:cd14003  208 FRKILKGK-YPIPSHLSPDARDLIRRMLVVDPSKRITIEEI 247
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
730-1006 9.80e-33

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK2 is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK) and is also called MAP3K10. MAP3Ks phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MLK2 is abundant in brain, skeletal muscle, and testis. It functions upstream of the MAPK, c-Jun N-terminal kinase. It binds hippocalcin, a calcium-sensor protein that protects neurons against calcium-induced cell death. Both MLK2 and hippocalcin may be associated with the pathogenesis of Parkinson's disease. MLK2 also binds to normal huntingtin (Htt), which is important in neuronal transcription, development, and survival. MLK2 does not bind to the polyglutamine-expanded Htt, which is implicated in the pathogeneis of Huntington's disease, leading to neuronal toxicity. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. The MLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 271050 [Multi-domain]  Cd Length: 258  Bit Score: 127.80  E-value: 9.80e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  730 LGEGEFGKVVKATafhlkGRAgyTTVAVKMLKENasPSE-----LRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIV 804
Cdd:cd14148    2 IGVGGFGKVYKGL-----WRG--EEVAVKAARQD--PDEdiavtAENVRQEARLFWMLQHPNIIALRGVCLNPPHLCLVM 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  805 EYAKYGSLRGFLrESRKVGPGYlgsggsrnsssldhpderaltmgdLISFAWQISQGMQYL---AEMKLVHRDLAARNIL 881
Cdd:cd14148   73 EYARGGALNRAL-AGKKVPPHV------------------------LVNWAVQIARGMNYLhneAIVPIIHRDLKSSNIL 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  882 VAE--------GRKMKISDFGLSRdvyEEDSYVKRSQGRIpVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTlGGNPYp 953
Cdd:cd14148  128 ILEpienddlsGKTLKITDFGLAR---EWHKTTKMSAAGT-YAWMAPEVIRLSLFSKSSDVWSFGVLLWELLT-GEVPY- 201
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  954 gippeRLFNLLKT--GHRMER-----PDNCSEEMYRLMLQCWKQEPDKRPVFADISKDLE 1006
Cdd:cd14148  202 -----REIDALAVayGVAMNKltlpiPSTCPEPFARLLEECWDPDPHGRPDFGSILKRLE 256
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
724-1001 1.39e-32

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK1 is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK) and is also called MAP3K9. MAP3Ks phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Little is known about the specific function of MLK1. It is capable of activating the c-Jun N-terminal kinase pathway. Mice lacking both MLK1 and MLK2 are viable, fertile, and have normal life spans. There could be redundancy in the function of MLKs. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. The MLK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271047 [Multi-domain]  Cd Length: 270  Bit Score: 127.85  E-value: 1.39e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  724 LVLGKTLGEGEFGKVVKATAfhlkgraGYTTVAVKMLKENasPSE-----LRDLLSEFNVLKQVNHPHVIKLYGACSQDG 798
Cdd:cd14145    8 LVLEEIIGIGGFGKVYRAIW-------IGDEVAVKAARHD--PDEdisqtIENVRQEAKLFAMLKHPNIIALRGVCLKEP 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  799 PLLLIVEYAKYGSLRGFLrESRKVGPGYlgsggsrnsssldhpderaltmgdLISFAWQISQGMQYL---AEMKLVHRDL 875
Cdd:cd14145   79 NLCLVMEFARGGPLNRVL-SGKRIPPDI------------------------LVNWAVQIARGMNYLhceAIVPVIHRDL 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  876 AARNILVAE--------GRKMKISDFGLSRDVYEedsyVKRSQGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTl 947
Cdd:cd14145  134 KSSNILILEkvengdlsNKILKITDFGLAREWHR----TTKMSAAGTYAWMAPEVIRSSMFSKGSDVWSYGVLLWELLT- 208
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 10862703  948 GGNPYPGIPPERL-FNLLKTGHRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADI 1001
Cdd:cd14145  209 GEVPFRGIDGLAVaYGVAMNKLSLPIPSTCPEPFARLMEDCWNPDPHSRPPFTNI 263
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
731-1008 3.13e-32

Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated protein Triple Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLTK, also called zipper sterile-alpha-motif kinase (ZAK), contains a catalytic kinase domain and a leucine zipper. There are two alternatively-spliced variants, MLTK-alpha and MLTK-beta. MLTK-alpha contains a sterile-alpha-motif (SAM) at the C-terminus. MLTK regulates the c-Jun N-terminal kinase, extracellular signal-regulated kinase, p38 MAPK, and NF-kB pathways. ZAK is the MAP3K involved in the signaling cascade that leads to the ribotoxic stress response initiated by cellular damage due to Shiga toxins and ricin. It may also play a role in cell transformation and cancer development. MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals.The MLTK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270962 [Multi-domain]  Cd Length: 242  Bit Score: 125.84  E-value: 3.13e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  731 GEGEFGKVVKAtafhlKGRAGYTTVAVKMLKENASPSELRDLLSefnvlkqvnHPHVIKLYGACSQDGPLLLIVEYAKYG 810
Cdd:cd14060    2 GGGSFGSVYRA-----IWVSQDKEVAVKKLLKIEKEAEILSVLS---------HRNIIQFYGAILEAPNYGIVTEYASYG 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  811 SLRGFLRESrkvgpgylgsggsrnsssldhpDERALTMGDLISFAWQISQGMQYL---AEMKLVHRDLAARNILVAEGRK 887
Cdd:cd14060   68 SLFDYLNSN----------------------ESEEMDMDQIMTWATDIAKGMHYLhmeAPVKVIHRDLKSRNVVIAADGV 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  888 MKISDFGLSRDVYEedSYVKRSQGRIPvkWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLGgNPYPGIPPERL-FNLLKT 966
Cdd:cd14060  126 LKICDFGASRFHSH--TTHMSLVGTFP--WMAPEVIQSLPVSETCDTYSYGVVLWEMLTRE-VPFKGLEGLQVaWLVVEK 200
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 10862703  967 GHRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADISKDLEKM 1008
Cdd:cd14060  201 NERPTIPSSCPRSFAELMRRCWEADVKERPSFKQIIGILESM 242
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
730-1008 6.33e-32

Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LIMKs phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They act downstream of Rho GTPases and are expressed ubiquitously. As regulators of actin dynamics, they contribute to diverse cellular functions such as cell motility, morphogenesis, differentiation, apoptosis, meiosis, mitosis, and neurite extension. LIMKs contain the LIM (two repeats), PDZ, and catalytic kinase domains. Vertebrate have two members, LIMK1 and LIMK2. The LIMK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271056 [Multi-domain]  Cd Length: 272  Bit Score: 126.08  E-value: 6.33e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  730 LGEGEFGKVVKATafHlkgragYTTVAVKMLKE--NASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVEYA 807
Cdd:cd14154    1 LGKGFFGQAIKVT--H------RETGEVMVMKEliRFDEEAQRNFLKEVKVMRSLDHPNVLKFIGVLYKDKKLNLITEYI 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  808 KYGSLRGFLRESrkvgpgylgsggsrnsssldhpdERALTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNILVAEGRK 887
Cdd:cd14154   73 PGGTLKDVLKDM-----------------------ARPLPWAQRVRFAKDIASGMAYLHSMNIIHRDLNSHNCLVREDKT 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  888 MKISDFGLSRDVYEE-------DSYVKRSQGRIPVK-----------WMAIESLFDHIYTTQSDVWSFGVLLWEIVtlgG 949
Cdd:cd14154  130 VVVADFGLARLIVEErlpsgnmSPSETLRHLKSPDRkkrytvvgnpyWMAPEMLNGRSYDEKVDIFSFGIVLCEII---G 206
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 10862703  950 NPY--PGIPPERL-FNLLKTGHRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADISKDLEKM 1008
Cdd:cd14154  207 RVEadPDYLPRTKdFGLNVDSFREKFCAGCPPPFFKLAFLCCDLDPEKRPPFETLEEWLEAL 268
PTK_Jak_rpt1 cd05037
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak ...
724-1005 7.83e-32

Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily is composed of Jak1, Jak2, Jak3, TYK2, and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal catalytic tyr kinase domain. The pseudokinase domain shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. It modulates the kinase activity of the C-terminal catalytic domain. In the case of Jak2, the presumed pseudokinase (repeat 1) domain exhibits dual-specificity kinase activity, phosphorylating two negative regulatory sites in Jak2: Ser523 and Tyr570. Most Jaks are expressed in a wide variety of tissues, except for Jak3, which is expressed only in hematopoietic cells. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). Jaks are also involved in regulating the surface expression of some cytokine receptors. The Jak-STAT pathway is involved in many biological processes including hematopoiesis, immunoregulation, host defense, fertility, lactation, growth, and embryogenesis. The Jak subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270633 [Multi-domain]  Cd Length: 259  Bit Score: 125.29  E-value: 7.83e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  724 LVLGKTLGEGEFGKVVKATAFH-LKGRAGYTTVAVKMLKENAspselRDLLSEF----NVLKQVNHPHVIKLYGACSQDg 798
Cdd:cd05037    1 ITFHEHLGQGTFTNIYDGILREvGDGRVQEVEVLLKVLDSDH-----RDISESFfetaSLMSQISHKHLVKLYGVCVAD- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  799 PLLLIVEYAKYGSLRGFLReSRKVGPgylgsggsrnsssldhpderalTMGDLISFAWQISQGMQYLAEMKLVHRDLAAR 878
Cdd:cd05037   75 ENIMVQEYVRYGPLDKYLR-RMGNNV----------------------PLSWKLQVAKQLASALHYLEDKKLIHGNVRGR 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  879 NILVAE------GRKMKISDFGLSRDVYEEDSYVKrsqgRIPvkWMAIESLFD--HIYTTQSDVWSFGVLLWEIVTLGGN 950
Cdd:cd05037  132 NILLARegldgyPPFIKLSDPGVPITVLSREERVD----RIP--WIAPECLRNlqANLTIAADKWSFGTTLWEICSGGEE 205
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 10862703  951 PYPGIPPERLFNLLKTGHRMERPDncSEEMYRLMLQCWKQEPDKRPVFADISKDL 1005
Cdd:cd05037  206 PLSALSSQEKLQFYEDQHQLPAPD--CAELAELIMQCWTYEPTKRPSFRAILRDL 258
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
724-1008 1.37e-30

Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. KSR is a scaffold protein that functions downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. KSR proteins regulate the assembly and activation of the Raf/MEK/ERK module upon Ras activation at the membrane by direct association of its components. They are widely regarded as pseudokinases, but there is some debate in this designation as a few groups have reported detecting kinase catalytic activity for KSRs, specifically KSR1. Vertebrates contain two KSR proteins, KSR1 and KSR2. The KSR subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270965 [Multi-domain]  Cd Length: 271  Bit Score: 122.07  E-value: 1.37e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  724 LVLGKTLGEGEFGKVVKAtafHLKGRagyttVAVKMLKENaSPSELRDLLSEFNVL--KQVNHPHVIKLYGACSQDGPLL 801
Cdd:cd14063    2 LEIKEVIGKGRFGRVHRG---RWHGD-----VAIKLLNID-YLNEEQLEAFKEEVAayKNTRHDNLVLFMGACMDPPHLA 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  802 LIVEYAKYGSLRGFLRESRKVgpgylgsggsrnsssldhpderaLTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNIL 881
Cdd:cd14063   73 IVTSLCKGRTLYSLIHERKEK-----------------------FDFNKTVQIAQQICQGMGYLHAKGIIHKDLKSKNIF 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  882 VaEGRKMKISDFGLSRDVYEEDSYVKRSQGRIPVKW-----------MAIESLFDHI--YTTQSDVWSFGVLLWEIVTlG 948
Cdd:cd14063  130 L-ENGRVVITDFGLFSLSGLLQPGRREDTLVIPNGWlcylapeiiraLSPDLDFEESlpFTKASDVYAFGTVWYELLA-G 207
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 10862703  949 GNPYPGIPPERLFNLLKTGHRMERPD-NCSEEMYRLMLQCWKQEPDKRPVFADISKDLEKM 1008
Cdd:cd14063  208 RWPFKEQPAESIIWQVGCGKKQSLSQlDIGREVKDILMQCWAYDPEKRPTFSDLLRMLERL 268
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
717-1008 9.00e-30

Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. B-Raf activates ERK with the strongest magnitude, compared with other Raf kinases. Mice embryos deficient in B-Raf die around midgestation due to vascular hemorrhage caused by apoptotic endothelial cells. Mutations in B-Raf have been implicated in initiating tumorigenesis and tumor progression, and are found in malignant cutaneous melanoma, papillary thyroid cancer, as well as in ovarian and colorectal carcinomas. Most oncogenic B-Raf mutations are located at the activation loop of the kinase and surrounding regions; the V600E mutation accounts for around 90% of oncogenic mutations. The V600E mutant constitutively activates MEK, resulting in sustained activation of ERK. B-Raf is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. They function in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. The B-Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271053 [Multi-domain]  Cd Length: 274  Bit Score: 119.78  E-value: 9.00e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  717 WEFPRKNLVLGKTLGEGEFGKVVKATafhlkgraGYTTVAVKMLKENA-SPSELRDLLSEFNVLKQVNHPHVIkLYGACS 795
Cdd:cd14151    3 WEIPDGQITVGQRIGSGSFGTVYKGK--------WHGDVAVKMLNVTApTPQQLQAFKNEVGVLRKTRHVNIL-LFMGYS 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  796 QDGPLLLIVEYAKYGSLRGFLresrkvgpgylgsggsrnsssldHPDERALTMGDLISFAWQISQGMQYLAEMKLVHRDL 875
Cdd:cd14151   74 TKPQLAIVTQWCEGSSLYHHL-----------------------HIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDL 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  876 AARNILVAEGRKMKISDFGLSRDVYEEDSYVKRSQGRIPVKWMAIESLF---DHIYTTQSDVWSFGVLLWEIVTlGGNPY 952
Cdd:cd14151  131 KSNNIFLHEDLTVKIGDFGLATVKSRWSGSHQFEQLSGSILWMAPEVIRmqdKNPYSFQSDVYAFGIVLYELMT-GQLPY 209
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 10862703  953 PGIpPERLFNLLKTGHRMERPD------NCSEEMYRLMLQCWKQEPDKRPVFADISKDLEKM 1008
Cdd:cd14151  210 SNI-NNRDQIIFMVGRGYLSPDlskvrsNCPKAMKRLMAECLKKKRDERPLFPQILASIELL 270
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
730-1008 1.90e-29

Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LIMK1 activation is induced by bone morphogenic protein, vascular endothelial growth factor, and thrombin. It plays roles in microtubule disassembly and cell cycle progression, and is critical in the regulation of neurite outgrowth. LIMK1 knockout mice show abnormalities in dendritic spine morphology and synaptic function. LIMK1 is one of the genes deleted in patients with Williams Syndrome, which is characterized by distinct craniofacial features, cardiovascular problems, as well as behavioral and neurological abnormalities. LIMKs phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They act downstream of Rho GTPases and are expressed ubiquitously. As regulators of actin dynamics, they contribute to diverse cellular functions such as cell motility, morphogenesis, differentiation, apoptosis, meiosis, mitosis, and neurite extension. LIMKs contain the LIM (two repeats), PDZ, and catalytic kinase domains. The LIMK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271123 [Multi-domain]  Cd Length: 267  Bit Score: 118.91  E-value: 1.90e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  730 LGEGEFGKVVKATafHLKgragytTVAVKMLKENASPSE--LRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVEYA 807
Cdd:cd14221    1 LGKGCFGQAIKVT--HRE------TGEVMVMKELIRFDEetQRTFLKEVKVMRCLEHPNVLKFIGVLYKDKRLNFITEYI 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  808 KYGSLRGFLRESRKVGPgylgsggsrnsssldhpderaltMGDLISFAWQISQGMQYLAEMKLVHRDLAARNILVAEGRK 887
Cdd:cd14221   73 KGGTLRGIIKSMDSHYP-----------------------WSQRVSFAKDIASGMAYLHSMNIIHRDLNSHNCLVRENKS 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  888 MKISDFGLSRDVYEEDSYVKRSQGRIPVK------------WMAIESLFDHIYTTQSDVWSFGVLLWEIVTLgGNPYPGI 955
Cdd:cd14221  130 VVVADFGLARLMVDEKTQPEGLRSLKKPDrkkrytvvgnpyWMAPEMINGRSYDEKVDVFSFGIVLCEIIGR-VNADPDY 208
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 10862703  956 PPERLFNLLKTGHRMER--PDNCSEEMYRLMLQCWKQEPDKRPVFADISKDLEKM 1008
Cdd:cd14221  209 LPRTMDFGLNVRGFLDRycPPNCPPSFFPIAVLCCDLDPEKRPSFSKLEHWLETL 263
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
730-1008 3.71e-29

Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LIMK2 activation is induced by transforming growth factor-beta l (TGFb-l) and shares the same subcellular location as the cofilin family member twinfilin, which may be its biological substrate. LIMK2 plays a role in spermatogenesis, and may contribute to tumor progression and metastasis formation in some cancer cells. LIMKs phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They act downstream of Rho GTPases and are expressed ubiquitously. As regulators of actin dynamics, they contribute to diverse cellular functions such as cell motility, morphogenesis, differentiation, apoptosis, meiosis, mitosis, and neurite extension. LIMKs contain the LIM (two repeats), PDZ, and catalytic kinase domains. The LIMK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271124 [Multi-domain]  Cd Length: 272  Bit Score: 118.12  E-value: 3.71e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  730 LGEGEFGKVVKATAfhlkgRAgytTVAVKMLKENASPSE--LRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVEYA 807
Cdd:cd14222    1 LGKGFFGQAIKVTH-----KA---TGKVMVMKELIRCDEetQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKRLNLLTEFI 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  808 KYGSLRGFLResrkvgpgylgsggsrnsssldhpDERALTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNILVAEGRK 887
Cdd:cd14222   73 EGGTLKDFLR------------------------ADDPFPWQQKVSFAKGIASGMAYLHSMSIIHRDLNSHNCLIKLDKT 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  888 MKISDFGLSRDVYEED--------SYVKRSQGRIPVK----------WMAIESLFDHIYTTQSDVWSFGVLLWEIVtlgG 949
Cdd:cd14222  129 VVVADFGLSRLIVEEKkkpppdkpTTKKRTLRKNDRKkrytvvgnpyWMAPEMLNGKSYDEKVDIFSFGIVLCEII---G 205
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 10862703  950 NPY--PGIPPERL-FNL-LKTGHRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADISKDLEKM 1008
Cdd:cd14222  206 QVYadPDCLPRTLdFGLnVRLFWEKFVPKDCPPAFFPLAAICCRLEPDSRPAFSKLEDSFEAL 268
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
728-1001 4.43e-29

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Nek family is composed of 11 different mammalian members (Nek1-11) with similarity to the catalytic domain of Aspergillus nidulans NIMA kinase, the founding member of the Nek family, which was identified in a screen for cell cycle mutants that were prevented from entering mitosis. Neks contain a conserved N-terminal catalytic domain and a more divergent C-terminal regulatory region of various sizes and structures. They are involved in the regulation of downstream processes following the activation of Cdc2, and many of their functions are cell cycle-related. They play critical roles in microtubule dynamics during ciliogenesis and mitosis. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270855 [Multi-domain]  Cd Length: 258  Bit Score: 117.18  E-value: 4.43e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  728 KTLGEGEFGKVVKATafHLKGRAGYttVAVKMLKENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVEYA 807
Cdd:cd08215    6 RVIGKGSFGSAYLVR--RKSDGKLY--VLKEIDLSNMSEKEREEALNEVKLLSKLKHPNIVKYYESFEENGKLCIVMEYA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  808 KYGSLRGFLRESRKVGPGYlgsggsrnsssldhPDERALTMgdlisFAwQISQGMQYLAEMKLVHRDLAARNILVAEGRK 887
Cdd:cd08215   82 DGGDLAQKIKKQKKKGQPF--------------PEEQILDW-----FV-QICLALKYLHSRKILHRDLKTQNIFLTKDGV 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  888 MKISDFGLSRdVYEEDSYVKRSQGRIPVkWMAIESLFDHIYTTQSDVWSFGVLLWEIVTL----GGNPYPGipperLFNL 963
Cdd:cd08215  142 VKLGDFGISK-VLESTTDLAKTVVGTPY-YLSPELCENKPYNYKSDIWALGCVLYELCTLkhpfEANNLPA-----LVYK 214
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 10862703  964 LKTGHRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADI 1001
Cdd:cd08215  215 IVKGQYPPIPSQYSSELRDLVNSMLQKDPEKRPSANEI 252
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
723-996 1.16e-28

Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and similar proteins; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include MAPKKs from plants, kinetoplastids, alveolates, and mycetozoa. The MAPKK, LmxPK4, from Leishmania mexicana, is important in differentiation and virulence. Dictyostelium discoideum MEK1 is required for proper chemotaxis; MEK1 null mutants display severe defects in cell polarization and directional movement. Plants contain multiple MAPKKs like other eukaryotes. The Arabidopsis genome encodes for 10 MAPKKs while poplar and rice contain 13 MAPKKs each. The functions of these proteins have not been fully elucidated. There is evidence to suggest that MAPK cascades are involved in plant stress responses. In Arabidopsis, MKK3 plays a role in pathogen signaling; MKK2 is involved in cold and salt stress signaling; MKK4/MKK5 participates in innate immunity; and MKK7 regulates basal and systemic acquired resistance. The MAPKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132954 [Multi-domain]  Cd Length: 264  Bit Score: 116.15  E-value: 1.16e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  723 NLVLGKTLGEGEFGKVVKATafHLKGRAgytTVAVKMLKENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLL 802
Cdd:cd06623    2 DLERVKVLGQGSSGVVYKVR--HKPTGK---IYALKKIHVDGDEEFRKQLLRELKTLRSCESPYVVKCYGAFYKEGEISI 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  803 IVEYAKYGSLRGFLRESRKVGPGYLGsggsrnsssldhpderaltmgdliSFAWQISQGMQYL-AEMKLVHRDLAARNIL 881
Cdd:cd06623   77 VLEYMDGGSLADLLKKVGKIPEPVLA------------------------YIARQILKGLDYLhTKRHIIHRDIKPSNLL 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  882 VAEGRKMKISDFGLSRDV----YEEDSYVkrsqGRIPvkWMAIESLFDHIYTTQSDVWSFGVLLWEIVtLGGNPYPGIPP 957
Cdd:cd06623  133 INSKGEVKIADFGISKVLentlDQCNTFV----GTVT--YMSPERIQGESYSYAADIWSLGLTLLECA-LGKFPFLPPGQ 205
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 10862703  958 ERLFNLLKtgHRMERP------DNCSEEMYRLMLQCWKQEPDKRP 996
Cdd:cd06623  206 PSFFELMQ--AICDGPppslpaEEFSPEFRDFISACLQKDPKKRP 248
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
730-996 6.15e-28

Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of MST1, MST2, and related proteins including Drosophila Hippo and Dictyostelium discoideum Krs1 (kinase responsive to stress 1). MST1/2 and Hippo are involved in a conserved pathway that governs cell contact inhibition, organ size control, and tumor development. MST1 activates the mitogen-activated protein kinases (MAPKs) p38 and c-Jun N-terminal kinase (JNK) through MKK7 and MEKK1 by acting as a MAPK kinase kinase kinase. Activation of JNK by MST1 leads to caspase activation and apoptosis. MST1 has also been implicated in cell proliferation and differentiation. Krs1 may regulate cell growth arrest and apoptosis in response to cellular stress. The MST1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132943 [Multi-domain]  Cd Length: 256  Bit Score: 113.90  E-value: 6.15e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  730 LGEGEFGKVVKATafHLKGRagyTTVAVKMLKENaspSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVEYAKY 809
Cdd:cd06612   11 LGEGSYGSVYKAI--HKETG---QVVAIKVVPVE---EDLQEIIKEISILKQCDSPYIVKYYGSYFKNTDLWIVMEYCGA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  810 GSLRGFLRESRKVgpgylgsggsrnsssldhpderaLTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNILVAEGRKMK 889
Cdd:cd06612   83 GSVSDIMKITNKT-----------------------LTEEEIAAILYQTLKGLEYLHSNKKIHRDIKAGNILLNEEGQAK 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  890 ISDFGLSRDVyeEDSYVKRSQ--GRiPVkWMAIESLFDHIYTTQSDVWSFGVLLWEIVTlGGNPYPGIPPERLFNLLKTG 967
Cdd:cd06612  140 LADFGVSGQL--TDTMAKRNTviGT-PF-WMAPEVIQEIGYNNKADIWSLGITAIEMAE-GKPPYSDIHPMRAIFMIPNK 214
                        250       260       270
                 ....*....|....*....|....*....|.
gi 10862703  968 --HRMERPDNCSEEMYRLMLQCWKQEPDKRP 996
Cdd:cd06612  215 ppPTLSDPEKWSPEFNDFVKKCLVKDPEERP 245
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
717-1006 2.55e-27

Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. C-Raf, also known as Raf-1 or c-Raf-1, is ubiquitously expressed and was the first Raf identified. It was characterized as the acquired oncogene from an acutely transforming murine sarcoma virus (3611-MSV) and the transforming agent from the avian retrovirus MH2. C-Raf-deficient mice embryos die around midgestation with increased apoptosis of embryonic tissues, especially in the fetal liver. One of the main functions of C-Raf is restricting caspase activation to promote survival in response to specific stimuli such as Fas stimulation, macrophage apoptosis, and erythroid differentiation. C-Raf is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. It functions in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. The C-Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271051 [Multi-domain]  Cd Length: 283  Bit Score: 113.20  E-value: 2.55e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  717 WEFPRKNLVLGKTLGEGEFGKVVKATafhlkgraGYTTVAVKMLK-ENASPSELRDLLSEFNVLKQVNHPHVIKLYGACS 795
Cdd:cd14149    7 WEIEASEVMLSTRIGSGSFGTVYKGK--------WHGDVAVKILKvVDPTPEQFQAFRNEVAVLRKTRHVNILLFMGYMT 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  796 QDGpLLLIVEYAKYGSLRGFLresrkvgpgylgsggsrnsssldHPDERALTMGDLISFAWQISQGMQYLAEMKLVHRDL 875
Cdd:cd14149   79 KDN-LAIVTQWCEGSSLYKHL-----------------------HVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDM 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  876 AARNILVAEGRKMKISDFGLS--RDVYEEDSYVKRSQGRIpvKWMAIESLF---DHIYTTQSDVWSFGVLLWEIVTlGGN 950
Cdd:cd14149  135 KSNNIFLHEGLTVKIGDFGLAtvKSRWSGSQQVEQPTGSI--LWMAPEVIRmqdNNPFSFQSDVYSYGIVLYELMT-GEL 211
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 10862703  951 PYPGIpPERLFNLLKTGHRMERPD------NCSEEMYRLMLQCWKQEPDKRPVFADISKDLE 1006
Cdd:cd14149  212 PYSHI-NNRDQIIFMVGRGYASPDlsklykNCPKAMKRLVADCIKKVKEERPLFPQILSSIE 272
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
725-996 2.93e-27

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 117.04  E-value: 2.93e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  725 VLGKTLGEGEFGKVVKATAFHLkGRagytTVAVKMLKEN--ASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLL 802
Cdd:COG0515   10 RILRLLGRGGMGVVYLARDLRL-GR----PVALKVLRPElaADPEARERFRREARALARLNHPNIVRVYDVGEEDGRPYL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  803 IVEYAKYGSLRGFLREsrkvgpgylgsggsrnsssldhpdERALTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNILV 882
Cdd:COG0515   85 VMEYVEGESLADLLRR------------------------RGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILL 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  883 AEGRKMKISDFGLSRDVyeEDSYVKRSQGRI-PVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTlGGNPYPGIPPERLF 961
Cdd:COG0515  141 TPDGRVKLIDFGIARAL--GGATLTQTGTVVgTPGYMAPEQARGEPVDPRSDVYSLGVTLYELLT-GRPPFDGDSPAELL 217
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 10862703  962 nllkTGHRMERP-------DNCSEEMYRLMLQCWKQEPDKRP 996
Cdd:COG0515  218 ----RAHLREPPpppselrPDLPPALDAIVLRALAKDPEERY 255
PK_GC cd13992
Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows ...
730-1008 5.34e-27

Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. Membrane (or particulate) GCs consist of an extracellular ligand-binding domain, a single transmembrane region, and an intracellular tail that contains a PK-like domain, an amphiphatic region and a catalytic GC domain that catalyzes the conversion of GTP into cGMP and pyrophosphate. Membrane GCs act as receptors that transduce an extracellular signal to the intracellular production of cGMP, which has been implicated in many processes including cell proliferation, phototransduction, and muscle contractility, through its downstream effectors such as PKG. The PK-like domain of GCs lack a critical aspartate involved in ATP binding and does not exhibit kinase activity. It functions as a negative regulator of the catalytic GC domain and may also act as a docking site for interacting proteins such as GC-activating proteins. The GC subfamily is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270894 [Multi-domain]  Cd Length: 268  Bit Score: 111.71  E-value: 5.34e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  730 LGEGEFGKvvkaTAFHLKGRagytTVAVKMLKENASPSelRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVEYAKY 809
Cdd:cd13992   11 TGEPKYVK----KVGVYGGR----TVAIKHITFSRTEK--RTILQELNQLKELVHDNLNKFIGICINPPNIAVVTEYCTR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  810 GSLRGFLRESrkvgpgylgsggsrnssslDHPderaltMGDL--ISFAWQISQGMQYLAEMKL-VHRDLAARNILVAEGR 886
Cdd:cd13992   81 GSLQDVLLNR-------------------EIK------MDWMfkSSFIKDIVKGMNYLHSSSIgYHGRLKSSNCLVDSRW 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  887 KMKISDFGLSRdvYEEDSYVKRSQGRIPVK---WMAIE----SLFDHIYTTQSDVWSFGVLLWEIVTLGGnPYPGIPPER 959
Cdd:cd13992  136 VVKLTDFGLRN--LLEEQTNHQLDEDAQHKkllWTAPEllrgSLLEVRGTQKGDVYSFAIILYEILFRSD-PFALEREVA 212
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 10862703  960 LF-NLLKTGHRMERP------DNCSEEMYRLMLQCWKQEPDKRPVFADISKDLEKM 1008
Cdd:cd13992  213 IVeKVISGGNKPFRPelavllDEFPPRLVLLVKQCWAENPEKRPSFKQIKKTLTEN 268
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
728-1008 6.88e-27

Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. A-Raf cooperates with C-Raf in regulating ERK transient phosphorylation that is associated with cyclin D expression and cell cycle progression. Mice deficient in A-Raf are born alive but show neurological and intestinal defects. A-Raf demonstrates low kinase activity to MEK, compared with B- and C-Raf, and may also have alternative functions other than in the ERK signaling cascade. It regulates the M2 type pyruvate kinase, a key glycolytic enzyme. It also plays a role in endocytic membrane trafficking. A-Raf is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. It functions in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. The A-Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271052 [Multi-domain]  Cd Length: 265  Bit Score: 111.26  E-value: 6.88e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  728 KTLGEGEFGKVvkatafhLKGRaGYTTVAVKMLK-ENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGpLLLIVEY 806
Cdd:cd14150    6 KRIGTGSFGTV-------FRGK-WHGDVAVKILKvTEPTPEQLQAFKNEMQVLRKTRHVNILLFMGFMTRPN-FAIITQW 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  807 AKYGSLRGFLresrkvgpgylgsggsrnsssldHPDERALTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNILVAEGR 886
Cdd:cd14150   77 CEGSSLYRHL-----------------------HVTETRFDTMQLIDVARQTAQGMDYLHAKNIIHRDLKSNNIFLHEGL 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  887 KMKISDFGLS--RDVYEEDSYVKRSQGRIpvKWMAIESLF---DHIYTTQSDVWSFGVLLWEIVTlGGNPYPGIpPERLF 961
Cdd:cd14150  134 TVKIGDFGLAtvKTRWSGSQQVEQPSGSI--LWMAPEVIRmqdTNPYSFQSDVYAYGVVLYELMS-GTLPYSNI-NNRDQ 209
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 10862703  962 NLLKTGHRMERPD------NCSEEMYRLMLQCWKQEPDKRPVFADISKDLEKM 1008
Cdd:cd14150  210 IIFMVGRGYLSPDlsklssNCPKAMKRLLIDCLKFKREERPLFPQILVSIELL 262
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
714-1012 1.50e-26

Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase or LOK); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK10/LOK is also called polo-like kinase kinase 1 in Xenopus (xPlkk1). It is highly expressed in lymphocytes and is responsible in regulating leukocyte function associated antigen (LFA-1)-mediated lymphocyte adhesion. It plays a role in regulating the CD28 responsive element in T cells, and may also function as a regulator of polo-like kinase 1 (Plk1), a protein which is overexpressed in multiple tumor types. The STK10 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132975 [Multi-domain]  Cd Length: 292  Bit Score: 110.89  E-value: 1.50e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  714 DPK--WEfprknlVLGKtLGEGEFGKVVKAtafhlKGRAGYTTVAVKMLkENASPSELRDLLSEFNVLKQVNHPHVIKLY 791
Cdd:cd06644    9 DPNevWE------IIGE-LGDGAFGKVYKA-----KNKETGALAAAKVI-ETKSEEELEDYMVEIEILATCNHPYIVKLL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  792 GACSQDGPLLLIVEYAKYGSLRGFLREsrkvgpgylgsggsrnsssLDhpdeRALTMGDLISFAWQISQGMQYLAEMKLV 871
Cdd:cd06644   76 GAFYWDGKLWIMIEFCPGGAVDAIMLE-------------------LD----RGLTEPQIQVICRQMLEALQYLHSMKII 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  872 HRDLAARNILVAEGRKMKISDFGLS----RDVYEEDSYVKRSQgripvkWMA-----IESLFDHIYTTQSDVWSFGVLLW 942
Cdd:cd06644  133 HRDLKAGNVLLTLDGDIKLADFGVSaknvKTLQRRDSFIGTPY------WMApevvmCETMKDTPYDYKADIWSLGITLI 206
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 10862703  943 EIVTLgGNPYPGIPPERLfnLLKTGHR----MERPDNCSEEMYRLMLQCWKQEPDKRPVFADIskdLEKMMVKR 1012
Cdd:cd06644  207 EMAQI-EPPHHELNPMRV--LLKIAKSepptLSQPSKWSMEFRDFLKTALDKHPETRPSAAQL---LEHPFVSS 274
PTKc_Aatyk2 cd05086
Catalytic domain of the Protein Tyrosine Kinase, Apoptosis-associated tyrosine kinase 2; PTKs ...
730-1005 1.62e-26

Catalytic domain of the Protein Tyrosine Kinase, Apoptosis-associated tyrosine kinase 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Aatyk2 is a member of the Aatyk subfamily of proteins, which are receptor kinases containing a transmembrane segment and a long C-terminal cytoplasmic tail with a catalytic domain. Aatyk2 is also called lemur tyrosine kinase 2 (Lmtk2) or brain-enriched kinase (Brek). It is expressed at high levels in early postnatal brain, and has been shown to play a role in nerve growth factor (NGF) signaling. Studies with knockout mice reveal that Aatyk2 is essential for late stage spermatogenesis. Although it is classified as a PTK based on sequence similarity and the phylogenetic tree, Aatyk2 has been functionally characterized as a serine/threonine kinase. The Aatyk2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270669 [Multi-domain]  Cd Length: 271  Bit Score: 110.34  E-value: 1.62e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  730 LGEGEFGKVVKATAFHlkgRAGYTTVAVKMLKENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVEYAKY 809
Cdd:cd05086    5 IGNGWFGKVLLGEIYT---GTSVARVVVKELKASANPKEQDDFLQQGEPYYILQHPNILQCVGQCVEAIPYLLVFEFCDL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  810 GSLRGFLRESRkvgpgylgsggsrnssslDHPDERALTMgDLISFAWQISQGMQYLAEMKLVHRDLAARNILVAEGRKMK 889
Cdd:cd05086   82 GDLKTYLANQQ------------------EKLRGDSQIM-LLQRMACEIAAGLAHMHKHNFLHSDLALRNCYLTSDLTVK 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  890 ISDFGLSRDVYEEDSYVKRSQGRIPVKWMAIE---SLFDHIY----TTQSDVWSFGVLLWEIVTLGGNPYPGIP------ 956
Cdd:cd05086  143 VGDYGIGFSRYKEDYIETDDKKYAPLRWTAPElvtSFQDGLLaaeqTKYSNIWSLGVTLWELFENAAQPYSDLSdrevln 222
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 10862703  957 ---PERLFNLLKTghRMERPdnCSEEMYRLMLQCWkQEPDKRPVFADISKDL 1005
Cdd:cd05086  223 hviKERQVKLFKP--HLEQP--YSDRWYEVLQFCW-LSPEKRPTAEEVHRLL 269
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
728-1001 1.67e-26

Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Chlamydomonas reinhardtii CNK2 has both cilliary and cell cycle functions. It influences flagellar length through promoting flagellar disassembly, and it regulates cell size, through influencing the size threshold at which cells commit to mitosis. This subfamily belongs to the (NIMA)-related kinase (Nek) family, which includes seven different Chlamydomonas Neks (CNKs 1-6 and Fa2). This subfamily includes CNK1, and -2. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270869 [Multi-domain]  Cd Length: 256  Bit Score: 109.79  E-value: 1.67e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  728 KTLGEGEFGKVVKAtafhlKGRAGYTTVAVKMLK-ENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVEY 806
Cdd:cd08530    6 KKLGKGSYGSVYKV-----KRLSDNQVYALKEVNlGSLSQKEREDSVNEIRLLASVNHPNIIRYKEAFLDGNRLCIVMEY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  807 AKYGSLRGFLRESRKVGpgylgsggsrnsssldhpdeRALTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNILVAEGR 886
Cdd:cd08530   81 APFGDLSKLISKRKKKR--------------------RLFPEDDIWRIFIQMLRGLKALHDQKILHRDLKSANILLSAGD 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  887 KMKISDFGLSRDVyeeDSYVKRSQGRIPVkWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLgGNPYPGIPPERLFNLLKT 966
Cdd:cd08530  141 LVKIGDLGISKVL---KKNLAKTQIGTPL-YAAPEVWKGRPYDYKSDIWSLGCLLYEMATF-RPPFEARTMQELRYKVCR 215
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 10862703  967 GHRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADI 1001
Cdd:cd08530  216 GKFPPIPPVYSQDLQQIIRSLLQVNPKKRPSCDKL 250
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
730-1006 1.77e-26

Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TNNI3K, also called cardiac ankyrin repeat kinase (CARK), is a cardiac-specific troponin I-interacting kinase that promotes cardiac myogenesis, improves cardiac performance, and protects the myocardium from ischemic injury. It contains N-terminal ankyrin repeats, a catalytic kinase domain, and a C-terminal serine-rich domain. TNNI3K exerts a disease-accelerating effect on cardiac dysfunction and reduced survival in mouse models of cardiomyopathy. The TNNI3K subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270966 [Multi-domain]  Cd Length: 254  Bit Score: 109.54  E-value: 1.77e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  730 LGEGEFGKVvkatafhLKGRAGYTTVAVKMLKENA--SPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIV-EY 806
Cdd:cd14064    1 IGSGSFGKV-------YKGRCRNKIVAIKRYRANTycSKSDVDMFCREVSILCRLNHPCVIQFVGACLDDPSQFAIVtQY 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  807 AKYGSLRGFLRESRKVgpgylgsggsrnsssldhpderaLTMGDLISFAWQISQGMQYLAEMK--LVHRDLAARNILVAE 884
Cdd:cd14064   74 VSGGSLFSLLHEQKRV-----------------------IDLQSKLIIAVDVAKGMEYLHNLTqpIIHRDLNSHNILLYE 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  885 GRKMKISDFGLSRDV--YEEDSYVKRSQGripVKWMAIEsLFDHI--YTTQSDVWSFGVLLWEIVTlGGNPYPGIPPERL 960
Cdd:cd14064  131 DGHAVVADFGESRFLqsLDEDNMTKQPGN---LRWMAPE-VFTQCtrYSIKADVFSYALCLWELLT-GEIPFAHLKPAAA 205
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 10862703  961 FNLLKTGH-RMERPDNCSEEMYRLMLQCWKQEPDKRPVFADISKDLE 1006
Cdd:cd14064  206 AADMAYHHiRPPIGYSIPKPISSLLMRGWNAEPESRPSFVEIVALLE 252
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
726-996 2.43e-26

Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Mos (or c-Mos) is a germ-cell specific kinase that plays roles in both the release of primary arrest and the induction of secondary arrest in oocytes. It is expressed towards the end of meiosis I and is quickly degraded upon fertilization. It is a component of the cytostatic factor (CSF), which is responsible for metaphase II arrest. In addition, Mos activates a phoshorylation cascade that leads to the activation of the p34 subunit of MPF (mitosis-promoting factor or maturation promoting factor), a cyclin-dependent kinase that is responsible for the release of primary arrest in meiosis I. The Mos subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270881 [Multi-domain]  Cd Length: 265  Bit Score: 109.78  E-value: 2.43e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  726 LGKTLGEGEFGKVVKATafhLKGRagytTVAVKMLKENASPSELRDLL-SEFNVLKqVNHPHVIKLYGA---CSQDGPLL 801
Cdd:cd13979    7 LQEPLGSGGFGSVYKAT---YKGE----TVAVKIVRRRRKNRASRQSFwAELNAAR-LRHENIVRVLAAetgTDFASLGL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  802 LIVEYAKYGSLRGFLRESRKvgpgylgsggsrnsssldhpderALTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNIL 881
Cdd:cd13979   79 IIMEYCGNGTLQQLIYEGSE-----------------------PLPLAHRILISLDIARALRFCHSHGIVHLDVKPANIL 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  882 VAEGRKMKISDFGLSRDVYEEDSYV-KRSQGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTlGGNPYPGIPPERL 960
Cdd:cd13979  136 ISEQGVCKLCDFGCSVKLGEGNEVGtPRSHIGGTYTYRAPELLKGERVTPKADIYSFGITLWQMLT-RELPYAGLRQHVL 214
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 10862703  961 FNLLKTGHRMERPDNCSEEM---YR-LMLQCWKQEPDKRP 996
Cdd:cd13979  215 YAVVAKDLRPDLSGLEDSEFgqrLRsLISRCWSAQPAERP 254
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
731-995 6.60e-26

Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK36, also called Fused (or Fu) kinase, is involved in the Hedgehog signaling pathway. It is activated by the Smoothened (SMO) signal transducer, resulting in the stabilization of GLI transcription factors and the phosphorylation of SUFU to facilitate the nuclear accumulation of GLI. In Drosophila, Fused kinase is maternally required for proper segmentation during embryonic development and for the development of legs and wings during the larval stage. In mice, STK36 is not necessary for embryonic development, although mice deficient in STK36 display growth retardation postnatally. The STK36 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270904 [Multi-domain]  Cd Length: 253  Bit Score: 108.11  E-value: 6.60e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  731 GEGEFGKVvkatafhLKGRAGYT--TVAVKML-KENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVEYA 807
Cdd:cd14002   10 GEGSFGKV-------YKGRRKYTgqVVALKFIpKRGKSEKELRNLRQEIEILRKLNHPNIIEMLDSFETKKEFVVVTEYA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  808 KyGSLRGFLResrkvgpgylgsggsrnsssldhpDERALTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNILVAEGRK 887
Cdd:cd14002   83 Q-GELFQILE------------------------DDGTLPEEEVRSIAKQLVSALHYLHSNRIIHRDMKPQNILIGKGGV 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  888 MKISDFGLSRDVyEEDSYVKRSQGRIPVkWMAIESLFDHIYTTQSDVWSFGVLLWEIVTlggnpypGIPP---ERLFNLL 964
Cdd:cd14002  138 VKLCDFGFARAM-SCNTLVLTSIKGTPL-YMAPELVQEQPYDHTADLWSLGCILYELFV-------GQPPfytNSIYQLV 208
                        250       260       270
                 ....*....|....*....|....*....|...
gi 10862703  965 K--TGHRMERPDNCSEEMYRLMLQCWKQEPDKR 995
Cdd:cd14002  209 QmiVKDPVKWPSNMSPEFKSFLQGLLNKDPSKR 241
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
727-1008 9.28e-26

Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain, and a C-terminal domain; IRAK-4 lacks the C-terminal domain. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK4 plays a critical role in NFkB activation by its interaction with MyD88, which acts as a scaffold that enables IRAK4 to phosphorylate and activate IRAK1 and/or IRAK2. It also plays an important role in type I IFN production induced by TLR7/8/9. The IRAK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271060 [Multi-domain]  Cd Length: 288  Bit Score: 108.74  E-value: 9.28e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  727 GKTLGEGEFGKVvkatafhLKGRAGYTTVAVKMLKE--NASPSELRDLL-SEFNVLKQVNHPHVIKLYGaCSQDGP-LLL 802
Cdd:cd14158   20 GNKLGEGGFGVV-------FKGYINDKNVAVKKLAAmvDISTEDLTKQFeQEIQVMAKCQHENLVELLG-YSCDGPqLCL 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  803 IVEYAKYGSLRGFLresrkvgpgylgsggsrnsSSLDHpdERALTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNILV 882
Cdd:cd14158   92 VYTYMPNGSLLDRL-------------------ACLND--TPPLSWHMRCKIAQGTANGINYLHENNHIHRDIKSANILL 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  883 AEGRKMKISDFGLSRDVYEEDSYVKRSQGRIPVKWMAIESLFDHIyTTQSDVWSFGVLLWEIVTlggnpypGIPP---ER 959
Cdd:cd14158  151 DETFVPKISDFGLARASEKFSQTIMTERIVGTTAYMAPEALRGEI-TPKSDIFSFGVVLLEIIT-------GLPPvdeNR 222
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 10862703  960 LFNLLKTgHRMERPD------------------NCSEEMYRLMLQCWKQEPDKRPVFADISKDLEKM 1008
Cdd:cd14158  223 DPQLLLD-IKEEIEDeektiedyvdkkmgdwdsTSIEAMYSVASQCLNDKKNRRPDIAKVQQLLQEL 288
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
727-996 1.58e-25

Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of plant MAPK kinase kinases (MAPKKKs) including Arabidopsis thaliana MEKK1 and MAPKKK3. Arabidopsis thaliana MEKK1 activates MPK4, a MAPK that regulates systemic acquired resistance. MEKK1 also participates in the regulation of temperature-sensitive and tissue-specific cell death. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The plant MEKK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270802 [Multi-domain]  Cd Length: 259  Bit Score: 107.10  E-value: 1.58e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  727 GKTLGEGEFGKVVKAtafhLKGRAGyTTVAVKMLKENASPSELRD----LLSEFNVLKQVNHPHVIKLYGACSQDGPLLL 802
Cdd:cd06632    5 GQLLGSGSFGSVYEG----FNGDTG-DFFAVKEVSLVDDDKKSREsvkqLEQEIALLSKLRHPNIVQYYGTEREEDNLYI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  803 IVEYAKYGSLRGFLResrKVGPgylgsggsrnsssLDHPDERALTMgdlisfawQISQGMQYLAEMKLVHRDLAARNILV 882
Cdd:cd06632   80 FLEYVPGGSIHKLLQ---RYGA-------------FEEPVIRLYTR--------QILSGLAYLHSRNTVHRDIKGANILV 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  883 AEGRKMKISDFGLSRDVyEEDSYVKRSQGRipVKWMAIESL--FDHIYTTQSDVWSFGVLLWEIVTlGGNPYPGIPP-ER 959
Cdd:cd06632  136 DTNGVVKLADFGMAKHV-EAFSFAKSFKGS--PYWMAPEVImqKNSGYGLAVDIWSLGCTVLEMAT-GKPPWSQYEGvAA 211
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 10862703  960 LFNLLKTGHRMERPDNCSEEMYRLMLQCWKQEPDKRP 996
Cdd:cd06632  212 IFKIGNSGELPPIPDHLSPDAKDFIRLCLQRDPEDRP 248
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
730-1012 8.24e-25

Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TESK proteins phosphorylate cofilin and induce actin cytoskeletal reorganization. In the Drosphila eye, TESK is required for epithelial cell organization. Mammals contain two TESK proteins, TESK1 and TESK2, which are highly expressed in testis and play roles in spermatogenesis. TESK1 is found in testicular germ cells while TESK2 is expressed mainly in nongerminal Sertoli cells. TESK1 is stimulated by integrin-mediated signaling pathways. It regulates cell spreading and focal adhesion formation. The TESK subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271057 [Multi-domain]  Cd Length: 253  Bit Score: 104.86  E-value: 8.24e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  730 LGEGEFGKVVKATafHlkgragYTTVAVKMLKENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVEYAKY 809
Cdd:cd14155    1 IGSGFFSEVYKVR--H------RTSGQVMALKMNTLSSNRANMLREVQLMNRLSHPNILRFMGVCVHQGQLHALTEYING 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  810 GSLRGFLrESRKVgpgylgsggsrnsssldhpderaLTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNILV---AEGR 886
Cdd:cd14155   73 GNLEQLL-DSNEP-----------------------LSWTVRVKLALDIARGLSYLHSKGIFHRDLTSKNCLIkrdENGY 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  887 KMKISDFGLSRDVYEEDSYVKRsqgrIPV----KWMAIESLFDHIYTTQSDVWSFGVLLWEIVT-LGGNPyPGIPPERLF 961
Cdd:cd14155  129 TAVVGDFGLAEKIPDYSDGKEK----LAVvgspYWMAPEVLRGEPYNEKADVFSYGIILCEIIArIQADP-DYLPRTEDF 203
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 10862703  962 NLLKTGHRMERPDnCSEEMYRLMLQCWKQEPDKRPVFADISKDLEKMMVKR 1012
Cdd:cd14155  204 GLDYDAFQHMVGD-CPPDFLQLAFNCCNMDPKSRPSFHDIVKTLEEILEKL 253
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
728-1003 8.29e-25

Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MST3 phosphorylates the STK NDR and may play a role in cell cycle progression and cell morphology. It may also regulate paxillin and consequently, cell migration. MST3 is present in human placenta, where it plays an essential role in the oxidative stress-induced apoptosis of trophoblasts in normal spontaneous delivery. Dysregulation of trophoblast apoptosis may result in pregnancy complications such as preeclampsia and intrauterine growth retardation. The MST3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270809 [Multi-domain]  Cd Length: 277  Bit Score: 105.54  E-value: 8.29e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  728 KTLGEGEFGKVVKATAFHLKgragyTTVAVKMLKENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVEYA 807
Cdd:cd06641   10 EKIGKGSFGEVFKGIDNRTQ-----KVVAIKIIDLEEAEDEIEDIQQEITVLSQCDSPYVTKYYGSYLKDTKLWIIMEYL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  808 KYGSLRGFLResrkvgPGYLgsggsrnsssldhpDERALTmgdliSFAWQISQGMQYLAEMKLVHRDLAARNILVAEGRK 887
Cdd:cd06641   85 GGGSALDLLE------PGPL--------------DETQIA-----TILREILKGLDYLHSEKKIHRDIKAANVLLSEHGE 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  888 MKISDFGLSRDVyeEDSYVKRSQGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTlGGNPYPGIPPERLFNLLKTG 967
Cdd:cd06641  140 VKLADFGVAGQL--TDTQIKRN*FVGTPFWMAPEVIKQSAYDSKADIWSLGITAIELAR-GEPPHSELHPMKVLFLIPKN 216
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 10862703  968 HRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADISK 1003
Cdd:cd06641  217 NPPTLEGNYSKPLKEFVEACLNKEPSFRPTAKELLK 252
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
725-1011 1.17e-24

The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. CaMKII is a signaling molecule that translates upstream calcium and reactive oxygen species (ROS) signals into downstream responses that play important roles in synaptic function and cardiovascular physiology. CAMKIV is implicated in regulating several transcription factors like CREB, MEF2, and retinoid orphan receptors, as well as in T-cell development and signaling. The CAMK family also consists of other related kinases including the Phosphorylase kinase Gamma subunit (PhKG), the C-terminal kinase domains of Ribosomal S6 kinase (RSK) and Mitogen and stress-activated kinase (MSK), Doublecortin-like kinase (DCKL), and the MAPK-activated protein kinases MK2, MK3, and MK5, among others. The CAMK family is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270687 [Multi-domain]  Cd Length: 258  Bit Score: 104.48  E-value: 1.17e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  725 VLGKTLGEGEFGKVVKAtafhlKGRAGYTTVAVKML-KENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLI 803
Cdd:cd05117    3 ELGKVLGRGSFGVVRLA-----VHKKTGEEYAVKIIdKKKLKSEDEEMLRREIEILKRLDHPNIVKLYEVFEDDKNLYLV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  804 VEYAKYGSL------RGFLREsrkvgpgylgsggsrnsssldhpDERALTMgdlisfaWQISQGMQYLAEMKLVHRDLAA 877
Cdd:cd05117   78 MELCTGGELfdrivkKGSFSE-----------------------REAAKIM-------KQILSAVAYLHSQGIVHRDLKP 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  878 RNILVAEGRK---MKISDFGLSRdVYEEDSYVKRSQGRIpvKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTlggnpypG 954
Cdd:cd05117  128 ENILLASKDPdspIKIIDFGLAK-IFEEGEKLKTVCGTP--YYVAPEVLKGKGYGKKCDIWSLGVILYILLC-------G 197
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 10862703  955 IPPerlFNllktghrmerpDNCSEEMYRLMLQC-WKQEPdkrPVFADIS---KDL-EKMMVK 1011
Cdd:cd05117  198 YPP---FY-----------GETEQELFEKILKGkYSFDS---PEWKNVSeeaKDLiKRLLVV 242
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
730-1002 2.08e-24

Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RIP1 harbors a C-terminal Death domain (DD), which binds death receptors (DRs) including TNF receptor 1, Fas, TNF-related apoptosis-inducing ligand receptor 1 (TRAILR1), and TRAILR2. It also interacts with other DD-containing adaptor proteins such as TRADD and FADD. RIP1 can also recruit other kinases including MEKK1, MEKK3, and RIP3 through an intermediate domain (ID) that bears a RIP homotypic interaction motif (RHIM). RIP1 plays a crucial role in determining a cell's fate, between survival or death, following exposure to stress signals. It is important in the signaling of NF-kappaB and MAPKs, and it links DR-associated signaling to reactive oxygen species (ROS) production. Abnormal RIP1 function may result in ROS accummulation affecting inflammatory responses, innate immunity, stress responses, and cell survival. RIP kinases serve as essential sensors of cellular stress. The RIP1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270929 [Multi-domain]  Cd Length: 267  Bit Score: 104.12  E-value: 2.08e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  730 LGEGEFGKVvkATAFHlkgrAGYTTVAVKMLKENASPSELRD-LLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVEYAK 808
Cdd:cd14027    1 LDSGGFGKV--SLCFH----RTQGLVVLKTVYTGPNCIEHNEaLLEEGKMMNRLRHSRVVKLLGVILEEGKYSLVMEYME 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  809 YGSLRGFLResrKVgpgylgsggsrnsssldhpdERALTMGDliSFAWQISQGMQYLAEMKLVHRDLAARNILVAEGRKM 888
Cdd:cd14027   75 KGNLMHVLK---KV--------------------SVPLSVKG--RIILEIIEGMAYLHGKGVIHKDLKPENILVDNDFHI 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  889 KISDFGL------SRDVYEEDSYVKRSQGRIP-----VKWMAIESLFD-HIYTTQ-SDVWSFGVLLWEIVTlGGNPYP-G 954
Cdd:cd14027  130 KIADLGLasfkmwSKLTKEEHNEQREVDGTAKknagtLYYMAPEHLNDvNAKPTEkSDVYSFAIVLWAIFA-NKEPYEnA 208
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 10862703  955 IPPERLFNLLKTGHR---MERPDNCSEEMYRLMLQCWKQEPDKRPVFADIS 1002
Cdd:cd14027  209 INEDQIIMCIKSGNRpdvDDITEYCPREIIDLMKLCWEANPEARPTFPGIE 259
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
730-995 2.16e-24

Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent Protein Kinase Kinase, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Both LKB1 and CaMKKs can phosphorylate and activate AMP-activated protein kinase (AMPK). LKB1, also called STK11, serves as a master upstream kinase that activates AMPK and most AMPK-like kinases. LKB1 and AMPK are part of an energy-sensing pathway that links cell energy to metabolism and cell growth. They play critical roles in the establishment and maintenance of cell polarity, cell proliferation, cytoskeletal organization, as well as T-cell metabolism, including T-cell development, homeostasis, and effector function. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMPK. Vertebrates contain two CaMKKs, CaMKK1 (or alpha) and CaMKK2 (or beta). CaMKK1 is involved in the regulation of glucose uptake in skeletal muscles. CaMKK2 is involved in regulating energy balance, glucose metabolism, adiposity, hematopoiesis, inflammation, and cancer. The LKB1/CaMKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270910 [Multi-domain]  Cd Length: 267  Bit Score: 103.79  E-value: 2.16e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  730 LGEGEFGKVVKAT-----------AFH---LKGRAGYTTVAVKmlKENAspseLRDLLSEFNVLKQVNHPHVIKLYGACs 795
Cdd:cd14008    1 LGRGSFGKVKLALdtetgqlyaikIFNksrLRKRREGKNDRGK--IKNA----LDDVRREIAIMKKLDHPNIVRLYEVI- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  796 qDGP----LLLIVEYAKYGSLrgflresrkvgpgylgsggsrnsSSLDHPDER-ALTMGDLISFAWQISQGMQYLAEMKL 870
Cdd:cd14008   74 -DDPesdkLYLVLEYCEGGPV-----------------------MELDSGDRVpPLPEETARKYFRDLVLGLEYLHENGI 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  871 VHRDLAARNILVAEGRKMKISDFGLSRDVYEEDSYVKRSQGRiPVkWMAIEsLFDHIYTTQS----DVWSFGVLLWEIVT 946
Cdd:cd14008  130 VHRDIKPENLLLTADGTVKISDFGVSEMFEDGNDTLQKTAGT-PA-FLAPE-LCDGDSKTYSgkaaDIWALGVTLYCLVF 206
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 10862703  947 -----LGGNPYpgippeRLFNLLKTGHRM-ERPDNCSEEMYRLMLQCWKQEPDKR 995
Cdd:cd14008  207 grlpfNGDNIL------ELYEAIQNQNDEfPIPPELSPELKDLLRRMLEKDPEKR 255
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
726-1001 2.29e-24

Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Aurora kinases are key regulators of mitosis and are essential for the accurate and equal division of genomic material from parent to daughter cells. Yeast contains only one Aurora kinase while most higher eukaryotes have two. Vertebrates contain at least 2 Aurora kinases (A and B); mammals contains a third Aurora kinase gene (C). Aurora-A regulates cell cycle events from the late S-phase through the M-phase including centrosome maturation, mitotic entry, centrosome separation, spindle assembly, chromosome alignment, cytokinesis, and mitotic exit. Aurora-A activation depends on its autophosphorylation and binding to the microtubule-associated protein TPX2. Aurora-B is most active at the transition during metaphase to the end of mitosis. It is critical for accurate chromosomal segregation, cytokinesis, protein localization to the centrosome and kinetochore, correct microtubule-kinetochore attachments, and regulation of the mitotic checkpoint. Aurora-C is mainly expressed in meiotically dividing cells; it was originally discovered in mice as a testis-specific STK called Aie1. Both Aurora-B and -C are chromosomal passenger proteins that can form complexes with INCENP and survivin, and they may have redundant cellular functions. The Aurora subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270909 [Multi-domain]  Cd Length: 253  Bit Score: 103.32  E-value: 2.29e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  726 LGKTLGEGEFGKVVKATafHLKGRagyTTVAVKMLkenaSPSELRDLLSEFNVLKQV------NHPHVIKLYGACSQDGP 799
Cdd:cd14007    4 IGKPLGKGKFGNVYLAR--EKKSG---FIVALKVI----SKSQLQKSGLEHQLRREIeiqshlRHPNILRLYGYFEDKKR 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  800 LLLIVEYAKYGSLRGFLRESRKVgpgylgsggsrnsssldhPDERALTmgdlisFAWQISQGMQYLAEMKLVHRDLAARN 879
Cdd:cd14007   75 IYLILEYAPNGELYKELKKQKRF------------------DEKEAAK------YIYQLALALDYLHSKNIIHRDIKPEN 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  880 ILVAEGRKMKISDFGLSrdVYEEDSyvKRSQGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTlGGNPYPGIPPER 959
Cdd:cd14007  131 ILLGSNGELKLADFGWS--VHAPSN--RRKTFCGTLDYLPPEMVEGKEYDYKVDIWSLGVLCYELLV-GKPPFESKSHQE 205
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 10862703  960 LFNLLKTGHrMERPDNCSEEMYRLMLQCWKQEPDKRPVFADI 1001
Cdd:cd14007  206 TYKRIQNVD-IKFPSSVSPEAKDLISKLLQKDPSKRLSLEQV 246
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
722-1020 2.46e-24

Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include the MAPKKs Byr1 from Schizosaccharomyces pombe, FUZ7 from Ustilago maydis, and related proteins. Byr1 phosphorylates its downstream target, the MAPK Spk1, and is regulated by the MAPKK kinase Byr2. The Spk1 cascade is pheromone-responsive and is essential for sporulation and sexual differentiation in fission yeast. FUZ7 phosphorylates and activates its target, the MAPK Crk1, which is required in mating and virulence in U. maydis. MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The Byr-1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270792 [Multi-domain]  Cd Length: 286  Bit Score: 104.44  E-value: 2.46e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  722 KNLVLGKTLGEGEFGKVVKATafHLKGRagyTTVAVKMLKENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLL 801
Cdd:cd06620    5 QDLETLKDLGAGNGGSVSKVL--HIPTG---TIMAKKVIHIDAKSSVRKQILRELQILHECHSPYIVSFYGAFLNENNNI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  802 LI-VEYAKYGSLRGFLresRKVGPgylgsggsrnsssldhpdERALTMGDlISFAwqISQGMQYL-AEMKLVHRDLAARN 879
Cdd:cd06620   80 IIcMEYMDCGSLDKIL---KKKGP------------------FPEEVLGK-IAVA--VLEGLTYLyNVHRIIHRDIKPSN 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  880 ILVAEGRKMKISDFGLSRDVYEE--DSYVKRSQgripvkWMAIESLFDHIYTTQSDVWSFGVLLWEIVTlGGNPYPGIP- 956
Cdd:cd06620  136 ILVNSKGQIKLCDFGVSGELINSiaDTFVGTST------YMSPERIQGGKYSVKSDVWSLGLSIIELAL-GEFPFAGSNd 208
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 10862703  957 -------PERLFNLLKT-----GHRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADISKDLEKMMVKRRDYLDLAA 1020
Cdd:cd06620  209 dddgyngPMGILDLLQRivnepPPRLPKDRIFPKDLRDFVDRCLLKDPRERPSPQLLLDHDPFIQAVRASDVDLRA 284
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
727-1003 2.88e-24

Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein Kinase Kinase Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include the MAPKKKs Schizosaccharomyces pombe Byr2, Saccharomyces cerevisiae and Cryptococcus neoformans Ste11, and related proteins. They contain an N-terminal SAM (sterile alpha-motif) domain, which mediates protein-protein interaction, and a C-terminal catalytic domain. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Fission yeast Byr2 is regulated by Ras1. It responds to pheromone signaling and controls mating through the MAPK pathway. Budding yeast Ste11 functions in MAPK cascades that regulate mating, high osmolarity glycerol, and filamentous growth responses. The Byr2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270798 [Multi-domain]  Cd Length: 267  Bit Score: 103.77  E-value: 2.88e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  727 GKTLGEGEFGKVVKAtafhLKGRAGyTTVAVKMLKENASPSELRD--------LLSEFNVLKQVNHPHVIKLYGACSQDG 798
Cdd:cd06628    5 GALIGSGSFGSVYLG----MNASSG-ELMAVKQVELPSVSAENKDrkksmldaLQREIALLRELQHENIVQYLGSSSDAN 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  799 PLLLIVEYAKYGSLRGFLRESrkvgpGYLgsggsrnsssldhpdERALTMgdliSFAWQISQGMQYLAEMKLVHRDLAAR 878
Cdd:cd06628   80 HLNIFLEYVPGGSVATLLNNY-----GAF---------------EESLVR----NFVRQILKGLNYLHNRGIIHRDIKGA 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  879 NILVAEGRKMKISDFGLSRDVyEEDSYVKRSQGRIP-----VKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTlGGNPYP 953
Cdd:cd06628  136 NILVDNKGGIKISDFGISKKL-EANSLSTKNNGARPslqgsVFWMAPEVVKQTSYTRKADIWSLGCLVVEMLT-GTHPFP 213
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 10862703  954 GIppERLFNLLKTGH--RMERPDNCSEEMYRLMLQCWKQEPDKRPVFADISK 1003
Cdd:cd06628  214 DC--TQMQAIFKIGEnaSPTIPSNISSEARDFLEKTFEIDHNKRPTADELLK 263
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
730-1004 2.89e-24

Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of the subfamily include SLK, STK10 (also called LOK for Lymphocyte-Oriented Kinase), SmSLK (Schistosoma mansoni SLK), and related proteins. SLK promotes apoptosis through apoptosis signal-regulating kinase 1 (ASK1) and the mitogen-activated protein kinase (MAPK) p38. It also plays a role in mediating actin reorganization. STK10 is responsible in regulating the CD28 responsive element in T cells, as well as leukocyte function associated antigen (LFA-1)-mediated lymphocyte adhesion. SmSLK is capable of activating the MAPK Jun N-terminal kinase (JNK) pathway in human embryonic kidney cells as well as in Xenopus oocytes. It may participate in regulating MAPK cascades during host-parasite interactions. The SLK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132942 [Multi-domain]  Cd Length: 280  Bit Score: 104.05  E-value: 2.89e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  730 LGEGEFGKVVKAtafhlKGRAGYTTVAVKMLKENASpSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVEYAKY 809
Cdd:cd06611   13 LGDGAFGKVYKA-----QHKETGLFAAAKIIQIESE-EELEDFMVEIDILSECKHPNIVGLYEAYFYENKLWILIEFCDG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  810 GSLRGFLRESrkvgpgylgsggsrnsssldhpdERALTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNILVAEGRKMK 889
Cdd:cd06611   87 GALDSIMLEL-----------------------ERGLTEPQIRYVCRQMLEALNFLHSHKVIHRDLKAGNILLTLDGDVK 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  890 ISDFGLSRDVYEEDSyvKRSQGRIPVKWMA-----IESLFDHIYTTQSDVWSFGVLLWEIVTlGGNPYPGIPPER-LFNL 963
Cdd:cd06611  144 LADFGVSAKNKSTLQ--KRDTFIGTPYWMApevvaCETFKDNPYDYKADIWSLGITLIELAQ-MEPPHHELNPMRvLLKI 220
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 10862703  964 LKTGH-RMERPDNCSEEMYRLMLQCWKQEPDKRPVFADISKD 1004
Cdd:cd06611  221 LKSEPpTLDQPSKWSSSFNDFLKSCLVKDPDDRPTAAELLKH 262
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
730-1008 8.67e-24

Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. This group is composed of uncharacterized proteins with similarity to LIMK and Testicular or testis-specific protein kinase (TESK). LIMKs are characterized as serine/threonine kinases (STKs) while TESKs are dual-specificity protein kinases. Both LIMK and TESK phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They are implicated in many cellular functions including cell spreading, motility, morphogenesis, meiosis, mitosis, and spermatogenesis. The LIMK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271058 [Multi-domain]  Cd Length: 256  Bit Score: 101.83  E-value: 8.67e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  730 LGEGEFGKVVKATAfhlkgRAGYTTVAVKMLKENAspsELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVEYAKY 809
Cdd:cd14156    1 IGSGFFSKVYKVTH-----GATGKVMVVKIYKNDV---DQHKIVREISLLQKLSHPNIVRYLGICVKDEKLHPILEYVSG 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  810 GSLRGFLRESrkvgpgylgsggsrnsssldhpdERALTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNILV---AEGR 886
Cdd:cd14156   73 GCLEELLARE-----------------------ELPLSWREKVELACDISRGMVYLHSKNIYHRDLNSKNCLIrvtPRGR 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  887 KMKISDFGLSRDVyeedsyvkrsqGRIPVK-------------WMAIESLFDHIYTTQSDVWSFGVLLWEIVT-LGGNPy 952
Cdd:cd14156  130 EAVVTDFGLAREV-----------GEMPANdperklslvgsafWMAPEMLRGEPYDRKVDVFSFGIVLCEILArIPADP- 197
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 10862703  953 PGIPPERLFNLLKTGHRmERPDNCSEEMYRLMLQCWKQEPDKRPVFADISKDLEKM 1008
Cdd:cd14156  198 EVLPRTGDFGLDVQAFK-EMVPGCPEPFLDLAASCCRMDAFKRPSFAELLDELEDI 252
PK_ILK cd14057
Pseudokinase domain of Integrin Linked Kinase; The pseudokinase domain shows similarity to ...
747-1008 9.05e-24

Pseudokinase domain of Integrin Linked Kinase; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. ILK contains N-terminal ankyrin repeats, a Pleckstrin Homology (PH) domain, and a C-terminal pseudokinase domain. It is a component of the IPP (ILK/PINCH/Parvin) complex that couples beta integrins to the actin cytoskeleton, and plays important roles in cell adhesion, spreading, invasion, and migration. ILK was initially thought to be an active kinase despite the lack of key conserved residues because of in vitro studies showing that it can phosphorylate certain protein substrates. However, in vivo experiments in Caenorhabditis elegans, Drosophila melanogaster, and mice (ILK-null and knock-in) proved that ILK is not an active kinase. In addition to actin cytoskeleton regulation, ILK also influences the microtubule network and mitotic spindle orientation. The pseudokinase domain of ILK binds several adaptor proteins including the parvins and paxillin. The ILK subfamily is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270959 [Multi-domain]  Cd Length: 251  Bit Score: 101.80  E-value: 9.05e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  747 KGRAGYTTVAVKMLK-ENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVEYAKYGSLRGFLRESRKVgpg 825
Cdd:cd14057   13 KGRWQGNDIVAKILKvRDVTTRISRDFNEEYPRLRIFSHPNVLPVLGACNSPPNLVVISQYMPYGSLYNVLHEGTGV--- 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  826 ylgsggsrnssSLDHpderaltmGDLISFAWQISQGMQYLAEMK-LVHR-DLAARNILVAEGRKMKISdfglSRDVyeed 903
Cdd:cd14057   90 -----------VVDQ--------SQAVKFALDIARGMAFLHTLEpLIPRhHLNSKHVMIDEDMTARIN----MADV---- 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  904 SYVKRSQGRI--PVkWMAIESL---FDHIYTTQSDVWSFGVLLWEIVTLgGNPYPGIPP-ERLFNLLKTGHRMERPDNCS 977
Cdd:cd14057  143 KFSFQEPGKMynPA-WMAPEALqkkPEDINRRSADMWSFAILLWELVTR-EVPFADLSNmEIGMKIALEGLRVTIPPGIS 220
                        250       260       270
                 ....*....|....*....|....*....|.
gi 10862703  978 EEMYRLMLQCWKQEPDKRPVFADISKDLEKM 1008
Cdd:cd14057  221 PHMCKLMKICMNEDPGKRPKFDMIVPILEKM 251
STKc_RIP4_like cd14025
Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar ...
730-1011 1.49e-23

Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of RIP4, ankyrin (ANK) repeat and kinase domain containing 1 (ANKK1), and similar proteins, all of which harbor C-terminal ANK repeats. RIP4, also called Protein Kinase C-associated kinase (PKK), regulates keratinocyte differentiation and cutaneous inflammation. It activates NF-kappaB and is important in the survival of diffuse large B-cell lymphoma cells. The ANKK1 protein, also called PKK2, has not been studied extensively. The ANKK1 gene, located less than 10kb downstream of the D2 dopamine receptor (DRD2) locus, is altered in the Taq1 A1 polymorphism, which is related to a reduced DRD2 binding affinity and consequently, to mental disorders. The RIP4-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270927 [Multi-domain]  Cd Length: 267  Bit Score: 101.42  E-value: 1.49e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  730 LGEGEFGKVVKATAFHLKgragyTTVAVKMLKE-NASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQdgPLLLIVEYAK 808
Cdd:cd14025    4 VGSGGFGQVYKVRHKHWK-----TWLAIKCPPSlHVDDSERMELLEEAKKMEMAKFRHILPVYGICSE--PVGLVMEYME 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  809 YGSLRGFLREsrkvgpgylgsggsrnsssldHPderalTMGDL-ISFAWQISQGMQYLAEMK--LVHRDLAARNILVAEG 885
Cdd:cd14025   77 TGSLEKLLAS---------------------EP-----LPWELrFRIIHETAVGMNFLHCMKppLLHLDLKPANILLDAH 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  886 RKMKISDFGLSRdvYEEDSY---VKRSQGRIPVKWMAIESLF--DHIYTTQSDVWSFGVLLWEIVTlGGNPYPGiPPERL 960
Cdd:cd14025  131 YHVKISDFGLAK--WNGLSHshdLSRDGLRGTIAYLPPERFKekNRCPDTKHDVYSFAIVIWGILT-QKKPFAG-ENNIL 206
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  961 FNLLKT--GHRME-------RPDNCSEeMYRLMLQCWKQEPDKRPVFADISKDLEKMMVK 1011
Cdd:cd14025  207 HIMVKVvkGHRPSlspiprqRPSECQQ-MICLMKRCWDQDPRKRPTFQDITSETENLLSL 265
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
725-1004 1.54e-23

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 11; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek11 is involved, through direct phosphorylation, in regulating the degradation of Cdc25A (Cell Division Cycle 25 homolog A), which plays a role in cell cycle progression and in activating cyclin dependent kinases. Nek11 is activated by CHK1 (CHeckpoint Kinase 1) and may be involved in the G2/M checkpoint. Nek11 may also play a role in the S-phase checkpoint as well as in DNA replication and genotoxic stress responses. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270861 [Multi-domain]  Cd Length: 260  Bit Score: 101.35  E-value: 1.54e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  725 VLGKTLGEGEFGkvvkaTAFHLKGRAGYTTVAVKMLKE----NASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPL 800
Cdd:cd08222    3 RVVRKLGSGNFG-----TVYLVSDLKATADEELKVLKEisvgELQPDETVDANREAKLLSKLDHPAIVKFHDSFVEKESF 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  801 LLIVEYAKYGSLRGFLRESRKVGpgylgsggsrnssslDHPDERALtmgdlisFAW--QISQGMQYLAEMKLVHRDLAAR 878
Cdd:cd08222   78 CIVTEYCEGGDLDDKISEYKKSG---------------TTIDENQI-------LDWfiQLLLAVQYMHERRILHRDLKAK 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  879 NILVAEGrKMKISDFGLSRDVYEEDSYVKRSQGrIPVkWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLgGNPYPGippE 958
Cdd:cd08222  136 NIFLKNN-VIKVGDFGISRILMGTSDLATTFTG-TPY-YMSPEVLKHEGYNSKSDIWSLGCILYEMCCL-KHAFDG---Q 208
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 10862703  959 RLFNLLKT---GHRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADISKD 1004
Cdd:cd08222  209 NLLSVMYKiveGETPSLPDKYSKELNAIYSRMLNKDPALRPSAAEILKI 257
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
728-1009 1.55e-23

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase Kinase; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MAPKKs are dual-specificity PKs that phosphorylate their downstream targets, MAPKs, at specific threonine and tyrosine residues. The MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The pathways involve a triple kinase core cascade comprising the MAPK, which is phosphorylated and activated by a MAPK kinase (MAPKK or MKK or MAP2K), which itself is phosphorylated and activated by a MAPKK kinase (MAPKKK or MKKK or MAP3K). There are three MAPK subfamilies: extracellular signal-regulated kinase (ERK), c-Jun N-terminal kinase (JNK), and p38. In mammalian cells, there are seven MAPKKs (named MKK1-7) and 20 MAPKKKs. Each MAPK subfamily can be activated by at least two cognate MAPKKs and by multiple MAPKKKs. The MAPKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270782 [Multi-domain]  Cd Length: 265  Bit Score: 101.27  E-value: 1.55e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  728 KTLGEGEFGKVVKAtafhlKGRAGYTTVAVKMLKENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVEYA 807
Cdd:cd06605    7 GELGEGNGGVVSKV-----RHRPSGQIMAVKVIRLEIDEALQKQILRELDVLHKCNSPYIVGFYGAFYSEGDISICMEYM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  808 KYGSLRGFLRESRKVGPGYLGSggsrnsssldhpderaltmgdlISFAwqISQGMQYLAE-MKLVHRDLAARNILVAEGR 886
Cdd:cd06605   82 DGGSLDKILKEVGRIPERILGK----------------------IAVA--VVKGLIYLHEkHKIIHRDVKPSNILVNSRG 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  887 KMKISDFGLSRDVYeeDSYVKRSQGRIPvkWMAIESLFDHIYTTQSDVWSFGVLLWEIVTlGGNPYPGI---PPERLFNL 963
Cdd:cd06605  138 QVKLCDFGVSGQLV--DSLAKTFVGTRS--YMAPERISGGKYTVKSDIWSLGLSLVELAT-GRFPYPPPnakPSMMIFEL 212
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 10862703  964 LKTGHRMERP----DNCSEEMYRLMLQCWKQEPDKRPvfadiskDLEKMM 1009
Cdd:cd06605  213 LSYIVDEPPPllpsGKFSPDFQDFVSQCLQKDPTERP-------SYKELM 255
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
728-1030 1.60e-23

N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. Mammals possess four RSK isoforms (RSK1-4) from distinct genes. RSK proteins are also referred to as MAP kinase-activated protein kinases (MAPKAPKs), p90-RSKs, or p90S6Ks. The RSK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270734 [Multi-domain]  Cd Length: 317  Bit Score: 102.86  E-value: 1.60e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  728 KTLGEGEFGKV--VKatafHLKGRAGYTTVAVKMLKEnaSPSELRDLLS---EFNVLKQVNHPHVIKLYGACSQDGPLLL 802
Cdd:cd05582    1 KVLGQGSFGKVflVR----KITGPDAGTLYAMKVLKK--ATLKVRDRVRtkmERDILADVNHPFIVKLHYAFQTEGKLYL 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  803 IVEYAKYGSLrgFLRESRKVgpgylgsggsrnsssldhpderALTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNILV 882
Cdd:cd05582   75 ILDFLRGGDL--FTRLSKEV----------------------MFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILL 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  883 AEGRKMKISDFGLSRDVYEEDSYVKRSQGriPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTlGGNPYPGIPPERLFN 962
Cdd:cd05582  131 DEDGHIKLTDFGLSKESIDHEKKAYSFCG--TVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLT-GSLPFQGKDRKETMT 207
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  963 L-LKTghRMERPDNCSEEMYRLMLQCWKQEPDKR--------------PVFADIskDLEKMMvkRRDY---LDLAASTPS 1024
Cdd:cd05582  208 MiLKA--KLGMPQFLSPEAQSLLRALFKRNPANRlgagpdgveeikrhPFFATI--DWNKLY--RKEIkppFKPAVSRPD 281

                 ....*.
gi 10862703 1025 DSLIYD 1030
Cdd:cd05582  282 DTFYFD 287
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
730-996 3.38e-23

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. PAKs are implicated in the regulation of many cellular processes including growth factor receptor-mediated proliferation, cell polarity, cell motility, cell death and survival, and actin cytoskeleton organization. PAK deregulation is associated with tumor development. PAKs from higher eukaryotes are classified into two groups (I and II), according to their biochemical and structural features. Group I PAKs contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). Group II PAKs contain a PBD and a catalytic domain, but lack other motifs found in group I PAKs. Since group II PAKs do not contain an obvious AID, they may be regulated differently from group I PAKs. Group I PAKs interact with the SH3 containing proteins Nck, Grb2 and PIX; no such binding has been demonstrated for group II PAKs. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270789 [Multi-domain]  Cd Length: 255  Bit Score: 99.98  E-value: 3.38e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  730 LGEGEFGKVVKATAFHlKGRagytTVAVKMLKENASPSELrdLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVEYAKY 809
Cdd:cd06614    8 IGEGASGEVYKATDRA-TGK----EVAIKKMRLRKQNKEL--IINEILIMKECKHPNIVDYYDSYLVGDELWVVMEYMDG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  810 GSLRGFLRESRKvgpgylgsggsrnsssldhpderALTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNILVAEGRKMK 889
Cdd:cd06614   81 GSLTDIITQNPV-----------------------RMNESQIAYVCREVLQGLEYLHSQNVIHRDIKSDNILLSKDGSVK 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  890 ISDFG----LSRDVYEEDSYVkrsqGrIPVkWMAIESLFDHIYTTQSDVWSFGVLLWEIVTlGGNPYPGIPPERLFNLLK 965
Cdd:cd06614  138 LADFGfaaqLTKEKSKRNSVV----G-TPY-WMAPEVIKRKDYGPKVDIWSLGIMCIEMAE-GEPPYLEEPPLRALFLIT 210
                        250       260       270
                 ....*....|....*....|....*....|...
gi 10862703  966 TG--HRMERPDNCSEEMYRLMLQCWKQEPDKRP 996
Cdd:cd06614  211 TKgiPPLKNPEKWSPEFKDFLNKCLVKDPEKRP 243
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
730-954 4.19e-23

Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. CDKs are partly regulated by their subcellular localization, which defines substrate phosphorylation and the resulting specific function. CDK1, CDK2, CDK4, and CDK6 have well-defined functions in the cell cycle, such as the regulation of the early G1 phase by CDK4 or CDK6, the G1/S phase transition by CDK2, or the entry of mitosis by CDK1. They also exhibit overlapping cyclin specificity and functions in certain conditions. Knockout mice with a single CDK deleted remain viable with specific phenotypes, showing that some CDKs can compensate for each other. For example, CDK4 can compensate for the loss of CDK6, however, double knockout mice with both CDK4 and CDK6 deleted die in utero. CDK8 and CDK9 are mainly involved in transcription while CDK5 is implicated in neuronal function. CDK7 plays essential roles in both the cell cycle as a CDK-Activating Kinase (CAK) and in transcription as a component of the general transcription factor TFIIH. The CDK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270823 [Multi-domain]  Cd Length: 282  Bit Score: 100.63  E-value: 4.19e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  730 LGEGEFGKVVKAtafhlKGRAGYTTVAVKMLK-----ENASPSELRdllsEFNVLKQVNHPHVIKLYGACSQDGPLLLIV 804
Cdd:cd07829    7 LGEGTYGVVYKA-----KDKKTGEIVALKKIRldneeEGIPSTALR----EISLLKELKHPNIVKLLDVIHTENKLYLVF 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  805 EYAKYgSLRGFLRESRkvgpgylgsggsrnsssldhpdeRALTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNILVAE 884
Cdd:cd07829   78 EYCDQ-DLKKYLDKRP-----------------------GPLPPNLIKSIMYQLLRGLAYCHSHRILHRDLKPQNLLINR 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  885 GRKMKISDFGLSRDVyeedsyvkrsqgRIPVK---------WM-AIESLF-DHIYTTQSDVWSFGVLLWEIVTlgGNP-Y 952
Cdd:cd07829  134 DGVLKLADFGLARAF------------GIPLRtythevvtlWYrAPEILLgSKHYSTAVDIWSVGCIFAELIT--GKPlF 199

                 ..
gi 10862703  953 PG 954
Cdd:cd07829  200 PG 201
PTK_Jak2_rpt1 cd05078
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 2; Jak2 is widely ...
724-1005 4.28e-23

Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 2; Jak2 is widely expressed in many tissues. It is essential for the signaling of hormone-like cytokines such as growth hormone, erythropoietin, thrombopoietin, and prolactin, as well as some IFNs and cytokines that signal through the IL-3 and gp130 receptors. Disruption of Jak2 in mice results in an embryonic lethal phenotype with multiple defects including erythropoietic and cardiac abnormalities. It is the only Jak gene that results in a lethal phenotype when disrupted in mice. A mutation in the pseudokinase domain of Jak2, V617F, is present in many myeloproliferative diseases, including almost all patients with polycythemia vera, and 50% of patients with essential thrombocytosis and myelofibrosis. Jak2 is a cytoplasmic (or nonreceptor) PTK containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase domain. The pseudokinase domain shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. Despite this, the presumed pseudokinase (repeat 1) domain of Jak2 exhibits dual-specificity kinase activity, phosphorylating two negative regulatory sites in Jak2: Ser523 and Tyr570. Inactivation of the repeat 1 domain increased Jak2 basal activity, suggesting that it modulates the kinase activity of the C-terminal catalytic (repeat 2) domain. The Jak2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270663 [Multi-domain]  Cd Length: 262  Bit Score: 100.02  E-value: 4.28e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  724 LVLGKTLGEGEFGKVVKATAFHLK--GRAGYTTVAVKML-KENASPSElrDLLSEFNVLKQVNHPHVIKLYGACSQDGPL 800
Cdd:cd05078    1 LIFNESLGQGTFTKIFKGIRREVGdyGQLHETEVLLKVLdKAHRNYSE--SFFEAASMMSQLSHKHLVLNYGVCVCGDEN 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  801 LLIVEYAKYGSLRGFLRESRKVgpgylgsggsrnsssldhpderaltmgdlISFAW------QISQGMQYLAEMKLVHRD 874
Cdd:cd05078   79 ILVQEYVKFGSLDTYLKKNKNC-----------------------------INILWklevakQLAWAMHFLEEKTLVHGN 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  875 LAARNILV--AEGRK------MKISDFGLSRDVYEEDSYVKRsqgrIPvkWMAIESLFD-HIYTTQSDVWSFGVLLWEIV 945
Cdd:cd05078  130 VCAKNILLirEEDRKtgnppfIKLSDPGISITVLPKDILLER----IP--WVPPECIENpKNLSLATDKWSFGTTLWEIC 203
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  946 TLGGNPYPGIPPERLFNLLKTGHRMERPDncSEEMYRLMLQCWKQEPDKRPVFADISKDL 1005
Cdd:cd05078  204 SGGDKPLSALDSQRKLQFYEDRHQLPAPK--WTELANLINNCMDYEPDHRPSFRAIIRDL 261
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
717-995 4.37e-23

Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SLK promotes apoptosis through apoptosis signal-regulating kinase 1 (ASK1) and the mitogen-activated protein kinase (MAPK) p38. It acts as a MAPK kinase kinase by phosphorylating ASK1, resulting in the phosphorylation of p38. SLK also plays a role in mediating actin reorganization. It is part of a microtubule-associated complex that is targeted at adhesion sites, and is required in focal adhesion turnover and in regulating cell migration. The SLK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270811 [Multi-domain]  Cd Length: 283  Bit Score: 100.49  E-value: 4.37e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  717 WEfprknlVLGKtLGEGEFGKVVKAtafhlKGRAGYTTVAVKMLkENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQ 796
Cdd:cd06643    7 WE------IVGE-LGDGAFGKVYKA-----QNKETGILAAAKVI-DTKSEEELEDYMVEIDILASCDHPNIVKLLDAFYY 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  797 DGPLLLIVEYAKYGSLRGFLRESrkvgpgylgsggsrnsssldhpdERALTMGDLISFAWQISQGMQYLAEMKLVHRDLA 876
Cdd:cd06643   74 ENNLWILIEFCAGGAVDAVMLEL-----------------------ERPLTEPQIRVVCKQTLEALVYLHENKIIHRDLK 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  877 ARNILVAEGRKMKISDFGLS----RDVYEEDSYVKRSQgripvkWMAIESLF-----DHIYTTQSDVWSFGVLLWEIVTL 947
Cdd:cd06643  131 AGNILFTLDGDIKLADFGVSakntRTLQRRDSFIGTPY------WMAPEVVMcetskDRPYDYKADVWSLGVTLIEMAQI 204
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 10862703  948 gGNPYPGIPPERLfnLLKTGHR----MERPDNCSEEMYRLMLQCWKQEPDKR 995
Cdd:cd06643  205 -EPPHHELNPMRV--LLKIAKSepptLAQPSRWSPEFKDFLRKCLEKNVDAR 253
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
754-996 7.34e-23

Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and Ste20-related proline alanine-rich kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SPAK is also referred to as STK39 or PASK (proline-alanine-rich STE20-related kinase). OSR1 and SPAK regulate the activity of cation-chloride cotransporters through direct interaction and phosphorylation. They are also implicated in cytoskeletal rearrangement, cell differentiation, transformation and proliferation. OSR1 and SPAK contain a conserved C-terminal (CCT) domain, which recognizes a unique motif ([RK]FX[VI]) present in their activating kinases (WNK1/WNK4) and their substrates. The OSR1 and SPAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270787 [Multi-domain]  Cd Length: 267  Bit Score: 99.35  E-value: 7.34e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  754 TVAVKMLKENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVEYAKYGSLRGFLRESRKVGpgylgsggsr 833
Cdd:cd06610   28 KVAIKRIDLEKCQTSMDELRKEIQAMSQCNHPNVVSYYTSFVVGDELWLVMPLLSGGSLLDIMKSSYPRG---------- 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  834 nssSLDHPderaltmgdLISFAW-QISQGMQYLAEMKLVHRDLAARNILVAEGRKMKISDFGLSRDVYEEDSYVKRSQGR 912
Cdd:cd06610   98 ---GLDEA---------IIATVLkEVLKGLEYLHSNGQIHRDVKAGNILLGEDGSVKIADFGVSASLATGGDRTRKVRKT 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  913 I---PVkWMAIESLF-DHIYTTQSDVWSFGVLLWEIVTlGGNPYPGIPPERLFNLLKTGHRMERPDN-----CSEEMYRL 983
Cdd:cd06610  166 FvgtPC-WMAPEVMEqVRGYDFKADIWSFGITAIELAT-GAAPYSKYPPMKVLMLTLQNDPPSLETGadykkYSKSFRKM 243
                        250
                 ....*....|...
gi 10862703  984 MLQCWKQEPDKRP 996
Cdd:cd06610  244 ISLCLQKDPSKRP 256
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
726-1003 1.07e-22

Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK1 and TSSK2 are expressed specifically in meiotic and postmeiotic spermatogenic cells, respectively. TSSK3 has been reported to be expressed in the interstitial Leydig cells of adult testis. TSSK4, also called TSSK5, is expressed in testis from haploid round spermatids to mature spermatozoa. TSSK6, also called SSTK, is expressed at the head of elongated sperm. TSSK1/TSSK2 double knock-out and TSSK6 null mice are sterile without manifesting other defects, making these kinases viable targets for male contraception. The TSSK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270982 [Multi-domain]  Cd Length: 262  Bit Score: 98.79  E-value: 1.07e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  726 LGKTLGEGEFGKVVKATAFHLKGRagyTTVAVKMLKENASPselRDLLSEF-----NVLKQVNHPHVIKLYGACsQDGPL 800
Cdd:cd14080    4 LGKTIGEGSYSKVKLAEYTKSGLK---EKVACKIIDKKKAP---KDFLEKFlprelEILRKLRHPNIIQVYSIF-ERGSK 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  801 LLIV-EYAKYGSLRGFLRESRKVgpgylgsggsrnsssldhPDERALTMgdlisFAwQISQGMQYLAEMKLVHRDLAARN 879
Cdd:cd14080   77 VFIFmEYAEHGDLLEYIQKRGAL------------------SESQARIW-----FR-QLALAVQYLHSLDIAHRDLKCEN 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  880 ILVAEGRKMKISDFGLSRDVYEEDSYVKrSQ---GRIpvKWMAIESLFDHIYT-TQSDVWSFGVLLWEIVTlGGNPYPGI 955
Cdd:cd14080  133 ILLDSNNNVKLSDFGFARLCPDDDGDVL-SKtfcGSA--AYAAPEILQGIPYDpKKYDIWSLGVILYIMLC-GSMPFDDS 208
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 10862703  956 pperlfNLLKTGHR-MERP-------DNCSEEMYRLMLQCWKQEPDKRPVFADISK 1003
Cdd:cd14080  209 ------NIKKMLKDqQNRKvrfpssvKKLSPECKDLIDQLLEPDPTKRATIEEILN 258
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
728-1002 1.88e-22

Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NUAK proteins are classified as AMP-activated protein kinase (AMPK)-related kinases, which like AMPK are activated by the major tumor suppressor LKB1. Vertebrates contain two NUAK proteins, called NUAK1 and NUAK2. NUAK2, also called SNARK (Sucrose, non-fermenting 1/AMP-activated protein kinase-related kinase), is involved in energy metabolism. It is activated by hyperosmotic stress, DNA damage, and nutrients such as glucose and glutamine. NUAK2-knockout mice develop obesity, altered serum lipid profiles, hyperinsulinaemia, hyperglycaemia, and impaired glucose tolerance. NUAK2 is implicated in regulating actin stress fiber assembly through its association with myosin phosphatase Rho-interacting protein (MRIP), which leads to an increase in myosin regulatory light chain (MLC) phosphorylation. It is also associated with tumor growth, migration, and oncogenicity of melanoma cells. The NUAK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271063 [Multi-domain]  Cd Length: 255  Bit Score: 98.10  E-value: 1.88e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  728 KTLGEGEFGKVVKAtafhlKGRAGyTTVAVKMLKENASPSElRDLL---SEFNVLKQVNHPHVIKLYGACSQDGPLLLIV 804
Cdd:cd14161    9 ETLGKGTYGRVKKA-----RDSSG-RLVAIKSIRKDRIKDE-QDLLhirREIEIMSSLNHPHIISVYEVFENSSKIVIVM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  805 EYAKYGSLRGFLRESRKvgpgylgsggsrnsssLDHPDERaltmgdliSFAWQISQGMQYLAEMKLVHRDLAARNILVAE 884
Cdd:cd14161   82 EYASRGDLYDYISERQR----------------LSELEAR--------HFFRQIVSAVHYCHANGIVHRDLKLENILLDA 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  885 GRKMKISDFGLSrDVYEEDSYVKRSQGRiPVkWMAIESLFDHIYT-TQSDVWSFGVLLWeIVTLGGNPYPGIPPERLFNL 963
Cdd:cd14161  138 NGNIKIADFGLS-NLYNQDKFLQTYCGS-PL-YASPEIVNGRPYIgPEVDSWSLGVLLY-ILVHGTMPFDGHDYKILVKQ 213
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 10862703  964 LKTGHRMERP---DNCSEEMYRLMLQcwkqePDKRPVFADIS 1002
Cdd:cd14161  214 ISSGAYREPTkpsDACGLIRWLLMVN-----PERRATLEDVA 250
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
730-995 2.65e-22

Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. AGC kinases regulate many cellular processes including division, growth, survival, metabolism, motility, and differentiation. Many are implicated in the development of various human diseases. Members of this family include cAMP-dependent Protein Kinase (PKA), cGMP-dependent Protein Kinase (PKG), Protein Kinase C (PKC), Protein Kinase B (PKB), G protein-coupled Receptor Kinase (GRK), Serum- and Glucocorticoid-induced Kinase (SGK), and 70 kDa ribosomal Protein S6 Kinase (p70S6K or S6K), among others. AGC kinases share an activation mechanism based on the phosphorylation of up to three sites: the activation loop (A-loop), the hydrophobic motif (HM) and the turn motif. Phosphorylation at the A-loop is required of most AGC kinases, which results in a disorder-to-order transition of the A-loop. The ordered conformation results in the access of substrates and ATP to the active site. A subset of AGC kinases with C-terminal extensions containing the HM also requires phosphorylation at this site. Phosphorylation at the HM allows the C-terminal extension to form an ordered structure that packs into the hydrophobic pocket of the catalytic domain, which then reconfigures the kinase into an active bi-lobed state. In addition, growth factor-activated AGC kinases such as PKB, p70S6K, RSK, MSK, PKC, and SGK, require phosphorylation at the turn motif (also called tail or zipper site), located N-terminal to the HM at the C-terminal extension. The AGC family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and Phosphoinositide 3-Kinase.


Pssm-ID: 270693 [Multi-domain]  Cd Length: 250  Bit Score: 97.59  E-value: 2.65e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  730 LGEGEFGKVVKAtafhlKGRAGYTTVAVKMLK--ENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVEYA 807
Cdd:cd05123    1 LGKGSFGKVLLV-----RKKDTGKLYAMKVLRkkEIIKRKEVEHTLNERNILERVNHPFIVKLHYAFQTEEKLYLVLDYV 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  808 KYGSLRGFLRESRKVgpgylgsggsrnsssldhPDERALTmgdlisFAWQISQGMQYLAEMKLVHRDLAARNILV-AEGR 886
Cdd:cd05123   76 PGGELFSHLSKEGRF------------------PEERARF------YAAEIVLALEYLHSLGIIYRDLKPENILLdSDGH 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  887 kMKISDFGLSRDVYEEDSYVKRSQGRIPvkWMAIESLFDHIYTTQSDVWSFGVLLWEIVTlGGNPYPGIPPERLFNLLKT 966
Cdd:cd05123  132 -IKLTDFGLAKELSSDGDRTYTFCGTPE--YLAPEVLLGKGYGKAVDWWSLGVLLYEMLT-GKPPFYAENRKEIYEKILK 207
                        250       260
                 ....*....|....*....|....*....
gi 10862703  967 GhRMERPDNCSEEMYRLMLQCWKQEPDKR 995
Cdd:cd05123  208 S-PLKFPEYVSPEAKSLISGLLQKDPTKR 235
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
726-1001 1.02e-21

Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Chlamydomonas reinhardtii FA2 was discovered in a genetic screen for deflagellation-defective mutants. It is essential for basal-body/centriole-associated microtubule severing, and plays a role in cell cycle progression. No cellular function has yet been ascribed to CNK4. The Chlamydomonas reinhardtii FA2-like subfamily belongs to the (NIMA)-related kinase (Nek) family, which includes seven different Chlamydomonas Neks (CNKs 1-6 and Fa2). This subfamily contains FA2 and CNK4. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270868 [Multi-domain]  Cd Length: 256  Bit Score: 95.94  E-value: 1.02e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  726 LGKTLGEGEFGKVVKAtafhlKGRAGYTTVAVKMLK-ENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIV 804
Cdd:cd08529    4 ILNKLGKGSFGVVYKV-----VRKVDGRVYALKQIDiSRMSRKMREEAIDEARVLSKLNSPYVIKYYDSFVDKGKLNIVM 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  805 EYAKYGSLRGFLRESRKvgpgylgsggsrnsssldhpdeRALTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNILVAE 884
Cdd:cd08529   79 EYAENGDLHSLIKSQRG----------------------RPLPEDQIWKFFIQTLLGLSHLHSKKILHRDIKSMNIFLDK 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  885 GRKMKISDFGLSRDVYEEDSYVKRSQGrIPVkWMAIESLFDHIYTTQSDVWSFGVLLWEIVTlGGNPYPGIPPERLFNLL 964
Cdd:cd08529  137 GDNVKIGDLGVAKILSDTTNFAQTIVG-TPY-YLSPELCEDKPYNEKSDVWALGCVLYELCT-GKHPFEAQNQGALILKI 213
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 10862703  965 KTGHRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADI 1001
Cdd:cd08529  214 VRGKYPPISASYSQDLSQLIDSCLTKDYRQRPDTTEL 250
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
726-1001 1.05e-21

Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BRSK1, also called SAD-B or SAD1 (Synapses of Amphids Defective homolog 1), and BRSK2, also called SAD-A, are highly expressed in mammalian forebrain. They play important roles in establishing neuronal polarity. BRSK1/2 double knock-out mice die soon after birth, showing thin cerebral cortices due to disordered subplate layers and neurons that lack distinct axons and dendrites. BRSK1 regulates presynaptic neurotransmitter release. Its activity fluctuates during cell cysle progression and it acts as a regulator of centrosome duplication. BRSK2 is also abundant in pancreatic islets, where it is involved in the regulation of glucose-stimulated insulin secretion. The BRSK1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270983 [Multi-domain]  Cd Length: 255  Bit Score: 95.78  E-value: 1.05e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  726 LGKTLGEGEFGKVvkATAFHLK-GRagytTVAVKML-KENAS-PSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLL 802
Cdd:cd14081    5 LGKTLGKGQTGLV--KLAKHCVtGQ----KVAIKIVnKEKLSkESVLMKVEREIAIMKLIEHPNVLKLYDVYENKKYLYL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  803 IVEYAKYGSLRGFLRESRKvgpgylgsggsrnsssldhpderaLTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNILV 882
Cdd:cd14081   79 VLEYVSGGELFDYLVKKGR------------------------LTEKEARKFFRQIISALDYCHSHSICHRDLKPENLLL 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  883 AEGRKMKISDFGLSRdVYEEDSYVKRSQGRiPvKWMAIESLFDHIYTTQ-SDVWSFGVLLWEIVTlGGNPYPGIPPERLF 961
Cdd:cd14081  135 DEKNNIKIADFGMAS-LQPEGSLLETSCGS-P-HYACPEVIKGEKYDGRkADIWSCGVILYALLV-GALPFDDDNLRQLL 210
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 10862703  962 NLLKTGhRMERPDNCSEE---MYRLMLQCwkqEPDKRPVFADI 1001
Cdd:cd14081  211 EKVKRG-VFHIPHFISPDaqdLLRRMLEV---NPEKRITIEEI 249
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
728-1001 1.50e-21

Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NUAK proteins are classified as AMP-activated protein kinase (AMPK)-related kinases, which like AMPK are activated by the major tumor suppressor LKB1. Vertebrates contain two NUAK proteins, called NUAK1 and NUAK2. NUAK1, also called ARK5 (AMPK-related protein kinase 5), regulates cell proliferation and displays tumor suppression through direct interaction and phosphorylation of p53. It is also involved in cell senescence and motility. High NUAK1 expression is associated with invasiveness of nonsmall cell lung cancer (NSCLC) and breast cancer cells. NUAK2, also called SNARK (Sucrose, non-fermenting 1/AMP-activated protein kinase-related kinase), is involved in energy metabolism. It is activated by hyperosmotic stress, DNA damage, and nutrients such as glucose and glutamine. NUAK2-knockout mice develop obesity, altered serum lipid profiles, hyperinsulinaemia, hyperglycaemia, and impaired glucose tolerance. The NUAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270975 [Multi-domain]  Cd Length: 254  Bit Score: 95.53  E-value: 1.50e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  728 KTLGEGEFGKVVKATAfHLKGRagytTVAVKMLKENA--SPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVE 805
Cdd:cd14073    7 ETLGKGTYGKVKLAIE-RATGR----EVAIKSIKKDKieDEQDMVRIRREIEIMSSLNHPHIIRIYEVFENKDKIVIVME 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  806 YAKYGSLRGFLRESRKvgpgylgsggsrnsssldhpderaLTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNILVAEG 885
Cdd:cd14073   82 YASGGELYDYISERRR------------------------LPEREARRIFRQIVSAVHYCHKNGVVHRDLKLENILLDQN 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  886 RKMKISDFGLSrDVYEEDSYVKRSQGRiPVkWMAIESLFDHIYT-TQSDVWSFGVLLWEIVtLGGNPYPGIPPERLFNLL 964
Cdd:cd14073  138 GNAKIADFGLS-NLYSKDKLLQTFCGS-PL-YASPEIVNGTPYQgPEVDCWSLGVLLYTLV-YGTMPFDGSDFKRLVKQI 213
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 10862703  965 KTGhRMERPDNCSEE--MYRLMLQCwkqEPDKRPVFADI 1001
Cdd:cd14073  214 SSG-DYREPTQPSDAsgLIRWMLTV---NPKRRATIEDI 248
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
722-996 1.57e-21

Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include the MAPKKs Pek1/Skh1 from Schizosaccharomyces pombe and MKK2 from Saccharomyces cerevisiae, and related proteins. Both fission yeast Pek1 and baker's yeast MKK2 are components of the cell integrity MAPK pathway. In fission yeast, Pek1 phosphorylates and activates Pmk1/Spm1 and is regulated by the MAPKK kinase Mkh1. In baker's yeast, the pathway involves the MAPK Slt2, the MAPKKs MKK1 and MKK2, and the MAPKK kinase Bck1. The cell integrity MAPK cascade is activated by multiple stress conditions, and is essential in cell wall construction, morphogenesis, cytokinesis, and ion homeostasis. MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The MAPKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270793 [Multi-domain]  Cd Length: 287  Bit Score: 95.95  E-value: 1.57e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  722 KNLVLGKTLGEGEFGKVVKAtafhlKGRAGYTTVAVKMLKENASPSELRDLLSEFNVLKQVNHPHVIKLYGAC--SQDGP 799
Cdd:cd06621    1 DKIVELSSLGEGAGGSVTKC-----RLRNTKTIFALKTITTDPNPDVQKQILRELEINKSCASPYIVKYYGAFldEQDSS 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  800 LLLIVEYAKYGSLRGFLRESRKVGpgylgsggsrnssslDHPDERALTmgdliSFAWQISQGMQYLAEMKLVHRDLAARN 879
Cdd:cd06621   76 IGIAMEYCEGGSLDSIYKKVKKKG---------------GRIGEKVLG-----KIAESVLKGLSYLHSRKIIHRDIKPSN 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  880 ILVAEGRKMKISDFGLSRDVYEE-------DSYvkrsqgripvkWMAIESLFDHIYTTQSDVWSFGVLLWEiVTLGGNPY 952
Cdd:cd06621  136 ILLTRKGQVKLCDFGVSGELVNSlagtftgTSY-----------YMAPERIQGGPYSITSDVWSLGLTLLE-VAQNRFPF 203
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 10862703  953 P--GIPPERLFNLLKTGHRM------ERPDNC---SEEMYRLMLQCWKQEPDKRP 996
Cdd:cd06621  204 PpeGEPPLGPIELLSYIVNMpnpelkDEPENGikwSESFKDFIEKCLEKDGTRRP 258
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
730-1003 1.62e-21

Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK25 is also called Ste20/oxidant stress response kinase 1 (SOK1) or yeast Sps1/Ste20-related kinase 1 (YSK1). It is localized in the Golgi apparatus through its interaction with the Golgi matrix protein GM130. It may be involved in the regulation of cell migration and polarization. STK25 binds and phosphorylates CCM3 (cerebral cavernous malformation 3), also called PCD10 (programmed cell death 10), and may play a role in apoptosis. Human STK25 is a candidate gene responsible for pseudopseudohypoparathyroidism (PPHP), a disease that shares features with the Albright hereditary osteodystrophy (AHO) phenotype. The STK25 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270810 [Multi-domain]  Cd Length: 277  Bit Score: 95.89  E-value: 1.62e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  730 LGEGEFGKVVKATAFHLKgragyTTVAVKMLKENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVEYAKY 809
Cdd:cd06642   12 IGKGSFGEVYKGIDNRTK-----EVVAIKIIDLEEAEDEIEDIQQEITVLSQCDSPYITRYYGSYLKGTKLWIIMEYLGG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  810 GSLRGFLResrkvgPGylgsggsrnsssldhPDERALtmgdLISFAWQISQGMQYLAEMKLVHRDLAARNILVAEGRKMK 889
Cdd:cd06642   87 GSALDLLK------PG---------------PLEETY----IATILREILKGLDYLHSERKIHRDIKAANVLLSEQGDVK 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  890 ISDFGLSRDVyeEDSYVKRSQGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTlGGNPYPGIPPERLFNLLKTGHR 969
Cdd:cd06642  142 LADFGVAGQL--TDTQIKRNTFVGTPFWMAPEVIKQSAYDFKADIWSLGITAIELAK-GEPPNSDLHPMRVLFLIPKNSP 218
                        250       260       270
                 ....*....|....*....|....*....|....
gi 10862703  970 MERPDNCSEEMYRLMLQCWKQEPDKRPVFADISK 1003
Cdd:cd06642  219 PTLEGQHSKPFKEFVEACLNKDPRFRPTAKELLK 252
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
723-996 1.77e-21

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek6 is required for the transition from metaphase to anaphase. It also plays important roles in mitotic spindle formation and cytokinesis. Activated by Nek9 during mitosis, Nek6 phosphorylates Eg5, a kinesin that is important for spindle bipolarity. Nek6 localizes to spindle microtubules during metaphase and anaphase, and to the midbody during cytokinesis. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270865 [Multi-domain]  Cd Length: 268  Bit Score: 95.48  E-value: 1.77e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  723 NLVLGKTLGEGEFGKVVKATAfHLKGRagytTVAVKMLK--ENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPL 800
Cdd:cd08228    3 NFQIEKKIGRGQFSEVYRATC-LLDRK----PVALKKVQifEMMDAKARQDCVKEIDLLKQLNHPNVIKYLDSFIEDNEL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  801 LLIVEYAKYGSLRGFLRESRKvgpgylgsggsrnsssldhpDERALTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNI 880
Cdd:cd08228   78 NIVLELADAGDLSQMIKYFKK--------------------QKRLIPERTVWKYFVQLCSAVEHMHSRRVMHRDIKPANV 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  881 LVAEGRKMKISDFGLSRdVYEEDSYVKRSQGRIPVkWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLgGNPYPGippeRL 960
Cdd:cd08228  138 FITATGVVKLGDLGLGR-FFSSKTTAAHSLVGTPY-YMSPERIHENGYNFKSDIWSLGCLLYEMAAL-QSPFYG----DK 210
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 10862703  961 FNLLKTGHRMERPD-------NCSEEMYRLMLQCWKQEPDKRP 996
Cdd:cd08228  211 MNLFSLCQKIEQCDypplpteHYSEKLRELVSMCIYPDPDQRP 253
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
723-1002 2.18e-21

Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related kinase 6 and 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek6 and Nek7 are the shortest Neks, consisting only of the catalytic domain and a very short N-terminal extension. They show distinct expression patterns and both appear to be downstream substrates of Nek9. They are required for mitotic spindle formation and cytokinesis. They may also be regulators of the p70 ribosomal S6 kinase. Nek6/7 is part of a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270863 [Multi-domain]  Cd Length: 262  Bit Score: 95.03  E-value: 2.18e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  723 NLVLGKTLGEGEFGKVVKATAFHLKgragyTTVAVKMLK--ENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPL 800
Cdd:cd08224    1 NYEIEKKIGKGQFSVVYRARCLLDG-----RLVALKKVQifEMMDAKARQDCLKEIDLLQQLNHPNIIKYLASFIENNEL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  801 LLIVEYAKYGSLRGFLRESRKVGpgylgsggsrnsssldhpdeRALTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNI 880
Cdd:cd08224   76 NIVLELADAGDLSRLIKHFKKQK--------------------RLIPERTIWKYFVQLCSALEHMHSKRIMHRDIKPANV 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  881 LVAEGRKMKISDFGLSRdVYEEDSYVKRSQGRIPVkWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLgGNPYPGippERL 960
Cdd:cd08224  136 FITANGVVKLGDLGLGR-FFSSKTTAAHSLVGTPY-YMSPERIREQGYDFKSDIWSLGCLLYEMAAL-QSPFYG---EKM 209
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 10862703  961 fNLLKTGHRMER------PDNC-SEEMYRLMLQCWKQEPDKRPvfaDIS 1002
Cdd:cd08224  210 -NLYSLCKKIEKceypplPADLySQELRDLVAACIQPDPEKRP---DIS 254
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
730-996 2.19e-21

Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LRRKs are also classified as ROCO proteins because they contain a ROC (Ras of complex proteins)/GTPase domain followed by a COR (C-terminal of ROC) domain of unknown function. In addition, LRRKs contain a catalytic kinase domain and protein-protein interaction motifs including a WD40 domain, LRRs and ankyrin (ANK) repeats. LRRKs possess both GTPase and kinase activities, with the ROC domain acting as a molecular switch for the kinase domain, cycling between a GTP-bound state which drives kinase activity and a GDP-bound state which decreases the activity. Vertebrates contain two members, LRRK1 and LRRK2, which show complementary expression in the brain. Mutations in LRRK2 are linked to both familial and sporadic forms of Parkinson's disease. The normal roles of LRRKs are not clearly defined. They may be involved in mitogen-activated protein kinase (MAPK) pathways, protein translation control, programmed cell death pathways, and cytoskeletal dynamics. The LRRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270902 [Multi-domain]  Cd Length: 275  Bit Score: 95.37  E-value: 2.19e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  730 LGEGEFGKVVKAT---------AFHLKGRAGYTTVAVKM----LKENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQ 796
Cdd:cd14000    2 LGDGGFGSVYRASykgepvavkIFNKHTSSNFANVPADTmlrhLRATDAMKNFRLLRQELTVLSHLHHPSIVYLLGIGIH 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  797 dgPLLLIVEYAKYGSLRGFLRESRKVGPgylgsggsrnsssldhPDERALTMgdliSFAWQISQGMQYLAEMKLVHRDLA 876
Cdd:cd14000   82 --PLMLVLELAPLGSLDHLLQQDSRSFA----------------SLGRTLQQ----RIALQVADGLRYLHSAMIIYRDLK 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  877 ARNILV-----AEGRKMKISDFGLSRDVYEEDsyVKRSQGriPVKWMAIESL-FDHIYTTQSDVWSFGVLLWEIVTlGGN 950
Cdd:cd14000  140 SHNVLVwtlypNSAIIIKIADYGISRQCCRMG--AKGSEG--TPGFRAPEIArGNVIYNEKVDVFSFGMLLYEILS-GGA 214
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 10862703  951 PYPG---IPPErlFNLLK-----TGHRMERPDNCSEEmyrLMLQCWKQEPDKRP 996
Cdd:cd14000  215 PMVGhlkFPNE--FDIHGglrppLKQYECAPWPEVEV---LMKKCWKENPQQRP 263
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
725-996 3.40e-21

Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The CMGC family consists of Cyclin-Dependent protein Kinases (CDKs), Mitogen-activated protein kinases (MAPKs) such as Extracellular signal-regulated kinase (ERKs), c-Jun N-terminal kinases (JNKs), and p38, and other kinases. CDKs belong to a large subfamily of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. MAPKs serve as important mediators of cellular responses to extracellular signals. They control critical cellular functions including differentiation, proliferation, migration, and apoptosis. They are also implicated in the pathogenesis of many diseases including multiple types of cancer, stroke, diabetes, and chronic inflammation. Other members of the CMGC family include casein kinase 2 (CK2), Dual-specificity tYrosine-phosphorylated and -Regulated Kinase (DYRK), Glycogen Synthase Kinase 3 (GSK3), among many others. The CMGC family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270688 [Multi-domain]  Cd Length: 249  Bit Score: 94.22  E-value: 3.40e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  725 VLGKtLGEGEFGKVVKATaFHLKGRagytTVAVKMLK-----ENASPSELRdLLSEFNvlKQVNHPHVIKLYGAC--SQD 797
Cdd:cd05118    3 VLRK-IGEGAFGTVWLAR-DKVTGE----KVAIKKIKndfrhPKAALREIK-LLKHLN--DVEGHPNIVKLLDVFehRGG 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  798 GPLLLIVEYAKYgSLRGFLRESRKvgpgylgsggsrnssSLDHPDERaltmgdliSFAWQISQGMQYLAEMKLVHRDLAA 877
Cdd:cd05118   74 NHLCLVFELMGM-NLYELIKDYPR---------------GLPLDLIK--------SYLYQLLQALDFLHSNGIIHRDLKP 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  878 RNILV-AEGRKMKISDFGLSRdVYEEDSYVKRSQgriPVKWMAIESLFDHIYTTQS-DVWSFGVLLWEIVTlgGNP-YPG 954
Cdd:cd05118  130 ENILInLELGQLKLADFGLAR-SFTSPPYTPYVA---TRWYRAPEVLLGAKPYGSSiDIWSLGCILAELLT--GRPlFPG 203
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 10862703  955 IPP----ERLFNLLKTghrmerpdncsEEMYRLMLQCWKQEPDKRP 996
Cdd:cd05118  204 DSEvdqlAKIVRLLGT-----------PEALDLLSKMLKYDPAKRI 238
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
730-1005 3.91e-21

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. eIF-2 phosphorylation is induced in response to cellular stresses including virus infection, heat shock, nutrient deficiency, and the accummulation of unfolded proteins, among others. There are four distinct kinases that phosphorylate eIF-2 and control protein synthesis under different stress conditions: General Control Non-derepressible-2 (GCN2) which is activated during amino acid or serum starvation; protein kinase regulated by RNA (PKR) which is activated by double stranded RNA; heme-regulated inhibitor kinase (HRI) which is activated under heme-deficient conditions; and PKR-like endoplasmic reticulum kinase (PERK) which is activated when misfolded proteins accumulate in the ER. The EIF2AK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270898 [Multi-domain]  Cd Length: 273  Bit Score: 94.67  E-value: 3.91e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  730 LGEGEFGKVVKAtafhlKGRAGYTTVAVKMLKENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVEYAKY 809
Cdd:cd13996   14 LGSGGFGSVYKV-----RNKVDGVTYAIKKIRLTEKSSASEKVLREVKALAKLNHPNIVRYYTAWVEEPPLYIQMELCEG 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  810 GSLRGFLRESRKvgpgylgsggsrnSSSLDHPDERALTMgdlisfawQISQGMQYLAEMKLVHRDLAARNILVAEG-RKM 888
Cdd:cd13996   89 GTLRDWIDRRNS-------------SSKNDRKLALELFK--------QILKGVSYIHSKGIVHRDLKPSNIFLDNDdLQV 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  889 KISDFGLSRDV-------YEEDSYVKRSQGRIPVK-----WMAIESLFDHIYTTQSDVWSFGVLLWEIVtlggnpypgIP 956
Cdd:cd13996  148 KIGDFGLATSIgnqkrelNNLNNNNNGNTSNNSVGigtplYASPEQLDGENYNEKADIYSLGIILFEML---------HP 218
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 10862703  957 P----ERlFNLLKTGHRMERPDNCSEEMYR---LMLQCWKQEPDKRPVFADISKDL 1005
Cdd:cd13996  219 FktamER-STILTDLRNGILPESFKAKHPKeadLIQSLLSKNPEERPSAEQLLRSL 273
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
730-1000 4.14e-21

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK3 mRNA is up-regulated in fibroblasts after Ras-induced senescence, and its overexpression induces both autophagy and senescence in a fibroblast cell line. ULK3, through its kinase activity, positively regulates Gli proteins, mediators of the Sonic hedgehog (Shh) signaling pathway that is implicated in tissue homeostasis maintenance and neurogenesis. It is inhibited by binding to Suppressor of Fused (Sufu). The ULK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271023 [Multi-domain]  Cd Length: 252  Bit Score: 93.89  E-value: 4.14e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  730 LGEGEFGKVVKAtaFHLKGRAgyTTVAVK-MLKENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVEYAK 808
Cdd:cd14121    3 LGSGTYATVYKA--YRKSGAR--EVVAVKcVSKSSLNKASTENLLTEIELLKKLKHPHIVELKDFQWDEEHIYLIMEYCS 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  809 YGSLRGFLReSRKVGPGYLGSggsrnsssldhpderaltmgdliSFAWQISQGMQYLAEMKLVHRDLAARNILVAEGRK- 887
Cdd:cd14121   79 GGDLSRFIR-SRRTLPESTVR-----------------------RFLQQLASALQFLREHNISHMDLKPQNLLLSSRYNp 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  888 -MKISDFGLSRDVYEEDSyvKRSQGRIPVkWMAIESLFDHIYTTQSDVWSFGVLLWEIVtLGGNPYPGIPPERLFNLLKT 966
Cdd:cd14121  135 vLKLADFGFAQHLKPNDE--AHSLRGSPL-YMAPEMILKKKYDARVDLWSVGVILYECL-FGRAPFASRSFEELEEKIRS 210
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 10862703  967 GHRMERP------DNCSEEMYRLMlqcwKQEPDKRPVFAD 1000
Cdd:cd14121  211 SKPIEIPtrpelsADCRDLLLRLL----QRDPDRRISFEE 246
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
730-1003 6.09e-21

Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Schizosaccharomyces pombe Nak1, Saccharomyces cerevisiae Kic1p (kinase that interacts with Cdc31p) and related proteins. Nak1 (also called N-rich kinase 1), is required by fission yeast for polarizing the tips of actin cytoskeleton and is involved in cell growth, cell separation, cell morphology and cell-cycle progression. Kic1p is required by budding yeast for cell integrity and morphogenesis. Kic1p interacts with Cdc31p, the yeast homologue of centrin, and phosphorylates substrates in a Cdc31p-dependent manner. The Nak1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270822 [Multi-domain]  Cd Length: 277  Bit Score: 94.08  E-value: 6.09e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  730 LGEGEFGKVVKAtaFHLKGRAgytTVAVKMLKENASPSELRDLLSEFNVLKQVNH---PHVIKLYGACSQDGPLLLIVEY 806
Cdd:cd06917    9 VGRGSYGAVYRG--YHVKTGR---VVALKVLNLDTDDDDVSDIQKEVALLSQLKLgqpKNIIKYYGSYLKGPSLWIIMDY 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  807 AKYGSLRGFLResrkvgPGYLgsggsrnsssldhpDER--ALTMGDLIsfawqisQGMQYLAEMKLVHRDLAARNILVAE 884
Cdd:cd06917   84 CEGGSIRTLMR------AGPI--------------AERyiAVIMREVL-------VALKFIHKDGIIHRDIKAANILVTN 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  885 GRKMKISDFGLSRDVYEEDSyvKRSQGRIPVKWMAIESLFD-HIYTTQSDVWSFGVLLWEIVTlGGNPYPGIPPERLFNL 963
Cdd:cd06917  137 TGNVKLCDFGVAASLNQNSS--KRSTFVGTPYWMAPEVITEgKYYDTKADIWSLGITTYEMAT-GNPPYSDVDALRAVML 213
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 10862703  964 LKTGHRMERPDNC-SEEMYRLMLQCWKQEPDKRPVFADISK 1003
Cdd:cd06917  214 IPKSKPPRLEGNGySPLLKEFVAACLDEEPKDRLSADELLK 254
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
726-996 6.38e-21

Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK6, also called SSTK, is expressed at the head of elongated sperm. It can phosphorylate histones and associate with heat shock protens HSP90 and HSC70. Male mice deficient in TSSK6 are infertile, showing spermatogenic impairment including reduced sperm counts, impaired DNA condensation, abnormal morphology and decreased motility rates. The TSSK6-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271066 [Multi-domain]  Cd Length: 256  Bit Score: 93.77  E-value: 6.38e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  726 LGKTLGEGEFGKVVKATAFHLKGragytTVAVKMLKENASPSEL--RDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLI 803
Cdd:cd14164    4 LGTTIGEGSFSKVKLATSQKYCC-----KVAIKIVDRRRASPDFvqKFLPRELSILRRVNHPNIVQMFECIEVANGRLYI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  804 VEYAKYGSLRGFLRESRKVgPGylgsggsrnsssldhPDERALtmgdlisFAwQISQGMQYLAEMKLVHRDLAARNILV- 882
Cdd:cd14164   79 VMEAAATDLLQKIQEVHHI-PK---------------DLARDM-------FA-QMVGAVNYLHDMNIVHRDLKCENILLs 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  883 AEGRKMKISDFGLSRDVyeeDSYVKRSQGRIPVK-WMAIESLFDHIYTTQS-DVWSFGVLLWEIVTlGGNPYPGIpperL 960
Cdd:cd14164  135 ADDRKIKIADFGFARFV---EDYPELSTTFCGSRaYTPPEVILGTPYDPKKyDVWSLGVVLYVMVT-GTMPFDET----N 206
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 10862703  961 FNLLKtghRMERPDN------CSEEMYRLMLQCWKQEPDKRP 996
Cdd:cd14164  207 VRRLR---LQQRGVLypsgvaLEEPCRALIRTLLQFNPSTRP 245
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
730-1001 7.22e-21

Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes yeast ATG1 and metazoan homologs including vertebrate ULK1-3. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. It is involved in nutrient sensing and signaling, the assembly of autophagy factors and the execution of autophagy. In metazoans, ATG1 homologs display additional functions. Unc-51 and ULKs have been implicated in neuronal and axonal development. The ATG1/ULK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270911 [Multi-domain]  Cd Length: 251  Bit Score: 93.44  E-value: 7.22e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  730 LGEGEFGKVVKAtaFHLKGRagyTTVAVK-MLKENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVEYAK 808
Cdd:cd14009    1 IGRGSFATVWKG--RHKQTG---EVVAIKeISRKKLNKKLQENLESEIAILKSIKHPNIVRLYDVQKTEDFIYLVLEYCA 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  809 YGSLRGFLRESRKVgpgylgsggsrnsssldhPDERALtmgdliSFAWQISQGMQYLAEMKLVHRDLAARNILVAEGRK- 887
Cdd:cd14009   76 GGDLSQYIRKRGRL------------------PEAVAR------HFMQQLASGLKFLRSKNIIHRDLKPQNLLLSTSGDd 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  888 --MKISDFGLSRDVyEEDSYVKRSQGRiPVkWMAIESLFDHIYTTQSDVWSFGVLLWEIVTlGGNPYPGI-PPERLFNLL 964
Cdd:cd14009  132 pvLKIADFGFARSL-QPASMAETLCGS-PL-YMAPEILQFQKYDAKADLWSVGAILFEMLV-GKPPFRGSnHVQLLRNIE 207
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 10862703  965 KTGHRMERPDNC--SEEMYRLMLQCWKQEPDKRPVFADI 1001
Cdd:cd14009  208 RSDAVIPFPIAAqlSPDCKDLLRRLLRRDPAERISFEEF 246
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
728-954 8.41e-21

Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SIKs are part of a complex network that regulates Na,K-ATPase to maintain sodium homeostasis and blood pressure. Vertebrates contain three forms of SIKs (SIK1-3) from three distinct genes, which display tissue-specific effects. SIK1, also called SNF1LK, controls steroidogenic enzyme production in adrenocortical cells. In the brain, both SIK1 and SIK2 regulate energy metabolism. SIK2, also called QIK or SNF1LK2, is involved in the regulation of gluconeogenesis in the liver and lipogenesis in adipose tissues, where it phosphorylates the insulin receptor substrate-1. In the liver, SIK3 (also called QSK) regulates cholesterol and bile acid metabolism. In addition, SIK2 plays an important role in the initiation of mitosis and regulates the localization of C-Nap1, a centrosome linker protein. The SIK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270973 [Multi-domain]  Cd Length: 253  Bit Score: 93.23  E-value: 8.41e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  728 KTLGEGEFGkVVKaTAFHlkgRAGYTTVAVKML-KENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVEY 806
Cdd:cd14071    6 RTIGKGNFA-VVK-LARH---RITKTEVAIKIIdKSQLDEENLKKIYREVQIMKMLNHPHIIKLYQVMETKDMLYLVTEY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  807 AKYGSLRGFLRESRKvgpgylgsggsrnsssLDHPDERAltmgdliSFaWQISQGMQYLAEMKLVHRDLAARNILVAEGR 886
Cdd:cd14071   81 ASNGEIFDYLAQHGR----------------MSEKEARK-------KF-WQILSAVEYCHKRHIVHRDLKAENLLLDANM 136
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 10862703  887 KMKISDFGLSrDVYEEDSYVKRSQGRIPvkWMAIESLFDHIYT-TQSDVWSFGVLLWEIVTlGGNPYPG 954
Cdd:cd14071  137 NIKIADFGFS-NFFKPGELLKTWCGSPP--YAAPEVFEGKEYEgPQLDIWSLGVVLYVLVC-GALPFDG 201
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
725-1004 9.08e-21

Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein Kinase Kinase Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include the MAPKKKs Saccharomyces cerevisiae Bck1 and Schizosaccharomyces pombe Mkh1, and related proteins. Budding yeast Bck1 is part of the cell integrity MAPK pathway, which is activated by stresses and aggressions to the cell wall. The MAPKKK Bck1, MAPKKs Mkk1 and Mkk2, and the MAPK Slt2 make up the cascade that is important in the maintenance of cell wall homeostasis. Fission yeast Mkh1 is involved in MAPK cascades regulating cell morphology, cell wall integrity, salt resistance, and filamentous growth in response to stress. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The Bck1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270799 [Multi-domain]  Cd Length: 270  Bit Score: 93.60  E-value: 9.08e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  725 VLGKTLGEGEFGKVVkaTAFHLkgragyTT---VAVKMLKENASPSELRD---------LLSEFNVLKQVNHPHVIKLYG 792
Cdd:cd06629    4 VKGELIGKGTYGRVY--LAMNA------TTgemLAVKQVELPKTSSDRADsrqktvvdaLKSEIDTLKDLDHPNIVQYLG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  793 ACSQDGPLLLIVEYAKYGSLRGFLRESRKVGPgylgsggsrnsssldhpderaltmgDLI-SFAWQISQGMQYLAEMKLV 871
Cdd:cd06629   76 FEETEDYFSIFLEYVPGGSIGSCLRKYGKFEE-------------------------DLVrFFTRQILDGLAYLHSKGIL 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  872 HRDLAARNILVAEGRKMKISDFGLSR---DVYEEDSYVKRsQGRIPvkWMAIE--SLFDHIYTTQSDVWSFGVLLWEIVT 946
Cdd:cd06629  131 HRDLKADNILVDLEGICKISDFGISKksdDIYGNNGATSM-QGSVF--WMAPEviHSQGQGYSAKVDIWSLGCVVLEMLA 207
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 10862703  947 lGGNPYPgiPPERLFNLLKTGHRMERPD-----NCSEEMYRLMLQCWKQEPDKRPVFADISKD 1004
Cdd:cd06629  208 -GRRPWS--DDEAIAAMFKLGNKRSAPPvpedvNLSPEALDFLNACFAIDPRDRPTAAELLSH 267
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
722-951 1.45e-20

Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PDK1 carries an N-terminal catalytic domain and a C-terminal pleckstrin homology (PH) domain that binds phosphoinositides. It phosphorylates the activation loop of AGC kinases that are regulated by PI3K such as PKB, SGK, and PKC, among others, and is crucial for their activation. Thus, it contributes in regulating many processes including metabolism, growth, proliferation, and survival. PDK1 also has the ability to autophosphorylate and is constitutively active in mammalian cells. It is essential for normal embryo development and is important in regulating cell volume. The PDK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270733 [Multi-domain]  Cd Length: 278  Bit Score: 93.05  E-value: 1.45e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  722 KNLVLGKTLGEGEFGKVVKATAfhlkgRAGYTTVAVKML------KENASPSELRdllsEFNVLKQVNHPHVIKLYGACS 795
Cdd:cd05581    1 NDFKFGKPLGEGSYSTVVLAKE-----KETGKEYAIKVLdkrhiiKEKKVKYVTI----EKEVLSRLAHPGIVKLYYTFQ 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  796 QDGPLLLIVEYAKYGSLRGFLResrKVGpgylgsggsrnssSLDHPDERAltmgdlisFAWQISQGMQYLAEMKLVHRDL 875
Cdd:cd05581   72 DESKLYFVLEYAPNGDLLEYIR---KYG-------------SLDEKCTRF--------YTAEIVLALEYLHSKGIIHRDL 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  876 AARNILVAEGRKMKISDFGL-----SRDVYEEDSYVKRSQGRIPVK----------WMAIESLFDHIYTTQSDVWSFGVL 940
Cdd:cd05581  128 KPENILLDEDMHIKITDFGTakvlgPDSSPESTKGDADSQIAYNQAraasfvgtaeYVSPELLNEKPAGKSSDLWALGCI 207
                        250
                 ....*....|.
gi 10862703  941 LWEIVTlgGNP 951
Cdd:cd05581  208 IYQMLT--GKP 216
PTK_Jak1_rpt1 cd05077
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 1; Jak1 is widely ...
757-1005 1.69e-20

Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 1; Jak1 is widely expressed in many tissues. Many cytokines are dependent on Jak1 for signaling, including those that use the shared receptor subunits, common gamma chain (IL-2, IL-4, IL-7, IL-9, IL-15, IL-21) and gp130 (IL-6, IL-11, oncostatin M, G-CSF, and IFNs, among others). The many varied interactions of Jak1 and its ubiquitous expression suggest many biological roles. Jak1 is important in neurological development, as well as in lymphoid development and function. It also plays a role in the pathophysiology of cardiac hypertrophy and heart failure. A mutation in the ATP-binding site of Jak1 was identified in a human uterine leiomyosarcoma cell line, resulting in defective cytokine induction and antigen presentation, thus allowing the tumor to evade the immune system. Jak1 is a cytoplasmic (or nonreceptor) PTK containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase domain. The pseudokinase domain shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. It modulates the kinase activity of the C-terminal catalytic domain. The Jak1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270662 [Multi-domain]  Cd Length: 266  Bit Score: 92.69  E-value: 1.69e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  757 VKMLKENASPSElRDLLSEF----NVLKQVNHPHVIKLYGACSQDGPLLLIVEYAKYGSLRGFLResRKVGPgylgsggs 832
Cdd:cd05077   37 IKVILKVLDPSH-RDISLAFfetaSMMRQVSHKHIVLLYGVCVRDVENIMVEEFVEFGPLDLFMH--RKSDV-------- 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  833 rnsssldhpderaLTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNILVAE-------GRKMKISDFGLSRDVYEEDSY 905
Cdd:cd05077  106 -------------LTTPWKFKVAKQLASALSYLEDKDLVHGNVCTKNILLARegidgecGPFIKLSDPGIPITVLSRQEC 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  906 VKrsqgRIPvkWMAIESLFD-HIYTTQSDVWSFGVLLWEIVTLGGNPYPG---IPPERLFNllktGHRMERPDNCsEEMY 981
Cdd:cd05077  173 VE----RIP--WIAPECVEDsKNLSIAADKWSFGTTLWEICYNGEIPLKDktlAEKERFYE----GQCMLVTPSC-KELA 241
                        250       260
                 ....*....|....*....|....
gi 10862703  982 RLMLQCWKQEPDKRPVFADISKDL 1005
Cdd:cd05077  242 DLMTHCMNYDPNQRPFFRAIMRDI 265
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
730-1004 2.38e-20

Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily are mitogen-activated protein kinase (MAPK) kinase kinases (MAPKKKs or MKKKs) and include ASK1, ASK2, and MAPKKK15. ASK1 (also called MAPKKK5) functions in the c-Jun N-terminal kinase (JNK) and p38 MAPK signaling pathways by directly activating their respective MAPKKs, MKK4/MKK7 and MKK3/MKK6. It plays important roles in cytokine and stress responses, as well as in reactive oxygen species-mediated cellular responses. ASK1 is implicated in various diseases mediated by oxidative stress including inschemic heart disease, hypertension, vessel injury, brain ischemia, Fanconi anemia, asthma, and pulmonary edema, among others. ASK2 (also called MAPKKK6) functions only in a heteromeric complex with ASK1, and can activate ASK1 by direct phosphorylation. The function of MAPKKK15 is still unknown. The ASK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270794 [Multi-domain]  Cd Length: 268  Bit Score: 92.09  E-value: 2.38e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  730 LGEGEFGKVVKATAFHLKGRagyttVAVKMLKENASpSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVEYAKY 809
Cdd:cd06624   16 LGKGTFGVVYAARDLSTQVR-----IAIKEIPERDS-REVQPLHEEIALHSRLSHKNIVQYLGSVSEDGFFKIFMEQVPG 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  810 GSLRGFLREsrKVGPgyLGSggsrnsssldhpDERALtmgdlISFAWQISQGMQYLAEMKLVHRDLAARNILV-AEGRKM 888
Cdd:cd06624   90 GSLSALLRS--KWGP--LKD------------NENTI-----GYYTKQILEGLKYLHDNKIVHRDIKGDNVLVnTYSGVV 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  889 KISDFGLSrdvyeedsyvKRSQGRIPV--------KWMAIEsLFDH---IYTTQSDVWSFGVLLWEIVTlGGNPY--PGI 955
Cdd:cd06624  149 KISDFGTS----------KRLAGINPCtetftgtlQYMAPE-VIDKgqrGYGPPADIWSLGCTIIEMAT-GKPPFieLGE 216
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 10862703  956 PPERLFnllKTG----HRmERPDNCSEEMYRLMLQCWKQEPDKRPVFADISKD 1004
Cdd:cd06624  217 PQAAMF---KVGmfkiHP-EIPESLSEEAKSFILRCFEPDPDKRATASDLLQD 265
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
723-954 2.72e-20

Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MARKs, also called Partitioning-defective 1 (Par1) proteins, function as regulators of diverse cellular processes in nematodes, Drosophila, yeast, and vertebrates. They are involved in embryogenesis, epithelial cell polarization, cell signaling, and neuronal differentiation. MARKs phosphorylate tau and related microtubule-associated proteins (MAPs), and regulates microtubule-based intracellular transport. Vertebrates contain four isoforms, namely MARK1 (or Par1c), MARK2 (or Par1b), MARK3 (Par1a), and MARK4 (or MARKL1). Known substrates of MARKs include the cell cycle-regulating phosphatase Cdc25, tyrosine phosphatase PTPH1, MAPK scaffolding protein KSR1, class IIa histone deacetylases, and plakophilin 2. The MARK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270974 [Multi-domain]  Cd Length: 253  Bit Score: 91.81  E-value: 2.72e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  723 NLVLGKTLGEGEFGKVvKATAFHLKGRagytTVAVKML-KENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLL 801
Cdd:cd14072    1 NYRLLKTIGKGNFAKV-KLARHVLTGR----EVAIKIIdKTQLNPSSLQKLFREVRIMKILNHPNIVKLFEVIETEKTLY 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  802 LIVEYAKYGSLRGFLresrkVGPGylgsggsrnssSLDHPDERAltmgdliSFAwQISQGMQYLAEMKLVHRDLAARNIL 881
Cdd:cd14072   76 LVMEYASGGEVFDYL-----VAHG-----------RMKEKEARA-------KFR-QIVSAVQYCHQKRIVHRDLKAENLL 131
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 10862703  882 VAEGRKMKISDFGLSRDvYEEDSYVKRSQGRIPvkWMAIESLFDHIYT-TQSDVWSFGVLLWEIVTlGGNPYPG 954
Cdd:cd14072  132 LDADMNIKIADFGFSNE-FTPGNKLDTFCGSPP--YAAPELFQGKKYDgPEVDVWSLGVILYTLVS-GSLPFDG 201
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
723-996 3.36e-20

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek7 is required for mitotic spindle formation and cytokinesis. It is enriched in the centrosome and is critical for microtubule nucleation. Nek7 is activated by Nek9 during mitosis, and may regulate the p70 ribosomal S6 kinase. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270866 [Multi-domain]  Cd Length: 292  Bit Score: 92.40  E-value: 3.36e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  723 NLVLGKTLGEGEFGKVVKATAFhlkgrAGYTTVAVKMLK--ENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPL 800
Cdd:cd08229   25 NFRIEKKIGRGQFSEVYRATCL-----LDGVPVALKKVQifDLMDAKARADCIKEIDLLKQLNHPNVIKYYASFIEDNEL 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  801 LLIVEYAKYGSLRGFLRESRKvgpgylgsggsrnsssldhpDERALTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNI 880
Cdd:cd08229  100 NIVLELADAGDLSRMIKHFKK--------------------QKRLIPEKTVWKYFVQLCSALEHMHSRRVMHRDIKPANV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  881 LVAEGRKMKISDFGLSRdVYEEDSYVKRSQGRIPVkWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLgGNPYPGiPPERL 960
Cdd:cd08229  160 FITATGVVKLGDLGLGR-FFSSKTTAAHSLVGTPY-YMSPERIHENGYNFKSDIWSLGCLLYEMAAL-QSPFYG-DKMNL 235
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 10862703  961 FNLLKTGHRMERP----DNCSEEMYRLMLQCWKQEPDKRP 996
Cdd:cd08229  236 YSLCKKIEQCDYPplpsDHYSEELRQLVNMCINPDPEKRP 275
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
726-1011 3.42e-20

Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. Dusty protein kinase is also called Receptor-interacting protein kinase 5 (RIPK5 or RIP5) or RIP-homologous kinase. It is widely distributed in the central nervous system, and may be involved in inducing both caspase-dependent and caspase-independent cell death. The Dusty subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270877 [Multi-domain]  Cd Length: 262  Bit Score: 91.78  E-value: 3.42e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  726 LGKTLGEGEFGKVvkataFHLKGRAGYTTVAVKmlkeNASPSELR---DLLSEFNVLKQV-NHPHVIKLYGAC------S 795
Cdd:cd13975    4 LGRELGRGQYGVV-----YACDSWGGHFPCALK----SVVPPDDKhwnDLALEFHYTRSLpKHERIVSLHGSVidysygG 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  796 QDGP-LLLIVEyakygslrgflRESRKVGPGYlgsggsrnsssldhpdERALTMGDLISFAWQISQGMQYLAEMKLVHRD 874
Cdd:cd13975   75 GSSIaVLLIME-----------RLHRDLYTGI----------------KAGLSLEERLQIALDVVEGIRFLHSQGLVHRD 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  875 LAARNILVAEGRKMKISDFGLSRdvyeEDSYVKRSQGRIPVKwMAIEsLFDHIYTTQSDVWSFGVLLWEI----VTLGGN 950
Cdd:cd13975  128 IKLKNVLLDKKNRAKITDLGFCK----PEAMMSGSIVGTPIH-MAPE-LFSGKYDNSVDVYAFGILFWYLcaghVKLPEA 201
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 10862703  951 PYPGIPPERLFNLLKTGHRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADISKDLEKMMVK 1011
Cdd:cd13975  202 FEQCASKDHLWNNVRKGVRPERLPVFDEECWNLMEACWSGDPSQRPLLGIVQPKLQGIMDR 262
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
730-996 3.61e-20

Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. This subfamily is composed of the dual-specificity kinase Myt1, the protein tyrosine kinase Wee1, and similar proteins. These proteins are cell cycle checkpoint kinases that are involved in the regulation of cyclin-dependent kinase CDK1, the master engine for mitosis. CDK1 is kept inactivated through phosphorylation of N-terminal thr (T14 by Myt1) and tyr (Y15 by Myt1 and Wee1) residues. Mitosis progression is ensured through activation of CDK1 by dephoshorylation and inactivation of Myt1/Wee1. The Wee1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270899 [Multi-domain]  Cd Length: 252  Bit Score: 91.29  E-value: 3.61e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  730 LGEGEFGKVVKATAFhLKGRAgyttVAVKMLKEN-ASPSELRDLLSEFN---VLKQvnHPHVIKLYGACSQDGPLLLIVE 805
Cdd:cd13997    8 IGSGSFSEVFKVRSK-VDGCL----YAVKKSKKPfRGPKERARALREVEahaALGQ--HPNIVRYYSSWEEGGHLYIQME 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  806 YAKYGSLRGFLRESrkvgpgylgsggsrnsssldhPDERALTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNILVAEG 885
Cdd:cd13997   81 LCENGSLQDALEEL---------------------SPISKLSEAEVWDLLLQVALGLAFIHSKGIVHLDIKPDNIFISNK 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  886 RKMKISDFGL------SRDVYEEDSyvkrsqgripvKWMAIESLFDHI-YTTQSDVWSFGVLLWEIVTlgGNPYP----- 953
Cdd:cd13997  140 GTCKIGDFGLatrletSGDVEEGDS-----------RYLAPELLNENYtHLPKADIFSLGVTVYEAAT--GEPLPrngqq 206
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 10862703  954 ------GIPPeRLFNLLKtghrmerpdncSEEMYRLMLQCWKQEPDKRP 996
Cdd:cd13997  207 wqqlrqGKLP-LPPGLVL-----------SQELTRLLKVMLDPDPTRRP 243
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
730-1011 3.73e-20

Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MST4 is sometimes referred to as MASK (MST3 and SOK1-related kinase). It plays a role in mitogen-activated protein kinase (MAPK) signaling during cytoskeletal rearrangement, morphogenesis, and apoptosis. It influences cell growth and transformation by modulating the extracellular signal-regulated kinase (ERK) pathway. MST4 may also play a role in tumor formation and progression. It localizes in the Golgi apparatus by interacting with the Golgi matrix protein GM130 and may play a role in cell migration. The MST4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132971 [Multi-domain]  Cd Length: 277  Bit Score: 92.04  E-value: 3.73e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  730 LGEGEFGKVVKAtafhLKGRAgYTTVAVKMLKENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVEYAKY 809
Cdd:cd06640   12 IGKGSFGEVFKG----IDNRT-QQVVAIKIIDLEEAEDEIEDIQQEITVLSQCDSPYVTKYYGSYLKGTKLWIIMEYLGG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  810 GSLRGFLResrkVGPGylgsggsrnsssldhpDERALTmgdliSFAWQISQGMQYLAEMKLVHRDLAARNILVAEGRKMK 889
Cdd:cd06640   87 GSALDLLR----AGPF----------------DEFQIA-----TMLKEILKGLDYLHSEKKIHRDIKAANVLLSEQGDVK 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  890 ISDFGLSRDVyeEDSYVKRSQGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTlGGNPYPGIPPERLFNLLKTGHR 969
Cdd:cd06640  142 LADFGVAGQL--TDTQIKRNTFVGTPFWMAPEVIQQSAYDSKADIWSLGITAIELAK-GEPPNSDMHPMRVLFLIPKNNP 218
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 10862703  970 MERPDNCSEEMYRLMLQCWKQEPDKRPVFADISKdlEKMMVK 1011
Cdd:cd06640  219 PTLVGDFSKPFKEFIDACLNKDPSFRPTAKELLK--HKFIVK 258
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
730-1003 4.60e-20

Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LKB1, also called STK11, was first identified as a tumor suppressor responsible for Peutz-Jeghers syndrome, a disorder that leads to an increased risk of spontaneous epithelial cancer. It serves as a master upstream kinase that activates AMP-activated protein kinase (AMPK) and most AMPK-like kinases. LKB1 and AMPK are part of an energy-sensing pathway that links cell energy to metabolism and cell growth. They play critical roles in the establishment and maintenance of cell polarity, cell proliferation, cytoskeletal organization, as well as T-cell metabolism, including T-cell development, homeostasis, and effector function. To be activated, LKB1 requires the adaptor proteins STe20-Related ADaptor (STRAD) and mouse protein 25 (MO25). The LKB1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271021 [Multi-domain]  Cd Length: 255  Bit Score: 91.16  E-value: 4.60e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  730 LGEGEFGKVVKATAFHLKGRagyttVAVKMLKEnaspSELR-------DLLSEFNVLKQVNHPHVIKLYGACSQD--GPL 800
Cdd:cd14119    1 LGEGSYGKVKEVLDTETLCR-----RAVKILKK----RKLRripngeaNVKREIQILRRLNHRNVIKLVDVLYNEekQKL 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  801 LLIVEYAkYGSLRGFLRESrkvgpgylgsggsrnsssldhPDERaLTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNI 880
Cdd:cd14119   72 YMVMEYC-VGGLQEMLDSA---------------------PDKR-LPIWQAHGYFVQLIDGLEYLHSQGIIHKDIKPGNL 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  881 LVAEGRKMKISDFGLSR--DVYEEDSYVKRSQGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTlGGNPYPGIPPE 958
Cdd:cd14119  129 LLTTDGTLKISDFGVAEalDLFAEDDTCTTSQGSPAFQPPEIANGQDSFSGFKVDIWSAGVTLYNMTT-GKYPFEGDNIY 207
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 10862703  959 RLFNLLKTGhRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADISK 1003
Cdd:cd14119  208 KLFENIGKG-EYTIPDDVDPDLQDLLRGMLEKDPEKRFTIEQIRQ 251
PTK_Jak3_rpt1 cd14208
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 3; Jak3 is ...
724-1005 5.55e-20

Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 3; Jak3 is expressed only in hematopoietic cells. It binds the shared receptor subunit, common gamma chain and thus, is essential in the signaling of cytokines that use it such as IL-2, IL-4, IL-7, IL-9, IL-15, and IL-21. Jak3 is important in lymphoid development and myeloid cell differentiation. Inactivating mutations in Jak3 have been reported in humans with severe combined immunodeficiency (SCID). Jak3 is a cytoplasmic (or nonreceptor) PTK containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase domain. The pseudokinase domain shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. It modulates the kinase activity of the C-terminal catalytic domain. Jaks are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The Jak3 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271110 [Multi-domain]  Cd Length: 260  Bit Score: 91.12  E-value: 5.55e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  724 LVLGKTLGEGEFGKVVKATAFHLK-GRAGYTTVAVKMLK---ENASPSelrdLLSEFNVLKQVNHPHVIKLYGACsQDGP 799
Cdd:cd14208    1 LTFMESLGKGSFTKIYRGLRTDEEdDERCETEVLLKVMDpthGNCQES----FLEAASIMSQISHKHLVLLHGVC-VGKD 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  800 LLLIVEYAKYGSLRGFLRESRKVGPgylgsggsrnsssldhpderaLTMGDLISFAWQISQGMQYLAEMKLVHRDLAARN 879
Cdd:cd14208   76 SIMVQEFVCHGALDLYLKKQQQKGP---------------------VAISWKLQVVKQLAYALNYLEDKQLVHGNVSAKK 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  880 ILVA-EGRK-----MKISDFGLSRDVYEEDSYVKrsqgRIPvkWMAIESLFD-HIYTTQSDVWSFGVLLWEIVTLGGNPY 952
Cdd:cd14208  135 VLLSrEGDKgsppfIKLSDPGVSIKVLDEELLAE----RIP--WVAPECLSDpQNLALEADKWGFGATLWEIFSGGHMPL 208
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 10862703  953 PGIPPERLFNLLKTghRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADISKDL 1005
Cdd:cd14208  209 SALDPSKKLQFYND--RKQLPAPHWIELASLIQQCMSYNPLLRPSFRAIIRDL 259
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
725-954 6.03e-20

Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDKL1-5 and similar proteins. Some CDKLs, like CDKL1 and CDKL3, may be implicated in transformation and others, like CDKL3 and CDKL5, are associated with mental retardation when impaired. CDKL2 plays a role in learning and memory. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270827 [Multi-domain]  Cd Length: 288  Bit Score: 91.61  E-value: 6.03e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  725 VLGkTLGEGEFGKVVKAtafhlKGRAGYTTVAVKMLKENASPSELRDL-LSEFNVLKQVNHPHVIKLYGACSQDGPLLLI 803
Cdd:cd07833    5 VLG-VVGEGAYGVVLKC-----RNKATGEIVAIKKFKESEDDEDVKKTaLREVKVLRQLRHENIVNLKEAFRRKGRLYLV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  804 VEYAKYgSLRGFLRESrkvgPGYLGsggsrnsssldhPDERALTMgdlisfaWQISQGMQYLAEMKLVHRDLAARNILVA 883
Cdd:cd07833   79 FEYVER-TLLELLEAS----PGGLP------------PDAVRSYI-------WQLLQAIAYCHSHNIIHRDIKPENILVS 134
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 10862703  884 EGRKMKISDFGLSRDVYEE-----DSYVKRSQGRIPvkwmaiESLF-DHIYTTQSDVWSFGVLLWEIVTlgGNP-YPG 954
Cdd:cd07833  135 ESGVLKLCDFGFARALTARpasplTDYVATRWYRAP------ELLVgDTNYGKPVDVWAIGCIMAELLD--GEPlFPG 204
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
723-942 7.77e-20

Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. AMPK, also called SNF1 (sucrose non-fermenting1) in yeasts and SnRK1 (SNF1-related kinase1) in plants, is a heterotrimeric enzyme composed of a catalytic alpha subunit and two regulatory subunits, beta and gamma. It is a stress-activated kinase that serves as master regulator of glucose and lipid metabolism by monitoring carbon and energy supplies, via sensing the cell's AMP:ATP ratio. In response to decreased ATP levels, it enhances energy-producing processes and inhibits energy-consuming pathways. Once activated, AMPK phosphorylates a broad range of downstream targets, with effects in carbohydrate metabolism and uptake, lipid and fatty acid biosynthesis, carbon energy storage, and inflammation, among others. Defects in energy homeostasis underlie many human diseases including Type 2 diabetes, obesity, heart disease, and cancer. As a result, AMPK has emerged as a therapeutic target in the treatment of these diseases. The AMPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270981 [Multi-domain]  Cd Length: 256  Bit Score: 90.41  E-value: 7.77e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  723 NLVLGKTLGEGEFGKVVKATafHLkgRAGYTtVAVKML---KENASPSELRdLLSEFNVLKQVNHPHVIKLYGACSQDGP 799
Cdd:cd14079    3 NYILGKTLGVGSFGKVKLAE--HE--LTGHK-VAVKILnrqKIKSLDMEEK-IRREIQILKLFRHPHIIRLYEVIETPTD 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  800 LLLIVEYAKYGSLRGFLRESRKvgpgylgsggsrnsssLDHPDERAltmgdlisFAWQISQGMQYLAEMKLVHRDLAARN 879
Cdd:cd14079   77 IFMVMEYVSGGELFDYIVQKGR----------------LSEDEARR--------FFQQIISGVEYCHRHMVVHRDLKPEN 132
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 10862703  880 ILVAEGRKMKISDFGLSrDVYEEDSYVKRSQGRiPvKWMAIESLFDHIYT-TQSDVWSFGVLLW 942
Cdd:cd14079  133 LLLDSNMNVKIADFGLS-NIMRDGEFLKTSCGS-P-NYAAPEVISGKLYAgPEVDVWSCGVILY 193
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
712-996 8.05e-20

N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Class III myosins are motor proteins with an N-terminal kinase catalytic domain and a C-terminal actin-binding motor domain. Class III myosins are present in the photoreceptors of invertebrates and vertebrates and in the auditory hair cells of mammals. The kinase domain of myosin III can phosphorylate several cytoskeletal proteins, conventional myosin regulatory light chains, and can autophosphorylate the C-terminal motor domain. Myosin III may play an important role in maintaining the structural integrity of photoreceptor cell microvilli. It may also function as a cargo carrier during light-dependent translocation, in photoreceptor cells, of proteins such as transducin and arrestin. The Drosophila class III myosin, called NinaC (Neither inactivation nor afterpotential protein C), is critical in normal adaptation and termination of photoresponse. Vertebrates contain two isoforms of class III myosin, IIIA and IIIB. This subfamily also includes mammalian NIK-like embryo-specific kinase (NESK), Traf2- and Nck-interacting kinase (TNIK), and mitogen-activated protein kinase (MAPK) kinase kinase kinase 4/6. MAP4Ks are involved in some MAPK signaling pathways by activating a MAPK kinase kinase. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. The class III myosin-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270785 [Multi-domain]  Cd Length: 275  Bit Score: 90.82  E-value: 8.05e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  712 LEDP--KWEfprknlvLGKTLGEGEFGKVVKATafHLK-GRagytTVAVKMLKENASPSElrDLLSEFNVLKQV-NHPHV 787
Cdd:cd06608    1 LPDPagIFE-------LVEVIGEGTYGKVYKAR--HKKtGQ----LAAIKIMDIIEDEEE--EIKLEINILRKFsNHPNI 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  788 IKLYGACSQDGP------LLLIVEYAKYGSLRGFLRESRKVGpgylgsggsrnsssldhpdeRALTmGDLISFAWQ-ISQ 860
Cdd:cd06608   66 ATFYGAFIKKDPpggddqLWLVMEYCGGGSVTDLVKGLRKKG--------------------KRLK-EEWIAYILReTLR 124
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  861 GMQYLAEMKLVHRDLAARNILVAEGRKMKISDFGLSRDVyeeDSYVKRSQGRI--PVkWMAIESL-----FDHIYTTQSD 933
Cdd:cd06608  125 GLAYLHENKVIHRDIKGQNILLTEEAEVKLVDFGVSAQL---DSTLGRRNTFIgtPY-WMAPEVIacdqqPDASYDARCD 200
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 10862703  934 VWSFGVLLWEIVTlGGNPYPGIPPER-LFNLLKT-GHRMERPDNCSEEMYRLMLQCWKQEPDKRP 996
Cdd:cd06608  201 VWSLGITAIELAD-GKPPLCDMHPMRaLFKIPRNpPPTLKSPEKWSKEFNDFISECLIKNYEQRP 264
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
728-1001 1.08e-19

Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of fungal Wee1 proteins, also called Swe1 in budding yeast and Mik1 in fission yeast. Yeast Wee1 is required to control cell size. Wee1 is a cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. The fungal Wee1 subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270954 [Multi-domain]  Cd Length: 278  Bit Score: 90.56  E-value: 1.08e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  728 KTLGEGEFGKVVKATAFHLKGRAgyttVAVKMLKENAS-PSELRDLLSEFNVLKQV---NHPHVIKLYGACSQDGPLLLI 803
Cdd:cd14052    6 ELIGSGEFSQVYKVSERVPTGKV----YAVKKLKPNYAgAKDRLRRLEEVSILRELtldGHDNIVQLIDSWEYHGHLYIQ 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  804 VEYAKYGSLRGFLRESRKVGpgylgsggsrnssSLDHPDeraltmgdlisfAWQI----SQGMQYLAEMKLVHRDLAARN 879
Cdd:cd14052   82 TELCENGSLDVFLSELGLLG-------------RLDEFR------------VWKIlvelSLGLRFIHDHHFVHLDLKPAN 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  880 ILVAEGRKMKISDFGLSrDVYEEDSYVKRSQGRipvKWMAIESLFDHIYTTQSDVWSFGVLLWEI---VTLGGNpypGIP 956
Cdd:cd14052  137 VLITFEGTLKIGDFGMA-TVWPLIRGIEREGDR---EYIAPEILSEHMYDKPADIFSLGLILLEAaanVVLPDN---GDA 209
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 10862703  957 PERL-------FNLLKTG--HRMERPDNCSEE--------------MYRLMLQCwkqEPDKRPVFADI 1001
Cdd:cd14052  210 WQKLrsgdlsdAPRLSSTdlHSASSPSSNPPPdppnmpilsgsldrVVRWMLSP---EPDRRPTADDV 274
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
730-996 1.96e-19

Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of MST3, MST4, STK25, Schizosaccharomyces pombe Nak1 and Sid1, Saccharomyces cerevisiae sporulation-specific protein 1 (SPS1), and related proteins. Nak1 is required by fission yeast for polarizing the tips of actin cytoskeleton and is involved in cell growth, cell separation, cell morphology and cell-cycle progression. Sid1 is a component in the septation initiation network (SIN) signaling pathway, and plays a role in cytokinesis. SPS1 plays a role in regulating proteins required for spore wall formation. MST4 plays a role in mitogen-activated protein kinase (MAPK) signaling during cytoskeletal rearrangement, morphogenesis, and apoptosis. MST3 phosphorylates the STK NDR and may play a role in cell cycle progression and cell morphology. STK25 may play a role in the regulation of cell migration and polarization. The MST3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270786 [Multi-domain]  Cd Length: 274  Bit Score: 89.61  E-value: 1.96e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  730 LGEGEFGKVVKATAFHLKgragyTTVAVKMLKENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVEYAKY 809
Cdd:cd06609    9 IGKGSFGEVYKGIDKRTN-----QVVAIKVIDLEEAEDEIEDIQQEIQFLSQCDSPYITKYYGSFLKGSKLWIIMEYCGG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  810 GSLRGFLResrkvgPGYLgsggsrnsssldhpDERAltmgdlISF-AWQISQGMQYLAEMKLVHRDLAARNILVAEGRKM 888
Cdd:cd06609   84 GSVLDLLK------PGPL--------------DETY------IAFiLREVLLGLEYLHSEGKIHRDIKAANILLSEEGDV 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  889 KISDFGLSRDVyeEDSYVKRSQ--GrIPVkWMAIESLFDHIYTTQSDVWSFGVLLWEIVTlGGNPYPGIPPER-LFNLLK 965
Cdd:cd06609  138 KLADFGVSGQL--TSTMSKRNTfvG-TPF-WMAPEVIKQSGYDEKADIWSLGITAIELAK-GEPPLSDLHPMRvLFLIPK 212
                        250       260       270
                 ....*....|....*....|....*....|.
gi 10862703  966 TGHRMERPDNCSEEMYRLMLQCWKQEPDKRP 996
Cdd:cd06609  213 NNPPSLEGNKFSKPFKDFVELCLNKDPKERP 243
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
730-1006 2.25e-19

Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes three leucine-rich repeat receptor-like kinases (LRR-RLKs): Arabidopsis thaliana BAK1 and CLAVATA1 (CLV1), and Physcomitrella patens CLL1B clavata1-like receptor S/T protein kinase. BAK1 functions in various signaling pathways. It plays a role in BR (brassinosteroid)-regulated plant development as a co-receptor of BRASSINOSTEROID (BR) INSENSITIVE 1 (BRI1), the receptor for BRs, and is required for full activation of BR signaling. It also modulates pathways involved in plant resistance to pathogen infection (pattern-triggered immunity, PTI) and herbivore attack (wound- or herbivore feeding-induced accumulation of jasmonic acid (JA) and JA-isoleucine. CLV1, directly binds small signaling peptides, CLAVATA3 (CLV3) and CLAVATA3/EMBRYO SURROUNDING REGI0N (CLE), to restrict stem cell proliferation: the CLV3-CLV1-WUS (WUSCHEL) module influences stem cell maintenance in the shoot apical meristem, and the CLE40 (CLAVATA3/EMBRYO SURROUNDING REGION40) -ACR4 (CRINKLY4) -CLV1- WOX5 (WUSCHEL-RELATED HOMEOBOX5) module at the root apical meristem. The STK_BAK1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271134 [Multi-domain]  Cd Length: 270  Bit Score: 89.48  E-value: 2.25e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  730 LGEGEFGKVVKATAfhlkgrAGYTTVAVKMLKENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVEYAKY 809
Cdd:cd14664    1 IGRGGAGTVYKGVM------PNGTLVAVKRLKGEGTQGGDHGFQAEIQTLGMIRHRNIVRLRGYCSNPTTNLLVYEYMPN 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  810 GSLRGFLRESRKVGPgylgsggsrnssSLDHPDERALTMGDlisfawqiSQGMQYL---AEMKLVHRDLAARNILVAEGR 886
Cdd:cd14664   75 GSLGELLHSRPESQP------------PLDWETRQRIALGS--------ARGLAYLhhdCSPLIIHRDVKSNNILLDEEF 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  887 KMKISDFGLSRDVYEEDSYVKRS-QGRIpvKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTlGGNPYPGIPPERLFNLLK 965
Cdd:cd14664  135 EAHVADFGLAKLMDDKDSHVMSSvAGSY--GYIAPEYAYTGKVSEKSDVYSYGVVLLELIT-GKRPFDEAFLDDGVDIVD 211
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 10862703  966 TGHRMERpDNCSE-----------------EMYRLMLQCWKQEPDKRPVFADISKDLE 1006
Cdd:cd14664  212 WVRGLLE-EKKVEalvdpdlqgvykleeveQVFQVALLCTQSSPMERPTMREVVRMLE 268
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
723-1001 2.71e-19

Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of MEKK3, MEKK2, and related proteins; all contain an N-terminal PB1 domain, which mediates oligomerization, and a C-terminal catalytic domain. MEKK2 and MEKK3 are MAPK kinase kinases (MAPKKKs or MKKK) that activate MEK5 (also called MKK5), which activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK3 plays an essential role in embryonic angiogenesis and early heart development. MEKK2 and MEKK3 can also activate the MAPKs, c-Jun N-terminal kinase (JNK) and p38, through their respective MAPKKs. The MEKK3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270795 [Multi-domain]  Cd Length: 260  Bit Score: 88.95  E-value: 2.71e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  723 NLVLGKTLGEGEFGKVVKATAFHlKGRagytTVAVKML----KENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDG 798
Cdd:cd06625    1 NWKQGKLLGQGAFGQVYLCYDAD-TGR----ELAVKQVeidpINTEASKEVKALECEIQLLKNLQHERIVQYYGCLQDEK 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  799 PLLLIVEYAKYGSLRGFLResrKVGpgylgsggsrnsssldhpderALTMGDLISFAWQISQGMQYLAEMKLVHRDLAAR 878
Cdd:cd06625   76 SLSIFMEYMPGGSVKDEIK---AYG---------------------ALTENVTRKYTRQILEGLAYLHSNMIVHRDIKGA 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  879 NILVAEGRKMKISDFGLSRDVyeedSYVKRSQGRIPVK----WMAIESLFDHIYTTQSDVWSFGVLLWEIVTLGgnpypg 954
Cdd:cd06625  132 NILRDSNGNVKLGDFGASKRL----QTICSSTGMKSVTgtpyWMSPEVINGEGYGRKADIWSVGCTVVEMLTTK------ 201
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 10862703  955 iPP-------ERLFNLLKTGHRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADI 1001
Cdd:cd06625  202 -PPwaefepmAAIFKIATQPTNPQLPPHVSEDARDFLSLIFVRNKKQRPSAEEL 254
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
727-1003 2.95e-19

Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK1 is a MAPK kinase kinase (MAPKKK or MKKK) that phosphorylates and activates activates the ERK1/2 and c-Jun N-terminal kinase (JNK) pathways by activating their respective MAPKKs, MEK1/2 and MKK4/MKK7, respectively. MEKK1 is important in regulating cell survival and apoptosis. MEKK1 also plays a role in cell migration, tissue maintenance and homeostasis, and wound healing. The MEKK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270800 [Multi-domain]  Cd Length: 268  Bit Score: 89.03  E-value: 2.95e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  727 GKTLGEGEFgkvvkATAFHLKGRAGYTTVAVKMLKE-NASPSELRD----LLSEFNVLKQVNHPHVIKLYGACSQDGPLL 801
Cdd:cd06630    5 GPLLGTGAF-----SSCYQARDVKTGTLMAVKQVSFcRNSSSEQEEvveaIREEIRMMARLNHPNIVRMLGATQHKSHFN 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  802 LIVEYAKYGSLRGFLResrKVGPgylgsggsrnsssldhpderaLTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNIL 881
Cdd:cd06630   80 IFVEWMAGGSVASLLS---KYGA---------------------FSENVIINYTLQILRGLAYLHDNQIIHRDLKGANLL 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  882 V-AEGRKMKISDFGLSRDVYEEDSYVKRSQGRI--PVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTlggnpypGIPP- 957
Cdd:cd06630  136 VdSTGQRLRIADFGAAARLASKGTGAGEFQGQLlgTIAFMAPEVLRGEQYGRSCDVWSVGCVIIEMAT-------AKPPw 208
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 10862703  958 ------ERLFNLLKTGHRMER---PDNCSEEMYRLMLQCWKQEPDKRPVFADISK 1003
Cdd:cd06630  209 naekisNHLALIFKIASATTPppiPEHLSPGLRDVTLRCLELQPEDRPPARELLK 263
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
730-1001 3.90e-19

Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include the MAPKKs Polymyxin B resistance protein 2 (PBS2) from Saccharomyces cerevisiae, Wis1 from Schizosaccharomyces pombe, and related proteins. PBS2 and Wis1 are components of stress-activated MAPK cascades in budding and fission yeast, respectively. PBS2 is the specific activator of the MAPK Hog1, which plays a central role in the response of budding yeast to stress including exposure to arsenite and hyperosmotic environments. Wis1 phosphorylates and activates the MAPK Sty1 (also called Spc1 or Phh1), which stimulates a transcriptional response to a wide range of cellular insults through the bZip transcription factors Atf1, Pcr1, and Pap1. The PBS2 subfamily is part of a larger superfamily that includes the catalytic domains of STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132953 [Multi-domain]  Cd Length: 286  Bit Score: 89.14  E-value: 3.90e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  730 LGEGEFGKVVKAtaFHlkgRAGYTTVAVKMLKENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVEYAKY 809
Cdd:cd06622    9 LGKGNYGSVYKV--LH---RPTGVTMAMKEIRLELDESKFNQIIMELDILHKAVSPYIVDFYGAFFIEGAVYMCMEYMDA 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  810 GSLRGFLRESRKVGpgylgsggsrnssSLDHPDERALTmgdlisfaWQISQGMQYLAE-MKLVHRDLAARNILVAEGRKM 888
Cdd:cd06622   84 GSLDKLYAGGVATE-------------GIPEDVLRRIT--------YAVVKGLKFLKEeHNIIHRDVKPTNVLVNGNGQV 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  889 KISDFGLSRDVyeEDSYVKRSQGriPVKWMAIESLFDH------IYTTQSDVWSFGVLLWEIvTLGGNPYPGIPPERLFN 962
Cdd:cd06622  143 KLCDFGVSGNL--VASLAKTNIG--CQSYMAPERIKSGgpnqnpTYTVQSDVWSLGLSILEM-ALGRYPYPPETYANIFA 217
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 10862703  963 LLKT---GHRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADI 1001
Cdd:cd06622  218 QLSAivdGDPPTLPSGYSDDAQDFVAKCLNKIPNRRPTYAQL 259
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
728-1003 1.06e-18

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Neks are involved in the regulation of downstream processes following the activation of Cdc2, and many of their functions are cell cycle-related. They play critical roles in microtubule dynamics during ciliogenesis and mitosis. The specific function of Nek5 is unknown. Nek5 is one in a family of 11 different Neks (Nek1-11). The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173765 [Multi-domain]  Cd Length: 257  Bit Score: 86.94  E-value: 1.06e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  728 KTLGEGEFGKVVKAtafhlKGRAGYTTVAVKMLKENASPSELRDL-LSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVEY 806
Cdd:cd08225    6 KKIGEGSFGKIYLA-----KAKSDSEHCVIKEIDLTKMPVKEKEAsKKEVILLAKMKHPNIVTFFASFQENGRLFIVMEY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  807 AKYGSLRGFLRESRKVgpgylgsggsrnsssLDHPDEraltmgdLISFAWQISQGMQYLAEMKLVHRDLAARNILVAE-G 885
Cdd:cd08225   81 CDGGDLMKRINRQRGV---------------LFSEDQ-------ILSWFVQISLGLKHIHDRKILHRDIKSQNIFLSKnG 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  886 RKMKISDFGLSRDVYEEDSYVKRSQGrIPVkWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLgGNPYPGIPPERLFNLLK 965
Cdd:cd08225  139 MVAKLGDFGIARQLNDSMELAYTCVG-TPY-YLSPEICQNRPYNNKTDIWSLGCVLYELCTL-KHPFEGNNLHQLVLKIC 215
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 10862703  966 TGHRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADISK 1003
Cdd:cd08225  216 QGYFAPISPNFSRDLRSLISQLFKVSPRDRPSITSILK 253
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
725-954 1.42e-18

Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CCRK was previously called p42. It is a Cyclin-Dependent Kinase (CDK)-Activating Kinase (CAK) which is essential for the activation of CDK2. It is indispensable for cell growth and has been implicated in the progression of glioblastoma multiforme. In the heart, a splice variant of CCRK with a different C-terminal half is expressed; this variant promotes cardiac cell growth and survival and is significantly down-regulated during the development of heart failure. The CCRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270826 [Multi-domain]  Cd Length: 287  Bit Score: 87.38  E-value: 1.42e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  725 VLGKtLGEGEFGKVVKAtafhlKGRAGYTTVAVKML----KENASPSELrdlLSEFNVLKQVN-HPHVIKLYGACSQDGP 799
Cdd:cd07832    4 ILGR-IGEGAHGIVFKA-----KDRETGETVALKKValrkLEGGIPNQA---LREIKALQACQgHPYVVKLRDVFPHGTG 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  800 LLLIVEYAKyGSLRGFLRESrkvgpgylgsggsrnsssldhpdERALTMGDLISFAWQISQGMQYLAEMKLVHRDLAARN 879
Cdd:cd07832   75 FVLVFEYML-SSLSEVLRDE-----------------------ERPLTEAQVKRYMRMLLKGVAYMHANRIMHRDLKPAN 130
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 10862703  880 ILVAEGRKMKISDFGLSRDVYEEDSYVKRSQgrIPVKW-MAIESLF-DHIYTTQSDVWSFGVLLWEIvtLGGNP-YPG 954
Cdd:cd07832  131 LLISSTGVLKIADFGLARLFSEEDPRLYSHQ--VATRWyRAPELLYgSRKYDEGVDLWAVGCIFAEL--LNGSPlFPG 204
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
730-1001 1.59e-18

Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LRRK2 is one of two vertebrate LRRKs which show complementary expression in the brain. Mutations in LRRK2, found in the kinase, ROC-COR, and WD40 domains, are linked to both familial and sporadic forms of Parkinson's disease. The most prevalent mutation, G2019S located in the activation loop of the kinase domain, increases kinase activity. The R1441C/G mutations in the GTPase domain have also been reported to influence kinase activity. LRRKs are also classified as ROCO proteins because they contain a ROC (Ras of complex proteins)/GTPase domain followed by a COR (C-terminal of ROC) domain of unknown function. In addition, LRRKs contain a catalytic kinase domain and protein-protein interaction motifs including a WD40 domain, LRRs and ankyrin (ANK) repeats. LRRKs possess both GTPase and kinase activities, with the ROC domain acting as a molecular switch for the kinase domain, cycling between a GTP-bound state which drives kinase activity and a GDP-bound state which decreases the activity. The LRRK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270970 [Multi-domain]  Cd Length: 252  Bit Score: 86.54  E-value: 1.59e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  730 LGEGEFGKVVKATafhLKGRagytTVAVKMLKENASpseLRDLLSEFNVLKQVNHPHVIKLYGACSQdgPLLLIVEYAKY 809
Cdd:cd14068    2 LGDGGFGSVYRAV---YRGE----DVAVKIFNKHTS---FRLLRQELVVLSHLHHPSLVALLAAGTA--PRMLVMELAPK 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  810 GSLRGFLREsrkvgpgylgsggsrnsssldhpDERALTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNILVAEGRK-- 887
Cdd:cd14068   70 GSLDALLQQ-----------------------DNASLTRTLQHRIALHVADGLRYLHSAMIIYRDLKPHNVLLFTLYPnc 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  888 ---MKISDFGLSRdvYEEDSYVKRSQGRIPVKWMAIeSLFDHIYTTQSDVWSFGVLLWEIVTLGGNPYPGIPPERLFNLL 964
Cdd:cd14068  127 aiiAKIADYGIAQ--YCCRMGIKTSEGTPGFRAPEV-ARGNVIYNQQADVYSFGLLLYDILTCGERIVEGLKFPNEFDEL 203
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 10862703  965 KTGHRMERP---DNCS--EEMYRLMLQCWKQEPDKRPVFADI 1001
Cdd:cd14068  204 AIQGKLPDPvkeYGCApwPGVEALIKDCLKENPQCRPTSAQV 245
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
728-1001 1.64e-18

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Nek2 subfamily includes Aspergillus nidulans NIMA kinase, the founding member of the Nek family, which was identified in a screen for cell cycle mutants prevented from entering mitosis. NIMA is essential for mitotic entry and progression through mitosis, and its degradation is essential for mitotic exit. NIMA is involved in nuclear membrane fission. Vertebrate Nek2 is a cell cycle-regulated STK, localized in centrosomes and kinetochores, that regulates centrosome splitting at the G2/M phase. It also interacts with other mitotic kinases such as Polo-like kinase 1 and may play a role in spindle checkpoint. An increase in the expression of the human NEK2 gene is strongly associated with the progression of non-Hodgkin lymphoma. Nek2 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. It The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270857 [Multi-domain]  Cd Length: 265  Bit Score: 86.83  E-value: 1.64e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  728 KTLGEGEFGKVVKAtafhlKGRAGYTTVAVKMLK-ENASPSELRDLLSEFNVLKQVNHPHVIKLYG-----ACSQdgpLL 801
Cdd:cd08217    6 ETIGKGSFGTVRKV-----RRKSDGKILVWKEIDyGKMSEKEKQQLVSEVNILRELKHPNIVRYYDrivdrANTT---LY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  802 LIVEYAKYGSLRGFLRESRKVGpGYLgsggsrnsssldhpDEraltmgdliSFAWQI-SQGMQYLAE--------MKLVH 872
Cdd:cd08217   78 IVMEYCEGGDLAQLIKKCKKEN-QYI--------------PE---------EFIWKIfTQLLLALYEchnrsvggGKILH 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  873 RDLAARNILVAEGRKMKISDFGLSRDVYEEDSYVKRSQGrIPVkWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLGgnpy 952
Cdd:cd08217  134 RDLKPANIFLDSDNNVKLGDFGLARVLSHDSSFAKTYVG-TPY-YMSPELLNEQSYDEKSDIWSLGCLIYELCALH---- 207
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 10862703  953 pgiPP------ERLFNLLKTGHRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADI 1001
Cdd:cd08217  208 ---PPfqaanqLELAKKIKEGKFPRIPSRYSSELNEVIKSMLNVDPDKRPSVEEL 259
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
725-954 1.67e-18

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK7 plays essential roles in the cell cycle and in transcription. It associates with cyclin H and MAT1 and acts as a CDK-Activating Kinase (CAK) by phosphorylating and activating cell cycle CDKs (CDK1/2/4/6). In the brain, it activates CDK5. CDK7 is also a component of the general transcription factor TFIIH, which phosphorylates the C-terminal domain (CTD) of RNA polymerase II when it is bound with unphosphorylated DNA, as present in the pre-initiation complex. Following phosphorylation, the CTD dissociates from the DNA which allows transcription initiation. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK7 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270833 [Multi-domain]  Cd Length: 298  Bit Score: 87.24  E-value: 1.67e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  725 VLGKTLGEGEFGKVVKATAfHLKGRagytTVAVKMLKENaSPSELRD-----LLSEFNVLKQVNHPHVIKLYGACSQDGP 799
Cdd:cd07841    3 EKGKKLGEGTYAVVYKARD-KETGR----IVAIKKIKLG-ERKEAKDginftALREIKLLQELKHPNIIGLLDVFGHKSN 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  800 LLLIVEYAKyGSLRGFLRESRKVgpgylgsggsrnsssldhpderaLTMGDLISFAWQISQGMQYLAEMKLVHRDLAARN 879
Cdd:cd07841   77 INLVFEFME-TDLEKVIKDKSIV-----------------------LTPADIKSYMLMTLRGLEYLHSNWILHRDLKPNN 132
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 10862703  880 ILVAEGRKMKISDFGLSRDvYEEDSYVKRSQgrIPVKWM-AIESLFD-HIYTTQSDVWSFGVLLWEIvtLGGNPY-PG 954
Cdd:cd07841  133 LLIASDGVLKLADFGLARS-FGSPNRKMTHQ--VVTRWYrAPELLFGaRHYGVGVDMWSVGCIFAEL--LLRVPFlPG 205
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
730-989 1.71e-18

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK phosphorylates myosin regulatory light chain and controls the contraction of all muscle types. In vertebrates, different MLCKs function in smooth (MLCK1), skeletal (MLCK2), and cardiac (MLCK3) muscles. A fourth protein, MLCK4, has also been identified through comprehensive genome analysis although it has not been biochemically characterized. MLCK4 (or MYLK4 or SgK085) contains a single kinase domain near the C-terminus. The MLCK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271095 [Multi-domain]  Cd Length: 261  Bit Score: 86.51  E-value: 1.71e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  730 LGEGEFGKVVKATAfhlkgRAGYTTVAVKMLKENaSPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVEYAKY 809
Cdd:cd14193   12 LGGGRFGQVHKCEE-----KSSGLKLAAKIIKAR-SQKEKEEVKNEIEVMNQLNHANLIQLYDAFESRNDIVLVMEYVDG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  810 GSLRgflreSRKVGPGYlgsggsrnsssldhpderALTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNILVA--EGRK 887
Cdd:cd14193   86 GELF-----DRIIDENY------------------NLTELDTILFIKQICEGIQYMHQMYILHLDLKPENILCVsrEANQ 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  888 MKISDFGLSRdvyeedSYVKRSQGRIPV---KWMAIESLFDHIYTTQSDVWSFGVLLWEIVTlGGNPYPGIPP-ERLFNL 963
Cdd:cd14193  143 VKIIDFGLAR------RYKPREKLRVNFgtpEFLAPEVVNYEFVSFPTDMWSLGVIAYMLLS-GLSPFLGEDDnETLNNI 215
                        250       260       270
                 ....*....|....*....|....*....|....
gi 10862703  964 LKTGHRMERPD--NCSEE----MYRLML--QCWK 989
Cdd:cd14193  216 LACQWDFEDEEfaDISEEakdfISKLLIkeKSWR 249
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
730-1002 1.95e-18

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 10; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. No function has yet been ascribed to Nek10. The gene encoding Nek10 is a putative causative gene for breast cancer; it is located within a breast cancer susceptibility loci on chromosome 3p24. Nek10 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270867 [Multi-domain]  Cd Length: 270  Bit Score: 86.79  E-value: 1.95e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  730 LGEGEFGKVVKATafhlKGRAGYTTVAVKML---------KENASPSELRDLLSEFNVLK-QVNHPHVIKLYGACSQDGP 799
Cdd:cd08528    8 LGSGAFGCVYKVR----KKSNGQTLLALKEInmtnpafgrTEQERDKSVGDIISEVNIIKeQLRHPNIVRYYKTFLENDR 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  800 LLLIVEYAKYGSLRGFLRESRKVGPGYlgsggsrnsssldhPDERALTMgdlisFAwQISQGMQYL-AEMKLVHRDLAAR 878
Cdd:cd08528   84 LYIVMELIEGAPLGEHFSSLKEKNEHF--------------TEDRIWNI-----FV-QMVLALRYLhKEKQIVHRDLKPN 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  879 NILVAEGRKMKISDFGLSRDVYEEDSYVKRSQGRIpVKWMAiESLFDHIYTTQSDVWSFGVLLWEIVTLGgnpypgiPPE 958
Cdd:cd08528  144 NIMLGEDDKVTITDFGLAKQKGPESSKMTSVVGTI-LYSCP-EIVQNEPYGEKADIWALGCILYQMCTLQ-------PPF 214
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 10862703  959 RLFNLLKTGHRM--ERPDNCSEEMYRLMLQ-----CWKQEPDKRPVFADIS 1002
Cdd:cd08528  215 YSTNMLTLATKIveAEYEPLPEGMYSDDITfvirsCLTPDPEARPDIVEVS 265
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
725-996 2.24e-18

Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of human MAK and MAK-related kinase (MRK), Saccharomyces cerevisiae Ime2p, Schizosaccharomyces pombe Mei4-dependent protein 3 (Mde3) and Pit1, Caenorhabditis elegans dyf-5, Arabidopsis thaliana MHK, and similar proteins. These proteins play important roles during meiosis. MAK is highly expressed in testicular cells specifically in the meiotic phase, but is not essential for spermatogenesis and fertility. It functions as a coactivator of the androgen receptor in prostate cells. MRK, also called Intestinal Cell Kinase (ICK), is expressed ubiquitously, with highest expression in the ovary and uterus. A missense mutation in MRK causes endocrine-cerebro-osteodysplasia, suggesting that this protein plays an important role in the development of many organs. MAK and MRK may be involved in regulating cell cycle and cell fate. Ime2p is a meiosis-specific kinase that is important during meiotic initiation and during the later stages of meiosis. Mde3 functions downstream of the transcription factor Mei-4 which is essential for meiotic prophase I. The MAK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270824 [Multi-domain]  Cd Length: 283  Bit Score: 86.82  E-value: 2.24e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  725 VLGKTLGEGEFGKVVKAtafhlKGRAGYTTVAVKMLKEN-ASPSE---LRDLLSefnvLKQVN-HPHVIKLYGACSQDGP 799
Cdd:cd07830    2 KVIKQLGDGTFGSVYLA-----RNKETGELVAIKKMKKKfYSWEEcmnLREVKS----LRKLNeHPNIVKLKEVFRENDE 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  800 LLLIVEYAKyGSLRGFLReSRKVGPgylgsggsrnsssldhpderaLTMGDLISFAWQISQGMQYLAEMKLVHRDLAARN 879
Cdd:cd07830   73 LYFVFEYME-GNLYQLMK-DRKGKP---------------------FSESVIRSIIYQILQGLAHIHKHGFFHRDLKPEN 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  880 ILVAEGRKMKISDFGLSRDVYEED---SYVKRSQGRIPvkwmaiESLFDH-IYTTQSDVWSFGVLLWEIVTL-----G-- 948
Cdd:cd07830  130 LLVSGPEVVKIADFGLAREIRSRPpytDYVSTRWYRAP------EILLRStSYSSPVDIWALGCIMAELYTLrplfpGss 203
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 10862703  949 ------------GNPYPGIPPE--RLFNLL------KTGHRMERP-DNCSEEMYRLMLQCWKQEPDKRP 996
Cdd:cd07830  204 eidqlykicsvlGTPTKQDWPEgyKLASKLgfrfpqFAPTSLHQLiPNASPEAIDLIKDMLRWDPKKRP 272
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
728-995 2.66e-18

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKB-beta is the predominant PKB isoform expressed in insulin-responsive tissues. It plays a critical role in the regulation of glucose homeostasis. It is also implicated in muscle cell differentiation. Mice deficient in PKB-beta display normal growth weights but exhibit severe insulin resistance and diabetes, accompanied by lipoatrophy and B-cell failure. PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain.The PKB-beta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173686 [Multi-domain]  Cd Length: 323  Bit Score: 87.37  E-value: 2.66e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  728 KTLGEGEFGKVV----KATAFHLkgragyttvAVKMLKENA--SPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLL 801
Cdd:cd05595    1 KLLGKGTFGKVIlvreKATGRYY---------AMKILRKEViiAKDEVAHTVTESRVLQNTRHPFLTALKYAFQTHDRLC 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  802 LIVEYAKYGSLrgFLRESRkvgpgylgsggsrnsssldhpdERALTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNIL 881
Cdd:cd05595   72 FVMEYANGGEL--FFHLSR----------------------ERVFTEDRARFYGAEIVSALEYLHSRDVVYRDIKLENLM 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  882 VAEGRKMKISDFGLSRDVYEEDSYVKRSQGrIPvKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTlGGNPYPGIPPERLF 961
Cdd:cd05595  128 LDKDGHIKITDFGLCKEGITDGATMKTFCG-TP-EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPFYNQDHERLF 204
                        250       260       270
                 ....*....|....*....|....*....|....
gi 10862703  962 NLLKTgHRMERPDNCSEEMYRLMLQCWKQEPDKR 995
Cdd:cd05595  205 ELILM-EEIRFPRTLSPEAKSLLAGLLKKDPKQR 237
STKc_RIP2 cd14026
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze ...
730-1009 2.67e-18

Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RIP2, also called RICK or CARDIAK, harbors a C-terminal Caspase Activation and Recruitment domain (CARD) belonging to the Death domain (DD) superfamily. It functions as an effector kinase downstream of the pattern recognition receptors from the Nod-like (NLR) family, Nod1 and Nod2, which recognizes bacterial peptidoglycans released upon infection. RIP2 may also be involved in regulating wound healing and keratinocyte proliferation. RIP kinases serve as essential sensors of cellular stress. The RIP2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270928 [Multi-domain]  Cd Length: 284  Bit Score: 86.51  E-value: 2.67e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  730 LGEGEFGKVVKATafHLKGRagyTTVAVKMLKENA--SPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVEYA 807
Cdd:cd14026    5 LSRGAFGTVSRAR--HADWR---VTVAIKCLKLDSpvGDSERNCLLKEAEILHKARFSYILPILGICNEPEFLGIVTEYM 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  808 KYGSLRGFLRESRkvgpgylgsggsrnssslDHPDeraltmgdlisFAW--------QISQGMQYLAEMK--LVHRDLAA 877
Cdd:cd14026   80 TNGSLNELLHEKD------------------IYPD-----------VAWplrlrilyEIALGVNYLHNMSppLLHHDLKT 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  878 RNILVAEGRKMKISDFGLSRdvYEEDSYVK-RSQGRIP----VKWMAIESlFDHIYTTQS----DVWSFGVLLWEIVTLg 948
Cdd:cd14026  131 QNILLDGEFHVKIADFGLSK--WRQLSISQsRSSKSAPeggtIIYMPPEE-YEPSQKRRAsvkhDIYSYAIIMWEVLSR- 206
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 10862703  949 GNPYPGI--PPERLFNLLKtGHR---------MERPDNcsEEMYRLMLQCWKQEPDKRPVFADISKDLEKMM 1009
Cdd:cd14026  207 KIPFEEVtnPLQIMYSVSQ-GHRpdtgedslpVDIPHR--ATLINLIESGWAQNPDERPSFLKCLIELEPVL 275
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
730-954 3.08e-18

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK2 (or MYLK2) phosphorylates myosin regulatory light chain and controls the contraction of skeletal muscles. MLCK2 contains a single kinase domain near the C-terminus followed by a regulatory segment containing an autoinhibitory Ca2+/calmodulin binding site. The MLCK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271092 [Multi-domain]  Cd Length: 261  Bit Score: 85.74  E-value: 3.08e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  730 LGEGEFGKVVKATafhlKGRAGYTTVAVKMLKENASPSELrdLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVEYAKY 809
Cdd:cd14190   12 LGGGKFGKVHTCT----EKRTGLKLAAKVINKQNSKDKEM--VLLEIQVMNQLNHRNLIQLYEAIETPNEIVLFMEYVEG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  810 GSLrgFLResrkvgpgylgsggsrnssSLDhpDERALTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNILV--AEGRK 887
Cdd:cd14190   86 GEL--FER-------------------IVD--EDYHLTEVDAMVFVRQICEGIQFMHQMRVLHLDLKPENILCvnRTGHQ 142
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 10862703  888 MKISDFGLSRDvYEEDSYVKRSQGrIPvKWMAIESL-FDHIyTTQSDVWSFGVLLWEIVTlGGNPYPG 954
Cdd:cd14190  143 VKIIDFGLARR-YNPREKLKVNFG-TP-EFLSPEVVnYDQV-SFPTDMWSMGVITYMLLS-GLSPFLG 205
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
730-894 3.37e-18

Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large family of typical PKs that includes serine/threonine kinases (STKs), protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins, as well as pseudokinases that lack crucial residues for catalytic activity and/or ATP binding. It also includes phosphoinositide 3-kinases (PI3Ks), aminoglycoside 3'-phosphotransferases (APHs), choline kinase (ChoK), Actin-Fragmin Kinase (AFK), and the atypical RIO and Abc1p-like protein kinases. These proteins catalyze the transfer of the gamma-phosphoryl group from ATP to their target substrates; these include serine/threonine/tyrosine residues in proteins for typical or atypical PKs, the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives for PI3Ks, the 4-hydroxyl of PtdIns for PI4Ks, and other small molecule substrates for APH/ChoK and similar proteins such as aminoglycosides, macrolides, choline, ethanolamine, and homoserine.


Pssm-ID: 270870 [Multi-domain]  Cd Length: 136  Bit Score: 82.10  E-value: 3.37e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  730 LGEGEFGKVVKAtafhlKGRAGYTTVAVKMLKENASPsELRDLLSEFNVLKQV-NH-PHVIKLYGACSQDGPLLLIVEYA 807
Cdd:cd13968    1 MGEGASAKVFWA-----EGECTTIGVAVKIGDDVNNE-EGEDLESEMDILRRLkGLeLNIPKVLVTEDVDGPNILLMELV 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  808 KYGSLRgflresrkvgpgylgsggsrnssslDHPDERALTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNILVAEGRK 887
Cdd:cd13968   75 KGGTLI-------------------------AYTQEEELDEKDVESIMYQLAECMRLLHSFHLIHRDLNNDNILLSEDGN 129

                 ....*..
gi 10862703  888 MKISDFG 894
Cdd:cd13968  130 VKLIDFG 136
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
722-952 3.55e-18

Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK1 and TSSK2 are expressed specifically in meiotic and postmeiotic spermatogenic cells, respectively. TSSK2 is localized in the sperm neck, equatorial segment, and mid-piece of the sperm tail. Both TSSK1 and TSSK2 phosphorylate their common substrate TSKS (testis-specific-kinase-substrate). TSSK1/TSSK2 double knock-out mice are sterile without manifesting other defects, making these kinases viable targets for male contraception. The TSSK1/2-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271067 [Multi-domain]  Cd Length: 263  Bit Score: 85.60  E-value: 3.55e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  722 KNLVLGKTLGEGEFGKVVKATAFHLKgragyTTVAVKMLKENASPSEL--RDLLSEFNVLKQVNHPHVIKLYGAC-SQDG 798
Cdd:cd14165    1 RGYILGINLGEGSYAKVKSAYSERLK-----CNVAIKIIDKKKAPDDFveKFLPRELEILARLNHKSIIKTYEIFeTSDG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  799 PLLLIVEYAKYGSLRGFLResrkvgpgylgsggsrNSSSLDHPDERALTmgdlisfaWQISQGMQYLAEMKLVHRDLAAR 878
Cdd:cd14165   76 KVYIVMELGVQGDLLEFIK----------------LRGALPEDVARKMF--------HQLSSAIKYCHELDIVHRDLKCE 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  879 NILVAEGRKMKISDFGLSRDVyeedsyVKRSQGRIPVK--------WMAIESLFDHIYTTQ-SDVWSFGVLLWeIVTLGG 949
Cdd:cd14165  132 NLLLDKDFNIKLTDFGFSKRC------LRDENGRIVLSktfcgsaaYAAPEVLQGIPYDPRiYDIWSLGVILY-IMVCGS 204

                 ...
gi 10862703  950 NPY 952
Cdd:cd14165  205 MPY 207
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
726-1004 3.69e-18

Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK4, also called TSSK5, is expressed in testis from haploid round spermatids to mature spermatozoa. It phosphorylates Cre-Responsive Element Binding protein (CREB), facilitating the binding of CREB to the specific cis cAMP responsive element (CRE), which is important in activating genes related to germ cell differentiation. Mutations in the human TSSK4 gene is associated with infertile Chinese men with impaired spermatogenesis. The TSSK4-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271064 [Multi-domain]  Cd Length: 259  Bit Score: 85.43  E-value: 3.69e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  726 LGKTLGEGEFGKVVKATAFHLKgragyTTVAVKMLKENASPSELRD--LLSEFNVLKQVNHPHVIKLYGACSQDGPLLLI 803
Cdd:cd14162    4 VGKTLGHGSYAVVKKAYSTKHK-----CKVAIKIVSKKKAPEDYLQkfLPREIEVIKGLKHPNLICFYEAIETTSRVYII 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  804 VEYAKYGSLRGFLRESrkvgpGYLgsggsrnsssldhPDERALTmgdlisfaW--QISQGMQYLAEMKLVHRDLAARNIL 881
Cdd:cd14162   79 MELAENGDLLDYIRKN-----GAL-------------PEPQARR--------WfrQLVAGVEYCHSKGVVHRDLKCENLL 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  882 VAEGRKMKISDFGLSRDVYE-EDSYVKRSQ---GRipVKWMAIESLFDHIYTTQ-SDVWSFGVLLWEIVtLGGNPYPGip 956
Cdd:cd14162  133 LDKNNNLKITDFGFARGVMKtKDGKPKLSEtycGS--YAYASPEILRGIPYDPFlSDIWSMGVVLYTMV-YGRLPFDD-- 207
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 10862703  957 pERLFNLLKTGHRMER-PDN--CSEEMYRLMLQCWKQEPdKRPVFADISKD 1004
Cdd:cd14162  208 -SNLKVLLKQVQRRVVfPKNptVSEECKDLILRMLSPVK-KRITIEEIKRD 256
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
719-1004 4.18e-18

Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNKs comprise a subfamily of STKs with an unusual placement of a catalytic lysine relative to all other protein kinases. They are critical in regulating ion balance and are thus, important components in the control of blood pressure. They are also involved in cell signaling, survival, proliferation, and organ development. WNKs are activated by hyperosmotic or low-chloride hypotonic stress and they function upstream of SPAK and OSR1 kinases, which regulate the activity of cation-chloride cotransporters through direct interaction and phosphorylation. There are four vertebrate WNKs which show varying expression patterns. WNK1 and WNK2 are widely expressed while WNK3 and WNK4 show a more restricted expression pattern. Because mutations in human WNK1 and WNK4 cause PseudoHypoAldosteronism type II (PHAII), characterized by hypertension (due to increased sodium reabsorption) and hyperkalemia (due to impaired renal potassium secretion), there are more studies conducted on these two proteins, compared to WNK2 and WNK3. The WNK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270885 [Multi-domain]  Cd Length: 258  Bit Score: 85.35  E-value: 4.18e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  719 FPRKNLVLGKtlgeGEFGKVVKAtafhlkgragYTT-----VAVKMLKEN-ASPSELRDLLSEFNVLKQVNHPHVIKLYG 792
Cdd:cd13983    2 YLKFNEVLGR----GSFKTVYRA----------FDTeegieVAWNEIKLRkLPKAERQRFKQEIEILKSLKHPNIIKFYD 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  793 ACSQDGP--LLLIVEYAKYGSLRGFLREsrkvgpgylgsggsrnsssLDHPDERALTmgdliSFAWQISQGMQYL--AEM 868
Cdd:cd13983   68 SWESKSKkeVIFITELMTSGTLKQYLKR-------------------FKRLKLKVIK-----SWCRQILEGLNYLhtRDP 123
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  869 KLVHRDLAARNILV--AEGrKMKISDFGLSRdvyeedsyVKRSQGRIPV----KWMAIEsLFDHIYTTQSDVWSFGVLLW 942
Cdd:cd13983  124 PIIHRDLKCDNIFIngNTG-EVKIGDLGLAT--------LLRQSFAKSVigtpEFMAPE-MYEEHYDEKVDIYAFGMCLL 193
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 10862703  943 EIVTlGGNPY--------------PGIPPERLfnllktgHRMERPdncseEMYRLMLQCWKQePDKRPVFADISKD 1004
Cdd:cd13983  194 EMAT-GEYPYsectnaaqiykkvtSGIKPESL-------SKVKDP-----ELKDFIEKCLKP-PDERPSARELLEH 255
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
725-1004 4.43e-18

Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Chk1 is implicated in many major checkpoints of the cell cycle, providing a link between upstream sensors and the cell cycle engine. It plays an important role in DNA damage response and maintaining genomic stability. Chk1 acts as an effector of the sensor kinase, ATR (ATM and Rad3-related), a member of the PI3K family, which is activated upon DNA replication stress. Chk1 delays mitotic entry in response to replication blocks by inhibiting cyclin dependent kinase (Cdk) activity. In addition, Chk1 contributes to the function of centrosome and spindle-based checkpoints, inhibits firing of origins of DNA replication (Ori), and represses transcription of cell cycle proteins including cyclin B and Cdk1. The Chk1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270971 [Multi-domain]  Cd Length: 261  Bit Score: 85.46  E-value: 4.43e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  725 VLGKTLGEGEFGKVvkataFHLKGRAGYTTVAVKML-KENASPSELRDLLSEFNVLKQVNHPHVIKLYGaCSQDGPLL-L 802
Cdd:cd14069    4 DLVQTLGEGAFGEV-----FLAVNRNTEEAVAVKFVdMKRAPGDCPENIKKEVCIQKMLSHKNVVRFYG-HRREGEFQyL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  803 IVEYAKYGSLrgFLRESRKVGpgylgsggsrnsssLDHPDERaltmgdliSFAWQISQGMQYLAEMKLVHRDLAARNILV 882
Cdd:cd14069   78 FLEYASGGEL--FDKIEPDVG--------------MPEDVAQ--------FYFQQLMAGLKYLHSCGITHRDIKPENLLL 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  883 AEGRKMKISDFGL-SRDVYEEDSYVKRSQ-GRIPvkWMAIESLFDHIYTTQ-SDVWSFGVLLweIVTLGGNPYPGIPPER 959
Cdd:cd14069  134 DENDNLKISDFGLaTVFRYKGKERLLNKMcGTLP--YVAPELLAKKKYRAEpVDVWSCGIVL--FAMLAGELPWDQPSDS 209
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 10862703  960 --LFNLLKTGHrmeRPDNC-----SEEMYRLMLQCWKQEPDKRPVFADISKD 1004
Cdd:cd14069  210 cqEYSDWKENK---KTYLTpwkkiDTAALSLLRKILTENPNKRITIEDIKKH 258
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
730-1012 7.28e-18

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK phosphorylates myosin regulatory light chain and controls the contraction of all muscle types. In vertebrates, different MLCKs function in smooth (MLCK1), skeletal (MLCK2), and cardiac (MLCK3) muscles. A fourth protein, MLCK4, has also been identified through comprehensive genome analysis although it has not been biochemically characterized. The MLCK1 gene expresses three transcripts in a cell-specific manner: a short MLCK1 which contains three immunoglobulin (Ig)-like and one fibronectin type III (FN3) domains, PEVK and actin-binding regions, and a kinase domain near the C-terminus; a long MLCK1 containing six additional Ig-like domains at the N-terminus compared to the short MLCK1; and the C-terminal Ig module. MLCK2, MLCK3, and MLCK4 share a simpler domain architecture of a single kinase domain near the C-terminus and the absence of Ig-like or FN3 domains. The MLCK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271005 [Multi-domain]  Cd Length: 250  Bit Score: 84.58  E-value: 7.28e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  730 LGEGEFGKVVKATAfhlkgRAGYTTVAVKMLKENaSPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVEYAKY 809
Cdd:cd14103    1 LGRGKFGTVYRCVE-----KATGKELAAKFIKCR-KAKDREDVRNEIEIMNQLRHPRLLQLYDAFETPREMVLVMEYVAG 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  810 GSLrgFLResrkvgpgylgsggsrnssSLDhpDERALTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNILVA--EGRK 887
Cdd:cd14103   75 GEL--FER-------------------VVD--DDFELTERDCILFMRQICEGVQYMHKQGILHLDLKPENILCVsrTGNQ 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  888 MKISDFGLSRDvYEEDSYVKRSQGrIPvKWMAIESL-FDHIyTTQSDVWSFGVLLWeiVTLGG-NPYPGipperlfnllk 965
Cdd:cd14103  132 IKIIDFGLARK-YDPDKKLKVLFG-TP-EFVAPEVVnYEPI-SYATDMWSVGVICY--VLLSGlSPFMG----------- 194
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 10862703  966 tghrmerpDNCSEEMYRLMLQCWKQEPDkrpVFADISKD----LEKMMVKR 1012
Cdd:cd14103  195 --------DNDAETLANVTRAKWDFDDE---AFDDISDEakdfISKLLVKD 234
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
730-951 7.85e-18

Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SBK1, also called BSK146, is predominantly expressed in the brain. Its expression is increased in the developing brain during the late embryonic stage, coinciding with dramatic neuronal proliferation, migration, and maturation. SBK1 may play an important role in regulating brain development. The SBK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270889 [Multi-domain]  Cd Length: 259  Bit Score: 84.68  E-value: 7.85e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  730 LGEGEFGKVVKATafHlKGRAgyTTVAVKMLKENASpsELRDLLSEFNV-LKQVNHPHVIKLYG-ACSQDGPLLLIVEYA 807
Cdd:cd13987    1 LGEGTYGKVLLAV--H-KGSG--TKMALKFVPKPST--KLKDFLREYNIsLELSVHPHIIKTYDvAFETEDYYVFAQEYA 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  808 KYGSLRGFLresrkvgpgylgsggsrnsssldhPDERALTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNILV--AEG 885
Cdd:cd13987   74 PYGDLFSII------------------------PPQVGLPEERVKRCAAQLASALDFMHSKNLVHRDIKPENVLLfdKDC 129
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 10862703  886 RKMKISDFGLSRDVyeeDSYVKRSQGRIPvkWMAIE----SLFDHIYTTQS-DVWSFGVLLWEIVTlgGNP 951
Cdd:cd13987  130 RRVKLCDFGLTRRV---GSTVKRVSGTIP--YTAPEvceaKKNEGFVVDPSiDVWAFGVLLFCCLT--GNF 193
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
723-995 8.26e-18

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-theta is selectively expressed in T-cells and plays an important and non-redundant role in several aspects of T-cell biology. Although T-cells also express other PKC isoforms, PKC-theta is unique in that upon antigen stimulation, it is translocated to the plasma membrane at the immunological synapse, where it mediates signals essential for T-cell activation. It is essential for TCR-induced proliferation, cytokine production, T-cell survival, and the differentiation and effector function of T-helper (Th) cells, particularly Th2 and Th17. PKC-theta is being developed as a therapeutic target for Th2-mediated allergic inflammation and Th17-mediated autoimmune diseases. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270770 [Multi-domain]  Cd Length: 331  Bit Score: 86.13  E-value: 8.26e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  723 NLVLGKTLGEGEFGKVVKAtafHLKGRAGYttVAVKMLKENA--SPSELRDLLSEFNVLKQV-NHPHVIKLYGACSQDGP 799
Cdd:cd05619    6 DFVLHKMLGKGSFGKVFLA---ELKGTNQF--FAIKALKKDVvlMDDDVECTMVEKRVLSLAwEHPFLTHLFCTFQTKEN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  800 LLLIVEYAKYGSLRGFLRESRKvgpgylgsggsrnsssLDHPdeRAltmgdlISFAWQISQGMQYLAEMKLVHRDLAARN 879
Cdd:cd05619   81 LFFVMEYLNGGDLMFHIQSCHK----------------FDLP--RA------TFYAAEIICGLQFLHSKGIVYRDLKLDN 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  880 ILVAEGRKMKISDFGLSRDVYEEDSYVKRSQGrIPvKWMAIESLFDHIYTTQSDVWSFGVLLWEIVtLGGNPYPGIPPER 959
Cdd:cd05619  137 ILLDKDGHIKIADFGMCKENMLGDAKTSTFCG-TP-DYIAPEILLGQKYNTSVDWWSFGVLLYEML-IGQSPFHGQDEEE 213
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 10862703  960 LFNLLKTGHRMeRPDNCSEEMYRLMLQCWKQEPDKR 995
Cdd:cd05619  214 LFQSIRMDNPF-YPRWLEKEAKDILVKLFVREPERR 248
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
729-1001 9.27e-18

Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Rad53 and Cds1 are the checkpoint kinase 2 (Chk2) homologs found in budding and fission yeast, respectively. They play a central role in the cell's response to DNA lesions to prevent genome rearrangements and maintain genome integrity. They are phosphorylated in response to DNA damage and incomplete replication, and are essential for checkpoint control. They help promote DNA repair by stalling the cell cycle prior to mitosis in the presence of DNA damage. The Rad53/Cds1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271000 [Multi-domain]  Cd Length: 265  Bit Score: 84.45  E-value: 9.27e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  729 TLGEGEFGKVVKATAfhlkgRAGYTTVAVKML---KENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVE 805
Cdd:cd14098    7 RLGSGTFAEVKKAVE-----VETGKMRAIKQIvkrKVAGNDKNLQLFQREINILKSLEHPGIVRLIDWYEDDQHIYLVME 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  806 YAKYGSLRGFLREsrkvgpgylgsggsrnSSSLDHPDERALTMgdlisfawQISQGMQYLAEMKLVHRDLAARNILVAEG 885
Cdd:cd14098   82 YVEGGDLMDFIMA----------------WGAIPEQHARELTK--------QILEAMAYTHSMGITHRDLKPENILITQD 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  886 --RKMKISDFGLSRdVYEEDSYVKRSQGRI----PVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTlGGNPYPGIPPER 959
Cdd:cd14098  138 dpVIVKISDFGLAK-VIHTGTFLVTFCGTMaylaPEILMSKEQNLQGGYSNLVDMWSVGCLVYVMLT-GALPFDGSSQLP 215
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 10862703  960 LFNLLKTGHRMERPD---NCSEEMYRLMLQCWKQEPDKRPVFADI 1001
Cdd:cd14098  216 VEKRIRKGRYTQPPLvdfNISEEAIDFILRLLDVDPEKRMTAAQA 260
PK_GC-A_B cd14042
Pseudokinase domain of the membrane Guanylate Cyclase receptors, GC-A and GC-B; The ...
732-1009 1.36e-17

Pseudokinase domain of the membrane Guanylate Cyclase receptors, GC-A and GC-B; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. GC-A binds and is activated by the atrial and B-type natriuretic peptides, ANP and BNP, which are important in blood pressure regulation and cardiac pathophysiology. GC-B binds the C-type natriuretic peptide, CNP, which is a potent vasorelaxant and functions in vascular remodeling and bone growth regulation. Membrane (or particulate) GCs consist of an extracellular ligand-binding domain, a single transmembrane region, and an intracellular tail that contains a PK-like domain, an amphiphatic region and a catalytic GC domain that catalyzes the conversion of GTP into cGMP and pyrophosphate. Membrane GCs act as receptors that transduce an extracellular signal to the intracellular production of cGMP, which has been implicated in many processes including cell proliferation, phototransduction, and muscle contractility, through its downstream effectors such as PKG. The PK-like domain of GCs functions as a negative regulator of the catalytic GC domain and may also act as a docking site for interacting proteins such as GC-activating proteins. The GC-A/B subfamily is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270944 [Multi-domain]  Cd Length: 279  Bit Score: 84.18  E-value: 1.36e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  732 EGEFGKVVKATAFHLKGragyTTVAVKMLKENasPSEL-RDLLSEFNVLKQVNHPHVIKLYGACSqDGPLLLIV-EYAKY 809
Cdd:cd14042   14 ASFDQSQIFTKTGYYKG----NLVAIKKVNKK--RIDLtREVLKELKHMRDLQHDNLTRFIGACV-DPPNICILtEYCPK 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  810 GSLRGFLR-ESRKvgpgylgsggsrnsssLDHPdERALTMGDLIsfawqisQGMQYL--AEMKlVHRDLAARNILVaEGR 886
Cdd:cd14042   87 GSLQDILEnEDIK----------------LDWM-FRYSLIHDIV-------KGMHYLhdSEIK-SHGNLKSSNCVV-DSR 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  887 KM-KISDFGLSR----DVYEEDSYVKRSQgripVKWMAIESLFD---HIYTTQ-SDVWSFGVLLWEIVTLGGnPY----- 952
Cdd:cd14042  141 FVlKITDFGLHSfrsgQEPPDDSHAYYAK----LLWTAPELLRDpnpPPPGTQkGDVYSFGIILQEIATRQG-PFyeegp 215
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 10862703  953 ---P-GIPPERLFNLLKTGHRMERPDN-CSEEMYRLMLQCWKQEPDKRPVFADISKDLEKMM 1009
Cdd:cd14042  216 dlsPkEIIKKKVRNGEKPPFRPSLDELeCPDEVLSLMQRCWAEDPEERPDFSTLRNKLKKLN 277
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
728-1001 1.86e-17

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 8; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek8 contains an N-terminal kinase catalytic domain and a C-terminal RCC1 (regulator of chromosome condensation) domain. A double point mutation in Nek8 causes cystic kidney disease in mice that genetically resembles human autosomal recessive polycystic kidney disease (ARPKD). Nek8 is also associated with a rare form of juvenile renal cystic disease, nephronophthisis type 9. It has been suggested that a defect in the ciliary localization of Nek8 contributes to the development of cysts manifested by these diseases. Nek8 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270859 [Multi-domain]  Cd Length: 256  Bit Score: 83.24  E-value: 1.86e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  728 KTLGEGEFGKVvkatafHL-KGRAGYTTVAVKMLK-ENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVE 805
Cdd:cd08220    6 RVVGRGAYGTV------YLcRRKDDNKLVIIKQIPvEQMTKEERQAALNEVKVLSMLHHPNIIEYYESFLEDKALMIVME 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  806 YAKYGSLRGFLRESRKVgpgylgsggsrnsssldhpderALTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNILVAEG 885
Cdd:cd08220   80 YAPGGTLFEYIQQRKGS----------------------LLSEEEILHFFVQILLALHHVHSKQILHRDLKTQNILLNKK 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  886 RKM-KISDFGLSRDVyeedsyVKRSQGRIPVK---WMAIESLFDHIYTTQSDVWSFGVLLWEIVTLggnpypgippERLF 961
Cdd:cd08220  138 RTVvKIGDFGISKIL------SSKSKAYTVVGtpcYISPELCEGKPYNQKSDIWALGCVLYELASL----------KRAF 201
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 10862703  962 ---NL----LK--TGHRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADI 1001
Cdd:cd08220  202 eaaNLpalvLKimRGTFAPISDRYSEELRHLILSMLHLDPNKRPTLSEI 250
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
736-996 2.56e-17

Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LRRK1 is one of two vertebrate LRRKs which show complementary expression in the brain. It can form heterodimers with LRRK2, and may influence the age of onset of LRRK2-associated Parkinson's disease. LRRKs are also classified as ROCO proteins because they contain a ROC (Ras of complex proteins)/GTPase domain followed by a COR (C-terminal of ROC) domain of unknown function. In addition, LRRKs contain a catalytic kinase domain and protein-protein interaction motifs including a WD40 domain, LRRs and ankyrin (ANK) repeats. LRRKs possess both GTPase and kinase activities, with the ROC domain acting as a molecular switch for the kinase domain, cycling between a GTP-bound state which drives kinase activity and a GDP-bound state which decreases the activity. The LRRK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270969 [Multi-domain]  Cd Length: 276  Bit Score: 83.48  E-value: 2.56e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  736 GKVVKATAFHLKGRAGYTTVA----VKMLKENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQdgPLLLIVEYAKYGS 811
Cdd:cd14067   17 GQPVAVKRFHIKKCKKRTDGSadtmLKHLRAADAMKNFSEFRQEASMLHSLQHPCIVYLIGISIH--PLCFALELAPLGS 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  812 LRGFLREsrkvgpgylgsggsrnssslDHPDERALTMGDLISF--AWQISQGMQYLAEMKLVHRDLAARNILV-----AE 884
Cdd:cd14067   95 LNTVLEE--------------------NHKGSSFMPLGHMLTFkiAYQIAAGLAYLHKKNIIFCDLKSDNILVwsldvQE 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  885 GRKMKISDFGLSRDVYEEDSY-VKRSQGripvkWMAIESLFDHIYTTQSDVWSFGVLLWEIVTlGGNPYPGIPPERLFNL 963
Cdd:cd14067  155 HINIKLSDYGISRQSFHEGALgVEGTPG-----YQAPEIRPRIVYDEKVDMFSYGMVLYELLS-GQRPSLGHHQLQIAKK 228
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 10862703  964 LKTGHR--MERPDNCseEMYR---LMLQCWKQEPDKRP 996
Cdd:cd14067  229 LSKGIRpvLGQPEEV--QFFRlqaLMMECWDTKPEKRP 264
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
716-961 2.68e-17

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK1 is required for efficient amino acid starvation-induced autophagy and mitochondrial clearance. It associates with three autophagy-related proteins (Atg13, FIP200 amd Atg101) to form the ULK1 complex. All fours proteins are essential for autophagosome formation. ULK1 is regulated by both mammalian target-of rapamycin complex 1 (mTORC1) and AMP-activated protein kinase (AMPK). mTORC1 negatively regulates the ULK1 complex in a nutrient-dependent manner while AMPK stimulates autophagy by inhibiting mTORC1. ULK1 also plays neuron-specific roles and is involved in non-clathrin-coated endocytosis in growth cones, filopodia extension, neurite extension, and axon branching. The ULK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271104 [Multi-domain]  Cd Length: 267  Bit Score: 83.14  E-value: 2.68e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  716 KWEFPRKNLVlgktlGEGEFGKVvkatafhLKGRAGYT---TVAVKML-KENASPSELRdLLSEFNVLKQVNHPHVIKLY 791
Cdd:cd14202    1 KFEFSRKDLI-----GHGAFAVV-------FKGRHKEKhdlEVAVKCInKKNLAKSQTL-LGKEIKILKELKHENIVALY 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  792 GACSQDGPLLLIVEYAKYGSLRGFLREsrkvgpgylgsggsrnsssldhpdERALTMGDLISFAWQISQGMQYLAEMKLV 871
Cdd:cd14202   68 DFQEIANSVYLVMEYCNGGDLADYLHT------------------------MRTLSEDTIRLFLQQIAGAMKMLHSKGII 123
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  872 HRDLAARNILVA--EGRK-------MKISDFGLSRdvYEEDSYVKRSQGRIPVkWMAIESLFDHIYTTQSDVWSFGVLLW 942
Cdd:cd14202  124 HRDLKPQNILLSysGGRKsnpnnirIKIADFGFAR--YLQNNMMAATLCGSPM-YMAPEVIMSQHYDAKADLWSIGTIIY 200
                        250       260
                 ....*....|....*....|.
gi 10862703  943 EIVTlGGNPYPGIPPE--RLF 961
Cdd:cd14202  201 QCLT-GKAPFQASSPQdlRLF 220
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
730-946 2.93e-17

Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of HAL4, Saccharomyces cerevisiae Ptk2/Stk2, and similar fungal proteins. Proteins in this subfamily are involved in regulating ion transporters. In budding and fission yeast, HAL4 promotes potassium ion uptake, which increases cellular resistance to other cations such as sodium, lithium, and calcium ions. HAL4 stabilizes the major high-affinity K+ transporter Trk1 at the plasma membrane under low K+ conditions, which prevents endocytosis and vacuolar degradation. Budding yeast Ptk2 phosphorylates and regulates the plasma membrane H+ ATPase, Pma1. The HAL4-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270896 [Multi-domain]  Cd Length: 265  Bit Score: 83.13  E-value: 2.93e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  730 LGEGEFGKVVKAtafHLKGRAGYTTVAVKMLKENASPSELRD----LLSEFNVLKQVNHPHVIKLYGAC-SQDGPLLLIV 804
Cdd:cd13994    1 IGKGATSVVRIV---TKKNPRSGVLYAVKEYRRRDDESKRKDyvkrLTSEYIISSKLHHPNIVKVLDLCqDLHGKWCLVM 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  805 EYAKYGSLRGFLRESRKVGPgylgsggsrnsssldhpDERALtmgdlisFAWQISQGMQYLAEMKLVHRDLAARNILVAE 884
Cdd:cd13994   78 EYCPGGDLFTLIEKADSLSL-----------------EEKDC-------FFKQILRGVAYLHSHGIAHRDLKPENILLDE 133
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 10862703  885 GRKMKISDFGLS---RDVYEEDS-YVKRSQGRIPvkWMAIESLFDHIYT-TQSDVWSFGVLLWEIVT 946
Cdd:cd13994  134 DGVLKLTDFGTAevfGMPAEKESpMSAGLCGSEP--YMAPEVFTSGSYDgRAVDVWSCGIVLFALFT 198
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
709-1001 3.34e-17

N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Class IIIA myosin is highly expressed in retina and in inner ear hair cells. It is localized to the distal ends of actin-bundled structures. Mutations in human myosin IIIA are responsible for progressive nonsyndromic hearing loss. Human myosin IIIA possesses ATPase and kinase activities, and the ability to move actin filaments in a motility assay. It may function as a cellular transporter capable of moving along actin bundles in sensory cells. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain. Class III myosins may play an important role in maintaining the structural integrity of photoreceptor cell microvilli. In photoreceptor cells, they may also function as cargo carriers during light-dependent translocation of proteins such as transducin and arrestin. The class III myosin subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132969 [Multi-domain]  Cd Length: 286  Bit Score: 83.52  E-value: 3.34e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  709 FKILEDPK--WEfprknlvLGKTLGEGEFGKVvkataFHLKGRAGYTTVAVKMLKENASPSElrDLLSEFNVLKQV-NHP 785
Cdd:cd06638   10 FDSFPDPSdtWE-------IIETIGKGTYGKV-----FKVLNKKNGSKAAVKILDPIHDIDE--EIEAEYNILKALsDHP 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  786 HVIKLYGA-----CSQDGPLLLIVEYAKYGSL----RGFLRESRKvgpgylgsggsrnsssLDHPderaltmgdLISFAW 856
Cdd:cd06638   76 NVVKFYGMyykkdVKNGDQLWLVLELCNGGSVtdlvKGFLKRGER----------------MEEP---------IIAYIL 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  857 QIS-QGMQYLAEMKLVHRDLAARNILVAEGRKMKISDFGLSRDVyeEDSYVKRSQGRIPVKWMAIESL-----FDHIYTT 930
Cdd:cd06638  131 HEAlMGLQHLHVNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQL--TSTRLRRNTSVGTPFWMAPEVIaceqqLDSTYDA 208
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 10862703  931 QSDVWSFGVLLWEIVTlGGNPYPGIPPER-LFNLLKT-GHRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADI 1001
Cdd:cd06638  209 RCDVWSLGITAIELGD-GDPPLADLHPMRaLFKIPRNpPPTLHQPELWSNEFNDFIRKCLTKDYEKRPTVSDL 280
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
730-958 3.55e-17

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MEK1 and MEK2 are MAPK kinases (MAPKKs or MKKs), and are dual-specificity PKs that phosphorylate and activate the downstream targets, ERK1 and ERK2, on specific threonine and tyrosine residues. The ERK cascade starts with extracellular signals including growth factors, hormones, and neurotransmitters, which act through receptors and ion channels to initiate intracellular signaling that leads to the activation at the MAPKKK (Raf-1 or MOS) level, which leads to the transmission of signals to MEK1/2, and finally to ERK1/2. The ERK cascade plays an important role in cell proliferation, differentiation, oncogenic transformation, and cell cycle control, as well as in apoptosis and cell survival under certain conditions. This cascade has also been implicated in synaptic plasticity, migration, morphological determination, and stress response immunological reactions. Gain-of-function mutations in genes encoding ERK cascade proteins, including MEK1/2, cause cardiofaciocutaneous (CFC) syndrome, a condition leading to multiple congenital anomalies and mental retardation in patients. The MEK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132946 [Multi-domain]  Cd Length: 308  Bit Score: 83.64  E-value: 3.55e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  730 LGEGEFGKVVKatafhLKGRAGYTTVAVKMLKENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVEYAKY 809
Cdd:cd06615    9 LGAGNGGVVTK-----VLHRPSGLIMARKLIHLEIKPAIRNQIIRELKVLHECNSPYIVGFYGAFYSDGEISICMEHMDG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  810 GSLRGFLRESRKVGPGYLGSggsrnsssldhpderaltmgdlISFAwqISQGMQYLAE-MKLVHRDLAARNILVAEGRKM 888
Cdd:cd06615   84 GSLDQVLKKAGRIPENILGK----------------------ISIA--VLRGLTYLREkHKIMHRDVKPSNILVNSRGEI 139
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 10862703  889 KISDFGLSRDVYEE--DSYV-KRSqgripvkWMAIESLFDHIYTTQSDVWSFGVLLWEIVTlggNPYPgIPPE 958
Cdd:cd06615  140 KLCDFGVSGQLIDSmaNSFVgTRS-------YMSPERLQGTHYTVQSDIWSLGLSLVEMAI---GRYP-IPPP 201
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
729-996 4.53e-17

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase Kinase 5; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK5 (also called MEK5) is a dual-specificity PK that phosphorylates its downstream target, extracellular signal-regulated kinase 5 (ERK5), on specific threonine and tyrosine residues. MKK5 is activated by MEKK2 and MEKK3 in response to mitogenic and stress stimuli. The ERK5 cascade promotes cell proliferation, differentiation, neuronal survival, and neuroprotection. This cascade plays an essential role in heart development. Mice deficient in either ERK5 or MKK5 die around embryonic day 10 due to cardiovascular defects including underdevelopment of the myocardium. In addition, MKK5 is associated with metastasis and unfavorable prognosis in prostate cancer. The MKK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132950 [Multi-domain]  Cd Length: 279  Bit Score: 83.00  E-value: 4.53e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  729 TLGEGEFGKVVKAtaFHLKGRagyTTVAVKMLKENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVEYAK 808
Cdd:cd06619    8 ILGHGNGGTVYKA--YHLLTR---RILAVKVIPLDITVELQKQIMSELEILYKCDSPYIIGFYGAFFVENRISICTEFMD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  809 YGSLRGFLRESRKVgpgylgsggsrnsssldhpderaltmgdLISFAWQISQGMQYLAEMKLVHRDLAARNILVAEGRKM 888
Cdd:cd06619   83 GGSLDVYRKIPEHV----------------------------LGRIAVAVVKGLTYLWSLKILHRDVKPSNMLVNTRGQV 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  889 KISDFGLSRDVYEE--DSYVKRSqgripvKWMAIESLFDHIYTTQSDVWSFGVLLWEIvTLGGNPYPGIP-------PER 959
Cdd:cd06619  135 KLCDFGVSTQLVNSiaKTYVGTN------AYMAPERISGEQYGIHSDVWSLGISFMEL-ALGRFPYPQIQknqgslmPLQ 207
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 10862703  960 LFNLLKTGHRMERPDN-CSEEMYRLMLQCWKQEPDKRP 996
Cdd:cd06619  208 LLQCIVDEDPPVLPVGqFSEKFVHFITQCMRKQPKERP 245
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
720-996 4.67e-17

N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Class IIIB myosin is expressed highly in retina. It is also present in the brain and testis. The human class IIIB myosin gene maps to a region that overlaps the locus for Bardet-Biedl syndrome, which is characterized by dysmorphic extremities, retinal dystrophy, obesity, male hypogenitalism, and renal abnormalities. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain. They may play an important role in maintaining the structural integrity of photoreceptor cell microvilli. They may also function as cargo carriers during light-dependent translocation, in photoreceptor cells, of proteins such as transducin and arrestin. The class III myosin subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270808 [Multi-domain]  Cd Length: 291  Bit Score: 83.12  E-value: 4.67e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  720 PRKNLVLGKTLGEGEFGKVVKATafhlkGRAGYTTVAVKMLKENASPSElrDLLSEFNVLKQV-NHPHVIKLYGACSQD- 797
Cdd:cd06639   20 PSDTWDIIETIGKGTYGKVYKVT-----NKKDGSLAAVKILDPISDVDE--EIEAEYNILRSLpNHPNVVKFYGMFYKAd 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  798 ----GPLLLIVEYAKYGSLRGFLRESRKVGpgylgsggsrnsSSLDHPDERALTMGDLIsfawqisqGMQYLAEMKLVHR 873
Cdd:cd06639   93 qyvgGQLWLVLELCNGGSVTELVKGLLKCG------------QRLDEAMISYILYGALL--------GLQHLHNNRIIHR 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  874 DLAARNILVAEGRKMKISDFGLSRDVyeEDSYVKRSQGRIPVKWMAIESL-----FDHIYTTQSDVWSFGVLLWEIVTlg 948
Cdd:cd06639  153 DVKGNNILLTTEGGVKLVDFGVSAQL--TSARLRRNTSVGTPFWMAPEVIaceqqYDYSYDARCDVWSLGITAIELAD-- 228
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 10862703  949 gnpypGIPPERLFNLLKTGHRMER--------PDNCSEEMYRLMLQCWKQEPDKRP 996
Cdd:cd06639  229 -----GDPPLFDMHPVKALFKIPRnppptllnPEKWCRGFSHFISQCLIKDFEKRP 279
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
730-944 4.70e-17

Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK4 and CDK6 partner with D-type cyclins to regulate the early G1 phase of the cell cycle. They are the first kinases activated by mitogenic signals to release cells from the G0 arrested state. CDK4 and CDK6 are both expressed ubiquitously, associate with all three D cyclins (D1, D2 and D3), and phosphorylate the retinoblastoma (pRb) protein. They are also regulated by the INK4 family of inhibitors which associate with either the CDK alone or the CDK/cyclin complex. CDK4 and CDK6 show differences in subcellular localization, sensitivity to some inhibitors, timing in activation, tumor selectivity, and possibly substrate profiles. Although CDK4 and CDK6 seem to show some redundancy, they also have discrete, nonoverlapping functions. CDK6 plays an important role in cell differentiation. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK4/6-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270831 [Multi-domain]  Cd Length: 287  Bit Score: 83.09  E-value: 4.70e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  730 LGEGEFGKVVKATAFHlKGRagytTVAVKMLK----ENASP-SELRdllsEFNVLKQV---NHPHVIKLYGACsqDGP-- 799
Cdd:cd07838    7 IGEGAYGTVYKARDLQ-DGR----FVALKKVRvplsEEGIPlSTIR----EIALLKQLesfEHPNVVRLLDVC--HGPrt 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  800 -----LLLIVEYAKYgSLRGFLreSRKVGPGYlgsggsrnsssldhPDERALtmgDLIsfaWQISQGMQYLAEMKLVHRD 874
Cdd:cd07838   76 drelkLTLVFEHVDQ-DLATYL--DKCPKPGL--------------PPETIK---DLM---RQLLRGLDFLHSHRIVHRD 132
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 10862703  875 LAARNILVAEGRKMKISDFGLSRdVYEEDSyvkrsqGRIPVK---WM-AIESLFDHIYTTQSDVWSFGVLLWEI 944
Cdd:cd07838  133 LKPQNILVTSDGQVKLADFGLAR-IYSFEM------ALTSVVvtlWYrAPEVLLQSSYATPVDMWSVGCIFAEL 199
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
720-995 5.33e-17

Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Group II PAKs, also called non-conventional PAKs, include PAK4, PAK5, and PAK6. Group II PAKs contain PBD (p21-binding domain) and catalytic domains, but lack other motifs found in group I PAKs, such as an AID (autoinhibitory domain) and SH3 binding sites. Since group II PAKs do not contain an obvious AID, they may be regulated differently from group I PAKs. While group I PAKs interact with the SH3 containing proteins Nck, Grb2 and PIX, no such binding has been demonstrated for group II PAKs. Some known substrates of group II PAKs are also substrates of group I PAKs such as Raf, BAD, LIMK and GEFH1. Unique group II substrates include MARK/Par-1 and PDZ-RhoGEF. Group II PAKs play important roles in filopodia formation, neuron extension, cytoskeletal organization, and cell survival. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270815 [Multi-domain]  Cd Length: 261  Bit Score: 82.11  E-value: 5.33e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  720 PRKNLVLGKTLGEGEFGKVVKATAFHlKGRagytTVAVKMLkeNASPSELRDLL-SEFNVLKQVNHPHVIKLYGACSQDG 798
Cdd:cd06648    5 PRSDLDNFVKIGEGSTGIVCIATDKS-TGR----QVAVKKM--DLRKQQRRELLfNEVVIMRDYQHPNIVEMYSSYLVGD 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  799 PLLLIVEYAKYGSLRGFLRESRkvgpgylgsggsrnsssLDHPDeraltmgdLISFAWQISQGMQYLAEMKLVHRDLAAR 878
Cdd:cd06648   78 ELWVVMEFLEGGALTDIVTHTR-----------------MNEEQ--------IATVCRAVLKALSFLHSQGVIHRDIKSD 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  879 NILVAEGRKMKISDFG----LSRDVYEEDSYVKRSQgripvkWMAIESLFDHIYTTQSDVWSFGVLLWEIVTlGGNPYPG 954
Cdd:cd06648  133 SILLTSDGRVKLSDFGfcaqVSKEVPRRKSLVGTPY------WMAPEVISRLPYGTEVDIWSLGIMVIEMVD-GEPPYFN 205
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 10862703  955 IPPERLFNLLKTGH--RMERPDNCSEEMYRLMLQCWKQEPDKR 995
Cdd:cd06648  206 EPPLQAMKRIRDNEppKLKNLHKVSPRLRSFLDRMLVRDPAQR 248
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
726-1004 5.33e-17

Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NIM1 is a widely-expressed kinase belonging to the AMP-activated protein kinase (AMPK) subfamily. Although present in most tissues, NIM1 kinase activity is only observed in the brain and testis. NIM1 is capable of autophosphorylating and activating itself, but may be present in other tissues in the inactive form. The physiological function of NIM1 has yet to be elucidated. The NIM1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270977 [Multi-domain]  Cd Length: 255  Bit Score: 82.00  E-value: 5.33e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  726 LGKTLGEGEFGKVvkATAFHLKGRagyTTVAVKMLKENASPSELRDLLS-EFNVLKQVNHPHVIKLYGACSQDGPLLLIV 804
Cdd:cd14075    6 IRGELGSGNFSQV--KLGIHQLTK---EKVAIKILDKTKLDQKTQRLLSrEISSMEKLHHPNIIRLYEVVETLSKLHLVM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  805 EYAKYGSLRGFLRESRKvgpgylgsggsrnsssLDHPDERALtmgdlisFAwQISQGMQYLAEMKLVHRDLAARNILVAE 884
Cdd:cd14075   81 EYASGGELYTKISTEGK----------------LSESEAKPL-------FA-QIVSAVKHMHENNIIHRDLKAENVFYAS 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  885 GRKMKISDFGLSrdvyeedSYVKRSQ------GRIPvkwMAIESLF--DHIYTTQSDVWSFGVLLWEIVTlGGNPYPGIP 956
Cdd:cd14075  137 NNCVKVGDFGFS-------THAKRGEtlntfcGSPP---YAAPELFkdEHYIGIYVDIWALGVLLYFMVT-GVMPFRAET 205
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 10862703  957 PERLFNLLKTGHrMERPDNCSEEMYRLMLQCWKQEPDKRPVFADISKD 1004
Cdd:cd14075  206 VAKLKKCILEGT-YTIPSYVSEPCQELIRGILQPVPSDRYSIDEIKNS 252
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
730-996 6.15e-17

Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes MAP4K3, MAP4K1, MAP4K2, MAP4K5, and related proteins. Vertebrate members contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. MAP4K1, also called haematopoietic progenitor kinase 1 (HPK1), is a hematopoietic-specific STK involved in many cellular signaling cascades including MAPK, antigen receptor, apoptosis, growth factor, and cytokine signaling. It participates in the regulation of T cell receptor signaling and T cell-mediated immune responses. MAP4K2 was referred to as germinal center (GC) kinase because of its preferred location in GC B cells. MAP4K3 plays a role in the nutrient-responsive pathway of mTOR (mammalian target of rapamycin) signaling. It is required in the activation of S6 kinase by amino acids and for the phosphorylation of the mTOR-regulated inhibitor of eukaryotic initiation factor 4E. MAP4K5, also called germinal center kinase-related enzyme (GCKR), has been shown to activate the MAPK c-Jun N-terminal kinase (JNK). The MAP4K3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270788 [Multi-domain]  Cd Length: 259  Bit Score: 81.97  E-value: 6.15e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  730 LGEGEFGKVVKAtafhlKGRAGYTTVAVKMLKenASPSE-LRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVEYAK 808
Cdd:cd06613    8 IGSGTYGDVYKA-----RNIATGELAAVKVIK--LEPGDdFEIIQQEISMLKECRHPNIVAYFGSYLRRDKLWIVMEYCG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  809 YGSLRGFLRESRkvgpgylgsggsrnsssldhpderALTMgDLISF-AWQISQGMQYLAEMKLVHRDLAARNILVAEGRK 887
Cdd:cd06613   81 GGSLQDIYQVTG------------------------PLSE-LQIAYvCRETLKGLAYLHSTGKIHRDIKGANILLTEDGD 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  888 MKISDFGLSRDVYEedSYVKRSQGRIPVKWMA---IESLFDHIYTTQSDVWSFGVLLWEIVTLgGNPYPGIPPER-LFNL 963
Cdd:cd06613  136 VKLADFGVSAQLTA--TIAKRKSFIGTPYWMApevAAVERKGGYDGKCDIWALGITAIELAEL-QPPMFDLHPMRaLFLI 212
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 10862703  964 LKTGH---RMERPDNCSEEMYRLMLQCWKQEPDKRP 996
Cdd:cd06613  213 PKSNFdppKLKDKEKWSPDFHDFIKKCLTKNPKKRP 248
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
728-996 9.64e-17

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek3 is primarily localized in the cytoplasm and shows no cell cycle-dependent changes in its activity. It is present in the axons of neurons and affects morphogenesis and polarity through its regulation of microtubule acetylation. Nek3 modulates the signaling of the prolactin receptor through its activation of Vav2 and contributes to prolactin-mediated motility of breast cancer cells. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173759 [Multi-domain]  Cd Length: 255  Bit Score: 81.17  E-value: 9.64e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  728 KTLGEGEFGKVVKATafHLKGRAGYttvAVKMLKENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVEYA 807
Cdd:cd08219    6 RVVGEGSFGRALLVQ--HVNSDQKY---AMKEIRLPKSSSAVEDSRKEAVLLAKMKHPNIVAFKESFEADGHLYIVMEYC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  808 KYGSLRGFLRESRKvgpgylgsggsrnsssldhpdeRALTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNILVAEGRK 887
Cdd:cd08219   81 DGGDLMQKIKLQRG----------------------KLFPEDTILQWFVQMCLGVQHIHEKRVLHRDIKSKNIFLTQNGK 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  888 MKISDFGLSRDVYEEDSYVKRSQGripVKWMAIESLFDHI-YTTQSDVWSFGVLLWEIVTLgGNPYPGIPPERLFNLLKT 966
Cdd:cd08219  139 VKLGDFGSARLLTSPGAYACTYVG---TPYYVPPEIWENMpYNNKSDIWSLGCILYELCTL-KHPFQANSWKNLILKVCQ 214
                        250       260       270
                 ....*....|....*....|....*....|
gi 10862703  967 GHRMERPDNCSEEMYRLMLQCWKQEPDKRP 996
Cdd:cd08219  215 GSYKPLPSHYSYELRSLIKQMFKRNPRSRP 244
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
730-1000 1.09e-16

Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This family is composed of MLCKs and related MLCK-like kinase domains from giant STKs such as titin, obscurin, SPEG, Unc-89, Trio, kalirin, and Twitchin. Also included in this family are Death-Associated Protein Kinases (DAPKs) and Death-associated protein kinase-Related Apoptosis-inducing protein Kinase (DRAKs). MLCK phosphorylates myosin regulatory light chain and controls the contraction of all muscle types. Titin, obscurin, Twitchin, and SPEG are muscle proteins involved in the contractile apparatus. The giant STKs are multidomain proteins containing immunoglobulin (Ig), fibronectin type III (FN3), SH3, RhoGEF, PH and kinase domains. Titin, obscurin, Twitchin, and SPEG contain many Ig domain repeats at the N-terminus, while Trio and Kalirin contain spectrin-like repeats. The MLCK-like family is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270908 [Multi-domain]  Cd Length: 247  Bit Score: 80.77  E-value: 1.09e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  730 LGEGEFGKVVKATAfhlkgRAGYTTVAVKMLKENASPSElrDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVEYAKY 809
Cdd:cd14006    1 LGRGRFGVVKRCIE-----KATGREFAAKFIPKRDKKKE--AVLREISILNQLQHPRIIQLHEAYESPTELVLILELCSG 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  810 GSLRGFLResrkvgpgylgsggsrnsssldhpDERALTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNILVAEGRK-- 887
Cdd:cd14006   74 GELLDRLA------------------------ERGSLSEEEVRTYMRQLLEGLQYLHNHHILHLDLKPENILLADRPSpq 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  888 MKISDFGLSRDVyeEDSYVKRSQGRIPvKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTlGGNPYPG-IPPERLFNLLKT 966
Cdd:cd14006  130 IKIIDFGLARKL--NPGEELKEIFGTP-EFVAPEIVNGEPVSLATDMWSIGVLTYVLLS-GLSPFLGeDDQETLANISAC 205
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 10862703  967 GHRMERP--DNCSEEMYRLMLQCWKQEPDKRPVFAD 1000
Cdd:cd14006  206 RVDFSEEyfSSVSQEAKDFIRKLLVKEPRKRPTAQE 241
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
725-942 1.37e-16

Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Kin4 is a central component of the spindle position checkpoint (SPOC), which monitors spindle position and regulates the mitotic exit network (MEN). Kin4 associates with spindle pole bodies in mother cells to inhibit MEN signaling and delay mitosis until the anaphase nucleus is properly positioned along the mother-bud axis. Kin4 activity is regulated by both the bud neck-associated kinase Elm1 and protein phosphatase 2A. The Kin4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270978 [Multi-domain]  Cd Length: 270  Bit Score: 81.38  E-value: 1.37e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  725 VLGKTLGEGEFGKVVKATAFHLKGRAGYTTVAVKMLKEN--ASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLL 802
Cdd:cd14076    4 ILGRTLGEGEFGKVKLGWPLPKANHRSGVQVAIKLIRRDtqQENCQTSKIMREINILKGLTHPNIVRLLDVLKTKKYIGI 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  803 IVEYAKYGSLRGFLRESRKVgpgylgsggsrnsssldhPDERALTMgdlisFAWQISqGMQYLAEMKLVHRDLAARNILV 882
Cdd:cd14076   84 VLEFVSGGELFDYILARRRL------------------KDSVACRL-----FAQLIS-GVAYLHKKGVVHRDLKLENLLL 139
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 10862703  883 AEGRKMKISDFGLSRDVYEEDSYVKRSQGRIPVkWMAIE-SLFDHIYT-TQSDVWSFGVLLW 942
Cdd:cd14076  140 DKNRNLVITDFGFANTFDHFNGDLMSTSCGSPC-YAAPElVVSDSMYAgRKADIWSCGVILY 200
PK_GC_unk cd14045
Pseudokinase domain of the unknown subfamily of membrane Guanylate Cyclase receptors; The ...
742-1008 1.39e-16

Pseudokinase domain of the unknown subfamily of membrane Guanylate Cyclase receptors; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. Membrane (or particulate) GCs consist of an extracellular ligand-binding domain, a single transmembrane region, and an intracellular tail that contains a PK-like domain, an amphiphatic region and a catalytic GC domain that catalyzes the conversion of GTP into cGMP and pyrophosphate. Membrane GCs act as receptors that transduce an extracellular signal to the intracellular production of cGMP, which has been implicated in many processes including cell proliferation, phototransduction, and muscle contractility, through its downstream effectors such as PKG. The PK-like domain of GCs lack a critical aspartate involved in ATP binding and does not exhibit kinase activity. It functions as a negative regulator of the catalytic GC domain and may also act as a docking site for interacting proteins such as GC-activating proteins. The GC subfamily is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270947 [Multi-domain]  Cd Length: 269  Bit Score: 81.06  E-value: 1.39e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  742 TAFHLKGRAGYTTVAVKMLKENASpSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVEYAKYGSLRGFLREsrk 821
Cdd:cd14045   20 KPFTQTGIYDGRTVAIKKIAKKSF-TLSKRIRKEVKQVRELDHPNLCKFIGGCIEVPNVAIITEYCPKGSLNDVLLN--- 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  822 vgpgylgsggsrnsssldhpDERALTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNILVAEGRKMKISDFGLsRDVYE 901
Cdd:cd14045   96 --------------------EDIPLNWGFRFSFATDIARGMAYLHQHKIYHGRLKSSNCVIDDRWVCKIADYGL-TTYRK 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  902 EDSYVKRS--QGRIPVKWMAIE--SLFDHIYTTQSDVWSFGVLLWEIVTLgGNPYPGIPPErlfnlLKTGHRMERPD--- 974
Cdd:cd14045  155 EDGSENASgyQQRLMQVYLPPEnhSNTDTEPTQATDVYSYAIILLEIATR-NDPVPEDDYS-----LDEAWCPPLPElis 228
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 10862703  975 -------NCSEEMYRLMLQCWKQEPDKRPVFADISKDLEKM 1008
Cdd:cd14045  229 gktenscPCPADYVELIRRCRKNNPAQRPTFEQIKKTLHKI 269
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
730-954 1.51e-16

Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDK9 and CDK12 from higher eukaryotes, yeast BUR1, C-type plant CDKs (CdkC), and similar proteins. CDK9, BUR1, and CdkC are functionally equivalent. They act as a kinase for the C-terminal domain of RNA polymerase II and participate in regulating mutliple steps of gene expression including transcription elongation and RNA processing. CDK9 and CdkC associate with T-type cyclins while BUR1 associates with the cyclin BUR2. CDK12 is a unique CDK that contains an arginine/serine-rich (RS) domain, which is predominantly found in splicing factors. CDK12 interacts with cyclins L1 and L2, and participates in regulating transcription and alternative splicing. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK9-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270832 [Multi-domain]  Cd Length: 291  Bit Score: 81.46  E-value: 1.51e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  730 LGEGEFGKVVKAtafhlkgRAGYT--TVAVK-MLKENASPSELRDLLSEFNVLKQVNHPHVIKLY------GACSQDGPL 800
Cdd:cd07840    7 IGEGTYGQVYKA-------RNKKTgeLVALKkIRMENEKEGFPITAIREIKLLQKLDHPNVVRLKeivtskGSAKYKGSI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  801 LLIVEYAKYgSLRGFLresrkvgpgylgsggsrnssslDHPDERaLTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNI 880
Cdd:cd07840   80 YMVFEYMDH-DLTGLL----------------------DNPEVK-FTESQIKCYMKQLLEGLQYLHSNGILHRDIKGSNI 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  881 LVAEGRKMKISDFGLSRdvyeedSYVKRSQGR-----IPVKWMAIESLF-DHIYTTQSDVWSFGVLLWEIVTlGGNPYPG 954
Cdd:cd07840  136 LINNDGVLKLADFGLAR------PYTKENNADytnrvITLWYRPPELLLgATRYGPEVDMWSVGCILAELFT-GKPIFQG 208
PTK_Tyk2_rpt1 cd05076
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; Tyk2 is ...
777-1005 1.56e-16

Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; Tyk2 is widely expressed in many tissues. It is involved in signaling via the cytokine receptors IFN-alphabeta, IL-6, IL-10, IL-12, IL-13, and IL-23. It mediates cell surface urokinase receptor (uPAR) signaling and plays a role in modulating vascular smooth muscle cell (VSMC) functional behavior in response to injury. Tyk2 is also important in dendritic cell function and T helper (Th)1 cell differentiation. A homozygous mutation of Tyk2 was found in a patient with hyper-IgE syndrome (HIES), a primary immunodeficiency characterized by recurrent skin abscesses, pneumonia, and elevated serum IgE. This suggests that Tyk2 may play important roles in multiple cytokine signaling involved in innate and adaptive immunity. Tyk2 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase domain. The pseudokinase domain shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. It modulates the kinase activity of the C-terminal catalytic domain. The Tyk2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270661 [Multi-domain]  Cd Length: 273  Bit Score: 81.11  E-value: 1.56e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  777 NVLKQVNHPHVIKLYGACSQDGPLLLIVEYAKYGSLRGFLREsrkvgpgylgsggsrnsssldhpDERALTMGDLISFAW 856
Cdd:cd05076   67 SLMSQVSHTHLVFVHGVCVRGSENIMVEEFVEHGPLDVWLRK-----------------------EKGHVPMAWKFVVAR 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  857 QISQGMQYLAEMKLVHRDLAARNILVA-----EGRK--MKISDFGLSRDVYEEDSYVKrsqgRIPvkWMAIESLfDHI-- 927
Cdd:cd05076  124 QLASALSYLENKNLVHGNVCAKNILLArlgleEGTSpfIKLSDPGVGLGVLSREERVE----RIP--WIAPECV-PGGns 196
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 10862703  928 YTTQSDVWSFGVLLWEIVTLGGNPYPGIPPERLFNLLKTGHRMERPDncSEEMYRLMLQCWKQEPDKRPVFADISKDL 1005
Cdd:cd05076  197 LSTAADKWGFGATLLEICFNGEAPLQSRTPSEKERFYQRQHRLPEPS--CPELATLISQCLTYEPTQRPSFRTILRDL 272
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
726-995 1.74e-16

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called Doublecortin-like and CAM kinase-like); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL (or DCAMKL) proteins belong to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. In addition, DCKL proteins contain a C-terminal kinase domain with similarity to CAMKs. They are involved in the regulation of cAMP signaling. Vertebrates contain three DCKL proteins (DCKL1-3); DCKL1 and 2 also contain a serine, threonine, and proline rich domain (SP), while DCKL3 contains only a single DCX domain instead of tandem domains. The DCKL subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270997 [Multi-domain]  Cd Length: 258  Bit Score: 80.45  E-value: 1.74e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  726 LGKTLGEGEFGkVVKatafHLKGRAGYTTVAVKML-KENASPSElrDLL-SEFNVLKQVNHPHVIKLYGACSQDGPLLLI 803
Cdd:cd14095    4 IGRVIGDGNFA-VVK----ECRDKATDKEYALKIIdKAKCKGKE--HMIeNEVAILRRVKHPNIVQLIEEYDTDTELYLV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  804 VEYAKYGSLRGFLRESRKVGpgylgsggsrnsssldhpdER--ALTMGDLisfawqiSQGMQYLAEMKLVHRDLAARNIL 881
Cdd:cd14095   77 MELVKGGDLFDAITSSTKFT-------------------ERdaSRMVTDL-------AQALKYLHSLSIVHRDIKPENLL 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  882 VAE---GRK-MKISDFGLSRDVYE-------EDSYVkrsqgripvkwmAIESLFDHIYTTQSDVWSFGVLLWEIVTlggn 950
Cdd:cd14095  131 VVEhedGSKsLKLADFGLATEVKEplftvcgTPTYV------------APEILAETGYGLKVDIWAAGVITYILLC---- 194
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  951 pypGIPP--------ERLFNLLKTGHrMERP----DNCSE---EMYRLMLQCwkqEPDKR 995
Cdd:cd14095  195 ---GFPPfrspdrdqEELFDLILAGE-FEFLspywDNISDsakDLISRMLVV---DPEKR 247
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
677-996 2.20e-16

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 82.18  E-value: 2.20e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703   677 RRPAQAFPV----SYSSSGARRPSLDSMENQVSVDAFKILEdpkwefpRKNLVlgktlGEGEFGKVVKATaFHLKGRagy 752
Cdd:PLN00034   37 RDPSLAVPLplppPSSSSSSSSSSSASGSAPSAAKSLSELE-------RVNRI-----GSGAGGTVYKVI-HRPTGR--- 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703   753 tTVAVKMLKENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVEYAKYGSLRGflresRKVGpgylgsggs 832
Cdd:PLN00034  101 -LYALKVIYGNHEDTVRRQICREIEILRDVNHPNVVKCHDMFDHNGEIQVLLEFMDGGSLEG-----THIA--------- 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703   833 rnsssldhpDERALTmgDLisfAWQISQGMQYLAEMKLVHRDLAARNILVAEGRKMKISDFGLSRDVYEEDSYVKRSQGR 912
Cdd:PLN00034  166 ---------DEQFLA--DV---ARQILSGIAYLHRRHIVHRDIKPSNLLINSAKNVKIADFGVSRILAQTMDPCNSSVGT 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703   913 IpvKWMAIE----SLFDHIYTTQS-DVWSFGVLLWEIVtLGGNPYpGIPPERLFNLLKTGHRM----ERPDNCSEEMYRL 983
Cdd:PLN00034  232 I--AYMSPErintDLNHGAYDGYAgDIWSLGVSILEFY-LGRFPF-GVGRQGDWASLMCAICMsqppEAPATASREFRHF 307
                         330
                  ....*....|...
gi 10862703   984 MLQCWKQEPDKRP 996
Cdd:PLN00034  308 ISCCLQREPAKRW 320
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
728-899 2.69e-16

Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or General Control Non-derepressible-2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GCN2 (or EIF2AK4) is activated by amino acid or serum starvation and UV irradiation. It induces GCN4, a transcriptional activator of amino acid biosynthetic genes, leading to increased production of amino acids under amino acid-deficient conditions. In serum-starved cells, GCN2 activation induces translation of the stress-responsive transcription factor ATF4, while under UV stress, GCN2 triggers transcriptional rescue via NF-kB signaling. GCN2 contains an N-terminal RWD, a degenerate kinase-like (repeat 1), the catalytic kinase (repeat 2), a histidyl-tRNA synthetase (HisRS)-like, and a C-terminal ribosome-binding and dimerization (RB/DD) domains. Its kinase domain is activated via conformational changes as a result of the binding of uncharged tRNA to the HisRS-like domain. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the overall downregulation of protein synthesis. The GCN2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270948 [Multi-domain]  Cd Length: 278  Bit Score: 80.49  E-value: 2.69e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  728 KTLGEGEFGKVVKATAfHLKGRAgYttvAVKMLKENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVEYA 807
Cdd:cd14046   12 QVLGKGAFGQVVKVRN-KLDGRY-Y---AIKKIKLRSESKNNSRILREVMLLSRLNHQHVVRYYQAWIERANLYIQMEYC 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  808 KYGSLRGFLREsrkvgpgylgsggsrnssSLDHPDERaltmgdlisfAW----QISQGMQYLAEMKLVHRDLAARNILVA 883
Cdd:cd14046   87 EKSTLRDLIDS------------------GLFQDTDR----------LWrlfrQILEGLAYIHSQGIIHRDLKPVNIFLD 138
                        170
                 ....*....|....*.
gi 10862703  884 EGRKMKISDFGLSRDV 899
Cdd:cd14046  139 SNGNVKIGDFGLATSN 154
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
730-999 2.73e-16

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase 1; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MEK1 is a dual-specificity PK and a MAPK kinase (MAPKK or MKK) that phosphorylates and activates the downstream targets, ERK1 and ERK2, on specific threonine and tyrosine residues. The ERK cascade starts with extracellular signals including growth factors, hormones, and neurotransmitters, which act through receptors and ion channels to initiate intracellular signaling that leads to the activation at the MAPKKK (Raf-1 or MOS) level, which leads to the transmission of signals to MEK1, and finally to ERK1/2. The ERK cascade plays an important role in cell proliferation, differentiation, oncogenic transformation, and cell cycle control, as well as in apoptosis and cell survival under certain conditions. Gain-of-function mutations in genes encoding ERK cascade proteins, including MEK1, cause cardiofaciocutaneous (CFC) syndrome, a condition leading to multiple congenital anomalies and mental retardation in patients. MEK1 also plays a role in cell cycle control. The MEK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270816 [Multi-domain]  Cd Length: 319  Bit Score: 81.25  E-value: 2.73e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  730 LGEGEFGKVvkataFHLKGRAGYTTVAVKMLKENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVEYAKY 809
Cdd:cd06650   13 LGAGNGGVV-----FKVSHKPSGLVMARKLIHLEIKPAIRNQIIRELQVLHECNSPYIVGFYGAFYSDGEISICMEHMDG 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  810 GSLRGFLRESRKVgpgylgsggsrnsssldhPDEralTMGDlISFAwqISQGMQYLAEM-KLVHRDLAARNILVAEGRKM 888
Cdd:cd06650   88 GSLDQVLKKAGRI------------------PEQ---ILGK-VSIA--VIKGLTYLREKhKIMHRDVKPSNILVNSRGEI 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  889 KISDFGLSRDVYEE--DSYV-KRSqgripvkWMAIESLFDHIYTTQSDVWSFGVLLWEIvTLGGNPYPgiPPERLFNLLK 965
Cdd:cd06650  144 KLCDFGVSGQLIDSmaNSFVgTRS-------YMSPERLQGTHYSVQSDIWSMGLSLVEM-AVGRYPIP--PPDAKELELM 213
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 10862703  966 TGHRMERPDNCSEEMYRLMLQCWKQE-PDKRPVFA 999
Cdd:cd06650  214 FGCQVEGDAAETPPRPRTPGRPLSSYgMDSRPPMA 248
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
727-967 2.91e-16

Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK33 is highly expressed in the testis and is present in low levels in most tissues. It may be involved in spermatogenesis and organ ontogenesis. It interacts with and phosphorylates vimentin and may be involved in regulating intermediate filament cytoskeletal dynamics. Its role in promoting the cell viability of KRAS-dependent cancer cells is under debate; some studies have found STK33 to promote cancer cell viability, while other studies have found it to be non-essential. KRAS is the most commonly mutated human oncogene, thus, studies on the role of STK33 in KRAS mutant cancer cells are important. The STK33 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270999 [Multi-domain]  Cd Length: 266  Bit Score: 80.29  E-value: 2.91e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  727 GKTLGEGEFGKVVKATafHLKGRagyTTVAVKML-KENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVE 805
Cdd:cd14097    6 GRKLGQGSFGVVIEAT--HKETQ---TKWAIKKInREKAGSSAVKLLEREVDILKHVNHAHIIHLEEVFETPKRMYLVME 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  806 YAKYGSLRGFLREsrkvgpgylgsggsrnsssldhpdERALTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNILV--- 882
Cdd:cd14097   81 LCEDGELKELLLR------------------------KGFFSENETRHIIQSLASAVAYLHKNDIVHRDLKLENILVkss 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  883 ----AEGRKMKISDFGLSRDVYEEDSYVKRSQGRIPVkWMAIESLFDHIYTTQSDVWSFGVLLWeIVTLGGNPYPGIPPE 958
Cdd:cd14097  137 iidnNDKLNIKVTDFGLSVQKYGLGEDMLQETCGTPI-YMAPEVISAHGYSQQCDIWSIGVIMY-MLLCGEPPFVAKSEE 214

                 ....*....
gi 10862703  959 RLFNLLKTG 967
Cdd:cd14097  215 KLFEEIRKG 223
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
728-954 3.02e-16

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK3 (or MYLK3) phosphorylates myosin regulatory light chain 2 and controls the contraction of cardiac muscles. It is expressed specifically in both the atrium and ventricle of the heart and its expression is regulated by the cardiac protein Nkx2-5. MLCK3 plays an important role in cardiogenesis by regulating the assembly of cardiac sarcomeres, the repeating contractile unit of striated muscle. MLCK3 contains a single kinase domain near the C-terminus and a unique N-terminal half, and unlike MLCK1/2, it does not appear to be regulated by Ca2+/calmodulin. The MLCK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271094 [Multi-domain]  Cd Length: 261  Bit Score: 80.01  E-value: 3.02e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  728 KTLGEGEFGKVVKATAfhlkgRAGYTTVAVKMLKENaSPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVEYA 807
Cdd:cd14192   10 EVLGGGRFGQVHKCTE-----LSTGLTLAAKIIKVK-GAKEREEVKNEINIMNQLNHVNLIQLYDAFESKTNLTLIMEYV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  808 KYGSLrgFLRESrkvgpgylgsggsrnsssldhpDER-ALTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNILVAE-- 884
Cdd:cd14192   84 DGGEL--FDRIT----------------------DESyQLTELDAILFTRQICEGVHYLHQHYILHLDLKPENILCVNst 139
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  885 GRKMKISDFGLSRDvYEEDSYVKRSQGrIPvKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTlGGNPYPG 954
Cdd:cd14192  140 GNQIKIIDFGLARR-YKPREKLKVNFG-TP-EFLAPEVVNYDFVSFPTDMWSVGVITYMLLS-GLSPFLG 205
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
728-954 3.09e-16

Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p70S6K (or S6K) contains only one catalytic kinase domain, unlike p90 ribosomal S6 kinases (RSKs). It acts as a downstream effector of the STK mTOR (mammalian Target of Rapamycin) and plays a role in the regulation of the translation machinery during protein synthesis. p70S6K also plays a pivotal role in regulating cell size and glucose homeostasis. Its targets include S6, the translation initiation factor eIF3, and the insulin receptor substrate IRS-1, among others. Mammals contain two isoforms of p70S6K, named S6K1 and S6K2 (or S6K-beta). The p70S6K subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270736 [Multi-domain]  Cd Length: 323  Bit Score: 81.30  E-value: 3.09e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  728 KTLGEGEFGKV--VKATAFHLKGRagytTVAVKMLKENASPSELRDLL---SEFNVLKQVNHPHVIKLYGACSQDGPLLL 802
Cdd:cd05584    2 KVLGKGGYGKVfqVRKTTGSDKGK----IFAMKVLKKASIVRNQKDTAhtkAERNILEAVKHPFIVDLHYAFQTGGKLYL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  803 IVEYAKYGSLrgFLresrkvgpgylgsggsrnsssldHPDERALTMGDLISFAW-QISQGMQYLAEMKLVHRDLAARNIL 881
Cdd:cd05584   78 ILEYLSGGEL--FM-----------------------HLEREGIFMEDTACFYLaEITLALGHLHSLGIIYRDLKPENIL 132
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 10862703  882 VAEGRKMKISDFGLSRDVYEEDSYVKRSQGRIpvKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTlGGNPYPG 954
Cdd:cd05584  133 LDAQGHVKLTDFGLCKESIHDGTVTHTFCGTI--EYMAPEILTRSGHGKAVDWWSLGALMYDMLT-GAPPFTA 202
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
728-1007 3.71e-16

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek1 is associated with centrosomes throughout the cell cycle. It is involved in the formation of primary cilium and in the maintenance of centrosomes. It cycles through the nucleus and may be capable of relaying signals between the cilium and the nucleus. Nek1 is implicated in the development of polycystic kidney disease, which is characterized by benign polycystic tumors formed by abnormal overgrowth of renal epithelial cells. It appears also to be involved in DNA damage response, and may be important for both correct DNA damage checkpoint activation and DNA repair. Nek1 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270858 [Multi-domain]  Cd Length: 256  Bit Score: 79.47  E-value: 3.71e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  728 KTLGEGEFGKVVKATafHLKGRAGYTTVAVKMLKenASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVEYA 807
Cdd:cd08218    6 KKIGEGSFGKALLVK--SKEDGKQYVIKEINISK--MSPKEREESRKEVAVLSKMKHPNIVQYQESFEENGNLYIVMDYC 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  808 KYGSLRGFLRESRKVgpgylgsggsrnssslDHPDERALTmgdlisfaW--QISQGMQYLAEMKLVHRDLAARNILVAEG 885
Cdd:cd08218   82 DGGDLYKRINAQRGV----------------LFPEDQILD--------WfvQLCLALKHVHDRKILHRDIKSQNIFLTKD 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  886 RKMKISDFGLSRdVYEEDSYVKRSQGRIPVkWMAIESLFDHIYTTQSDVWSFGVLLWEIVTL-----GGN---------- 950
Cdd:cd08218  138 GIIKLGDFGIAR-VLNSTVELARTCIGTPY-YLSPEICENKPYNNKSDIWALGCVLYEMCTLkhafeAGNmknlvlkiir 215
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 10862703  951 -PYPGIPPERlfnllktghrmerpdncSEEMYRLMLQCWKQEPDKRPvfaDISKDLEK 1007
Cdd:cd08218  216 gSYPPVPSRY-----------------SYDLRSLVSQLFKRNPRDRP---SINSILEK 253
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
726-995 3.87e-16

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called Doublecortin-like and CAM kinase-like 3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL3 (or DCAMKL3) belongs to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. DCKL3 contains a single DCX domain (instead of a tandem) and a C-terminal kinase domain with similarity to CAMKs. It has been shown to interact with tubulin and JIP1/2. The DCKL3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271087 [Multi-domain]  Cd Length: 258  Bit Score: 79.61  E-value: 3.87e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  726 LGKTLGEGEFGkVVKATAfHLKGRAGYttvAVKMLKEnaspSELR---DLL-SEFNVLKQVNHPHVIKLYGACSQDGPLL 801
Cdd:cd14185    4 IGRTIGDGNFA-VVKECR-HWNENQEY---AMKIIDK----SKLKgkeDMIeSEILIIKSLSHPNIVKLFEVYETEKEIY 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  802 LIVEYAKYGSLRGFLRESRKvgpgylgsggsrnsssLDHPDErALTMGDLisfawqiSQGMQYLAEMKLVHRDLAARNIL 881
Cdd:cd14185   75 LILEYVRGGDLFDAIIESVK----------------FTEHDA-ALMIIDL-------CEALVYIHSKHIVHRDLKPENLL 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  882 V---AEGRK-MKISDFGLSRDVYEEDSYVKRSQgripvKWMAIESLFDHIYTTQSDVWSFGVLLWeiVTLGGNPyPGIPP 957
Cdd:cd14185  131 VqhnPDKSTtLKLADFGLAKYVTGPIFTVCGTP-----TYVAPEILSEKGYGLEVDMWAAGVILY--ILLCGFP-PFRSP 202
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 10862703  958 ER----LFNLLKTGHRMERP---DNCSEEMYRLMLQCWKQEPDKR 995
Cdd:cd14185  203 ERdqeeLFQIIQLGHYEFLPpywDNISEAAKDLISRLLVVDPEKR 247
Cadherin pfam00028
Cadherin domain;
172-261 4.10e-16

Cadherin domain;


Pssm-ID: 394985 [Multi-domain]  Cd Length: 92  Bit Score: 74.64  E-value: 4.10e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703    172 PSFRIRENRPPGTF-HQFRLLPVQfLCPNISVAYRLLEG-EGLPFRCAPDSLEVSTRWALDREQREKYELVAVCTVHAG- 248
Cdd:pfam00028    1 YSASVPENAPVGTEvLTVTATDPD-LGPNGRIFYSILGGgPGGNFRIDPDTGDISTTKPLDRESIGEYELTVEATDSGGp 79
                           90
                   ....*....|...
gi 10862703    249 AREEVVMVPFPVT 261
Cdd:pfam00028   80 PLSSTATVTITVL 92
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
721-951 4.71e-16

Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Checkpoint Kinase 2 (Chk2) plays an important role in cellular responses to DNA double-strand breaks and related lesions. It is phosphorylated and activated by ATM kinase, resulting in its dissociation from sites of damage to phosphorylate downstream targets such as BRCA1, p53, cell cycle transcription factor E2F1, the promyelocytic leukemia protein (PML) involved in apoptosis, and CDC25 phosphatases, among others. Mutations in Chk2 is linked to a variety of cancers including familial breast cancer, myelodysplastic syndromes, prostate cancer, lung cancer, and osteosarcomas. Chk2 contains an N-terminal SQ/TQ cluster domain (SCD), a central forkhead-associated (FHA) domain, and a C-terminal catalytic kinase domain. The Chk2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270986 [Multi-domain]  Cd Length: 275  Bit Score: 79.74  E-value: 4.71e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  721 RKNLVLGKTLGEGEFGKVvkATAFHLKGRagyTTVAVKMLKENASP-------SELRDLLSEFNVLKQVNHPHVIKLYGA 793
Cdd:cd14084    5 RKKYIMSRTLGSGACGEV--KLAYDKSTC---KKVAIKIINKRKFTigsrreiNKPRNIETEIEILKKLSHPCIIKIEDF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  794 CSQDGPLLLIVEYAKYGSLRGFLRESRKvgpgylgsggsrnsssldhpderaltMGDLIS--FAWQISQGMQYLAEMKLV 871
Cdd:cd14084   80 FDAEDDYYIVLELMEGGELFDRVVSNKR--------------------------LKEAICklYFYQMLLAVKYLHSNGII 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  872 HRDLAARNILV---AEGRKMKISDFGLSRDVyEEDSYVKRSQGriPVKWMAIESLF---DHIYTTQSDVWSFGVLLWeiV 945
Cdd:cd14084  134 HRDLKPENVLLssqEEECLIKITDFGLSKIL-GETSLMKTLCG--TPTYLAPEVLRsfgTEGYTRAVDCWSLGVILF--I 208

                 ....*.
gi 10862703  946 TLGGNP 951
Cdd:cd14084  209 CLSGYP 214
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
728-996 4.75e-16

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 9; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek9, also called Nercc1, is primarily a cytoplasmic protein but can also localize in the nucleus. It is involved in modulating chromosome alignment and splitting during mitosis. It interacts with the gamma-tubulin ring complex and the Ran GTPase, and is implicated in microtubule organization. Nek9 associates with FACT (FAcilitates Chromatin Transcription) and modulates interphase progression. It also interacts with Nek6, and Nek7, during mitosis, resulting in their activation. Nek9 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270860 [Multi-domain]  Cd Length: 256  Bit Score: 79.40  E-value: 4.75e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  728 KTLGEGEFGKVVkatafhLKGRAGYTTVAVkmLKE----NASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLI 803
Cdd:cd08221    6 RVLGRGAFGEAV------LYRKTEDNSLVV--WKEvnlsRLSEKERRDALNEIDILSLLNHDNIITYYNHFLDGESLFIE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  804 VEYAKYGSLRGFLRESRkvgpGYLGsggsrnsssldhPDEraltmgDLISFAWQISQGMQYLAEMKLVHRDLAARNILVA 883
Cdd:cd08221   78 MEYCNGGNLHDKIAQQK----NQLF------------PEE------VVLWYLYQIVSAVSHIHKAGILHRDIKTLNIFLT 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  884 EGRKMKISDFGLSRDVYEEDSYVKRSQGrIPVkWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLgGNPYPGIPPERLFNL 963
Cdd:cd08221  136 KADLVKLGDFGISKVLDSESSMAESIVG-TPY-YMSPELVQGVKYNFKSDIWAVGCVLYELLTL-KRTFDATNPLRLAVK 212
                        250       260       270
                 ....*....|....*....|....*....|...
gi 10862703  964 LKTGHRMERPDNCSEEMYRLMLQCWKQEPDKRP 996
Cdd:cd08221  213 IVQGEYEDIDEQYSEEIIQLVHDCLHQDPEDRP 245
PK_GC-C cd14044
Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-C; The pseudokinase domain ...
747-1008 8.76e-16

Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-C; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. GC-C binds and is activated by the intestinal hormones, guanylin (GN) and uroguanylin (UGN), which are secreted after salty meals to inhibit sodium absorption and induce the secretion of chloride, bicarbonate, and water. GN and UGN are also present in the kidney, where they induce increased salt and water secretion. This prevents the development of hypernatremia and hypervolemia after ingestion of high amounts of salt. Membrane (or particulate) GCs consist of an extracellular ligand-binding domain, a single transmembrane region, and an intracellular tail that contains a PK-like domain, an amphiphatic region and a catalytic GC domain that catalyzes the conversion of GTP into cGMP and pyrophosphate. Membrane GCs act as receptors that transduce an extracellular signal to the intracellular production of cGMP, which has been implicated in many processes including cell proliferation, phototransduction, and muscle contractility, through its downstream effectors such as PKG. The PK-like domain of GCs functions as a negative regulator of the catalytic GC domain and may also act as a docking site for interacting proteins such as GC-activating proteins. The GC-C subfamily is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270946 [Multi-domain]  Cd Length: 271  Bit Score: 78.77  E-value: 8.76e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  747 KGRAGYTTVAVKMLKENASPSELRDLLsEFNVLKQVNHPHVIKLYGACSQDGPLLLIVEYAKYGSLRGFLRESrkvgpgy 826
Cdd:cd14044   26 QGKYDKKVVILKDLKNNEGNFTEKQKI-ELNKLLQIDYYNLTKFYGTVKLDTMIFGVIEYCERGSLRDVLNDK------- 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  827 lgsggsrnsssLDHPDERALTMGDLISFAWQISQGMQYLAEMKL-VHRDLAARNILVAEGRKMKISDFGLSRDVYEEDSY 905
Cdd:cd14044   98 -----------ISYPDGTFMDWEFKISVMYDIAKGMSYLHSSKTeVHGRLKSTNCVVDSRMVVKITDFGCNSILPPSKDL 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  906 vkrsqgripvkWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLGGNPYPGIPPERLFNLlktgHRMERPDNCSE------- 978
Cdd:cd14044  167 -----------WTAPEHLRQAGTSQKGDVYSYGIIAQEIILRKETFYTAACSDRKEKI----YRVQNPKGMKPfrpdlnl 231
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 10862703  979 --------EMYRLMLQCWKQEPDKRPVFADISKDLEKM 1008
Cdd:cd14044  232 esagererEVYGLVKNCWEEDPEKRPDFKKIENTLAKI 269
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
722-1001 8.80e-16

Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Aurora kinases are key regulators of mitosis and are essential for the accurate and equal division of genomic material from parent to daughter cells. Vertebrates contain at least 2 Aurora kinases (A and B); mammals contains a third Aurora kinase gene (C). Aurora-A regulates cell cycle events from the late S-phase through the M-phase including centrosome maturation, mitotic entry, centrosome separation, spindle assembly, chromosome alignment, cytokinesis, and mitotic exit. Aurora-A activation depends on its autophosphorylation and binding to the microtubule-associated protein TPX2, which also localizes the kinase to spindle microtubules. Aurora-A is overexpressed in many cancer types such as prostate, ovarian, breast, bladder, gastric, and pancreatic. The Aurora subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271018 [Multi-domain]  Cd Length: 258  Bit Score: 78.46  E-value: 8.80e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  722 KNLVLGKTLGEGEFGKVVKATAFHLKGRAGYTTVAVKMLKENASPSELRdllSEFNVLKQVNHPHVIKLYGACSQDGPLL 801
Cdd:cd14116    5 EDFEIGRPLGKGKFGNVYLAREKQSKFILALKVLFKAQLEKAGVEHQLR---REVEIQSHLRHPNILRLYGYFHDATRVY 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  802 LIVEYAKYGSLrgfLRESRKVGpgylgsggsrnssSLDhpDERALTmgdlisFAWQISQGMQYLAEMKLVHRDLAARNIL 881
Cdd:cd14116   82 LILEYAPLGTV---YRELQKLS-------------KFD--EQRTAT------YITELANALSYCHSKRVIHRDIKPENLL 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  882 VAEGRKMKISDFGLSrdVYEEDSyvKRSQGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTlggnpypGIPPERLF 961
Cdd:cd14116  138 LGSAGELKIADFGWS--VHAPSS--RRTTLCGTLDYLPPEMIEGRMHDEKVDLWSLGVLCYEFLV-------GKPPFEAN 206
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 10862703  962 NLLKTGHRMER-----PDNCSEEMYRLMLQCWKQEPDKRPVFADI 1001
Cdd:cd14116  207 TYQETYKRISRveftfPDFVTEGARDLISRLLKHNPSQRPMLREV 251
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
728-995 9.52e-16

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKB-gamma is predominantly expressed in neuronal tissues. Mice deficient in PKB-gamma show a reduction in brain weight due to the decreases in cell size and cell number. PKB-gamma has also been shown to be upregulated in estrogen-deficient breast cancer cells, androgen-independent prostate cancer cells, and primary ovarian tumors. It acts as a key mediator in the genesis of ovarian cancer. PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. The PKB-gamma subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270745 [Multi-domain]  Cd Length: 348  Bit Score: 80.13  E-value: 9.52e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  728 KTLGEGEFGKVVKatafhLKGRAGYTTVAVKMLKENA--SPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVE 805
Cdd:cd05593   21 KLLGKGTFGKVIL-----VREKASGKYYAMKILKKEViiAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVME 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  806 YAKYGSLrgFLRESRkvgpgylgsggsrnsssldhpdERALTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNILVAEG 885
Cdd:cd05593   96 YVNGGEL--FFHLSR----------------------ERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKD 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  886 RKMKISDFGLSRDVYEEDSYVKRSQGrIPvKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTlGGNPYPGIPPERLFNLLK 965
Cdd:cd05593  152 GHIKITDFGLCKEGITDAATMKTFCG-TP-EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPFYNQDHEKLFELIL 228
                        250       260       270
                 ....*....|....*....|....*....|
gi 10862703  966 TgHRMERPDNCSEEMYRLMLQCWKQEPDKR 995
Cdd:cd05593  229 M-EDIKFPRTLSADAKSLLSGLLIKDPNKR 257
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
721-995 1.16e-15

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271069 [Multi-domain]  Cd Length: 263  Bit Score: 78.15  E-value: 1.16e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  721 RKNLVLGKTLGEGEFGKVVKAtafhlKGRAGYTTVAVKMLKENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPL 800
Cdd:cd14167    2 RDIYDFREVLGTGAFSEVVLA-----EEKRTQKLVAIKCIAKKALEGKETSIENEIAVLHKIKHPNIVALDDIYESGGHL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  801 LLIVEYAKYGSLRgflreSRKVGPGYLgsggsrnsssldhpderalTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNI 880
Cdd:cd14167   77 YLIMQLVSGGELF-----DRIVEKGFY-------------------TERDASKLIFQILDAVKYLHDMGIVHRDLKPENL 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  881 L---VAEGRKMKISDFGLSRdvYEEDSYVKRSQGRIPvKWMAIESLFDHIYTTQSDVWSFGVLLWeIVTLGGNPYPGIPP 957
Cdd:cd14167  133 LyysLDEDSKIMISDFGLSK--IEGSGSVMSTACGTP-GYVAPEVLAQKPYSKAVDCWSIGVIAY-ILLCGYPPFYDEND 208
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 10862703  958 ERLF-NLLKTGHRMERP--DNCSEEMYRLMLQCWKQEPDKR 995
Cdd:cd14167  209 AKLFeQILKAEYEFDSPywDDISDSAKDFIQHLMEKDPEKR 249
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
723-945 1.36e-15

Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of yeast Kin1, Kin2, and similar proteins. Fission yeast Kin1 is a membrane-associated kinase that is involved in regulating cell surface cohesiveness during interphase. It also plays a role during mitosis, linking actomyosin ring assembly with septum synthesis and membrane closure to ensure separation of daughter cells. Budding yeast Kin1 and Kin2 act downstream of the Rab-GTPase Sec4 and are associated with the exocytic apparatus; they play roles in the secretory pathway. The Kin1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270979 [Multi-domain]  Cd Length: 267  Bit Score: 78.26  E-value: 1.36e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  723 NLVLGKTLGEGEFGKVVKAtafhlKGRAGYTTVAVKM--------LKENASPSELRDLLSEFNVLKQV------NHPHVI 788
Cdd:cd14077    2 NWEFVKTIGAGSMGKVKLA-----KHIRTGEKCAIKIiprasnagLKKEREKRLEKEISRDIRTIREAalssllNHPHIC 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  789 KLYGACSQDGPLLLIVEYAKYGSL------RGFLRE--SRKvgpgylgsggsrnsssldhpderaltmgdlisFAWQISQ 860
Cdd:cd14077   77 RLRDFLRTPNHYYMLFEYVDGGQLldyiisHGKLKEkqARK--------------------------------FARQIAS 124
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  861 GMQYLAEMKLVHRDLAARNILVAEGRKMKISDFGLSrDVYEEDSYVKRSQGRIpvKWMAIESLFDHIYT-TQSDVWSFGV 939
Cdd:cd14077  125 ALDYLHRNSIVHRDLKIENILISKSGNIKIIDFGLS-NLYDPRRLLRTFCGSL--YFAAPELLQAQPYTgPEVDVWSFGV 201

                 ....*.
gi 10862703  940 LLWEIV 945
Cdd:cd14077  202 VLYVLV 207
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
730-958 1.51e-15

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase 2; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MEK2 is a dual-specificity PK and a MAPK kinase (MAPKK or MKK) that phosphorylates and activates the downstream targets, ERK1 and ERK2, on specific threonine and tyrosine residues. The ERK cascade starts with extracellular signals including growth factors, hormones, and neurotransmitters, which act through receptors and ion channels to initiate intracellular signaling that leads to the activation at the MAPKKK (Raf-1 or MOS) level, which leads to the transmission of signals to MEK2, and finally to ERK1/2. The ERK cascade plays an important role in cell proliferation, differentiation, oncogenic transformation, and cell cycle control, as well as in apoptosis and cell survival under certain conditions. Gain-of-function mutations in genes encoding ERK cascade proteins, including MEK2, cause cardiofaciocutaneous (CFC) syndrome, a condition leading to multiple congenital anomalies and mental retardation in patients. The MEK subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132980 [Multi-domain]  Cd Length: 331  Bit Score: 79.32  E-value: 1.51e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  730 LGEGEFGKVVKatafhLKGRAGYTTVAVKMLKENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVEYAKY 809
Cdd:cd06649   13 LGAGNGGVVTK-----VQHKPSGLIMARKLIHLEIKPAIRNQIIRELQVLHECNSPYIVGFYGAFYSDGEISICMEHMDG 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  810 GSLRGFLRESRKVgpgylgsggsrnsssldhPDEralTMGDlISFAwqISQGMQYLAEM-KLVHRDLAARNILVAEGRKM 888
Cdd:cd06649   88 GSLDQVLKEAKRI------------------PEE---ILGK-VSIA--VLRGLAYLREKhQIMHRDVKPSNILVNSRGEI 143
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 10862703  889 KISDFGLSRDVYEE--DSYV-KRSqgripvkWMAIESLFDHIYTTQSDVWSFGVLLWEIvTLGGNPYPgiPPE 958
Cdd:cd06649  144 KLCDFGVSGQLIDSmaNSFVgTRS-------YMSPERLQGTHYSVQSDIWSMGLSLVEL-AIGRYPIP--PPD 206
PK_KSR2 cd14153
Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to ...
724-1008 1.74e-15

Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. KSR2 interacts with the protein phosphatase calcineurin and functions in calcium-mediated ERK signaling. It also functions in energy metabolism by regulating AMP kinase and AMPK-dependent processes such as glucose uptake and fatty acid oxidation. KSR proteins act as scaffold proteins that function downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. KSR proteins regulate the assembly and activation of the Raf/MEK/ERK module upon Ras activation at the membrane by direct association of its components. They are widely regarded as pseudokinases. The KSR2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271055 [Multi-domain]  Cd Length: 270  Bit Score: 78.13  E-value: 1.74e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  724 LVLGKTLGEGEFGKVvkataFHlkGRaGYTTVAVKMLK-ENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLL 802
Cdd:cd14153    2 LEIGELIGKGRFGQV-----YH--GR-WHGEVAIRLIDiERDNEEQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAI 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  803 IVEYAKYGSLRGFLRESRKVgpgylgsggsrnsssLDHPDERALtmgdlisfAWQISQGMQYLAEMKLVHRDLAARNILV 882
Cdd:cd14153   74 ITSLCKGRTLYSVVRDAKVV---------------LDVNKTRQI--------AQEIVKGMGYLHAKGILHKDLKSKNVFY 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  883 AEGrKMKISDFGLSRDVYEEDSYVKRSQGRIPVKWM-----------AIESLFDHI-YTTQSDVWSFGVLLWEIVTLGGn 950
Cdd:cd14153  131 DNG-KVVITDFGLFTISGVLQAGRREDKLRIQSGWLchlapeiirqlSPETEEDKLpFSKHSDVFAFGTIWYELHAREW- 208
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 10862703  951 PYPGIPPERLFNLLKTGHRMERPD-NCSEEMYRLMLQCWKQEPDKRPVFADISKDLEKM 1008
Cdd:cd14153  209 PFKTQPAEAIIWQVGSGMKPNLSQiGMGKEISDILLFCWAYEQEERPTFSKLMEMLEKL 267
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
730-1001 2.09e-15

Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAO3 is also known as JIK (c-Jun N-terminal kinase inhibitory kinase) or KFC (kinase from chicken). It specifically activates JNK, presumably by phosphorylating and activating MKK4/MKK7. In Saccharomyces cerevisiae, TAO3 is a component of the RAM (regulation of Ace2p activity and cellular morphogenesis) signaling pathway. TAO3 is upregulated in retinal ganglion cells after axotomy, and may play a role in apoptosis. TAO proteins possess mitogen-activated protein kinase (MAPK) kinase kinase activity. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. The TAO3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270803 [Multi-domain]  Cd Length: 313  Bit Score: 78.54  E-value: 2.09e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  730 LGEGEFGKVVKATAFHLKgragyTTVAVKMLKENASPS--ELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVEYA 807
Cdd:cd06633   29 IGHGSFGAVYFATNSHTN-----EVVAIKKMSYSGKQTneKWQDIIKEVKFLQQLKHPNTIEYKGCYLKDHTAWLVMEYC 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  808 kYGSLRGFLRESRKvgpgylgsggsrnssSLDHPDERALTMGDLisfawqisQGMQYLAEMKLVHRDLAARNILVAEGRK 887
Cdd:cd06633  104 -LGSASDLLEVHKK---------------PLQEVEIAAITHGAL--------QGLAYLHSHNMIHRDIKAGNILLTEPGQ 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  888 MKISDFGLSRDVYEEDSYVKRSQgripvkWMAIESLF---DHIYTTQSDVWSFGVLLWEIVTLGGNPYPGIPPERLFNLL 964
Cdd:cd06633  160 VKLADFGSASIASPANSFVGTPY------WMAPEVILamdEGQYDGKVDIWSLGITCIELAERKPPLFNMNAMSALYHIA 233
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 10862703  965 KTGHRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADI 1001
Cdd:cd06633  234 QNDSPTLQSNEWTDSFRGFVDYCLQKIPQERPSSAEL 270
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
714-1004 2.15e-15

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK1 functions as a positive regulator of mitosis, meiosis, and cytokinesis. Its localization changes during mitotic progression; associating first with centrosomes in prophase, with kinetochores in prometaphase and metaphase, at the central spindle in anaphase, and in the midbody during telophase. It carries multiple functions throughout the cell cycle through interactions with differrent substrates at these specific subcellular locations. PLK1 is overexpressed in many human cancers and is associated with poor prognosis. The PLK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271089 [Multi-domain]  Cd Length: 265  Bit Score: 77.67  E-value: 2.15e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  714 DPKwefPRKNLVLGKTLGEGEFGKVVKATAFHLKGRAGYTTVAVKMLkenASPSELRDLLSEFNVLKQVNHPHVIKLYGA 793
Cdd:cd14187    2 DPR---TRRRYVRGRFLGKGGFAKCYEITDADTKEVFAGKIVPKSLL---LKPHQKEKMSMEIAIHRSLAHQHVVGFHGF 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  794 CSQDGPLLLIVEYAKYGSLRGFlresrkvgpgylgsggsrnsssldHPDERALTMGDLISFAWQISQGMQYLAEMKLVHR 873
Cdd:cd14187   76 FEDNDFVYVVLELCRRRSLLEL------------------------HKRRKALTEPEARYYLRQIILGCQYLHRNRVIHR 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  874 DLAARNILVAEGRKMKISDFGLSRDVyEEDSYVKRSQGRIPvKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTlggnpyp 953
Cdd:cd14187  132 DLKLGNLFLNDDMEVKIGDFGLATKV-EYDGERKKTLCGTP-NYIAPEVLSKKGHSFEVDIWSIGCIMYTLLV------- 202
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 10862703  954 GIPPERLFNLLKTGHRMER-----PDNCSEEMYRLMLQCWKQEPDKRPVFADISKD 1004
Cdd:cd14187  203 GKPPFETSCLKETYLRIKKneysiPKHINPVAASLIQKMLQTDPTARPTINELLND 258
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
726-995 2.29e-15

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-beta subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271071 [Multi-domain]  Cd Length: 277  Bit Score: 77.62  E-value: 2.29e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  726 LGKTLGEGEFGKVVKAtafhlKGRAGYTTVAVKMLKENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVE 805
Cdd:cd14169    7 LKEKLGEGAFSEVVLA-----QERGSQRLVALKCIPKKALRGKEAMVENEIAVLRRINHENIVSLEDIYESPTHLYLAME 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  806 YAKYGSLrgflresrkvgpgylgsggsrnsssLDHPDERA-LTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNILVA- 883
Cdd:cd14169   82 LVTGGEL-------------------------FDRIIERGsYTEKDASQLIGQVLQAVKYLHQLGIVHRDLKPENLLYAt 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  884 --EGRKMKISDFGLSRdvYEEDSYVKRSQGrIPvKWMAIESLFDHIYTTQSDVWSFGVLLWeIVTLGGNPYPGIPPERLF 961
Cdd:cd14169  137 pfEDSKIMISDFGLSK--IEAQGMLSTACG-TP-GYVAPELLEQKPYGKAVDVWAIGVISY-ILLCGYPPFYDENDSELF 211
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 10862703  962 NL-LKTGHRMERP--DNCSEEMYRLMLQCWKQEPDKR 995
Cdd:cd14169  212 NQiLKAEYEFDSPywDDISESAKDFIRHLLERDPEKR 248
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
730-1000 2.30e-15

Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK1 is required for efficient amino acid starvation-induced autophagy and mitochondrial clearance. ULK2 is ubiquitously expressed and is essential in autophagy induction. ULK1 and ULK2 have unique and cell-type specific roles, but also display partially redundant roles in starvation-induced autophagy. They both display neuron-specific functions: ULK1 is involved in non-clathrin-coated endocytosis in growth cones, filopodia extension, and axon branching; ULK2 plays a role in axon development. The ULK1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271022 [Multi-domain]  Cd Length: 256  Bit Score: 77.41  E-value: 2.30e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  730 LGEGEFGKVVKATafHLKGRAgyTTVAVK-MLKENASPSElrDLLS-EFNVLKQVNHPHVIKLYGACSQDGPLLLIVEYA 807
Cdd:cd14120    1 IGHGAFAVVFKGR--HRKKPD--LPVAIKcITKKNLSKSQ--NLLGkEIKILKELSHENVVALLDCQETSSSVYLVMEYC 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  808 KYGSLRGFLREsrkvgpgylgsggsrnsssldhpdERALTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNILVAEGRK 887
Cdd:cd14120   75 NGGDLADYLQA------------------------KGTLSEDTIRVFLQQIAAAMKALHSKGIVHRDLKPQNILLSHNSG 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  888 ---------MKISDFGLSRdvYEEDSYVKRSQGRIPVkWMAIESLFDHIYTTQSDVWSFGVLLWEIVTlGGNPYPGIPPE 958
Cdd:cd14120  131 rkpspndirLKIADFGFAR--FLQDGMMAATLCGSPM-YMAPEVIMSLQYDAKADLWSIGTIVYQCLT-GKAPFQAQTPQ 206
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 10862703  959 RLFNLLKTGHRMER--PDNCSEEMYRLMLQCWKQEPDKRPVFAD 1000
Cdd:cd14120  207 ELKAFYEKNANLRPniPSGTSPALKDLLLGLLKRNPKDRIDFED 250
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
727-996 2.43e-15

Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. YSK4 is a putative MAPKKK, whose mammalian gene has been isolated. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The YSK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270801 [Multi-domain]  Cd Length: 266  Bit Score: 77.48  E-value: 2.43e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  727 GKTLGEGEFGKVVkatafhlkgrAGYTT----VAVKMLKENASPS-----ELRDLLSEFNVLKQVNHPHVIKLYGACSQD 797
Cdd:cd06631    6 GNVLGKGAYGTVY----------CGLTStgqlIAVKQVELDTSDKekaekEYEKLQEEVDLLKTLKHVNIVGYLGTCLED 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  798 GPLLLIVEYAKYGSLRGFLResrKVGPgylgsggsrnsssldhpderaLTMGDLISFAWQISQGMQYLAEMKLVHRDLAA 877
Cdd:cd06631   76 NVVSIFMEFVPGGSIASILA---RFGA---------------------LEEPVFCRYTKQILEGVAYLHNNNVIHRDIKG 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  878 RNILVAEGRKMKISDFGLSRDVYEEDSYVKRSQGRIPVK----WMAIESLFDHIYTTQSDVWSFGVLLWEIVTlGGNPYP 953
Cdd:cd06631  132 NNIMLMPNGVIKLIDFGCAKRLCINLSSGSQSQLLKSMRgtpyWMAPEVINETGHGRKSDIWSIGCTVFEMAT-GKPPWA 210
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 10862703  954 GIPP-ERLFNLLKTGHRMER-PDNCSEEMYRLMLQCWKQEPDKRP 996
Cdd:cd06631  211 DMNPmAAIFAIGSGRKPVPRlPDKFSPEARDFVHACLTRDQDERP 255
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
720-995 2.61e-15

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK2 plays a role in pro-apoptotic signaling. It is cleaved and activated by caspases leading to morphological changes during apoptosis. PAK2 is also activated in response to a variety of stresses including DNA damage, hyperosmolarity, serum starvation, and contact inhibition, and may play a role in coordinating the stress response. PAK2 also contributes to cancer cell invasion through a mechanism distinct from that of PAK1. It belongs to the group I PAKs, which contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132986 [Multi-domain]  Cd Length: 296  Bit Score: 77.84  E-value: 2.61e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  720 PRKNLVLGKTLGEGEFGKVVKATAFHLKgragyTTVAVKMLKENASPSElRDLLSEFNVLKQVNHPHVIKLYGACSQDGP 799
Cdd:cd06655   17 PKKKYTRYEKIGQGASGTVFTAIDVATG-----QEVAIKQINLQKQPKK-ELIINEILVMKELKNPNIVNFLDSFLVGDE 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  800 LLLIVEYAKYGSLRGFLRESrkvgpgylgsggsrnsssldhpderALTMGDLISFAWQISQGMQYLAEMKLVHRDLAARN 879
Cdd:cd06655   91 LFVVMEYLAGGSLTDVVTET-------------------------CMDEAQIAAVCRECLQALEFLHANQVIHRDIKSDN 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  880 ILVAEGRKMKISDFGLSRDVYEEDSyvKRSQGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTlGGNPYPGIPPER 959
Cdd:cd06655  146 VLLGMDGSVKLTDFGFCAQITPEQS--KRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVE-GEPPYLNENPLR 222
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 10862703  960 LFNLLKTGH--RMERPDNCSEEMYRLMLQCWKQEPDKR 995
Cdd:cd06655  223 ALYLIATNGtpELQNPEKLSPIFRDFLNRCLEMDVEKR 260
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
722-957 3.06e-15

Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the cAMP-dependent protein kinases, PKA and PRKX, and similar proteins. The inactive PKA holoenzyme is a heterotetramer composed of two phosphorylated and active catalytic subunits with a dimer of regulatory (R) subunits. Activation is achieved through the binding of the important second messenger cAMP to the R subunits, which leads to the dissociation of PKA into the R dimer and two active subunits. PKA is present ubiquitously in cells and interacts with many different downstream targets. It plays a role in the regulation of diverse processes such as growth, development, memory, metabolism, gene expression, immunity, and lipolysis. PRKX is also reulated by the R subunit and is is present in many tissues including fetal and adult brain, kidney, and lung. It is implicated in granulocyte/macrophage lineage differentiation, renal cell epithelial migration, and tubular morphogenesis in the developing kidney. The PKA-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270732 [Multi-domain]  Cd Length: 290  Bit Score: 77.62  E-value: 3.06e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  722 KNLVLGKTLGEGEFGKVVKAtafhlKGRAGYTTVAVKMLKEnASPSELRDL---LSEFNVLKQVNHPHVIKLYGACSQDG 798
Cdd:cd05580    1 DDFEFLKTLGTGSFGRVRLV-----KHKDSGKYYALKILKK-AKIIKLKQVehvLNEKRILSEVRHPFIVNLLGSFQDDR 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  799 PLLLIVEYAKYGSLRGFLRESRKVgpgylgsggsrnsssldhPDERALTmgdlisFAWQISQGMQYLAEMKLVHRDLAAR 878
Cdd:cd05580   75 NLYMVMEYVPGGELFSLLRRSGRF------------------PNDVAKF------YAAEVVLALEYLHSLDIVYRDLKPE 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  879 NILVAEGRKMKISDFGlsrdvyeedsYVKRSQGR------IPvKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTlggnpy 952
Cdd:cd05580  131 NLLLDSDGHIKITDFG----------FAKRVKDRtytlcgTP-EYLAPEIILSKGHGKAVDWWALGILIYEMLA------ 193

                 ....*
gi 10862703  953 pGIPP 957
Cdd:cd05580  194 -GYPP 197
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
726-1004 3.11e-15

Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SNRK is a kinase highly expressed in testis and brain that is found inactive in cells that lack the LKB1 tumour suppressor protein kinase. The regulatory subunits STRAD and MO25 are required for LKB1 to activate SNRK. The SNRK mRNA is increased 3-fold when granule neurons are cultured in low potassium, and may thus play a role in the survival responses in these cells. In some vertebrates, a second SNRK gene (snrkb or snrk-1) has been sequenced and/or identified. Snrk-1 is expressed specifically in embryonic zebrafish vasculature; it plays an essential role in angioblast differentiation, maintenance, and migration. The SNRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270976 [Multi-domain]  Cd Length: 258  Bit Score: 77.07  E-value: 3.11e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  726 LGKTLGEGEFGkVVKaTAFHLkgragYT--TVAVKMLKENASPSELRD-LLSEFNVLKQVNHPHVIKLYGACSQDGPLLL 802
Cdd:cd14074    7 LEETLGRGHFA-VVK-LARHV-----FTgeKVAVKVIDKTKLDDVSKAhLFQEVRCMKLVQHPNVVRLYEVIDTQTKLYL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  803 IVEYAKYGSLRGF-LRESRKVgpgylgsggsrnsssldhPDERALTMgdlisFAwQISQGMQYLAEMKLVHRDLAARNIL 881
Cdd:cd14074   80 ILELGDGGDMYDYiMKHENGL------------------NEDLARKY-----FR-QIVSAISYCHKLHVVHRDLKPENVV 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  882 VAEGRKM-KISDFGLSRDvYEEDSYVKRSQGRIpvKWMAIESLFDHIYTTQS-DVWSFGVLLWEIVTlggnpypGIPP-- 957
Cdd:cd14074  136 FFEKQGLvKLTDFGFSNK-FQPGEKLETSCGSL--AYSAPEILLGDEYDAPAvDIWSLGVILYMLVC-------GQPPfq 205
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 10862703  958 -----ERLFNLLKTghRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADISKD 1004
Cdd:cd14074  206 eandsETLTMIMDC--KYTVPAHVSPECKDLIRRMLIRDPKKRASLEEIENH 255
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
717-1003 3.38e-15

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase Kinase 4; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK4 is a dual-specificity PK that phosphorylates and activates the downstream targets, c-Jun N-terminal kinase (JNK) and p38 MAPK, on specific threonine and tyrosine residues. JNK and p38 are collectively known as stress-activated MAPKs, as they are activated in response to a variety of environmental stresses and pro-inflammatory cytokines. Their activation is associated with the induction of cell death. Mice deficient in MKK4 die during embryogenesis and display anemia, severe liver hemorrhage, and abnormal hepatogenesis. MKK4 may also play roles in the immune system and in cardiac hypertrophy. It plays a major role in cancer as a tumor and metastasis suppressor. Under certain conditions, MKK4 is pro-oncogenic. The MKK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270790 [Multi-domain]  Cd Length: 291  Bit Score: 77.41  E-value: 3.38e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  717 WEFPRKNLVLGKTLGEGEFGKVVKatafhLKGRAGYTTVAVKMLKENASPSELRDLLSEFNVLKQVNH-PHVIKLYGACS 795
Cdd:cd06616    1 YEFTAEDLKDLGEIGRGAFGTVNK-----MLHKPSGTIMAVKRIRSTVDEKEQKRLLMDLDVVMRSSDcPYIVKFYGALF 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  796 QDGPLLLIVEYAKYgSLRGFLRESRKVGPGYLgsggsrnsssldhpDERALTMgdlISFAwqISQGMQYLA-EMKLVHRD 874
Cdd:cd06616   76 REGDCWICMELMDI-SLDKFYKYVYEVLDSVI--------------PEEILGK---IAVA--TVKALNYLKeELKIIHRD 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  875 LAARNILVAEGRKMKISDFGLSRdvYEEDSYVK-RSQGRIPvkWMAIE----SLFDHIYTTQSDVWSFGVLLWEIVTlGG 949
Cdd:cd06616  136 VKPSNILLDRNGNIKLCDFGISG--QLVDSIAKtRDAGCRP--YMAPEridpSASRDGYDVRSDVWSLGITLYEVAT-GK 210
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 10862703  950 NPYP--------------GIPPerlfnLLKTGHRMERpdncSEEMYRLMLQCWKQEPDKRPVFADISK 1003
Cdd:cd06616  211 FPYPkwnsvfdqltqvvkGDPP-----ILSNSEEREF----SPSFVNFVNLCLIKDESKRPKYKELLK 269
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
730-944 3.87e-15

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK6 is regulated by D-type cyclins and INK4 inhibitors. It is active towards the retinoblastoma (pRb) protein, implicating it to function in regulating the early G1 phase of the cell cycle. It is expressed ubiquitously and is localized in the cytoplasm. It is also present in the ruffling edge of spreading fibroblasts and may play a role in cell spreading. It binds to the p21 inhibitor without any effect on its own activity and it is overexpressed in squamous cell carcinomas and neuroblastomas. CDK6 has also been shown to inhibit cell differentiation in many cell types. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270846 [Multi-domain]  Cd Length: 290  Bit Score: 77.38  E-value: 3.87e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  730 LGEGEFGKVVKATAFHLKGR-AGYTTVAVKMLKENASPSELRdllsEFNVLKQVN---HPHVIKLYGACS-----QDGPL 800
Cdd:cd07862    9 IGEGAYGKVFKARDLKNGGRfVALKRVRVQTGEEGMPLSTIR----EVAVLRHLEtfeHPNVVRLFDVCTvsrtdRETKL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  801 LLIVEYAKYgSLRGFLRESRKvgPGYlgsggsrnsssldhPDEralTMGDLIsfaWQISQGMQYLAEMKLVHRDLAARNI 880
Cdd:cd07862   85 TLVFEHVDQ-DLTTYLDKVPE--PGV--------------PTE---TIKDMM---FQLLRGLDFLHSHRVVHRDLKPQNI 141
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 10862703  881 LVAEGRKMKISDFGLSRdVYeedSYVKRSQGRIPVKWM-AIESLFDHIYTTQSDVWSFGVLLWEI 944
Cdd:cd07862  142 LVTSSGQIKLADFGLAR-IY---SFQMALTSVVVTLWYrAPEVLLQSSYATPVDLWSVGCIFAEM 202
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
728-996 4.31e-15

Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like protein kinases; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. This subfamily is composed of the dual-specificity DYRKs and YAK1, as well as the S/T kinases (STKs), HIPKs. DYRKs and YAK1 autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. Proteins in this subfamily play important roles in cell proliferation, differentiation, survival, growth, and development. The DYRK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271035 [Multi-domain]  Cd Length: 262  Bit Score: 76.54  E-value: 4.31e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  728 KTLGEGEFGKVVKATafhlkGRAGYTTVAVKMLKENasPSELRDLLSEFNVLKQVN------HPHVIKLYGACSQDGPLL 801
Cdd:cd14133    5 EVLGKGTFGQVVKCY-----DLLTGEEVALKIIKNN--KDYLDQSLDEIRLLELLNkkdkadKYHIVRLKDVFYFKNHLC 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  802 LIVEYAKYgSLRGFLRESRKVGpgylgsggsrnsssldhpderaLTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNIL 881
Cdd:cd14133   78 IVFELLSQ-NLYEFLKQNKFQY----------------------LSLPRIRKIAQQILEALVFLHSLGLIHCDLKPENIL 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  882 VAEGRK--MKISDFGLSRDVYEE-DSYVKRSQGRIPvkwmaiESLFDHIYTTQSDVWSFGVLLWEIVTlgGNP-YP---- 953
Cdd:cd14133  135 LASYSRcqIKIIDFGSSCFLTQRlYSYIQSRYYRAP------EVILGLPYDEKIDMWSLGCILAELYT--GEPlFPgase 206
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 10862703  954 -----------GIPPERLFNllktgHRMERpdncSEEMYRLMLQCWKQEPDKRP 996
Cdd:cd14133  207 vdqlariigtiGIPPAHMLD-----QGKAD----DELFVDFLKKLLEIDPKERP 251
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
730-966 4.44e-15

Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Pho85 is a multifunctional CDK in yeast. It is regulated by 10 different cyclins (Pcls) and plays a role in G1 progression, cell polarity, phosphate and glycogen metabolism, gene expression, and in signaling changes in the environment. It is not essential for yeast viability and is the functional homolog of mammalian CDK5, which plays a role in central nervous system development. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The Pho85 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143341 [Multi-domain]  Cd Length: 284  Bit Score: 77.14  E-value: 4.44e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  730 LGEGEFgkvvkATAFhlKGRAGYTT--VAVKMLK---ENASPSELrdlLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIV 804
Cdd:cd07836    8 LGEGTY-----ATVY--KGRNRTTGeiVALKEIHldaEEGTPSTA---IREISLMKELKHENIVRLHDVIHTENKLMLVF 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  805 EYAKyGSLRGFLREsrkvgpgylgsggsrnsssldHPDERALTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNILVAE 884
Cdd:cd07836   78 EYMD-KDLKKYMDT---------------------HGVRGALDPNTVKSFTYQLLKGIAFCHENRVLHRDLKPQNLLINK 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  885 GRKMKISDFGLSRDVyeedsyvkrsqgRIPVKWMAIES-----------LFDHIYTTQSDVWSFGVLLWEIVTlgGNP-Y 952
Cdd:cd07836  136 RGELKLADFGLARAF------------GIPVNTFSNEVvtlwyrapdvlLGSRTYSTSIDIWSVGCIMAEMIT--GRPlF 201
                        250
                 ....*....|....*...
gi 10862703  953 PGIPPE----RLFNLLKT 966
Cdd:cd07836  202 PGTNNEdqllKIFRIMGT 219
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
726-992 5.24e-15

Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-3 shows a restricted pattern of expression and is present in brain, kidney, and intestine. It is elevated in Alzheimer's disease (AD) and has been shown to associate with paired helical filaments (PHFs) and stimulate Tau phosphorylation. As AD progresses, phosphorylated Tau aggregates and forms PHFs, which leads to the formation of neurofibrillary tangles. In human glioma cells, PCTAIRE-3 induces cell cycle arrest and cell death. PCTAIRE-3 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PCTAIRE-3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270853 [Multi-domain]  Cd Length: 288  Bit Score: 76.97  E-value: 5.24e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  726 LGKtLGEGEFgkvvkATAFhlKGRAGYTT--VAVKMLK----ENASPSELRdllsEFNVLKQVNHPHVIKLYGACSQDGP 799
Cdd:cd07871   10 LDK-LGEGTY-----ATVF--KGRSKLTEnlVALKEIRleheEGAPCTAIR----EVSLLKNLKHANIVTLHDIIHTERC 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  800 LLLIVEYakygsLRGFLREsrkvgpgylgsggsrnssSLDHPDErALTMGDLISFAWQISQGMQYLAEMKLVHRDLAARN 879
Cdd:cd07871   78 LTLVFEY-----LDSDLKQ------------------YLDNCGN-LMSMHNVKIFMFQLLRGLSYCHKRKILHRDLKPQN 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  880 ILVAEGRKMKISDFGLSRdvyEEDSYVKRSQGRIPVKWMAIESLF--DHIYTTQSDVWSFGVLLWEIVTlgGNP-YPGIP 956
Cdd:cd07871  134 LLINEKGELKLADFGLAR---AKSVPTKTYSNEVVTLWYRPPDVLlgSTEYSTPIDMWGVGCILYEMAT--GRPmFPGST 208
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 10862703  957 PER----LFNLLKTGHRMERPDNCSEEMYR-LMLQCWKQEP 992
Cdd:cd07871  209 VKEelhlIFRLLGTPTEETWPGVTSNEEFRsYLFPQYRAQP 249
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
730-952 5.95e-15

Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase (IKK) beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IKKbeta is involved in the classical pathway of regulating Nuclear Factor-KappaB (NF-kB) proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. The classical pathway regulates the majority of genes activated by NF-kB including those encoding cytokines, chemokines, leukocyte adhesion molecules, and anti-apoptotic factors. It involves NEMO (NF-kB Essential MOdulator)- and IKKbeta-dependent phosphorylation and degradation of the Inhibitor of NF-kB (IkB), which liberates NF-kB dimers (typified by the p50-p65 heterodimer) from an inactive IkB/dimeric NF-kB complex, enabling them to migrate to the nucleus where they regulate gene transcription. The IKKbeta subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270940 [Multi-domain]  Cd Length: 290  Bit Score: 76.92  E-value: 5.95e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  730 LGEGEFGKVVKataFHLKGRAgyTTVAVKMLKENASPSELRDLLSEFNVLKQVNHPHVIK-------LYGACSQDGPLLL 802
Cdd:cd14038    2 LGTGGFGNVLR---WINQETG--EQVAIKQCRQELSPKNRERWCLEIQIMKRLNHPNVVAardvpegLQKLAPNDLPLLA 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  803 IvEYAKYGSLRGFLRESRKVGpgylgsggsrnsssldhpderALTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNILV 882
Cdd:cd14038   77 M-EYCQGGDLRKYLNQFENCC---------------------GLREGAILTLLSDISSALRYLHENRIIHRDLKPENIVL 134
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 10862703  883 AEGRKM---KISDFGLSRDVyEEDSYVKRSQGRIpvKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTlGGNPY 952
Cdd:cd14038  135 QQGEQRlihKIIDLGYAKEL-DQGSLCTSFVGTL--QYLAPELLEQQKYTVTVDYWSFGTLAFECIT-GFRPF 203
STKc_KSR1 cd14152
Catalytic domain of the Serine/Threonine Kinase, Kinase Suppressor of Ras 1; STKs catalyze the ...
726-1008 9.15e-15

Catalytic domain of the Serine/Threonine Kinase, Kinase Suppressor of Ras 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. KSR1 functions as a transducer of TNFalpha-stimulated C-Raf activation of ERK1/2 and NF-kB. Detected activity of KSR1 is cell type specific and context dependent. It is inactive in normal colon epithelial cells and becomes activated at the onset of inflammatory bowel disease (IBD). Similarly, KSR1 activity is undetectable prior to stimulation by EGF or ceramide in COS-7 or YAMC cells, respectively. KSR proteins are widely regarded as pseudokinases, however, this matter is up for debate as catalytic activity has been detected for KSR1 in some systems. The KSR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271054 [Multi-domain]  Cd Length: 279  Bit Score: 76.16  E-value: 9.15e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  726 LGKTLGEGEFGKVvkatafhLKGRaGYTTVAVKMLKENASPSE-LRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIV 804
Cdd:cd14152    4 LGELIGQGRWGKV-------HRGR-WHGEVAIRLLEIDGNNQDhLKLFKKEVMNYRQTRHENVVLFMGACMHPPHLAIIT 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  805 EYAKYGSLRGFLRESRKvgpgylgsggsrnsssldhpderALTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNILVAE 884
Cdd:cd14152   76 SFCKGRTLYSFVRDPKT-----------------------SLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDN 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  885 GrKMKISDFGL--SRDVYEEDSyvKRSQGRIPVKW-----------MAIESLFDHI-YTTQSDVWSFGVLLWEIVTLGGn 950
Cdd:cd14152  133 G-KVVITDFGLfgISGVVQEGR--RENELKLPHDWlcylapeivreMTPGKDEDCLpFSKAADVYAFGTIWYELQARDW- 208
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 10862703  951 PYPGIPPERLFNLLKTGHRMER---PDNCSEEMYRLMLQCWKQEPDKRPVFADISKDLEKM 1008
Cdd:cd14152  209 PLKNQPAEALIWQIGSGEGMKQvltTISLGKEVTEILSACWAFDLEERPSFTLLMDMLEKL 269
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
717-961 1.24e-14

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK2 is ubiquitously expressed and is essential in autophagy induction. It displays partially redundant functions with ULK1 and is able to compensate for the loss of ULK1 in non-selective autophagy. It also displays neuron-specific functions and is important in axon development. The ULK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271103 [Multi-domain]  Cd Length: 271  Bit Score: 75.43  E-value: 1.24e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  717 WEFPRKNLVlgktlGEGEFGKVvkatafhLKGRAGYTT---VAVKML-KENASPSELRdLLSEFNVLKQVNHPHVIKLYG 792
Cdd:cd14201    6 FEYSRKDLV-----GHGAFAVV-------FKGRHRKKTdweVAIKSInKKNLSKSQIL-LGKEIKILKELQHENIVALYD 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  793 ACSQDGPLLLIVEYAKYGSLRGFLREsrkvgpgylgsggsrnsssldhpdERALTMGDLISFAWQISQGMQYLAEMKLVH 872
Cdd:cd14201   73 VQEMPNSVFLVMEYCNGGDLADYLQA------------------------KGTLSEDTIRVFLQQIAAAMRILHSKGIIH 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  873 RDLAARNILVA---------EGRKMKISDFGLSRdvYEEDSYVKRSQGRIPVkWMAIESLFDHIYTTQSDVWSFGVLLWE 943
Cdd:cd14201  129 RDLKPQNILLSyasrkkssvSGIRIKIADFGFAR--YLQSNMMAATLCGSPM-YMAPEVIMSQHYDAKADLWSIGTVIYQ 205
                        250       260
                 ....*....|....*....|
gi 10862703  944 IVtLGGNPYPGIPPE--RLF 961
Cdd:cd14201  206 CL-VGKPPFQANSPQdlRMF 224
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
730-944 1.27e-14

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 2 or Protein Kinase regulated by RNA; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKR (or EIF2AK2) contains an N-terminal double-stranded RNA (dsRNA) binding domain and a C-terminal catalytic kinase domain. It is activated by dsRNA, which is produced as a replication intermediate in virally infected cells. It plays a key role in mediating innate immune responses to viral infection. PKR is also directly activated by PACT (protein activator of PKR) and heparin, and is inhibited by viral proteins and RNAs. PKR also regulates transcription and signal transduction in diseased cells, playing roles in tumorigenesis and neurodegenerative diseases. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. The PKR subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270949 [Multi-domain]  Cd Length: 267  Bit Score: 75.22  E-value: 1.27e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  730 LGEGEFGKVVKAtafhlKGRAGYTTVAVKMLKENASPSElrdllSEFNVLKQVNHPHVIKLYgaCSQDGP---------- 799
Cdd:cd14047   14 IGSGGFGQVFKA-----KHRIDGKTYAIKRVKLNNEKAE-----REVKALAKLDHPNIVRYN--GCWDGFdydpetsssn 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  800 --------LLLIVEYAKYGSLRGFLRESRKvgpgylgsggsrnsSSLDHpderaltMGDLISFaWQISQGMQYLAEMKLV 871
Cdd:cd14047   82 ssrsktkcLFIQMEFCEKGTLESWIEKRNG--------------EKLDK-------VLALEIF-EQITKGVEYIHSKKLI 139
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 10862703  872 HRDLAARNILVAEGRKMKISDFGLsrdVYEEDSYVKRSQGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEI 944
Cdd:cd14047  140 HRDLKPSNIFLVDTGKVKIGDFGL---VTSLKNDGKRTKSKGTLSYMSPEQISSQDYGKEVDIYALGLILFEL 209
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
701-995 1.42e-14

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKB-alpha is predominantly expressed in endothelial cells. It is critical for the regulation of angiogenesis and the maintenance of vascular integrity. It also plays a role in adipocyte differentiation. Mice deficient in PKB-alpha exhibit perinatal morbidity, growth retardation, reduction in body weight accompanied by reduced sizes of multiple organs, and enhanced apoptosis in some cell types. PKB-alpha activity has been reported to be frequently elevated in breast and prostate cancers. In some cancer cells, PKB-alpha may act as a suppressor of metastasis. PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. The PKB-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270746 [Multi-domain]  Cd Length: 356  Bit Score: 76.61  E-value: 1.42e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  701 ENQVSVDAFKILEDPKWEFPRKNLVLGKTLGEGEFGKVVKatafhLKGRAGYTTVAVKMLKENA--SPSELRDLLSEFNV 778
Cdd:cd05594    4 DNSGAEEMEVSLTKPKHKVTMNDFEYLKLLGKGTFGKVIL-----VKEKATGRYYAMKILKKEVivAKDEVAHTLTENRV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  779 LKQVNHPHVIKLYGACSQDGPLLLIVEYAKYGSLrgFLRESRkvgpgylgsggsrnsssldhpdERALTMGDLISFAWQI 858
Cdd:cd05594   79 LQNSRHPFLTALKYSFQTHDRLCFVMEYANGGEL--FFHLSR----------------------ERVFSEDRARFYGAEI 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  859 SQGMQYL-AEMKLVHRDLAARNILVAEGRKMKISDFGLSRDVYEEDSYVKRSQGrIPvKWMAIESLFDHIYTTQSDVWSF 937
Cdd:cd05594  135 VSALDYLhSEKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATMKTFCG-TP-EYLAPEVLEDNDYGRAVDWWGL 212
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 10862703  938 GVLLWEIVTlGGNPYPGIPPERLFNLLKTgHRMERPDNCSEEMYRLMLQCWKQEPDKR 995
Cdd:cd05594  213 GVVMYEMMC-GRLPFYNQDHEKLFELILM-EEIRFPRTLSPEAKSLLSGLLKKDPKQR 268
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
733-1001 1.79e-14

Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes MAST kinases, MAST-like (MASTL) kinases (also called greatwall kinase or Gwl), and fungal kinases with similarity to Saccharomyces cerevisiae Rim15 and Schizosaccharomyces pombe cek1. MAST kinases contain an N-terminal domain of unknown function, a central catalytic domain, and a C-terminal PDZ domain that mediates protein-protein interactions. MASTL kinases carry only a catalytic domain which contains a long insert relative to other kinases. The fungal kinases in this subfamily harbor other domains in addition to a central catalytic domain, which like in MASTL, also contains an insert relative to MAST kinases. Rim15 contains a C-terminal signal receiver (REC) domain while cek1 contains an N-terminal PAS domain. MAST kinases are cytoskeletal associated kinases of unknown function that are also expressed at neuromuscular junctions and postsynaptic densities. MASTL/Gwl is involved in the regulation of mitotic entry, mRNA stabilization, and DNA checkpoint recovery. The fungal proteins Rim15 and cek1 are involved in the regulation of meiosis and mitosis, respectively. The MAST-like kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270731 [Multi-domain]  Cd Length: 272  Bit Score: 74.95  E-value: 1.79e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  733 GEFGKVVKATafhlKGRAGyTTVAVK------MLKENASPSelrdLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVEY 806
Cdd:cd05579    4 GAYGRVYLAK----KKSTG-DLYAIKvikkrdMIRKNQVDS----VLAERNILSQAQNPFVVKLYYSFQGKKNLYLVMEY 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  807 AKYGSLRGFLRESrkvgpGYLgsggsrnsssldhpDERALTMgdlisFAWQISQGMQYLAEMKLVHRDLAARNILVAEGR 886
Cdd:cd05579   75 LPGGDLYSLLENV-----GAL--------------DEDVARI-----YIAEIVLALEYLHSHGIIHRDLKPDNILIDANG 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  887 KMKISDFGLSR-DVYEEDSYVKRSQGRIPVK------------WMAIESLFDHIYTTQSDVWSFGVLLWEIVTlggnpyp 953
Cdd:cd05579  131 HLKLTDFGLSKvGLVRRQIKLSIQKKSNGAPekedrrivgtpdYLAPEILLGQGHGKTVDWWSLGVILYEFLV------- 203
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 10862703  954 GIPP------ERLF-NLLKtgHRMERPD--NCSEEMYRLMLQCWKQEPDKR------------PVFADI 1001
Cdd:cd05579  204 GIPPfhaetpEEIFqNILN--GKIEWPEdpEVSDEAKDLISKLLTPDPEKRlgakgieeiknhPFFKGI 270
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
728-957 1.80e-14

Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include human PRKX (X chromosome-encoded protein kinase), Drosophila DC2, and similar proteins. PRKX is present in many tissues including fetal and adult brain, kidney, and lung. The PRKX gene is located in the Xp22.3 subregion and has a homolog called PRKY on the Y chromosome. An abnormal interchange between PRKX aand PRKY leads to the sex reversal disorder of XX males and XY females. PRKX is implicated in granulocyte/macrophage lineage differentiation, renal cell epithelial migration, and tubular morphogenesis in the developing kidney. The PRKX-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270763 [Multi-domain]  Cd Length: 292  Bit Score: 75.16  E-value: 1.80e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  728 KTLGEGEFGKVVKAtafhlKGRAGYTTVAVKMLK--ENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVE 805
Cdd:cd05612    7 KTIGTGTFGRVHLV-----RDRISEHYYALKVMAipEVIRLKQEQHVHNEKRVLKEVSHPFIIRLFWTEHDQRFLYMLME 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  806 YAKYGSLRGFLRESRKVGPgylgsggsrnsssldhpderalTMGDLisFAWQISQGMQYLAEMKLVHRDLAARNILVAEG 885
Cdd:cd05612   82 YVPGGELFSYLRNSGRFSN----------------------STGLF--YASEIVCALEYLHSKEIVYRDLKPENILLDKE 137
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 10862703  886 RKMKISDFGLSRDVYEEDSYVKRSQgripvKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTlggnpypGIPP 957
Cdd:cd05612  138 GHIKLTDFGFAKKLRDRTWTLCGTP-----EYLAPEVIQSKGHNKAVDWWALGILIYEMLV-------GYPP 197
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
727-1001 2.17e-14

Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. PLKs derive their names from homology to polo, a kinase first identified in Drosophila. There are five mammalian PLKs (PLK1-5) from distinct genes. There is good evidence that PLK1 may function as an oncogene while PLK2-5 have tumor suppressive properties. PLK1 functions as a positive regulator of mitosis, meiosis, and cytokinesis. PLK2 functions in G1 progression, S-phase arrest, and centriole duplication. PLK3 regulates angiogenesis and responses to DNA damage. PLK4 is required for late mitotic progression, cell survival, and embryonic development. PLK5 was first identified as a pseudogene containing a stop codon within the kinase domain, however, both murine and human genes encode expressed proteins. PLK5 functions in cell cycle arrest.


Pssm-ID: 271001 [Multi-domain]  Cd Length: 258  Bit Score: 74.51  E-value: 2.17e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  727 GKTLGEGEFGKVVKATAFHLKGRAGYTTVAVKMLKenaSPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVEY 806
Cdd:cd14099    6 GKFLGKGGFAKCYEVTDMSTGKVYAGKVVPKSSLT---KPKQREKLKSEIKIHRSLKHPNIVKFHDCFEDEENVYILLEL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  807 AKYGSLRGFLREsRKvgpgylgsggsrnsssldhpderALTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNILVAEGR 886
Cdd:cd14099   83 CSNGSLMELLKR-RK-----------------------ALTEPEVRYFMRQILSGVKYLHSNRIIHRDLKLGNLFLDENM 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  887 KMKISDFGLSRDVyEEDSYVKRSQGRIPvKWMAIESLFDHI-YTTQSDVWSFGVLLWEIVTlggnpypGIPPerlFNL-- 963
Cdd:cd14099  139 NVKIGDFGLAARL-EYDGERKKTLCGTP-NYIAPEVLEKKKgHSFEVDIWSLGVILYTLLV-------GKPP---FETsd 206
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 10862703  964 LKTGHRMER------PDNC--SEE---MYRLMLQcwkQEPDKRPVFADI 1001
Cdd:cd14099  207 VKETYKRIKkneysfPSHLsiSDEakdLIRSMLQ---PDPTKRPSLDEI 252
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
728-996 2.23e-14

Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRE1, also called Endoplasmic reticulum (ER)-to-nucleus signaling protein (or ERN), is an ER-localized type I transmembrane protein with kinase and endoribonuclease domains in the cytoplasmic side. It acts as an ER stress sensor and is the oldest and most conserved component of the unfolded protein response (UPR) in eukaryotes. The UPR is activated when protein misfolding is detected in the ER in order to decrease the synthesis of new proteins and increase the capacity of the ER to cope with the stress. During ER stress, IRE1 dimerizes and forms oligomers, allowing the kinase domain to undergo trans-autophosphorylation. This leads to a conformational change that stimulates its endoribonuclease activity and results in the cleavage of its mRNA substrate, HAC1 in yeast and XBP1 in metazoans, promoting a splicing event that enables translation into a transcription factor which activates the UPR. Mammals contain two IRE1 proteins, IRE1alpha (or ERN1) and IRE1beta (or ERN2). The Ire1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270884 [Multi-domain]  Cd Length: 269  Bit Score: 74.62  E-value: 2.23e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  728 KTLGEGEFGKVVKATAFhlKGRAgyttVAVK-MLKENASPSELR-DLLSEFNvlkqvNHPHVIKLYGACSQDGPLLLIVE 805
Cdd:cd13982    7 KVLGYGSEGTIVFRGTF--DGRP----VAVKrLLPEFFDFADREvQLLRESD-----EHPNVIRYFCTEKDRQFLYIALE 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  806 YAKyGSLRGFLRESRKVGPGylgsggsrnsssldhpDERALTMGDLISfawQISQGMQYLAEMKLVHRDLAARNILV--- 882
Cdd:cd13982   76 LCA-ASLQDLVESPRESKLF----------------LRPGLEPVRLLR---QIASGLAHLHSLNIVHRDLKPQNILIstp 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  883 -AEGR-KMKISDFGLSRDV-YEEDSYVKRSQGRIPVKWMAIESLFDHIYTTQS---DVWSFGVLLWEIVTLGGNPYpGIP 956
Cdd:cd13982  136 nAHGNvRAMISDFGLCKKLdVGRSSFSRRSGVAGTSGWIAPEMLSGSTKRRQTravDIFSLGCVFYYVLSGGSHPF-GDK 214
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 10862703  957 PERLFNLLKTGHRMERPD---NCSEEMYRLMLQCWKQEPDKRP 996
Cdd:cd13982  215 LEREANILKGKYSLDKLLslgEHGPEAQDLIERMIDFDPEKRP 257
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
720-952 2.29e-14

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK6 may play a role in stress responses through its activation by the mitogen-activated protein kinase (MAPK) p38 and MAPK kinase 6 (MKK6) pathway. PAK6 is highly expressed in the brain. It is not required for viability, but together with PAK5, it is required for normal levels of locomotion and activity, and for learning and memory. Increased expression of PAK6 is found in primary and metastatic prostate cancer. PAK6 may play a role in the regulation of motility. PAK6 belongs to the group II PAKs, which contain a PBD (p21-binding domain) and a C-terminal catalytic domain, but do not harbor an AID (autoinhibitory domain) or SH3 binding sites. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270821 [Multi-domain]  Cd Length: 297  Bit Score: 75.02  E-value: 2.29e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  720 PRKNLVLGKTLGEGEFGKVVKATAFHlKGRagytTVAVKMLkeNASPSELRDLL-SEFNVLKQVNHPHVIKLYGACSQDG 798
Cdd:cd06659   19 PRQLLENYVKIGEGSTGVVCIAREKH-SGR----QVAVKMM--DLRKQQRRELLfNEVVIMRDYQHPNVVEMYKSYLVGE 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  799 PLLLIVEYAKYGSLRGFLRESRkvgpgylgsggsrnsssldhpderaLTMGDLISFAWQISQGMQYLAEMKLVHRDLAAR 878
Cdd:cd06659   92 ELWVLMEYLQGGALTDIVSQTR-------------------------LNEEQIATVCEAVLQALAYLHSQGVIHRDIKSD 146
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 10862703  879 NILVAEGRKMKISDFG----LSRDVYEEDSYVKRSQgripvkWMAIESLFDHIYTTQSDVWSFGVLLWEIVTlGGNPY 952
Cdd:cd06659  147 SILLTLDGRVKLSDFGfcaqISKDVPKRKSLVGTPY------WMAPEVISRCPYGTEVDIWSLGIMVIEMVD-GEPPY 217
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
720-995 2.83e-14

Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine/threonine kinases (STKs), p21-activated kinase (PAK) 3, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. PAKs from higher eukaryotes are classified into two groups (I and II), according to their biochemical and structural features. PAK3 belongs to group I. Group I PAKs contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). PAK3 is highly expressed in the brain. It is implicated in neuronal plasticity, synapse formation, dendritic spine morphogenesis, cell cycle progression, neuronal migration, and apoptosis. Inactivating mutations in the PAK3 gene cause X-linked non-syndromic mental retardation, the severity of which depends on the site of the mutation.


Pssm-ID: 132987 [Multi-domain]  Cd Length: 297  Bit Score: 74.76  E-value: 2.83e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  720 PRKNLVLGKTLGEGEFGKVVKATAFhlkgrAGYTTVAVKMLKENASPSElRDLLSEFNVLKQVNHPHVIKLYGACSQDGP 799
Cdd:cd06656   17 PKKKYTRFEKIGQGASGTVYTAIDI-----ATGQEVAIKQMNLQQQPKK-ELIINEILVMRENKNPNIVNYLDSYLVGDE 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  800 LLLIVEYAKYGSLRGFLRESrkvgpgylgsggsrnsssldhpderALTMGDLISFAWQISQGMQYLAEMKLVHRDLAARN 879
Cdd:cd06656   91 LWVVMEYLAGGSLTDVVTET-------------------------CMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDN 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  880 ILVAEGRKMKISDFGLSRDVYEEDSyvKRSQGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTlGGNPYPGIPPER 959
Cdd:cd06656  146 ILLGMDGSVKLTDFGFCAQITPEQS--KRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVE-GEPPYLNENPLR 222
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 10862703  960 LFNLLKTGH--RMERPDNCSEEMYRLMLQCWKQEPDKR 995
Cdd:cd06656  223 ALYLIATNGtpELQNPERLSAVFRDFLNRCLEMDVDRR 260
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
730-946 2.95e-14

Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of Plant B-type Cyclin-Dependent protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDK, CDK2, and CDK3. CDK1 is also called Cell division control protein 2 (Cdc2) or p34 protein kinase, and is regulated by cyclins A, B, and E. The CDK1/cyclin A complex controls G2 phase entry and progression while the CDK1/cyclin B complex is critical for G2 to M phase transition. CDK2 is regulated by cyclin E or cyclin A. Upon activation by cyclin E, it phosphorylates the retinoblastoma (pRb) protein which activates E2F mediated transcription and allows cells to move into S phase. The CDK2/cyclin A complex plays a role in regulating DNA replication. Studies in knockout mice revealed that CDK1 can compensate for the loss of the cdk2 gene as it can also bind cyclin E and drive G1 to S phase transition. CDK3 is regulated by cyclin C and it phosphorylates pRB specifically during the G0/G1 transition. This phosphorylation is required for cells to exit G0 efficiently and enter the G1 phase. The plant-specific B-type CDKs are expressed from the late S to the M phase of the cell cycle. They are characterized by the cyclin binding motif PPT[A/T]LRE. They play a role in controlling mitosis and integrating developmental pathways, such as stomata and leaf development. CdkB has been shown to associate with both cyclin B, which controls G2/M transition, and cyclin D, which acts as a mediator in linking extracellular signals to the cell cycle. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270829 [Multi-domain]  Cd Length: 283  Bit Score: 74.63  E-value: 2.95e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  730 LGEGEFGKVVKAtafhlKGRAGYTTVAVK-----MLKENASPSELRdllsEFNVLKQVNHPHVIKLYGACSQDGPLLLIV 804
Cdd:cd07835    7 IGEGTYGVVYKA-----RDKLTGEIVALKkirleTEDEGVPSTAIR----EISLLKELNHPNIVRLLDVVHSENKLYLVF 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  805 EY-----AKYgslrgflresrkvgpgylgsggsrnsssLDHPDERALTMGDLISFAWQISQGMQYLAEMKLVHRDLAARN 879
Cdd:cd07835   78 EFldldlKKY----------------------------MDSSPLTGLDPPLIKSYLYQLLQGIAFCHSHRVLHRDLKPQN 129
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 10862703  880 ILVAEGRKMKISDFGLSRDVyeedsyvkrsqgRIPVK---------WM-AIESLF-DHIYTTQSDVWSFGVLLWEIVT 946
Cdd:cd07835  130 LLIDTEGALKLADFGLARAF------------GVPVRtythevvtlWYrAPEILLgSKHYSTPVDIWSVGCIFAEMVT 195
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
727-1001 3.60e-14

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK2, also called Snk (serum-inducible kinase), functions in G1 progression, S-phase arrest, and centriole duplication. Its gene is responsive to both growth factors and cellular stress, is a transcriptional target of p53, and activates a G2-M checkpoint. The PLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271090 [Multi-domain]  Cd Length: 255  Bit Score: 73.89  E-value: 3.60e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  727 GKTLGEGEFGKVVKATafHLKGRAGYttvAVKMLKEN--ASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIV 804
Cdd:cd14188    6 GKVLGKGGFAKCYEMT--DLTTNKVY---AAKIIPHSrvSKPHQREKIDKEIELHRILHHKHVVQFYHYFEDKENIYILL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  805 EYAKYGSLRGFLReSRKVgpgylgsggsrnsssLDHPDERaltmgdliSFAWQISQGMQYLAEMKLVHRDLAARNILVAE 884
Cdd:cd14188   81 EYCSRRSMAHILK-ARKV---------------LTEPEVR--------YYLRQIVSGLKYLHEQEILHRDLKLGNFFINE 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  885 GRKMKISDFGLSRDVyEEDSYVKRSQGRIPvKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTlggnpypGIPPERLFNLL 964
Cdd:cd14188  137 NMELKVGDFGLAARL-EPLEHRRRTICGTP-NYLSPEVLNKQGHGCESDIWALGCVMYTMLL-------GRPPFETTNLK 207
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 10862703  965 KTGH-----RMERPDNCSEEMYRLMLQCWKQEPDKRPVFADI 1001
Cdd:cd14188  208 ETYRcireaRYSLPSSLLAPAKHLIASMLSKNPEDRPSLDEI 249
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
731-947 3.75e-14

Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDK8, CDC2L6, and similar proteins. CDK8 functions as a negative or positive regulator of transcription, depending on the scenario. Together with its regulator, cyclin C, it reversibly associates with the multi-subunit core Mediator complex, a cofactor that is involved in regulating RNA polymerase II-dependent transcription. CDC2L6 also associates with Mediator in complexes lacking CDK8. In VP16-dependent transcriptional activation, CDK8 and CDC2L6 exerts opposing effects by positive and negative regulation, respectively, in similar conditions. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK8-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270834 [Multi-domain]  Cd Length: 316  Bit Score: 74.63  E-value: 3.75e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  731 GEGEFGKVVKAtafhlKGRAGYTT--VAVKMLK------ENASPSELRdllsEFNVLKQVNHPHVIKLYGAC--SQDGPL 800
Cdd:cd07842    9 GRGTYGRVYKA-----KRKNGKDGkeYAIKKFKgdkeqyTGISQSACR----EIALLRELKHENVVSLVEVFleHADKSV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  801 LLIVEYAKYgSLRGFLRESRkvgpgylgsggsrnsssldHPDERALTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNI 880
Cdd:cd07842   80 YLLFDYAEH-DLWQIIKFHR-------------------QAKRVSIPPSMVKSLLWQILNGIHYLHSNWVLHRDLKPANI 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  881 LV----AEGRKMKISDFGLSRDV-------YEEDSYVKRSQGRIPvkwmaiESLF--DHiYTTQSDVWSFGVLLWEIVTL 947
Cdd:cd07842  140 LVmgegPERGVVKIGDLGLARLFnaplkplADLDPVVVTIWYRAP------ELLLgaRH-YTKAIDIWAIGCIFAELLTL 212
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
726-954 3.88e-14

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK1 is the prototypical member of the subfamily and is also simply referred to as DAPK. It is Ca2+/calmodulin (CaM)-regulated and actin-associated protein that contains an N-terminal kinase domain followed by an autoinhibitory CaM binding region and a large C-terminal extension with multiple functional domains including ankyrin (ANK) repeats, a cytoskeletal binding domain, a Death domain, and a serine-rich tail. Loss of DAPK1 expression, usually because of DNA methylation, is implicated in many tumor types. DAPK1 is highly abundant in the brain and has also been associated with neurodegeneration. The DAPK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271096 [Multi-domain]  Cd Length: 269  Bit Score: 73.90  E-value: 3.88e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  726 LGKTLGEGEFGKVVKAtafhlKGRAGYTTVAVKMLKENASPSELR-----DLLSEFNVLKQVNHPHVIKLYGACSQDGPL 800
Cdd:cd14194    9 TGEELGSGQFAVVKKC-----REKSTGLQYAAKFIKKRRTKSSRRgvsreDIEREVSILKEIQHPNVITLHEVYENKTDV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  801 LLIVEYAKYGSLRGFLREsrkvgpgylgsggsrnsssldhpdERALTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNI 880
Cdd:cd14194   84 ILILELVAGGELFDFLAE------------------------KESLTEEEATEFLKQILNGVYYLHSLQIAHFDLKPENI 139
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 10862703  881 LV----AEGRKMKISDFGLSRDVYEEDSYvKRSQGrIPvKWMAIESLFDHIYTTQSDVWSFGVLLWeIVTLGGNPYPG 954
Cdd:cd14194  140 MLldrnVPKPRIKIIDFGLAHKIDFGNEF-KNIFG-TP-EFVAPEIVNYEPLGLEADMWSIGVITY-ILLSGASPFLG 213
STKc_IRAK1 cd14159
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; ...
730-946 4.13e-14

Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain, and a C-terminal domain; IRAK-4 lacks the C-terminal domain. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK1 plays a role in the activation of IRF3/7, STAT, and NFkB. It mediates IL-6 and IFN-gamma responses following IL-1 and IL-18 stimulation, respectively. It also plays an essential role in IFN-alpha induction downstream of TLR7 and TLR9. The IRAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271061 [Multi-domain]  Cd Length: 296  Bit Score: 74.48  E-value: 4.13e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  730 LGEGEFGKVVKATAFHlkgragyTTVAVKMLKENaspSEL------RDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLI 803
Cdd:cd14159    1 IGEGGFGCVYQAVMRN-------TEYAVKRLKED---SELdwsvvkNSFLTEVEKLSRFRHPNIVDLAGYSAQQGNYCLI 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  804 VEYAKYGSLRGFLresrkvgpgylgsggsrnsssldHPDER--ALTMGDLISFAWQISQGMQYLAEMK--LVHRDLAARN 879
Cdd:cd14159   71 YVYLPNGSLEDRL-----------------------HCQVScpCLSWSQRLHVLLGTARAIQYLHSDSpsLIHGDVKSSN 127
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 10862703  880 ILVAEGRKMKISDFGLSR-----DVYEEDSYVKRSQG-RIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVT 946
Cdd:cd14159  128 ILLDAALNPKLGDFGLARfsrrpKQPGMSSTLARTQTvRGTLAYLPEEYVKTGTLSVEIDVYSFGVVLLELLT 200
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
728-1004 4.87e-14

Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include Saccharomyces cerevisiae Rim15, Schizosaccharomyces pombe cek1, and similar fungal proteins. They contain a central catalytic domain, which contains an insert relative to MAST kinases. In addition, Rim15 contains a C-terminal signal receiver (REC) domain while cek1 contains an N-terminal PAS domain. Rim15 (or Rim15p) functions as a regulator of meiosis. It acts as a downstream effector of PKA and regulates entry into stationary phase (G0). Thus, it plays a crucial role in regulating yeast proliferation, differentiation, and aging. Cek1 may facilitate progression of mitotic anaphase. The Rim15-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270762 [Multi-domain]  Cd Length: 263  Bit Score: 73.67  E-value: 4.87e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  728 KTLGEGEFGKVVKAtafhlKGRAGYTTVAVKMLKENA--SPSELRDLLSE-FNVLKQVNHPHVIKLYGACSQDGPLLLIV 804
Cdd:cd05611    2 KPISKGAFGSVYLA-----KKRSTGDYFAIKVLKKSDmiAKNQVTNVKAErAIMMIQGESPYVAKLYYSFQSKDYLYLVM 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  805 EYAKYGSLRGFLRESrkvgpGYLgsggsrnsssldhPDERALTmgdlisFAWQISQGMQYLAEMKLVHRDLAARNILVAE 884
Cdd:cd05611   77 EYLNGGDCASLIKTL-----GGL-------------PEDWAKQ------YIAEVVLGVEDLHQRGIIHRDIKPENLLIDQ 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  885 GRKMKISDFGLSRDVYEedsyvKRSQGRI---PvKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTlGGNPYPGIPPERLF 961
Cdd:cd05611  133 TGHLKLTDFGLSRNGLE-----KRHNKKFvgtP-DYLAPETILGVGDDKMSDWWSLGCVIFEFLF-GYPPFHAETPDAVF 205
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 10862703  962 NLLKTGhRMERPDN----CSEE----MYRLM-LQCWK-------QEPDKRPVFADISKD 1004
Cdd:cd05611  206 DNILSR-RINWPEEvkefCSPEavdlINRLLcMDPAKrlgangyQEIKSHPFFKSINWD 263
STKc_TGFbR_I cd14056
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type ...
728-1008 5.88e-14

Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type I Receptors; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of type I receptors for the TGFbeta family of secreted signaling molecules including TGFbeta, bone morphogenetic proteins, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation through trans-phosphorylation by type II receptors, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. They are inhibited by the immunophilin FKBP12, which is thought to control leaky signaling caused by receptor oligomerization in the absence of ligand. The TGFbR-I subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270958 [Multi-domain]  Cd Length: 287  Bit Score: 73.85  E-value: 5.88e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  728 KTLGEGEFGKVVKAtafHLKGRAgyttVAVKMLKENASPSELRDLLSEFNVLkqVNHPHVIKLYGA-------CSQdgpL 800
Cdd:cd14056    1 KTIGKGRYGEVWLG---KYRGEK----VAVKIFSSRDEDSWFRETEIYQTVM--LRHENILGFIAAdikstgsWTQ---L 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  801 LLIVEYAKYGSLRGFLREsrkvgpgylgsggsrnsssldhpdeRALTMGDLISFAWQISQGMQYL-AEM-------KLVH 872
Cdd:cd14056   69 WLITEYHEHGSLYDYLQR-------------------------NTLDTEEALRLAYSAASGLAHLhTEIvgtqgkpAIAH 123
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  873 RDLAARNILVAEGRKMKISDFGL----SRDVYEEDSYVKRSQGriPVKWMAIESLFDHIYTT------QSDVWSFGVLLW 942
Cdd:cd14056  124 RDLKSKNILVKRDGTCCIADLGLavryDSDTNTIDIPPNPRVG--TKRYMAPEVLDDSINPKsfesfkMADIYSFGLVLW 201
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  943 EI---VTLGGNPYPGIPP-----------ERLFNLLKTghRMERP--------DNCSEEMYRLMLQCWKQEPDKRPVFAD 1000
Cdd:cd14056  202 EIarrCEIGGIAEEYQLPyfgmvpsdpsfEEMRKVVCV--EKLRPpipnrwksDPVLRSMVKLMQECWSENPHARLTALR 279

                 ....*...
gi 10862703 1001 ISKDLEKM 1008
Cdd:cd14056  280 VKKTLAKL 287
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
727-1004 8.73e-14

Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK4 is a MAPK kinase kinase that phosphorylates and activates the c-Jun N-terminal kinase (JNK) and p38 MAPK signaling pathways by directly activating their respective MAPKKs, MKK4/MKK7 and MKK3/MKK6. JNK and p38 are collectively known as stress-activated MAPKs, as they are activated in response to a variety of environmental stresses and pro-inflammatory cytokines. MEKK4 also plays roles in the re-polarization of the actin cytoskeleton in response to osmotic stress, in the proper closure of the neural tube, in cardiovascular development, and in immune responses. The MEKK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270796 [Multi-domain]  Cd Length: 265  Bit Score: 72.72  E-value: 8.73e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  727 GKTLGEGEFGKVvkatafhlkgragYTTV--------AVKMLK-ENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQD 797
Cdd:cd06626    5 GNKIGEGTFGKV-------------YTAVnldtgelmAMKEIRfQDNDPKTIKEIADEMKVLEGLDHPNLVRYYGVEVHR 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  798 GPLLLIVEYAKYGSLRGFLRESRKVgpgylgsggsrnsssldhpDERALTMgdlisFAWQISQGMQYLAEMKLVHRDLAA 877
Cdd:cd06626   72 EEVYIFMEYCQEGTLEELLRHGRIL-------------------DEAVIRV-----YTLQLLEGLAYLHENGIVHRDIKP 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  878 RNILVAEGRKMKISDFGLSrdVYEEDSYVKRSQGRI------PVkWMAIESLF---DHIYTTQSDVWSFGVLLWEIVTlG 948
Cdd:cd06626  128 ANIFLDSNGLIKLGDFGSA--VKLKNNTTTMAPGEVnslvgtPA-YMAPEVITgnkGEGHGRAADIWSLGCVVLEMAT-G 203
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  949 GNPYPGIPPER--LFNlLKTGHRMERPDN--CSEEMYRLMLQCWKQEPDKRPVFADISKD 1004
Cdd:cd06626  204 KRPWSELDNEWaiMYH-VGMGHKPPIPDSlqLSPEGKDFLSRCLESDPKKRPTASELLDH 262
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
728-967 1.01e-13

Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The inactive PKA holoenzyme is a heterotetramer composed of two phosphorylated and active catalytic subunits with a dimer of regulatory (R) subunits. Activation is achieved through the binding of the important second messenger cAMP to the R subunits, which leads to the dissociation of PKA into the R dimer and two active subunits. PKA is present ubiquitously in cells and interacts with many different downstream targets. It plays a role in the regulation of diverse processes such as growth, development, memory, metabolism, gene expression, immunity, and lipolysis. The PKA subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271111 [Multi-domain]  Cd Length: 290  Bit Score: 73.21  E-value: 1.01e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  728 KTLGEGEFGKVVKATafHLKGRAGYttvAVKML-KEN-ASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVE 805
Cdd:cd14209    7 KTLGTGSFGRVMLVR--HKETGNYY---AMKILdKQKvVKLKQVEHTLNEKRILQAINFPFLVKLEYSFKDNSNLYMVME 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  806 YAKYGSLRGFLRESRKvgpgylgsggsrnsssLDHPDERAltmgdlisFAWQISQGMQYLAEMKLVHRDLAARNILVAEG 885
Cdd:cd14209   82 YVPGGEMFSHLRRIGR----------------FSEPHARF--------YAAQIVLAFEYLHSLDLIYRDLKPENLLIDQQ 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  886 RKMKISDFGlsrdvyeedsYVKRSQGR------IPvKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTlGGNPYPGIPPER 959
Cdd:cd14209  138 GYIKVTDFG----------FAKRVKGRtwtlcgTP-EYLAPEIILSKGYNKAVDWWALGVLIYEMAA-GYPPFFADQPIQ 205

                 ....*...
gi 10862703  960 LFNLLKTG 967
Cdd:cd14209  206 IYEKIVSG 213
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
723-1003 1.36e-13

Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase Kinases 3 and 6; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK3 and MKK6 are dual-specificity PKs that phosphorylate and activate their downstream target, p38 MAPK, on specific threonine and tyrosine residues. MKK3/6 play roles in the regulation of cell cycle progression, cytokine- and stress-induced apoptosis, oncogenic transformation, and adult tissue regeneration. In addition, MKK6 plays a critical role in osteoclast survival in inflammatory disease while MKK3 is associated with tumor invasion, progression, and poor patient survival in glioma. The MKK3/6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173729 [Multi-domain]  Cd Length: 283  Bit Score: 72.46  E-value: 1.36e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  723 NLVLGKTLGEGEFGKVVKatafhLKGRAGYTTVAVKMLKENASPSELRDLLSEFNV-LKQVNHPHVIKLYGACSQDGPLL 801
Cdd:cd06617    2 DLEVIEELGRGAYGVVDK-----MRHVPTGTIMAVKRIRATVNSQEQKRLLMDLDIsMRSVDCPYTVTFYGALFREGDVW 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  802 LIVEYAKyGSLRGFLREsrkvgpgylgsggsrnssSLDHPderaLTMGD--LISFAWQISQGMQYLAE-MKLVHRDLAAR 878
Cdd:cd06617   77 ICMEVMD-TSLDKFYKK------------------VYDKG----LTIPEdiLGKIAVSIVKALEYLHSkLSVIHRDVKPS 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  879 NILVAEGRKMKISDFGLSRdvYEEDSYVKRSQ-GRIPvkWMAIE----SLFDHIYTTQSDVWSFGVLLWEIVTlGGNPYP 953
Cdd:cd06617  134 NVLINRNGQVKLCDFGISG--YLVDSVAKTIDaGCKP--YMAPErinpELNQKGYDVKSDVWSLGITMIELAT-GRFPYD 208
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 10862703  954 --GIPPERLFNLLKTGHRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADISK 1003
Cdd:cd06617  209 swKTPFQQLKQVVEEPSPQLPAEKFSPEFQDFVNKCLKKNYKERPNYPELLQ 260
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
730-966 1.39e-13

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK5 is unusual in that it is regulated by non-cyclin proteins, p35 and p39. It is highly expressed in the nervous system and is critical in normal neural development and function. It plays a role in neuronal migration and differentiation, and is also important in synaptic plasticity and learning. CDK5 also participates in protecting against cell death and promoting angiogenesis. Impaired CDK5 activity is implicated in Alzheimer's disease, amyotrophic lateral sclerosis, Parkinson's disease, Huntington's disease and acute neuronal injury. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143344 [Multi-domain]  Cd Length: 284  Bit Score: 72.47  E-value: 1.39e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  730 LGEGEFGKVVKAtafhlKGRAGYTTVAVKMLK-----ENASPSELRdllsEFNVLKQVNHPHVIKLYGACSQDGPLLLIV 804
Cdd:cd07839    8 IGEGTYGTVFKA-----KNRETHEIVALKRVRlddddEGVPSSALR----EICLLKELKHKNIVRLYDVLHSDKKLTLVF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  805 EYA-----KY-GSLRGflresrkvgpgylgsggsrnssSLDHPDERaltmgdliSFAWQISQGMQYLAEMKLVHRDLAAR 878
Cdd:cd07839   79 EYCdqdlkKYfDSCNG----------------------DIDPEIVK--------SFMFQLLKGLAFCHSHNVLHRDLKPQ 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  879 NILVAEGRKMKISDFGLSrdvyeedsyvkRSQGrIPVKWMAIE----------SLFD-HIYTTQSDVWSFGVLLWEIVTL 947
Cdd:cd07839  129 NLLINKNGELKLADFGLA-----------RAFG-IPVRCYSAEvvtlwyrppdVLFGaKLYSTSIDMWSAGCIFAELANA 196
                        250       260
                 ....*....|....*....|...
gi 10862703  948 GGNPYPGIPPE----RLFNLLKT 966
Cdd:cd07839  197 GRPLFPGNDVDdqlkRIFRLLGT 219
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
720-995 1.57e-13

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK1 is important in the regulation of many cellular processes including cytoskeletal dynamics, cell motility, growth, and proliferation. Although PAK1 has been regarded mainly as a cytosolic protein, recent reports indicate that PAK1 also exists in significant amounts in the nucleus, where it is involved in transcription modulation and in cell cycle regulatory events. PAK1 is also involved in transformation and tumorigenesis. Its overexpression, hyperactivation and increased nuclear accumulation is correlated to breast cancer invasiveness and progression. Nuclear accumulation is also linked to tamoxifen resistance in breast cancer cells. PAK1 belongs to the group I PAKs, which contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270820 [Multi-domain]  Cd Length: 296  Bit Score: 72.45  E-value: 1.57e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  720 PRKNLVLGKTLGEGEFGKVVKATAFhlkgrAGYTTVAVKMLKENASPSElRDLLSEFNVLKQVNHPHVIKLYGACSQDGP 799
Cdd:cd06654   18 PKKKYTRFEKIGQGASGTVYTAMDV-----ATGQEVAIRQMNLQQQPKK-ELIINEILVMRENKNPNIVNYLDSYLVGDE 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  800 LLLIVEYAKYGSLRGFLRESrkvgpgylgsggsrnsssldhpderALTMGDLISFAWQISQGMQYLAEMKLVHRDLAARN 879
Cdd:cd06654   92 LWVVMEYLAGGSLTDVVTET-------------------------CMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDN 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  880 ILVAEGRKMKISDFGLSRDVYEEDSyvKRSQGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTlGGNPYPGIPPER 959
Cdd:cd06654  147 ILLGMDGSVKLTDFGFCAQITPEQS--KRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIE-GEPPYLNENPLR 223
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 10862703  960 LFNLLKTGH--RMERPDNCSEEMYRLMLQCWKQEPDKR 995
Cdd:cd06654  224 ALYLIATNGtpELQNPEKLSAIFRDFLNRCLEMDVEKR 261
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
720-995 1.60e-13

Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Group I PAKs, also called conventional PAKs, include PAK1, PAK2, and PAK3. Group I PAKs contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). They interact with the SH3 domain containing proteins Nck, Grb2 and PIX. Binding of group I PAKs to activated GTPases leads to conformational changes that destabilize the AID, allowing autophosphorylation and full activation of the kinase domain. Known group I PAK substrates include MLCK, Bad, Raf, MEK1, LIMK, Merlin, Vimentin, Myc, Stat5a, and Aurora A, among others. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. PAKs are implicated in the regulation of many cellular processes including growth factor receptor-mediated proliferation, cell polarity, cell motility, cell death and survival, and actin cytoskeleton organization. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270814 [Multi-domain]  Cd Length: 261  Bit Score: 71.88  E-value: 1.60e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  720 PRKNLVLGKTLGEGEFGKVVKATAFhlkgrAGYTTVAVKMLKENASPS-ELrdLLSEFNVLKQVNHPHVIKLYGACSQDG 798
Cdd:cd06647    5 PKKKYTRFEKIGQGASGTVYTAIDV-----ATGQEVAIKQMNLQQQPKkEL--IINEILVMRENKNPNIVNYLDSYLVGD 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  799 PLLLIVEYAKYGSLRGFLRESrkvgpgylgsggsrnsssldhpderALTMGDLISFAWQISQGMQYLAEMKLVHRDLAAR 878
Cdd:cd06647   78 ELWVVMEYLAGGSLTDVVTET-------------------------CMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSD 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  879 NILVAEGRKMKISDFGLSRDVYEEDSyvKRSQGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTlGGNPYPGIPPE 958
Cdd:cd06647  133 NILLGMDGSVKLTDFGFCAQITPEQS--KRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVE-GEPPYLNENPL 209
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 10862703  959 RLFNLLKTGHRME--RPDNCSEEMYRLMLQCWKQEPDKR 995
Cdd:cd06647  210 RALYLIATNGTPElqNPEKLSAIFRDFLNRCLEMDVEKR 248
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
725-946 1.61e-13

Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), Bypass UAS Requirement 1, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BUR1, also called SGV1, is a yeast CDK that is functionally equivalent to mammalian CDK9. It associates with the cyclin BUR2. BUR genes were orginally identified in a genetic screen as factors involved in general transcription. The BUR1/BUR2 complex phosphorylates the C-terminal domain of RNA polymerase II. In addition, this complex regulates histone modification by phosporylating Rad6 and mediating the association of the Paf1 complex with chromatin. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The BUR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270849 [Multi-domain]  Cd Length: 311  Bit Score: 72.73  E-value: 1.61e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  725 VLGKtLGEGEFGKVVKAtafhlKGRAGYTTVAVKML-----KENASPSELRdllsEFNVLKQVNHPHVIKLygacsqdgp 799
Cdd:cd07866   12 ILGK-LGEGTFGEVYKA-----RQIKTGRVVALKKIlmhneKDGFPITALR----EIKILKKLKHPNVVPL--------- 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  800 LLLIVEYAKygslrgflRESRKVGPGYLGSGGSRNSSS--LDHPDERaLTMGDLISFAWQISQGMQYLAEMKLVHRDLAA 877
Cdd:cd07866   73 IDMAVERPD--------KSKRKRGSVYMVTPYMDHDLSglLENPSVK-LTESQIKCYMLQLLEGINYLHENHILHRDIKA 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  878 RNILVAEGRKMKISDFGLSRdVYEEDSYVKRSQGR---------IPVKWM-AIESLF-DHIYTTQSDVWSFGVLLWEIVT 946
Cdd:cd07866  144 ANILIDNQGILKIADFGLAR-PYDGPPPNPKGGGGggtrkytnlVVTRWYrPPELLLgERRYTTAVDIWGIGCVFAEMFT 222
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
721-995 2.32e-13

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I gamma; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-gamma subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271068 [Multi-domain]  Cd Length: 285  Bit Score: 71.95  E-value: 2.32e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  721 RKNLVLGKTLGEGEFGKVvkataFHLKGRAGYTTVAVKMLKENASPSElRDLLSEFNVLKQVNHPHVIKLYGACSQDGPL 800
Cdd:cd14166    2 RETFIFMEVLGSGAFSEV-----YLVKQRSTGKLYALKCIKKSPLSRD-SSLENEIAVLKRIKHENIVTLEDIYESTTHY 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  801 LLIVEYAKYGSLrgflresrkvgpgylgsggsrnsssLDHPDERAL-TMGDLISFAWQISQGMQYLAEMKLVHRDLAARN 879
Cdd:cd14166   76 YLVMQLVSGGEL-------------------------FDRILERGVyTEKDASRVINQVLSAVKYLHENGIVHRDLKPEN 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  880 ILV---AEGRKMKISDFGLSRdvyEEDSYVKRSQGRIPvKWMAIESLFDHIYTTQSDVWSFGVLLWeIVTLGGNPYPGIP 956
Cdd:cd14166  131 LLYltpDENSKIMITDFGLSK---MEQNGIMSTACGTP-GYVAPEVLAQKPYSKAVDCWSIGVITY-ILLCGYPPFYEET 205
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 10862703  957 PERLFNLLKTG-HRMERP--DNCSEEMYRLMLQCWKQEPDKR 995
Cdd:cd14166  206 ESRLFEKIKEGyYEFESPfwDDISESAKDFIRHLLEKNPSKR 247
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
728-957 2.94e-13

Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGK1 is ubiquitously expressed and is under transcriptional control of numerous stimuli including cell stress (cell shrinkage), serum, hormones (gluco- and mineralocorticoids), gonadotropins, growth factors, interleukin-6, and other cytokines. It plays roles in sodium retention and potassium elimination in the kidney, nutrient transport, salt sensitivity, memory consolidation, and cardiac repolarization. A common SGK1 variant is associated with increased blood pressure and body weight. SGK1 may also contribute to tumor growth, neurodegeneration, fibrosing disease, and ischemia. The SGK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270753 [Multi-domain]  Cd Length: 339  Bit Score: 72.36  E-value: 2.94e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  728 KTLGEGEFGKVVKAtafhlKGRAGYTTVAVKMLKENA--SPSELRDLLSEFNVL-KQVNHPHVIKLYGACSQDGPLLLIV 804
Cdd:cd05602   13 KVIGKGSFGKVLLA-----RHKSDEKFYAVKVLQKKAilKKKEEKHIMSERNVLlKNVKHPFLVGLHFSFQTTDKLYFVL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  805 EYAKYGSLRGFLRESRkvgpgylgsggsrnssSLDHPDERAltmgdlisFAWQISQGMQYLAEMKLVHRDLAARNILVAE 884
Cdd:cd05602   88 DYINGGELFYHLQRER----------------CFLEPRARF--------YAAEIASALGYLHSLNIVYRDLKPENILLDS 143
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 10862703  885 GRKMKISDFGLSRDVYEEDSYVKRSQGrIPvKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTlggnpypGIPP 957
Cdd:cd05602  144 QGHIVLTDFGLCKENIEPNGTTSTFCG-TP-EYLAPEVLHKQPYDRTVDWWCLGAVLYEMLY-------GLPP 207
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
726-966 2.95e-13

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 72.49  E-value: 2.95e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703   726 LGKTLGEGEFGKVVKATAFHLKgragyTTVAVKMLKENASPSELRD-------------LLSEFNVLKQVNHPHVIKLYG 792
Cdd:PTZ00024   13 KGAHLGEGTYGKVEKAYDTLTG-----KIVAIKKVKIIEISNDVTKdrqlvgmcgihftTLRELKIMNEIKHENIMGLVD 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703   793 ACSQDGPLLLIVEYAKYGSLRGFLRESRkvgpgylgsggsrnsssldhpderaLTMGDLISFAWQISQGMQYLAEMKLVH 872
Cdd:PTZ00024   88 VYVEGDFINLVMDIMASDLKKVVDRKIR-------------------------LTESQVKCILLQILNGLNVLHKWYFMH 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703   873 RDLAARNILVAEGRKMKISDFGLSR--------DVYEEDSYVKRSQ---GRIPVKWM-AIESLF-DHIYTTQSDVWSFGV 939
Cdd:PTZ00024  143 RDLSPANIFINSKGICKIADFGLARrygyppysDTLSKDETMQRREemtSKVVTLWYrAPELLMgAEKYHFAVDMWSVGC 222
                         250       260       270
                  ....*....|....*....|....*....|..
gi 10862703   940 LLWEIVTlgGNP-YPGIPP----ERLFNLLKT 966
Cdd:PTZ00024  223 IFAELLT--GKPlFPGENEidqlGRIFELLGT 252
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
726-986 3.38e-13

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called Doublecortin-like and CAM kinase-like 2); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL2 (or DCAMKL2) belongs to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. In addition, DCKL2 contains a serine, threonine, and proline rich domain (SP) and a C-terminal kinase domain with similarity to CAMKs. DCKL2 has been shown to interact with tubulin, JIP1/2, JNK, neurabin 2, and actin. It is associated with the terminal segments of axons and dendrites, and may function as a phosphorylation-dependent switch to control microtubule dynamics in neuronal growth cones. The DCKL2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271086 [Multi-domain]  Cd Length: 259  Bit Score: 70.83  E-value: 3.38e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  726 LGKTLGEGEFGkVVKATAFHLKGRAgyttVAVKMLKENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVE 805
Cdd:cd14184    5 IGKVIGDGNFA-VVKECVERSTGKE----FALKIIDKAKCCGKEHLIENEVSILRRVKHPNIIMLIEEMDTPAELYLVME 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  806 YAKYGSLRGFLRESRKvgpgylgsggsrnsssldhpderaLTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNILVAE- 884
Cdd:cd14184   80 LVKGGDLFDAITSSTK------------------------YTERDASAMVYNLASALKYLHGLCIVHRDIKPENLLVCEy 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  885 ---GRKMKISDFGLSrDVYEEDSYvkrSQGRIPVkWMAIESLFDHIYTTQSDVWSFGVLLWEIVTlggnpypGIPP---- 957
Cdd:cd14184  136 pdgTKSLKLGDFGLA-TVVEGPLY---TVCGTPT-YVAPEIIAETGYGLKVDIWAAGVITYILLC-------GFPPfrse 203
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 10862703  958 ----ERLFNLLKTGHrMERP----DNCSE---EMYRLMLQ 986
Cdd:cd14184  204 nnlqEDLFDQILLGK-LEFPspywDNITDsakELISHMLQ 242
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
728-1011 3.94e-13

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. PKCs undergo three phosphorylations in order to take mature forms. In addition, classical PKCs depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. Novel PKCs are calcium-independent, but require DAG and PS for activity, while atypical PKCs only require PS. PKCs phosphorylate and modify the activities of a wide variety of cellular proteins including receptors, enzymes, cytoskeletal proteins, transcription factors, and other kinases. They play a central role in signal transduction pathways that regulate cell migration and polarity, proliferation, differentiation, and apoptosis. Also included in this subfamily are the PKC-like proteins, called PKNs. The PKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270722 [Multi-domain]  Cd Length: 318  Bit Score: 71.86  E-value: 3.94e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  728 KTLGEGEFGKVVKAtafHLKGRAGytTVAVKMLKENASpseLRD-----LLSEFNVLKQVN-HPHVIKLYgACSQDGPLL 801
Cdd:cd05570    1 KVLGKGSFGKVMLA---ERKKTDE--LYAIKVLKKEVI---IEDddvecTMTEKRVLALANrHPFLTGLH-ACFQTEDRL 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  802 LIV-EYAKYGSLRGFLRESRKVgpgylgsggsrnsssldhPDERAltmgdlISFAWQISQGMQYLAEMKLVHRDLAARNI 880
Cdd:cd05570   72 YFVmEYVNGGDLMFHIQRARRF------------------TEERA------RFYAAEICLALQFLHERGIIYRDLKLDNV 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  881 LV-AEGRkMKISDFGLSRDVYEEDSYVKRSQGrIPvKWMAIESLFDHIYTTQSDVWSFGVLLWEIVtLGGNPYPGIPPER 959
Cdd:cd05570  128 LLdAEGH-IKIADFGMCKEGIWGGNTTSTFCG-TP-DYIAPEILREQDYGFSVDWWALGVLLYEML-AGQSPFEGDDEDE 203
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 10862703  960 LFNLLKtGHRMERPDNCSEEMYRLMLQCWKQEPDKR--------------PVFADIS-KDLEKMMVK 1011
Cdd:cd05570  204 LFEAIL-NDEVLYPRWLSREAVSILKGLLTKDPARRlgcgpkgeadikahPFFRNIDwDKLEKKEVE 269
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
728-995 4.61e-13

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. There are three PKB isoforms from different genes, PKB-alpha (or Akt1), PKB-beta (or Akt2), and PKB-gamma (or Akt3). PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. It is activated downstream of phosphoinositide 3-kinase (PI3K) and plays important roles in diverse cellular functions including cell survival, growth, proliferation, angiogenesis, motility, and migration. PKB also has a central role in a variety of human cancers, having been implicated in tumor initiation, progression, and metastasis. The PKB subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and PI3K.


Pssm-ID: 270723 [Multi-domain]  Cd Length: 322  Bit Score: 71.62  E-value: 4.61e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  728 KTLGEGEFGKVVKAtafhlKGRAGYTTVAVKMLKENA--SPSELRDLLSEFNVLKQVNHPHVIKL-YGACSQDgPLLLIV 804
Cdd:cd05571    1 KVLGKGTFGKVILC-----REKATGELYAIKILKKEViiAKDEVAHTLTENRVLQNTRHPFLTSLkYSFQTND-RLCFVM 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  805 EYAKYGSLRGFLRESRKVGpgylgsggsrnsssldhpDERALTMGDLISFAwqisqgMQYLAEMKLVHRDLAARNILVAE 884
Cdd:cd05571   75 EYVNGGELFFHLSRERVFS------------------EDRTRFYGAEIVLA------LGYLHSQGIVYRDLKLENLLLDK 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  885 GRKMKISDFGLSRdvyEEDSY--VKRSQGRIPvKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTlGGNPYPGIPPERLFN 962
Cdd:cd05571  131 DGHIKITDFGLCK---EEISYgaTTKTFCGTP-EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPFYNRDHEVLFE 205
                        250       260       270
                 ....*....|....*....|....*....|...
gi 10862703  963 LLKTGhRMERPDNCSEEMYRLMLQCWKQEPDKR 995
Cdd:cd05571  206 LILME-EVRFPSTLSPEAKSLLAGLLKKDPKKR 237
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
730-982 4.71e-13

Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-1 is expressed ubiquitously and is localized in the cytoplasm. Its kinase activity is cell cycle dependent and peaks at the S and G2 phases. PCTAIRE-1 is highly expressed in the brain and may play a role in regulating neurite outgrowth. It can also associate with Trap (Tudor repeat associator with PCTAIRE-2), a physiological partner of PCTAIRE-2; with p11, a small dimeric protein with similarity to S100; and with 14-3-3 proteins, mediators of phosphorylation-dependent interactions in many different proteins. PCTAIRE-1 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PCTAIRE-1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270854 [Multi-domain]  Cd Length: 297  Bit Score: 71.19  E-value: 4.71e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  730 LGEGEFGKVvkatafhLKGRAGYTT--VAVKMLK----ENASPSELRdllsEFNVLKQVNHPHVIKLYGACSQDGPLLLI 803
Cdd:cd07873   10 LGEGTYATV-------YKGRSKLTDnlVALKEIRleheEGAPCTAIR----EVSLLKDLKHANIVTLHDIIHTEKSLTLV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  804 VEYAKyGSLRGFLRESRKVgpgylgsggsrnsssldhpderaLTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNILVA 883
Cdd:cd07873   79 FEYLD-KDLKQYLDDCGNS-----------------------INMHNVKLFLFQLLRGLAYCHRRKVLHRDLKPQNLLIN 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  884 EGRKMKISDFGLSRdvyEEDSYVKRSQGRIPVKWMAIESLF--DHIYTTQSDVWSFGVLLWEIVTlgGNP-YPGIPPER- 959
Cdd:cd07873  135 ERGELKLADFGLAR---AKSIPTKTYSNEVVTLWYRPPDILlgSTDYSTQIDMWGVGCIFYEMST--GRPlFPGSTVEEq 209
                        250       260
                 ....*....|....*....|....*.
gi 10862703  960 ---LFNLLKTGHRMERPDNCSEEMYR 982
Cdd:cd07873  210 lhfIFRILGTPTEETWPGILSNEEFK 235
PK_GC-2D cd14043
Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-2D; The pseudokinase domain ...
762-1001 5.01e-13

Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-2D; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. GC-2D is allso called Retinal Guanylyl Cyclase 1 (RETGC-1) or Rod Outer Segment membrane Guanylate Cyclase (ROS-GC). It is found in the photoreceptors of the retina where it anchors the reciprocal feedback loop between calcium and cGMP, which regulates the dark, light, and recovery phases in phototransduction. It is also found in other sensory neurons and may be a universal transduction component that plays a role in the perception of all senses. Membrane (or particulate) GCs consist of an extracellular ligand-binding domain, a single transmembrane region, and an intracellular tail that contains a PK-like domain, an amphiphatic region and a catalytic GC domain that catalyzes the conversion of GTP into cGMP and pyrophosphate. Membrane GCs act as receptors that transduce an extracellular signal to the intracellular production of cGMP, which has been implicated in many processes including cell proliferation, phototransduction, and muscle contractility, through its downstream effectors such as PKG. The PK-like domain of GCs functions as a negative regulator of the catalytic GC domain and may also act as a docking site for interacting proteins such as GC-activating proteins. The GC-2D subfamily is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270945 [Multi-domain]  Cd Length: 267  Bit Score: 70.51  E-value: 5.01e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  762 ENASPSELR-DLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVEYAKYGSLRGFLRESrkvgpgylgsggsrnSSSLDH 840
Cdd:cd14043   32 PGGSHTELRpSTKNVFSKLRELRHENVNLFLGLFVDCGILAIVSEHCSRGSLEDLLRND---------------DMKLDW 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  841 PDERALTMgDLIsfawqisQGMQYLAEMKLVHRDLAARNILVaEGR-KMKISDFGLSRDVYEEDSYVKRSQGRiPVKWMA 919
Cdd:cd14043   97 MFKSSLLL-DLI-------KGMRYLHHRGIVHGRLKSRNCVV-DGRfVLKITDYGYNEILEAQNLPLPEPAPE-ELLWTA 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  920 IESLFD----HIYTTQSDVWSFGVLLWEIVTLGGnPYP--GIPPERLFNLLKTGHRMERP----DNCSEEMYRLMLQCWK 989
Cdd:cd14043  167 PELLRDprleRRGTFPGDVFSFAIIMQEVIVRGA-PYCmlGLSPEEIIEKVRSPPPLCRPsvsmDQAPLECIQLMKQCWS 245
                        250
                 ....*....|..
gi 10862703  990 QEPDKRPVFADI 1001
Cdd:cd14043  246 EAPERRPTFDQI 257
STKc_ACVR2 cd14053
Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the ...
733-995 5.04e-13

Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ACVR2 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins (BMPs), activins, growth and differentiation factors (GDFs), and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. Type II receptors, such as ACVR2, are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. ACVR2 acts primarily as the receptors for activins, nodal, myostatin, GDF11, and a subset of BMPs. ACVR2 signaling impacts many cellular and physiological processes including reproductive and gonadal functions, myogenesis, bone remodeling and tooth development, kidney organogenesis, apoptosis, fibrosis, inflammation, and neurogenesis. Vertebrates contain two ACVR2 proteins, ACVR2a (or ActRIIA) and ACVR2b (or ActRIIB). The ACVR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270955 [Multi-domain]  Cd Length: 290  Bit Score: 70.82  E-value: 5.04e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  733 GEFGKVVKATafhlkgragYT--TVAVKM--LKENASPSELRDLLSEFNVlkqvNHPHVIKLYGA----CSQDGPLLLIV 804
Cdd:cd14053    6 GRFGAVWKAQ---------YLnrLVAVKIfpLQEKQSWLTEREIYSLPGM----KHENILQFIGAekhgESLEAEYWLIT 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  805 EYAKYGSLRGFLREsrkvgpgylgsggsrnsssldhpdeRALTMGDLISFAWQISQGMQYLAE----------MKLVHRD 874
Cdd:cd14053   73 EFHERGSLCDYLKG-------------------------NVISWNELCKIAESMARGLAYLHEdipatngghkPSIAHRD 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  875 LAARNILVAEGRKMKISDFGLSRdVYEEDSYVKRSQGRIPVK-WMAIESLFDHI-YTTQS----DVWSFGVLLWEIVTLG 948
Cdd:cd14053  128 FKSKNVLLKSDLTACIADFGLAL-KFEPGKSCGDTHGQVGTRrYMAPEVLEGAInFTRDAflriDMYAMGLVLWELLSRC 206
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 10862703  949 GNPyPGIPPERLFNLLKTG--------------HRMERPDNCSE--------EMYRLMLQCWKQEPDKR 995
Cdd:cd14053  207 SVH-DGPVDEYQLPFEEEVgqhptledmqecvvHKKLRPQIRDEwrkhpglaQLCETIEECWDHDAEAR 274
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
728-957 5.34e-13

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 71.55  E-value: 5.34e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703   728 KTLGEGEFGKVVKATAfhlkGRAGYTTVAVKMLKENA--SPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVE 805
Cdd:PTZ00426   36 RTLGTGSFGRVILATY----KNEDFPPVAIKRFEKSKiiKQKQVDHVFSERKILNYINHPFCVNLYGSFKDESYLYLVLE 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703   806 YAKYGSLRGFLRESRKVgpgylgsggsrnsssldhPDERALTmgdlisFAWQISQGMQYLAEMKLVHRDLAARNILVAEG 885
Cdd:PTZ00426  112 FVIGGEFFTFLRRNKRF------------------PNDVGCF------YAAQIVLIFEYLQSLNIVYRDLKPENLLLDKD 167
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 10862703   886 RKMKISDFGLSRdVYEEDSYVKRSQGripvKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTlggnpypGIPP 957
Cdd:PTZ00426  168 GFIKMTDFGFAK-VVDTRTYTLCGTP----EYIAPEILLNVGHGKAADWWTLGIFIYEILV-------GCPP 227
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
726-942 5.63e-13

Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK3 has been reported to be expressed in the interstitial Leydig cells of adult testis. Its mRNA levels is low at birth, increases at puberty, and remains high throughout adulthood. The TSSK3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271065 [Multi-domain]  Cd Length: 257  Bit Score: 70.40  E-value: 5.63e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  726 LGKTLGEGEFGKVVKatAFHLKGRagyTTVAVKMLKENASPSEL--RDLLSEFNVLKQVNHPHVIKLYGAC-SQDGPLLL 802
Cdd:cd14163    4 LGKTIGEGTYSKVKE--AFSKKHQ---RKVAIKIIDKSGGPEEFiqRFLPRELQIVERLDHKNIIHVYEMLeSADGKIYL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  803 IVEYAKYGSLRGFLRESrkvGPgylgsggsrnsssldHPDERALTMgdlisfAWQISQGMQYLAEMKLVHRDLAARNILV 882
Cdd:cd14163   79 VMELAEDGDVFDCVLHG---GP---------------LPEHRAKAL------FRQLVEAIRYCHGCGVAHRDLKCENALL 134
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 10862703  883 aEGRKMKISDFGLSRDVYEEDSYVKRSQGRiPVKWMAIESL--FDHiYTTQSDVWSFGVLLW 942
Cdd:cd14163  135 -QGFTLKLTDFGFAKQLPKGGRELSQTFCG-STAYAAPEVLqgVPH-DSRKGDIWSMGVVLY 193
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
726-949 5.69e-13

Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein kinase subfamily 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The SnRKs form three different subfamilies designated SnRK1-3. SnRK3 is represented in this cd. The SnRK3 group contains members also known as CBL-interacting protein kinase, salt overly sensitive 2, SOS3-interacting proteins and protein kinase S. These kinases interact with calcium-binding proteins such as SOS3, SCaBPs, and CBL proteins, and are involved in responses to salt stress and in sugar and ABA signaling. The SnRKs belong to a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271133 [Multi-domain]  Cd Length: 256  Bit Score: 70.13  E-value: 5.69e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  726 LGKTLGEGEFGKVvkataFHLKGRAGYTTVAVKML-KENASPSELRDLLS-EFNVLKQVNHPHVIKLYGACSQDGPLLLI 803
Cdd:cd14663    4 LGRTLGEGTFAKV-----KFARNTKTGESVAIKIIdKEQVAREGMVEQIKrEIAIMKLLRHPNIVELHEVMATKTKIFFV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  804 VEYAKYGSLrgFlreSRKVGPGYLgsggsrnsssldhPDERALTMgdlisFAwQISQGMQYLAEMKLVHRDLAARNILVA 883
Cdd:cd14663   79 MELVTGGEL--F---SKIAKNGRL-------------KEDKARKY-----FQ-QLIDAVDYCHSRGVFHRDLKPENLLLD 134
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 10862703  884 EGRKMKISDFGLS--RDVYEEDSYVKRSQGrIPvKWMAIESLFDHIYT-TQSDVWSFGVLLWeiVTLGG 949
Cdd:cd14663  135 EDGNLKISDFGLSalSEQFRQDGLLHTTCG-TP-NYVAPEVLARRGYDgAKADIWSCGVILF--VLLAG 199
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
775-1001 6.32e-13

Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMP-activated protein kinase (AMPK). CaMKK2, also called CaMKK beta, is one of the most versatile CaMKs. It is involved in regulating energy balance, glucose metabolism, adiposity, hematopoiesis, inflammation, and cancer. CaMKK2 contains unique N- and C-terminal domains and a central catalytic kinase domain that is followed by a regulatory domain that bears overlapping autoinhibitory and CaM-binding regions. It can be activated by signaling through G-coupled receptors, IP3 receptors, plasma membrane ion channels, and Toll-like receptors. Thus, CaMKK2 acts as a molecular hub that is capable of receiving and decoding signals from diverse pathways. The CaMKK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271101 [Multi-domain]  Cd Length: 286  Bit Score: 70.76  E-value: 6.32e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  775 EFNVLKQVNHPHVIKLYGACsqDGP----LLLIVEYAKYGSLrgflresrkvgpgylgsggsrnsssLDHPDERALTMgD 850
Cdd:cd14199   75 EIAILKKLDHPNVVKLVEVL--DDPsedhLYMVFELVKQGPV-------------------------MEVPTLKPLSE-D 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  851 LISFAWQ-ISQGMQYLAEMKLVHRDLAARNILVAEGRKMKISDFGLSRDVYEEDSYVKRSQGrIPVkWMAIESLFD--HI 927
Cdd:cd14199  127 QARFYFQdLIKGIEYLHYQKIIHRDVKPSNLLVGEDGHIKIADFGVSNEFEGSDALLTNTVG-TPA-FMAPETLSEtrKI 204
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  928 YTTQS-DVWSFGVLLWEIVtLGGNPYPGippERLFNL---LKTgHRMERPD--NCSEEMYRLMLQCWKQEPDKRPVFADI 1001
Cdd:cd14199  205 FSGKAlDVWAMGVTLYCFV-FGQCPFMD---ERILSLhskIKT-QPLEFPDqpDISDDLKDLLFRMLDKNPESRISVPEI 279
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
730-944 8.90e-13

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK4 partners with all three D-type cyclins (D1, D2, and D3) and is also regulated by INK4 inhibitors. It is active towards the retinoblastoma (pRb) protein and plays a role in regulating the early G1 phase of the cell cycle. It is expressed ubiquitously and is localized in the nucleus. CDK4 also shows kinase activity towards Smad3, a signal transducer of TGF-beta signaling which modulates transcription and plays a role in cell proliferation and apoptosis. CDK4 is inhibited by the p21 inhibitor and is specifically mutated in human melanoma. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143368 [Multi-domain]  Cd Length: 288  Bit Score: 70.38  E-value: 8.90e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  730 LGEGEFGKVVKATAFHLKGRAGYTTVAVKMLKENASPSELRDLlSEFNVLKQVNHPHVIKLYGACS-----QDGPLLLIV 804
Cdd:cd07863    8 IGVGAYGTVYKARDPHSGHFVALKSVRVQTNEDGLPLSTVREV-ALLKRLEAFDHPNIVRLMDVCAtsrtdRETKVTLVF 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  805 EYAKYgSLRGFLResrKVGPgylgsggsrnsssldhPDERALTMGDLISfawQISQGMQYLAEMKLVHRDLAARNILVAE 884
Cdd:cd07863   87 EHVDQ-DLRTYLD---KVPP----------------PGLPAETIKDLMR---QFLRGLDFLHANCIVHRDLKPENILVTS 143
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 10862703  885 GRKMKISDFGLSRdVYeedSYVKRSQGRIPVKWM-AIESLFDHIYTTQSDVWSFGVLLWEI 944
Cdd:cd07863  144 GGQVKLADFGLAR-IY---SCQMALTPVVVTLWYrAPEVLLQSTYATPVDMWSVGCIFAEM 200
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
730-982 9.21e-13

Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-2 is specifically expressed in neurons in the central nervous system, mainly in terminally differentiated neurons. It associates with Trap (Tudor repeat associator with PCTAIRE-2) and could play a role in regulating mitochondrial function in neurons. PCTAIRE-2 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PCTAIRE-2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143377 [Multi-domain]  Cd Length: 309  Bit Score: 70.41  E-value: 9.21e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  730 LGEGEFgkvvkATAFhlKGRAGYTT--VAVKMLK----ENASPSELRdllsEFNVLKQVNHPHVIKLYGACSQDGPLLLI 803
Cdd:cd07872   14 LGEGTY-----ATVF--KGRSKLTEnlVALKEIRleheEGAPCTAIR----EVSLLKDLKHANIVTLHDIVHTDKSLTLV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  804 VEYAKyGSLRGFLRESRKVgpgylgsggsrnsssldhpderaLTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNILVA 883
Cdd:cd07872   83 FEYLD-KDLKQYMDDCGNI-----------------------MSMHNVKIFLYQILRGLAYCHRRKVLHRDLKPQNLLIN 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  884 EGRKMKISDFGLSRdvyEEDSYVKRSQGRIPVKWMAIESLF--DHIYTTQSDVWSFGVLLWEIVTlgGNP-YPGIPPER- 959
Cdd:cd07872  139 ERGELKLADFGLAR---AKSVPTKTYSNEVVTLWYRPPDVLlgSSEYSTQIDMWGVGCIFFEMAS--GRPlFPGSTVEDe 213
                        250       260
                 ....*....|....*....|....*.
gi 10862703  960 ---LFNLLKTGHRMERPDNCSEEMYR 982
Cdd:cd07872  214 lhlIFRLLGTPTEETWPGISSNDEFK 239
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
668-996 1.04e-12

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 71.97  E-value: 1.04e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703   668 PISSAEMTFRRPAQAFP-VSYSSSGARRPSLDSMENQV---SVDAFKILEDPKWEFPRKNLVLGKTLgegeFGKVVKATA 743
Cdd:PTZ00267    8 HGSASAELLNQYAKYFPhVLFTSEEAFEKYCADLDPEAykkCVDLPEGEEVPESNNPREHMYVLTTL----VGRNPTTAA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703   744 F-HLKGRAGYTTVAVK--MLKENASPSELRdllSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVEYAKYGSLRGFLRESR 820
Cdd:PTZ00267   84 FvATRGSDPKEKVVAKfvMLNDERQAAYAR---SELHCLAACDHFGIVKHFDDFKSDDKLLLIMEYGSGGDLNKQIKQRL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703   821 KvgpgylgsggsrnssslDHPDERALTMGDLIsfaWQISQGMQYLAEMKLVHRDLAARNILVAEGRKMKISDFGLSRDVY 900
Cdd:PTZ00267  161 K-----------------EHLPFQEYEVGLLF---YQIVLALDEVHSRKMMHRDLKSANIFLMPTGIIKLGDFGFSKQYS 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703   901 EEDSY-VKRSQGRIPVkWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLgGNPYPGIPPERLFNLLKTGHRMERPDNCSEE 979
Cdd:PTZ00267  221 DSVSLdVASSFCGTPY-YLAPELWERKRYSKKADMWSLGVILYELLTL-HRPFKGPSQREIMQQVLYGKYDPFPCPVSSG 298
                         330
                  ....*....|....*..
gi 10862703   980 MYRLMLQCWKQEPDKRP 996
Cdd:PTZ00267  299 MKALLDPLLSKNPALRP 315
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
728-954 1.19e-12

The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related Apoptosis-inducing protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DRAKs were named based on their similarity (around 50% identity) to the kinase domain of DAPKs. They contain an N-terminal kinase domain and a C-terminal regulatory domain. Vertebrates contain two subfamily members, DRAK1 and DRAK2 (also called STK17B). Both DRAKs are localized to the nucleus, autophosphorylate themselves, and phosphorylate myosin light chain as a substrate. DRAK2 has been implicated in inducing or enhancing apoptosis in beta cells, fibroblasts, and lymphoid cells, where it is highly expressed. It is involved in regulating many immune processes including the germinal center (GC) reaction, responses to thymus-dependent antigens, activated T cell survival, memory T cell responses. It may be involved in the development of autoimmunity. The DRAK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271100 [Multi-domain]  Cd Length: 270  Bit Score: 69.57  E-value: 1.19e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  728 KTLGEGEFGKVVKATAfhlkgRAGYTTVAVKMLKENASPSELR-DLLSEFNVLKQV-NHPHVIKLYGACSQDGPLLLIVE 805
Cdd:cd14198   14 KELGRGKFAVVRQCIS-----KSTGQEYAAKFLKKRRRGQDCRaEILHEIAVLELAkSNPRVVNLHEVYETTSEIILILE 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  806 YAKYGSLrgflresrkvgpgylgsggsrnsSSLDHPDERA-LTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNILVAE 884
Cdd:cd14198   89 YAAGGEI-----------------------FNLCVPDLAEmVSENDIIRLIRQILEGVYYLHQNNIVHLDLKPQNILLSS 145
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 10862703  885 GRKM---KISDFGLSRDVyEEDSYVKRSQGriPVKWMAIESL-FDHIyTTQSDVWSFGVLLWEIVTlGGNPYPG 954
Cdd:cd14198  146 IYPLgdiKIVDFGMSRKI-GHACELREIMG--TPEYLAPEILnYDPI-TTATDMWNIGVIAYMLLT-HESPFVG 214
PKc_TOPK cd14001
Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer ...
756-947 1.20e-12

Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer T-cell-originated protein kinase; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TOPK, also called PDZ-binding kinase (PBK), is activated at the early stage of mitosis and plays a critical role in cytokinesis. It partly functions as a mitogen-activated protein kinase (MAPK) kinase and is capable of phosphorylating p38, JNK1, and ERK2. TOPK also plays a role in DNA damage sensing and repair through its phosphorylation of histone H2AX. It contributes to cancer development and progression by downregulating the function of tumor suppressor p53 and reducing cell-cycle regulatory proteins. TOPK is found highly expressed in breast and skin cancer cells. The TOPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270903 [Multi-domain]  Cd Length: 292  Bit Score: 69.74  E-value: 1.20e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  756 AVKMLKENASPSELRD----LLSEFNVLKQVNHPHVIKLYG-ACSQDGPLLLIVEYAKyGSLRGFLRESRKVGPGylgsg 830
Cdd:cd14001   32 AVKKINSKCDKGQRSLyqerLKEEAKILKSLNHPNIVGFRAfTKSEDGSLCLAMEYGG-KSLNDLIEERYEAGLG----- 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  831 gsrnsssldhpderALTMGDLISFAWQISQGMQYL-AEMKLVHRDLAARNILV-AEGRKMKISDFGLSRDVYE------- 901
Cdd:cd14001  106 --------------PFPAATILKVALSIARALEYLhNEKKILHGDIKSGNVLIkGDFESVKLCDFGVSLPLTEnlevdsd 171
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 10862703  902 -EDSYVkrsqGRIPvkWMAIESLF-DHIYTTQSDVWSFGVLLWEIVTL 947
Cdd:cd14001  172 pKAQYV----GTEP--WKAKEALEeGGVITDKADIFAYGLVLWEMMTL 213
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
728-1043 1.40e-12

Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGK3 (also called cytokine-independent survival kinase or CISK) is expressed in most tissues and is most abundant in the embryo and adult heart and spleen. It was originally discovered in a screen for antiapoptotic genes. It phosphorylates and inhibits the proapoptotic proteins, Bad and FKHRL1. SGK3 also regulates many transporters, ion channels, and receptors. It plays a critical role in hair follicle morphogenesis and hair cycling. The SGK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270755 [Multi-domain]  Cd Length: 326  Bit Score: 69.99  E-value: 1.40e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  728 KTLGEGEFGKVVKAtafhlKGRAGYTTVAVKMLKENA--SPSELRDLLSEFNVL-KQVNHPHVIKLYGACSQDGPLLLIV 804
Cdd:cd05604    2 KVIGKGSFGKVLLA-----KRKRDGKYYAVKVLQKKVilNRKEQKHIMAERNVLlKNVKHPFLVGLHYSFQTTDKLYFVL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  805 EYAKYGSLRGFLRESRKVgpgylgsggsrnsssldhPDERALTmgdlisFAWQISQGMQYLAEMKLVHRDLAARNILVAE 884
Cdd:cd05604   77 DFVNGGELFFHLQRERSF------------------PEPRARF------YAAEIASALGYLHSINIVYRDLKPENILLDS 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  885 GRKMKISDFGLSRDVYEEDSYVKRSQGrIPvKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTlggnpypGIPP------- 957
Cdd:cd05604  133 QGHIVLTDFGLCKEGISNSDTTTTFCG-TP-EYLAPEVIRKQPYDNTVDWWCLGSVLYEMLY-------GLPPfycrdta 203
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  958 ERLFNLLKTGHRMeRPDnCSEEMYRLMLQCWKQEPDKR-------------PVFADIS-KDLEKMmvKRRDYLDLAASTP 1023
Cdd:cd05604  204 EMYENILHKPLVL-RPG-ISLTAWSILEELLEKDRQLRlgakedfleiknhPFFESINwTDLVQK--KIPPPFNPNVNGP 279
                        330       340
                 ....*....|....*....|
gi 10862703 1024 SDSLIYDDGLSEEETPLVDC 1043
Cdd:cd05604  280 DDISNFDAEFTEEMVPYSVC 299
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
730-962 1.74e-12

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKN has a C-terminal catalytic domain that is highly homologous to PKCs. Its unique N-terminal regulatory region contains antiparallel coiled-coil (ACC) domains. In mammals, there are three PKN isoforms from different genes (designated PKN-alpha, beta, and gamma), which show different enzymatic properties, tissue distribution, and varied functions. PKN can be activated by the small GTPase Rho, and by fatty acids such as arachidonic and linoleic acids. It is involved in many biological processes including cytokeletal regulation, cell adhesion, vesicle transport, glucose transport, regulation of meiotic maturation and embryonic cell cycles, signaling to the nucleus, and tumorigenesis. The PKN subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270741 [Multi-domain]  Cd Length: 326  Bit Score: 70.02  E-value: 1.74e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  730 LGEGEFGKVVKAtafHLKGRAGYttVAVKMLKEN--ASPSELRDLLSE---FNVLKQVNHPHVIKLYGACSQDGPLLLIV 804
Cdd:cd05589    7 LGRGHFGKVLLA---EYKPTGEL--FAIKALKKGdiIARDEVESLMCEkriFETVNSARHPFLVNLFACFQTPEHVCFVM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  805 EYAKYGSLRGFLRESRkvgpgylgsggsrnsssldHPDERAltmgdlISFAWQISQGMQYLAEMKLVHRDLAARNILV-A 883
Cdd:cd05589   82 EYAAGGDLMMHIHEDV-------------------FSEPRA------VFYAACVVLGLQFLHEHKIVYRDLKLDNLLLdT 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  884 EGRkMKISDFGLSRdvyEEDSYVKRSQ---GrIPvKWMAIESLFDHIYTTQSDVWSFGVLLWEIVtLGGNPYPGIPPERL 960
Cdd:cd05589  137 EGY-VKIADFGLCK---EGMGFGDRTStfcG-TP-EFLAPEVLTDTSYTRAVDWWGLGVLIYEML-VGESPFPGDDEEEV 209

                 ..
gi 10862703  961 FN 962
Cdd:cd05589  210 FD 211
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
730-946 2.04e-12

Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK2 is regulated by cyclin E or cyclin A. Upon activation by cyclin E, it phosphorylates the retinoblastoma (pRb) protein which activates E2F mediated transcription and allows cells to move into S phase. The CDK2/cyclin A complex plays a role in regulating DNA replication. CDK2, together with CDK4, also regulates embryonic cell proliferation. Despite these important roles, mice deleted for the cdk2 gene are viable and normal except for being sterile. This may be due to compensation provided by CDK1 (also called Cdc2), which can also bind cyclin E and drive the G1 to S phase transition. CDK3 is regulated by cyclin C and it phosphorylates pRB specifically during the G0/G1 transition. This phosphorylation is required for cells to exit G0 efficiently and enter the G1 phase. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK2/3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270844 [Multi-domain]  Cd Length: 284  Bit Score: 69.07  E-value: 2.04e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  730 LGEGEFGKVVKAtafhlKGRAGYTTVAVKMLKENAS----PSELrdlLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVE 805
Cdd:cd07860    8 IGEGTYGVVYKA-----RNKLTGEVVALKKIRLDTEtegvPSTA---IREISLLKELNHPNIVKLLDVIHTENKLYLVFE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  806 YAKYgSLRGFLRESRKVGpgylgsggsrnsssldhpderaLTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNILVAEG 885
Cdd:cd07860   80 FLHQ-DLKKFMDASALTG----------------------IPLPLIKSYLFQLLQGLAFCHSHRVLHRDLKPQNLLINTE 136
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 10862703  886 RKMKISDFGLSRDVyeedsyvkrsqgRIPVK----------WMAIESLFD-HIYTTQSDVWSFGVLLWEIVT 946
Cdd:cd07860  137 GAIKLADFGLARAF------------GVPVRtythevvtlwYRAPEILLGcKYYSTAVDIWSLGCIFAEMVT 196
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
723-1001 2.10e-12

Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of uncharacterized proteins with similarity to MEKK3, MEKK2, and related proteins; they contain an N-terminal PB1 domain, which mediates oligomerization, and a C-terminal catalytic domain. MEKK2 and MEKK3 are MAPK kinase kinases (MAPKKKs or MKKKs), proteins that phosphorylate and activate MAPK kinases (MAPKKs or MKKs), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MEKK2 and MEKK3 activate MEK5 (also called MKK5), which activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK3 plays an essential role in embryonic angiogenesis and early heart development. MEKK2 and MEKK3 can also activate the MAPKs, c-Jun N-terminal kinase (JNK) and p38, through their respective MAPKKs. The MEKK3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270819 [Multi-domain]  Cd Length: 264  Bit Score: 68.51  E-value: 2.10e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  723 NLVLGKTLGEGEFGKVVKATAFHlKGRAgyttVAVKML----KENASPSELRDLLSEFNVLKQVNHPHVIKLYGaCSQD- 797
Cdd:cd06653    3 NWRLGKLLGRGAFGEVYLCYDAD-TGRE----LAVKQVpfdpDSQETSKEVNALECEIQLLKNLRHDRIVQYYG-CLRDp 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  798 --GPLLLIVEYAKYGSLRGFLRESRkvgpgylgsggsrnsssldhpderALTMGDLISFAWQISQGMQYLAEMKLVHRDL 875
Cdd:cd06653   77 eeKKLSIFVEYMPGGSVKDQLKAYG------------------------ALTENVTRRYTRQILQGVSYLHSNMIVHRDI 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  876 AARNILVAEGRKMKISDFGLSR---DVYEEDSYVKRSQGrIPVkWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLGgnpy 952
Cdd:cd06653  133 KGANILRDSAGNVKLGDFGASKriqTICMSGTGIKSVTG-TPY-WMSPEVISGEGYGRKADVWSVACTVVEMLTEK---- 206
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 10862703  953 pgiPP-------ERLFNLLKTGHRMERPDNCSEEMYRLMLQCWKQEpDKRPVFADI 1001
Cdd:cd06653  207 ---PPwaeyeamAAIFKIATQPTKPQLPDGVSDACRDFLRQIFVEE-KRRPTAEFL 258
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
730-944 2.17e-12

Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TLKs play important functions during the cell cycle and are implicated in chromatin remodeling, DNA replication and repair, and mitosis. They phosphorylate and regulate Anti-silencing function 1 protein (Asf1), a histone H3/H4 chaperone that helps facilitate the assembly of chromatin following DNA replication during S phase. TLKs also phosphorylate the H3 histone tail and are essential in transcription. Vertebrates contain two subfamily members, TLK1 and TLK2. The TLK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270892 [Multi-domain]  Cd Length: 279  Bit Score: 68.88  E-value: 2.17e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  730 LGEGEFGKVVKAtaFHLKGragYTTVAVKMLKENASPSE------LRDLLSEFNVLKQVNHPHVIKLYGACSQD-GPLLL 802
Cdd:cd13990    8 LGKGGFSEVYKA--FDLVE---QRYVACKIHQLNKDWSEekkqnyIKHALREYEIHKSLDHPRIVKLYDVFEIDtDSFCT 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  803 IVEYAKYGSLRGFLRESRKVgpgylgsggsrnsssldhPDERAltmgdlISFAWQISQGMQYLAEMK--LVHRDLAARNI 880
Cdd:cd13990   83 VLEYCDGNDLDFYLKQHKSI------------------PEREA------RSIIMQVVSALKYLNEIKppIIHYDLKPGNI 138
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 10862703  881 LVAEGRK---MKISDFGLSRdVYEEDSYVK-----RSQGRIPVkWMAIESLFDH-----IYTTQSDVWSFGVLLWEI 944
Cdd:cd13990  139 LLHSGNVsgeIKITDFGLSK-IMDDESYNSdgmelTSQGAGTY-WYLPPECFVVgktppKISSKVDVWSVGVIFYQM 213
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
772-951 2.37e-12

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ULK4 is a functionally uncharacterized kinase that shows similarity to ATG1/ULKs. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. The ULK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270912 [Multi-domain]  Cd Length: 269  Bit Score: 68.47  E-value: 2.37e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  772 LLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVEYAKYGSLRGFLRESRKvgpgylgsggsrnsssldhpderaLTMGDL 851
Cdd:cd14010   41 VLNEVRLTHELKHPNVLKFYEWYETSNHLWLVVEYCTGGDLETLLRQDGN------------------------LPESSV 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  852 ISFAWQISQGMQYLAEMKLVHRDLAARNILVAEGRKMKISDFGLSR-----------DVYEEDSYVKRSQGRIPV---KW 917
Cdd:cd14010   97 RKFGRDLVRGLHYIHSKGIIYCDLKPSNILLDGNGTLKLSDFGLARregeilkelfgQFSDEGNVNKVSKKQAKRgtpYY 176
                        170       180       190
                 ....*....|....*....|....*....|....
gi 10862703  918 MAIESLFDHIYTTQSDVWSFGVLLWEIVTlgGNP 951
Cdd:cd14010  177 MAPELFQGGVHSFASDLWALGCVLYEMFT--GKP 208
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
712-1017 2.54e-12

Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TNIK is an effector of Rap2, a small GTP-binding protein from the Ras family. TNIK specifically activates the c-Jun N-terminal kinase (JNK) pathway and plays a role in regulating the actin cytoskeleton. The TNIK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270807 [Multi-domain]  Cd Length: 296  Bit Score: 68.98  E-value: 2.54e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  712 LEDPKWEFPRKNLVlgktlGEGEFGKVVKATafHLKGRagyTTVAVKMLkeNASPSELRDLLSEFNVLKQVNH-PHVIKL 790
Cdd:cd06637    1 LRDPAGIFELVELV-----GNGTYGQVYKGR--HVKTG---QLAAIKVM--DVTGDEEEEIKQEINMLKKYSHhRNIATY 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  791 YGACSQDGP------LLLIVEYAKYGSLRGFLRESRkvgpgylgsggsrnsssldhpderaltmGDLISFAW------QI 858
Cdd:cd06637   69 YGAFIKKNPpgmddqLWLVMEFCGAGSVTDLIKNTK----------------------------GNTLKEEWiayicrEI 120
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  859 SQGMQYLAEMKLVHRDLAARNILVAEGRKMKISDFGLSRDVyeeDSYVKRSQGRIPVK-WMAIESLF-----DHIYTTQS 932
Cdd:cd06637  121 LRGLSHLHQHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQL---DRTVGRRNTFIGTPyWMAPEVIAcdenpDATYDFKS 197
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  933 DVWSFGVLLWEIVTlGGNPYPGIPPER-LFNLLKTGHRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADISK-------- 1003
Cdd:cd06637  198 DLWSLGITAIEMAE-GAPPLCDMHPMRaLFLIPRNPAPRLKSKKWSKKFQSFIESCLVKNHSQRPSTEQLMKhpfirdqp 276
                        330
                 ....*....|....
gi 10862703 1004 DLEKMMVKRRDYLD 1017
Cdd:cd06637  277 NERQVRIQLKDHID 290
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
725-996 2.83e-12

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek4 is highly abundant in the testis. Its specific function is unknown. Neks are involved in the regulation of downstream processes following the activation of Cdc2, and many of their functions are cell cycle-related. They play critical roles in microtubule dynamics during ciliogenesis and mitosis. Nek4 is one in a family of 11 different Neks (Nek1-11). The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270862 [Multi-domain]  Cd Length: 257  Bit Score: 68.23  E-value: 2.83e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  725 VLGKTLGEGEFGKV--VKatafHLKGRAGYttVAVKMLKENASPSELRDLLSEFNVLKQVNHPHVIKlYGACSQ--DGPL 800
Cdd:cd08223    3 QFLRVIGKGSYGEVwlVR----HKRDRKQY--VIKKLNLKNASKRERKAAEQEAKLLSKLKHPNIVS-YKESFEgeDGFL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  801 LLIVEYAKYGSLRGFLRESRkvgpGYLGsggsrnsssldhpDERaltmgDLISFAWQISQGMQYLAEMKLVHRDLAARNI 880
Cdd:cd08223   76 YIVMGFCEGGDLYTRLKEQK----GVLL-------------EER-----QVVEWFVQIAMALQYMHERNILHRDLKTQNI 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  881 LVAEGRKMKISDFGLSRdVYEEDSYVKRSQGRIPVkWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLggnpypgippERL 960
Cdd:cd08223  134 FLTKSNIIKVGDLGIAR-VLESSSDMATTLIGTPY-YMSPELFSNKPYNHKSDVWALGCCVYEMATL----------KHA 201
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 10862703  961 FN----------LLKtGHRMERPDNCSEEMYRLMLQCWKQEPDKRP 996
Cdd:cd08223  202 FNakdmnslvykILE-GKLPPMPKQYSPELGELIKAMLHQDPEKRP 246
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
723-946 3.39e-12

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK2 is a MAPK kinase kinase (MAPKKK or MKKK), that phosphorylates and activates the MAPK kinase MEK5 (or MKK5), which in turn phosphorylates and activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK2 also activates ERK1/2, c-Jun N-terminal kinase (JNK) and p38 through their respective MAPKKs MEK1/2, JNK-activating kinase 2 (JNKK2), and MKK3/6. MEKK2 plays roles in T cell receptor signaling, immune synapse formation, cytokine gene expression, as well as in EGF and FGF receptor signaling. The MEKK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270818 [Multi-domain]  Cd Length: 264  Bit Score: 68.15  E-value: 3.39e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  723 NLVLGKTLGEGEFGKVVKATAFHlKGRAgyttVAVKMLKENA-SPS---ELRDLLSEFNVLKQVNHPHVIKLYGaCSQDG 798
Cdd:cd06652    3 NWRLGKLLGQGAFGRVYLCYDAD-TGRE----LAVKQVQFDPeSPEtskEVNALECEIQLLKNLLHERIVQYYG-CLRDP 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  799 P---LLLIVEYAKYGSLRGFLRESRkvgpgylgsggsrnsssldhpderALTMGDLISFAWQISQGMQYLAEMKLVHRDL 875
Cdd:cd06652   77 QertLSIFMEYMPGGSIKDQLKSYG------------------------ALTENVTRKYTRQILEGVHYLHSNMIVHRDI 132
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 10862703  876 AARNILVAEGRKMKISDFGLSRDVyeeDSYVKRSQGRIPVK----WMAIESLFDHIYTTQSDVWSFGVLLWEIVT 946
Cdd:cd06652  133 KGANILRDSVGNVKLGDFGASKRL---QTICLSGTGMKSVTgtpyWMSPEVISGEGYGRKADIWSVGCTVVEMLT 204
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
728-995 4.18e-12

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-delta plays a role in cell cycle regulation and programmed cell death in many cell types. It slows down cell proliferation, inducing cell cycle arrest and enhancing cell differentiation. PKC-delta is also involved in the regulation of transcription as well as immune and inflammatory responses. It plays a central role in the genotoxic stress response that leads to DNA damaged-induced apoptosis. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC-delta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173710 [Multi-domain]  Cd Length: 316  Bit Score: 68.43  E-value: 4.18e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  728 KTLGEGEFGKVVKAtafHLKGRAGYttVAVKMLKENAS--PSELRDLLSEFNVLKQV-NHPHVIKLYGACSQDGPLLLIV 804
Cdd:cd05620    1 KVLGKGSFGKVLLA---ELKGKGEY--FAVKALKKDVVliDDDVECTMVEKRVLALAwENPFLTHLYCTFQTKEHLFFVM 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  805 EYAKYGSLRGFLRESRKVgpgylgsggsrnsssldhpDERALTMgdlisFAWQISQGMQYLAEMKLVHRDLAARNILVAE 884
Cdd:cd05620   76 EFLNGGDLMFHIQDKGRF-------------------DLYRATF-----YAAEIVCGLQFLHSKGIIYRDLKLDNVMLDR 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  885 GRKMKISDFGLSRDVYEEDSYVKRSQGrIPvKWMAIESLFDHIYTTQSDVWSFGVLLWEIVtLGGNPYPGIPPERLFNLL 964
Cdd:cd05620  132 DGHIKIADFGMCKENVFGDNRASTFCG-TP-DYIAPEILQGLKYTFSVDWWSFGVLLYEML-IGQSPFHGDDEDELFESI 208
                        250       260       270
                 ....*....|....*....|....*....|...
gi 10862703  965 K--TGHrmeRPDNCSEEMYRLMLQCWKQEPDKR 995
Cdd:cd05620  209 RvdTPH---YPRWITKESKDILEKLFERDPTRR 238
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
746-1004 4.28e-12

Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMP-activated protein kinase (AMPK). Vertebrates contain two CaMKKs, CaMKK1 (or alpha) and CaMKK2 (or beta). CaMKK1 is involved in the regulation of glucose uptake in skeletal muscles. CaMKK2 is involved in regulating energy balance, glucose metabolism, adiposity, hematopoiesis, inflammation, and cancer. The CaMKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271020 [Multi-domain]  Cd Length: 275  Bit Score: 67.77  E-value: 4.28e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  746 LKGRAGYTTVAVKMlKENASPSELRDLLS----EFNVLKQVNHPHVIKLygacsqdgpllliVEyakygslrgflresrk 821
Cdd:cd14118   32 LLKQAGFFRRPPPR-RKPGALGKPLDPLDrvyrEIAILKKLDHPNVVKL-------------VE---------------- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  822 vgpgylgsggsrnssSLDHPDERALTM-------GDLISF----------AW----QISQGMQYLAEMKLVHRDLAARNI 880
Cdd:cd14118   82 ---------------VLDDPNEDNLYMvfelvdkGAVMEVptdnplseetARsyfrDIVLGIEYLHYQKIIHRDIKPSNL 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  881 LVAEGRKMKISDFGLSRDVYEEDSYVKRSQGrIPVkWMAIESLFD--HIYTTQS-DVWSFGVLLWEIVtLGGNPYPGIPP 957
Cdd:cd14118  147 LLGDDGHVKIADFGVSNEFEGDDALLSSTAG-TPA-FMAPEALSEsrKKFSGKAlDIWAMGVTLYCFV-FGRCPFEDDHI 223
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 10862703  958 ERLFNLLKTgHRMERPDNC--SEEMYRLMLQCWKQEPDKRPVFADISKD 1004
Cdd:cd14118  224 LGLHEKIKT-DPVVFPDDPvvSEQLKDLILRMLDKNPSERITLPEIKEH 271
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
726-996 4.30e-12

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK4, also called SAK or STK18, is structurally different from other PLKs in that it contains only one polo box that can form two adjacent polo boxes and a functional PDB by homodimerization. It is required for late mitotic progression, cell survival, and embryonic development. It localizes to centrosomes and is required for centriole duplication and chromosomal stability. Overexpression of PLK4 may be associated with colon tumors. The PLK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271088 [Multi-domain]  Cd Length: 256  Bit Score: 67.58  E-value: 4.30e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  726 LGKTLGEGEFGKVVKATAFHLkgragYTTVAVKMLKENA--SPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLI 803
Cdd:cd14186    5 VLNLLGKGSFACVYRARSLHT-----GLEVAIKMIDKKAmqKAGMVQRVRNEVEIHCQLKHPSILELYNYFEDSNYVYLV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  804 VEYAKYGSLRGFLRESRKvgpgylgsggsrnsssldhpderALTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNILVA 883
Cdd:cd14186   80 LEMCHNGEMSRYLKNRKK-----------------------PFTEDEARHFMHQIVTGMLYLHSHGILHRDLTLSNLLLT 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  884 EGRKMKISDFGLSRDVYEEDSYVKRSQGrIPvKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTlGGNPYPGIPPERLFNL 963
Cdd:cd14186  137 RNMNIKIADFGLATQLKMPHEKHFTMCG-TP-NYISPEIATRSAHGLESDVWSLGCMFYTLLV-GRPPFDTDTVKNTLNK 213
                        250       260       270
                 ....*....|....*....|....*....|...
gi 10862703  964 LKTGHrMERPDNCSEEMYRLMLQCWKQEPDKRP 996
Cdd:cd14186  214 VVLAD-YEMPAFLSREAQDLIHQLLRKNPADRL 245
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
721-940 5.49e-12

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270985 [Multi-domain]  Cd Length: 259  Bit Score: 67.40  E-value: 5.49e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  721 RKNLVLGKTLGEGEFGKVVKAtafhlKGRAGYTTVAVKMLKENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPL 800
Cdd:cd14083    2 RDKYEFKEVLGTGAFSEVVLA-----EDKATGKLVAIKCIDKKALKGKEDSLENEIAVLRKIKHPNIVQLLDIYESKSHL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  801 LLIVEYAKYGSLrgFlreSRKVGPGYLGsggsrnsssldhpdERALTmgDLISfawQISQGMQYLAEMKLVHRDLAARNI 880
Cdd:cd14083   77 YLVMELVTGGEL--F---DRIVEKGSYT--------------EKDAS--HLIR---QVLEAVDYLHSLGIVHRDLKPENL 132
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 10862703  881 LV---AEGRKMKISDFGLSRdvyEEDSYVKRSQGRIPvKWMAIESLFDHIYTTQSDVWSFGVL 940
Cdd:cd14083  133 LYyspDEDSKIMISDFGLSK---MEDSGVMSTACGTP-GYVAPEVLAQKPYGKAVDCWSIGVI 191
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
720-957 5.63e-12

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK5 is mainly expressed in the brain. It is not required for viability, but together with PAK6, it is required for normal levels of locomotion and activity, and for learning and memory. PAK5 cooperates with Inca (induced in neural crest by AP2) in the regulation of cell adhesion and cytoskeletal organization in the embryo and in neural crest cells during craniofacial development. PAK5 may also play a role in controlling the signaling of Raf-1, an effector of Ras, at the mitochondria. PAK5 belongs to the group II PAKs, which contain a PBD (p21-binding domain) and a C-terminal catalytic domain, but do not harbor an AID (autoinhibitory domain) or SH3 binding sites. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132989 [Multi-domain]  Cd Length: 292  Bit Score: 67.76  E-value: 5.63e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  720 PRKNLVLGKTLGEGEFGKVVKATAFHlKGRagytTVAVKmlKENASPSELRDLL-SEFNVLKQVNHPHVIKLYGACSQDG 798
Cdd:cd06658   20 PREYLDSFIKIGEGSTGIVCIATEKH-TGK----QVAVK--KMDLRKQQRRELLfNEVVIMRDYHHENVVDMYNSYLVGD 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  799 PLLLIVEYAKYGSLRGFLRESRkvgpgylgsggsrnsssldhpderaLTMGDLISFAWQISQGMQYLAEMKLVHRDLAAR 878
Cdd:cd06658   93 ELWVVMEFLEGGALTDIVTHTR-------------------------MNEEQIATVCLSVLRALSYLHNQGVIHRDIKSD 147
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 10862703  879 NILVAEGRKMKISDFGLSRDVYEEDSYVKRSQGrIPVkWMAIESLFDHIYTTQSDVWSFGVLLWEIVTlGGNPYPGIPP 957
Cdd:cd06658  148 SILLTSDGRIKLSDFGFCAQVSKEVPKRKSLVG-TPY-WMAPEVISRLPYGTEVDIWSLGIMVIEMID-GEPPYFNEPP 223
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
730-939 5.73e-12

Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAO proteins possess mitogen-activated protein kinase (MAPK) kinase kinase activity. They activate the MAPKs, p38 and c-Jun N-terminal kinase (JNK), by phosphorylating and activating the respective MAP/ERK kinases (MEKs, also known as MKKs or MAPKKs), MEK3/MEK6 and MKK4/MKK7. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. Vertebrates contain three TAO subfamily members, named TAO1, TAO2, and TAO3. The TAO subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270784 [Multi-domain]  Cd Length: 258  Bit Score: 67.09  E-value: 5.73e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  730 LGEGEFGKVVKATAFHLKgragyTTVAVKMLKENASPSELR--DLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVEYA 807
Cdd:cd06607    9 IGHGSFGAVYYARNKRTS-----EVVAIKKMSYSGKQSTEKwqDIIKEVKFLRQLRHPNTIEYKGCYLREHTAWLVMEYC 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  808 kYGSLRGFLRESRKvgpgylgsggsrnsssLDHPDE-RALTMGDLisfawqisQGMQYLAEMKLVHRDLAARNILVAEGR 886
Cdd:cd06607   84 -LGSASDIVEVHKK----------------PLQEVEiAAICHGAL--------QGLAYLHSHNRIHRDVKAGNILLTEPG 138
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 10862703  887 KMKISDFGLSRDVYEEDSYVKRSQgripvkWMAIE---SLFDHIYTTQSDVWSFGV 939
Cdd:cd06607  139 TVKLADFGSASLVCPANSFVGTPY------WMAPEvilAMDEGQYDGKVDVWSLGI 188
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
728-995 6.78e-12

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK6 is widely expressed in many tissues and is expressed as multiple splice variants with different domain architectures. It is post-translationally palmitoylated and localized in the membrane. GRK6 plays important roles in the regulation of dopamine, M3 muscarinic, opioid, and chemokine receptor signaling. It also plays maladaptive roles in addiction and Parkinson's disease. GRK6-deficient mice exhibit altered dopamine receptor regulation, decreased lymphocyte chemotaxis, and increased acute inflammation and neutrophil chemotaxis. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270779 [Multi-domain]  Cd Length: 285  Bit Score: 67.36  E-value: 6.78e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  728 KTLGEGEFGKV----VKATafhlkgraGYTTVAVKMLKENASPSELRDL-LSEFNVLKQVNHPHVIKLYGACSQDGPLLL 802
Cdd:cd05630    6 RVLGKGGFGEVcacqVRAT--------GKMYACKKLEKKRIKKRKGEAMaLNEKQILEKVNSRFVVSLAYAYETKDALCL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  803 IVEYAKYGSLRGFLRESRKVGpgylgsggsrnsssldHPDERAltmgdlISFAWQISQGMQYLAEMKLVHRDLAARNILV 882
Cdd:cd05630   78 VLTLMNGGDLKFHIYHMGQAG----------------FPEARA------VFYAAEICCGLEDLHRERIVYRDLKPENILL 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  883 AEGRKMKISDFGLSRDVyEEDSYVKrsqGRI-PVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTlGGNPY----PGIPP 957
Cdd:cd05630  136 DDHGHIRISDLGLAVHV-PEGQTIK---GRVgTVGYMAPEVVKNERYTFSPDWWALGCLLYEMIA-GQSPFqqrkKKIKR 210
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 10862703  958 ERLFNLLKTGHRmERPDNCSEEMYRLMLQCWKQEPDKR 995
Cdd:cd05630  211 EEVERLVKEVPE-EYSEKFSPQARSLCSMLLCKDPAER 247
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
724-954 7.66e-12

Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related Apoptosis-inducing protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DRAKs, also called STK17, were named based on their similarity (around 50% identity) to the kinase domain of DAPKs. They contain an N-terminal kinase domain and a C-terminal regulatory domain. Vertebrates contain two subfamily members, DRAK1 and DRAK2. Both DRAKs are localized to the nucleus, autophosphorylate themselves, and phosphorylate myosin light chain as a substrate. They may play a role in apoptotic signaling. The DRAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271008 [Multi-domain]  Cd Length: 268  Bit Score: 66.99  E-value: 7.66e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  724 LVLGKTLGEGEFGKVVKATafHLKGRAGYttvAVKMLKENASPSELR-DLLSEFNVLKQV-NHPHVIKLYGACSQDGPLL 801
Cdd:cd14106   10 TVESTPLGRGKFAVVRKCI--HKETGKEY---AAKFLRKRRRGQDCRnEILHEIAVLELCkDCPRVVNLHEVYETRSELI 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  802 LIVEYAKYGSLRGFLREsrkvgpgylgsggsrnsssldhpdERALTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNIL 881
Cdd:cd14106   85 LILELAAGGELQTLLDE------------------------EECLTEADVRRLMRQILEGVQYLHERNIVHLDLKPQNIL 140
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 10862703  882 VAEGRK---MKISDFGLSRdVYEEDSYVKRSQGriPVKWMAIESL-FDHIyTTQSDVWSFGVLLWEIVTlGGNPYPG 954
Cdd:cd14106  141 LTSEFPlgdIKLCDFGISR-VIGEGEEIREILG--TPDYVAPEILsYEPI-SLATDMWSIGVLTYVLLT-GHSPFGG 212
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
726-954 8.49e-12

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK2, also called DAPK-related protein 1 (DRP-1), is a Ca2+/calmodulin (CaM)-regulated protein containing an N-terminal kinase domain, a CaM autoinhibitory site and a dimerization module. It lacks the cytoskeletal binding regions of DAPK1 and the exogenous protein has been shown to be soluble and cytoplasmic. FLAG-tagged DAPK2, however, accumulated within membrane-enclosed autophagic vesicles. It is unclear where endogenous DAPK2 is localized. DAPK2 participates in TNF-alpha and FAS-receptor induced cell death and enhances neutrophilic maturation in myeloid leukemic cells. It contributes to the induction of anoikis and its down-regulation is implicated in the beta-catenin induced resistance of malignant epithelial cells to anoikis. The DAPK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271098 [Multi-domain]  Cd Length: 269  Bit Score: 66.90  E-value: 8.49e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  726 LGKTLGEGEFGKVVKAtafhlKGRAGYTTVAVKMLKENASPSELRDLLS-----EFNVLKQVNHPHVIKLYGACSQDGPL 800
Cdd:cd14196    9 IGEELGSGQFAIVKKC-----REKSTGLEYAAKFIKKRQSRASRRGVSReeierEVSILRQVLHPNIITLHDVYENRTDV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  801 LLIVEYAKYGSLRGFLREsrkvgpgylgsggsrnsssldhpdERALTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNI 880
Cdd:cd14196   84 VLILELVSGGELFDFLAQ------------------------KESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENI 139
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 10862703  881 LVAEGR----KMKISDFGLSRDVyeEDSYVKRSQGRIPvKWMAIESLFDHIYTTQSDVWSFGVLLWeIVTLGGNPYPG 954
Cdd:cd14196  140 MLLDKNipipHIKLIDFGLAHEI--EDGVEFKNIFGTP-EFVAPEIVNYEPLGLEADMWSIGVITY-ILLSGASPFLG 213
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
718-944 1.19e-11

Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAO1 is sometimes referred to as prostate-derived sterile 20-like kinase 2 (PSK2). TAO1 activates the p38 MAPK through direct interaction with and activation of MEK3. TAO1 is highly expressed in the brain and may play a role in neuronal apoptosis. TAO1 interacts with the checkpoint proteins BubR1 and Mad2, and plays an important role in regulating mitotic progression, which is required for both chromosome congression and checkpoint-induced anaphase delay. TAO1 may play a role in protecting genomic stability. TAO proteins possess MAPK kinase kinase activity. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. The TAO1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270805 [Multi-domain]  Cd Length: 317  Bit Score: 67.38  E-value: 1.19e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  718 EFPRKNLVLGKTLGEGEFGkvvkATAFHLKGRAGyTTVAVKMLKENASPS--ELRDLLSEFNVLKQVNHPHVIKLYGACS 795
Cdd:cd06635   21 EDPEKLFSDLREIGHGSFG----AVYFARDVRTS-EVVAIKKMSYSGKQSneKWQDIIKEVKFLQRIKHPNSIEYKGCYL 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  796 QDGPLLLIVEYAkYGSLRGFLRESRKvgpgylgsggsrnssSLDHPDERALTMGDLisfawqisQGMQYLAEMKLVHRDL 875
Cdd:cd06635   96 REHTAWLVMEYC-LGSASDLLEVHKK---------------PLQEIEIAAITHGAL--------QGLAYLHSHNMIHRDI 151
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 10862703  876 AARNILVAEGRKMKISDFGLSRDVYEEDSYVKRSQgripvkWMAIESLF---DHIYTTQSDVWSFGVLLWEI 944
Cdd:cd06635  152 KAGNILLTEPGQVKLADFGSASIASPANSFVGTPY------WMAPEVILamdEGQYDGKVDVWSLGITCIEL 217
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
768-996 1.22e-11

Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or General Control Non-derepressible-2; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the overall downregulation of protein synthesis. eIF-2 phosphorylation is induced in response to cellular stresses including virus infection, heat shock, nutrient deficiency, and the accummulation of unfolded proteins, among others. There are four distinct kinases that phosphorylate eIF-2 and control protein synthesis under different stress conditions: GCN2, protein kinase regulated by RNA (PKR), heme-regulated inhibitor kinase (HRI), and PKR-like endoplasmic reticulum kinase (PERK). GCN2 is activated by amino acid or serum starvation and UV irradiation. It induces GCN4, a transcriptional activator of amino acid biosynthetic genes, leading to increased production of amino acids under amino acid-deficient conditions. In serum-starved cells, GCN2 activation induces translation of the stress-responsive transcription factor ATF4, while under UV stress, GCN2 triggers transcriptional rescue via NF-kappaB signaling. GCN2 contains an N-terminal RWD, a degenerate kinase-like (repeat 1), the catalytic kinase (repeat 2), a histidyl-tRNA synthetase (HisRS)-like, and a C-terminal ribosome-binding and dimerization (RB/DD) domains. The degenerate pseudokinase domain of GCN2 may function as a regulatory domain. The GCN2 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270914 [Multi-domain]  Cd Length: 254  Bit Score: 66.23  E-value: 1.22e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  768 ELRDLLSEFNVLKQVNHPHVIKLYGAC------SQDGPLLLIVEYAKYGSLRGFLRESRKVgpgylgsggsrnsssldhP 841
Cdd:cd14012   41 QIQLLEKELESLKKLRHPNLVSYLAFSierrgrSDGWKVYLLTEYAPGGSLSELLDSVGSV------------------P 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  842 DERALtmgdliSFAWQISQGMQYLAEMKLVHRDLAARNILV---AEGRKMKISDFGLSRDVYEEDSYVKrSQGRIPVKWM 918
Cdd:cd14012  103 LDTAR------RWTLQLLEALEYLHRNGVVHKSLHAGNVLLdrdAGTGIVKLTDYSLGKTLLDMCSRGS-LDEFKQTYWL 175
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 10862703  919 AIE-SLFDHIYTTQSDVWSFGVLLWEIVTlgGNPypgiPPERLFNLLKTghrMERPDNcSEEMYRLMLQCWKQEPDKRP 996
Cdd:cd14012  176 PPElAQGSKSPTRKTDVWDLGLLFLQMLF--GLD----VLEKYTSPNPV---LVSLDL-SASLQDFLSKCLSLDPKKRP 244
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
722-954 1.25e-11

The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GSK3 is a mutifunctional kinase involved in many cellular processes including cell division, proliferation, differentiation, adhesion, and apoptosis. In plants, GSK3 plays a role in the response to osmotic stress. In Caenorhabditis elegans, it plays a role in regulating normal oocyte-to-embryo transition and response to oxidative stress. In Chlamydomonas reinhardtii, GSK3 regulates flagellar length and assembly. In mammals, there are two isoforms, GSK3alpha and GSK3beta, which show both distinct and redundant functions. The two isoforms differ mainly in their N-termini. They are both involved in axon formation and in Wnt signaling.They play distinct roles in cardiogenesis, with GSKalpha being essential in cardiomyocyte survival, and GSKbeta regulating heart positioning and left-right symmetry. GSK3beta was first identified as a regulator of glycogen synthesis, but has since been determined to play other roles. It regulates the degradation of beta-catenin and IkB. Beta-catenin is the main effector of Wnt, which is involved in normal haematopoiesis and stem cell function. IkB is a central inhibitor of NF-kB, which is critical in maintaining leukemic cell growth. GSK3beta is enriched in the brain and is involved in regulating neuronal signaling pathways. It is implicated in the pathogenesis of many diseases including Type II diabetes, obesity, mood disorders, Alzheimer's disease, osteoporosis, and some types of cancer, among others. The GSK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271039 [Multi-domain]  Cd Length: 293  Bit Score: 66.76  E-value: 1.25e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  722 KNLVLGKTLGEGEFGKVVKATAFHLKGRagyttVAVKM------LKENaspselrdllsEFNVLKQVNHPHVIKLYGAC- 794
Cdd:cd14137    4 ISYTIEKVIGSGSFGVVYQAKLLETGEV-----VAIKKvlqdkrYKNR-----------ELQIMRRLKHPNIVKLKYFFy 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  795 SQDGP-----LLLIVEYAKYgSLRGFLRESRKVGpgylgsggsrnsssldhpdeRALTMGDLISFAWQISQGMQYLAEMK 869
Cdd:cd14137   68 SSGEKkdevyLNLVMEYMPE-TLYRVIRHYSKNK--------------------QTIPIIYVKLYSYQLFRGLAYLHSLG 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  870 LVHRDLAARNILVaEGRKM--KISDFG----LSRDvyEED-SYV----KRsqgripvkwmAIESLFDHI-YTTQSDVWSF 937
Cdd:cd14137  127 ICHRDIKPQNLLV-DPETGvlKLCDFGsakrLVPG--EPNvSYIcsryYR----------APELIFGATdYTTAIDIWSA 193
                        250
                 ....*....|....*...
gi 10862703  938 GVLLWEIVTlgGNP-YPG 954
Cdd:cd14137  194 GCVLAELLL--GQPlFPG 209
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
728-995 1.36e-11

Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-theta is selectively expressed in T-cells and plays an important and non-redundant role in several aspects of T-cell biology. PKC-delta plays a role in cell cycle regulation and programmed cell death in many cell types. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. There are four nPKC isoforms, delta, epsilon, eta, and theta. The nPKC-theta-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270744 [Multi-domain]  Cd Length: 320  Bit Score: 67.02  E-value: 1.36e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  728 KTLGEGEFGKVVKAtafHLKGRAGYttVAVKMLKENASpseLRD-----LLSEFNVLK-QVNHPHVIKLYGACSQDGPLL 801
Cdd:cd05592    1 KVLGKGSFGKVMLA---ELKGTNQY--FAIKALKKDVV---LEDddvecTMIERRVLAlASQHPFLTHLFCTFQTESHLF 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  802 LIVEYAKYGSLRGFLRESRKVgpgylgsggsrnsssldhPDERALTmgdlisFAWQISQGMQYLAEMKLVHRDLAARNIL 881
Cdd:cd05592   73 FVMEYLNGGDLMFHIQQSGRF------------------DEDRARF------YGAEIICGLQFLHSRGIIYRDLKLDNVL 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  882 VAEGRKMKISDFGLSR-DVYEEdsyVKRSQGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVtLGGNPYPGIPPERL 960
Cdd:cd05592  129 LDREGHIKIADFGMCKeNIYGE---NKASTFCGTPDYIAPEILKGQKYNQSVDWWSFGVLLYEML-IGQSPFHGEDEDEL 204
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 10862703  961 F-NLLKTghRMERPDNCSEEMYRLMLQCWKQEPDKR 995
Cdd:cd05592  205 FwSICND--TPHYPRWLTKEAASCLSLLLERNPEKR 238
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
730-952 1.42e-11

Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase (IKK) alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IKKalpha is involved in the non-canonical or alternative pathway of regulating Nuclear Factor-KappaB (NF-kB) proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. The non-canonical pathway functions in cells lacking NEMO (NF-kB Essential MOdulator) and IKKbeta. It is induced by a subset of TNFR family members including CD40, RANK, and B cell-activating factor receptor. IKKalpha processes the Inhibitor of NF-kB (IkB)-like C-terminus of NF-kB2/p100 to produce p52, allowing the p52/RelB dimer to migrate to the nucleus. This pathway is dependent on NIK (NF-kB Inducing Kinase) which phosphorylates and activates IKKalpha. The IKKalpha subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270941 [Multi-domain]  Cd Length: 289  Bit Score: 66.48  E-value: 1.42e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  730 LGEGEFGKVvkataFHLKGRAGYTTVAVKMLKENASPSELRDLLSEFNVLKQVNHPHVIKlygACS---------QDGPL 800
Cdd:cd14039    1 LGTGGFGNV-----CLYQNQETGEKIAIKSCRLELSVKNKDRWCHEIQIMKKLNHPNVVK---ACDvpeemnflvNDVPL 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  801 LLIvEYAKYGSLRGFLRESRKVGpgylgsggsrnsssldhpderALTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNI 880
Cdd:cd14039   73 LAM-EYCSGGDLRKLLNKPENCC---------------------GLKESQVLSLLSDIGSGIQYLHENKIIHRDLKPENI 130
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 10862703  881 LVAE-GRKM--KISDFGLSRDVyEEDSYVKRSQGRIpvKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTlGGNPY 952
Cdd:cd14039  131 VLQEiNGKIvhKIIDLGYAKDL-DQGSLCTSFVGTL--QYLAPELFENKSYTVTVDYWSFGTMVFECIA-GFRPF 201
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
712-964 1.52e-11

N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase Kinase Kinase 4 and 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. MAP4K4 is also called Nck Interacting kinase (NIK). It facilitates the activation of the MAPKs, extracellular signal-regulated kinase (ERK) 1, ERK2, and c-Jun N-terminal kinase (JNK), by phosphorylating and activating MEKK1. MAP4K4 plays a role in tumor necrosis factor (TNF) alpha-induced insulin resistance. MAP4K4 silencing in skeletal muscle cells from type II diabetic patients restores insulin-mediated glucose uptake. MAP4K4, through JNK, also plays a broad role in cell motility, which impacts inflammation, homeostasis, as well as the invasion and spread of cancer. MAP4K4 is found to be highly expressed in most tumor cell lines relative to normal tissue. MAP4K6 (also called MINK for Misshapen/NIKs-related kinase) is activated after Ras induction and mediates activation of p38 MAPK. MAP4K6 plays a role in cell cycle arrest, cytoskeleton organization, cell adhesion, and cell motility. The MAP4K4/6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270806 [Multi-domain]  Cd Length: 282  Bit Score: 66.57  E-value: 1.52e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  712 LEDPKWEFPrknlvLGKTLGEGEFGKVVKATafHLKGRagyTTVAVKMLkeNASPSELRDLLSEFNVLKQVNH-PHVIKL 790
Cdd:cd06636   11 LRDPAGIFE-----LVEVVGNGTYGQVYKGR--HVKTG---QLAAIKVM--DVTEDEEEEIKLEINMLKKYSHhRNIATY 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  791 YGA------CSQDGPLLLIVEYAKYGSLRGFLREsrkvgpgylgsggsrnsssldhpderalTMGDLISFAW------QI 858
Cdd:cd06636   79 YGAfikkspPGHDDQLWLVMEFCGAGSVTDLVKN----------------------------TKGNALKEDWiayicrEI 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  859 SQGMQYLAEMKLVHRDLAARNILVAEGRKMKISDFGLSRDVyeeDSYVKRSQGRIPVK-WMAIESLF-----DHIYTTQS 932
Cdd:cd06636  131 LRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQL---DRTVGRRNTFIGTPyWMAPEVIAcdenpDATYDYRS 207
                        250       260       270
                 ....*....|....*....|....*....|..
gi 10862703  933 DVWSFGVLLWEIVTlGGNPYPGIPPERLFNLL 964
Cdd:cd06636  208 DIWSLGITAIEMAE-GAPPLCDMHPMRALFLI 238
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
723-1011 1.52e-11

N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK2 and MSK1 play nonredundant roles in activating histone H3 kinases, which play pivotal roles in compaction of the chromatin fiber. MSK2 is the required H3 kinase in response to stress stimuli and activation of the p38 MAPK pathway. MSK2 also plays a role in the pathogenesis of psoriasis. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family, similar to 90 kDa ribosomal protein S6 kinases (RSKs). MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270765 [Multi-domain]  Cd Length: 332  Bit Score: 67.25  E-value: 1.52e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  723 NLVLGKTLGEGEFGKV--VKATAFHLKGRagytTVAVKMLKENASPSELRDL---LSEFNVLKQVNH-PHVIKLYGACSQ 796
Cdd:cd05614    1 NFELLKVLGTGAYGKVflVRKVSGHDANK----LYAMKVLRKAALVQKAKTVehtRTERNVLEHVRQsPFLVTLHYAFQT 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  797 DGPLLLIVEYAKYGSLRGFLRESrkvgpgylgsggsrnssslDHPDERALTMgdlisFAWQISQGMQYLAEMKLVHRDLA 876
Cdd:cd05614   77 DAKLHLILDYVSGGELFTHLYQR-------------------DHFSEDEVRF-----YSGEIILALEHLHKLGIVYRDIK 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  877 ARNILVAEGRKMKISDFGLSRDVYEEDSYVKRS-QGRIpvKWMAIEslfdhIYTTQS------DVWSFGVLLWEIVTlGG 949
Cdd:cd05614  133 LENILLDSEGHVVLTDFGLSKEFLTEEKERTYSfCGTI--EYMAPE-----IIRGKSghgkavDWWSLGILMFELLT-GA 204
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 10862703  950 NPYPgipperlfnllktghrMERPDNCSEEMYRLMLQCwkqEPDKRPVFADISKD-LEKMMVK 1011
Cdd:cd05614  205 SPFT----------------LEGEKNTQSEVSRRILKC---DPPFPSFIGPVARDlLQKLLCK 248
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
725-965 1.63e-11

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Mutations in the gene encoding CDKL5, previously called STK9, are associated with early onset epilepsy and severe mental retardation [X-linked infantile spasm syndrome (ISSX) or West syndrome]. In addition, CDKL5 mutations also sometimes cause a phenotype similar to Rett syndrome (RTT), a progressive neurodevelopmental disorder. These pathogenic mutations are located in the N-terminal portion of the protein within the kinase domain. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270838 [Multi-domain]  Cd Length: 287  Bit Score: 66.56  E-value: 1.63e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  725 VLGkTLGEGEFGKVVKAtafhlKGRAGYTTVAVKMLKENASPSELRDL-LSEFNVLKQVNHPHVIKLYGACSQDGPLLLI 803
Cdd:cd07848    5 VLG-VVGEGAYGVVLKC-----RHKETKEIVAIKKFKDSEENEEVKETtLRELKMLRTLKQENIVELKEAFRRRGKLYLV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  804 VEYAKYGSLRgFLRESRKVGPgylgsggsrnsssldhPDEraltmgdLISFAWQISQGMQYLAEMKLVHRDLAARNILVA 883
Cdd:cd07848   79 FEYVEKNMLE-LLEEMPNGVP----------------PEK-------VRSYIYQLIKAIHWCHKNDIVHRDIKPENLLIS 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  884 EGRKMKISDFGLSRDVYEEDS-----YVKRSQGRIPvkwmaiESLFDHIYTTQSDVWSFGVLLWEIVTlgGNP-YPGIPP 957
Cdd:cd07848  135 HNDVLKLCDFGFARNLSEGSNanyteYVATRWYRSP------ELLLGAPYGKAVDMWSVGCILGELSD--GQPlFPGESE 206

                 ....*....
gi 10862703  958 -ERLFNLLK 965
Cdd:cd07848  207 iDQLFTIQK 215
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
730-1004 1.78e-11

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors, which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. GRKs play important roles in the cardiovascular, immune, respiratory, skeletal, and nervous systems. They contain a central catalytic domain, flanked by N- and C-terminal extensions. The N-terminus contains an RGS (regulator of G protein signaling) homology (RH) domain and several motifs. The C-terminus diverges among different groups of GRKs. There are seven types of GRKs, named GRK1 to GRK7, which are subdivided into three main groups: visual (GRK1/7); beta-adrenergic receptor kinases (GRK2/3); and GRK4-like (GRK4/5/6). Expression of GRK2/3/5/6 is widespread while GRK1/4/7 show a limited tissue distribution. The substrate spectrum of the widely expressed GRKs partially overlaps. The GRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270729 [Multi-domain]  Cd Length: 278  Bit Score: 66.01  E-value: 1.78e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  730 LGEGEFGKV----VKATAF----------HLKGRAGYTTVavkmlkenaspselrdlLSEFNVLKQVNHPHVIKLYGACS 795
Cdd:cd05577    1 LGRGGFGEVcacqVKATGKmyackkldkkRIKKKKGETMA-----------------LNEKIILEKVSSPFIVSLAYAFE 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  796 QDGPLLLIVEYAKYGSLRgflresrkvgpgylgsggsrnsSSLDHPDERALTMGDLISFAWQISQGMQYLAEMKLVHRDL 875
Cdd:cd05577   64 TKDKLCLVLTLMNGGDLK----------------------YHIYNVGTRGFSEARAIFYAAEIICGLEHLHNRFIVYRDL 121
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  876 AARNILVAEGRKMKISDFGLSRDVYEEdsyvKRSQGRI-PVKWMAIESLFDHI-YTTQSDVWSFGVLLWEIVTlGGNPY- 952
Cdd:cd05577  122 KPENILLDDHGHVRISDLGLAVEFKGG----KKIKGRVgTHGYMAPEVLQKEVaYDFSVDWFALGCMLYEMIA-GRSPFr 196
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 10862703  953 ---PGIPPERLFNLLKTgHRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADISKD 1004
Cdd:cd05577  197 qrkEKVDKEELKRRTLE-MAVEYPDSFSPEARSLCEGLLQKDPERRLGCRGGSAD 250
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
754-972 1.93e-11

Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Obscurin, approximately 800 kDa in size, is one of three giant proteins expressed in vetebrate striated muscle, together with titin and nebulin. It is a multidomain protein composed of tandem adhesion and signaling domains, including 49 immunoglobulin (Ig) and 2 fibronectin type III (FN3) domains at the N-terminus followed by a more complex region containing more Ig domains, a conserved SH3 domain near a RhoGEF and PH domains, non-modular regions, as well as IQ and phosphorylation motifs. The obscurin gene also encode two kinase domains, which are not expressed as part of the 800 kDa protein, but as a smaller, alternatively spliced product present mainly in the heart muscle, also called obscurin-MLCK. Obscurin is localized at the peripheries of Z-disks and M-lines, where it is able to communicate with the surrounding myoplasm. It interacts with diverse proteins including sAnk1, myosin, titin, and MyBP-C. It may act as a scaffold for the assembly of elements of the contractile apparatus. The obscurin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271012 [Multi-domain]  Cd Length: 257  Bit Score: 65.71  E-value: 1.93e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  754 TVAVKMLKENasPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVEYAkygslrgflresrkVGPGYLGSGGsr 833
Cdd:cd14110   30 MLAAKIIPYK--PEDKQLVLREYQVLRRLSHPRIAQLHSAYLSPRHLVLIEELC--------------SGPELLYNLA-- 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  834 nsssldhpdERAL-TMGDLISFAWQISQGMQYLAEMKLVHRDLAARNILVAEGRKMKISDFGLSRDVYEEDSYVKRSQGR 912
Cdd:cd14110   92 ---------ERNSySEAEVTDYLWQILSAVDYLHSRRILHLDLRSENMIITEKNLLKIVDLGNAQPFNQGKVLMTDKKGD 162
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 10862703  913 IpVKWMAIESLFDHIYTTQSDVWSFGVLLWeiVTLGGNpYP---GIPPERLFNLLKTGHRMER 972
Cdd:cd14110  163 Y-VETMAPELLEGQGAGPQTDIWAIGVTAF--IMLSAD-YPvssDLNWERDRNIRKGKVQLSR 221
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
726-995 1.96e-11

Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MELK is a cell cycle dependent protein which functions in cytokinesis, cell cycle, apoptosis, cell proliferation, and mRNA processing. It is found upregulated in many types of cancer cells, playing an indispensable role in cancer cell survival. It makes an attractive target in the design of inhibitors for use in the treatment of a wide range of human cancer. The MELK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270980 [Multi-domain]  Cd Length: 257  Bit Score: 65.48  E-value: 1.96e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  726 LGKTLGEGEFGKVVKATafHLkgrAGYTTVAVKMLKENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVE 805
Cdd:cd14078    7 LHETIGSGGFAKVKLAT--HI---LTGEKVAIKIMDKKALGDDLPRVKTEIEALKNLSHQHICRLYHVIETDNKIFMVLE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  806 YAKYGSLRGFLRESRKvgpgylgsggsrnsssLDHPDERAltmgdlisFAWQISQGMQYLAEMKLVHRDLAARNILVAEG 885
Cdd:cd14078   82 YCPGGELFDYIVAKDR----------------LSEDEARV--------FFRQIVSAVAYVHSQGYAHRDLKPENLLLDED 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  886 RKMKISDFGLsrdvyeedsyVKRSQGRIPvkwmaieslfDHIYT--------------------TQSDVWSFGVLLWEIV 945
Cdd:cd14078  138 QNLKLIDFGL----------CAKPKGGMD----------HHLETccgspayaapeliqgkpyigSEADVWSMGVLLYALL 197
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 10862703  946 TlGGNPYPGIPPERLFNLLKTGhRMERPDNCSE---EMYRLMLQCwkqEPDKR 995
Cdd:cd14078  198 C-GFLPFDDDNVMALYRKIQSG-KYEEPEWLSPsskLLLDQMLQV---DPKKR 245
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
756-951 2.09e-11

Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phosphorylase kinase (PhK) catalyzes the phosphorylation of inactive phosphorylase b to form the active phosphorylase a. It coordinates hormonal, metabolic, and neuronal signals to initiate the breakdown of glycogen stores, which enables the maintenance of blood-glucose homeostasis during fasting, and is also used as a source of energy for muscle contraction. PhK is one of the largest and most complex protein kinases, composed of a heterotetramer containing four molecules each of four subunit types: one catalytic (gamma) and three regulatory (alpha, beta, and delta). Each subunit has tissue-specific isoforms or splice variants. Vertebrates contain two isoforms of the gamma subunit (gamma 1 and gamma 2). The gamma subunit, when isolated, is constitutively active and does not require phosphorylation of the A-loop for activity. The regulatory subunits restrain this kinase activity until signals are received to relieve this inhibition. For example, the kinase is activated in response to hormonal stimulation, after autophosphorylation or phosphorylation by cAMP-dependent kinase of the alpha and beta subunits. The high-affinity binding of ADP to the beta subunit also stimulates kinase activity, whereas calcium relieves inhibition by binding to the delta (calmodulin) subunit. The PhKG subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270995 [Multi-domain]  Cd Length: 272  Bit Score: 65.84  E-value: 2.09e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  756 AVKMLK---ENASPSELRDLL----SEFNVLKQVN-HPHVIKLYGACSQDGPLLLIVEYAKYGSLRGFLREsrKVgpgyl 827
Cdd:cd14093   32 AVKIIDitgEKSSENEAEELReatrREIEILRQVSgHPNIIELHDVFESPTFIFLVFELCRKGELFDYLTE--VV----- 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  828 gsggsrnssSLDHPDERALtMGDLISfawqisqGMQYLAEMKLVHRDLAARNILVAEGRKMKISDFGLSRDVyEEDSYVK 907
Cdd:cd14093  105 ---------TLSEKKTRRI-MRQLFE-------AVEFLHSLNIVHRDLKPENILLDDNLNVKISDFGFATRL-DEGEKLR 166
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 10862703  908 RSQGrIPvKWMAIE----SLFDHI--YTTQSDVWSFGVLLWEIvtLGGNP 951
Cdd:cd14093  167 ELCG-TP-GYLAPEvlkcSMYDNApgYGKEVDMWACGVIMYTL--LAGCP 212
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
730-1010 2.65e-11

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher eukaryotes; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK1 is also called Cell division control protein 2 (Cdc2) or p34 protein kinase, and is regulated by cyclins A, B, and E. The CDK1/cyclin A complex controls G2 phase entry and progression. CDK1/cyclin A2 has also been implicated as an important regulator of S phase events. The CDK1/cyclin B complex is critical for G2 to M phase transition. It induces mitosis by activating nuclear enzymes that regulate chromatin condensation, nuclear membrane degradation, mitosis-specific microtubule and cytoskeletal reorganization. CDK1 also associates with cyclin E and plays a role in the entry into S phase. CDK1 transcription is stable throughout the cell cycle but is modulated in some pathological conditions. It may play a role in regulating apoptosis under these conditions. In breast cancer cells, HER2 can mediate apoptosis by inactivating CDK1. Activation of CDK1 may contribute to HIV-1 induced apoptosis as well as neuronal apoptosis in neurodegenerative diseases. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270845 [Multi-domain]  Cd Length: 285  Bit Score: 65.52  E-value: 2.65e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  730 LGEGEFGKVVKAtafhlKGRAGYTTVAVKMLK----ENASPSELrdlLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVE 805
Cdd:cd07861    8 IGEGTYGVVYKG-----RNKKTGQIVAMKKIRleseEEGVPSTA---IREISLLKELQHPNIVCLEDVLMQENRLYLVFE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  806 YAKYgSLRGFLrESRKVGpGYLgsggsrnsssldhpdERALtmgdLISFAWQISQGMQYLAEMKLVHRDLAARNILVAEG 885
Cdd:cd07861   80 FLSM-DLKKYL-DSLPKG-KYM---------------DAEL----VKSYLYQILQGILFCHSRRVLHRDLKPQNLLIDNK 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  886 RKMKISDFGLSRDVyeedsyvkrsqgRIPVK----------WMAIESLFDHI-YTTQSDVWSFGVLLWEIVTlgGNPYPG 954
Cdd:cd07861  138 GVIKLADFGLARAF------------GIPVRvythevvtlwYRAPEVLLGSPrYSTPVDIWSIGTIFAEMAT--KKPLFH 203
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 10862703  955 IPPE-----RLFNLLKTGHRMERPDNCSEEMYRLMLQCWKqEPDKRPVFADISKD----LEKMMV 1010
Cdd:cd07861  204 GDSEidqlfRIFRILGTPTEDIWPGVTSLPDYKNTFPKWK-KGSLRTAVKNLDEDgldlLEKMLI 267
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
728-995 2.75e-11

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I delta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-delta subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271070 [Multi-domain]  Cd Length: 301  Bit Score: 65.84  E-value: 2.75e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  728 KTLGEGEFGKVVKAtafhlKGRAGYTTVAVKMLKENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVEYA 807
Cdd:cd14168   16 EVLGTGAFSEVVLA-----EERATGKLFAVKCIPKKALKGKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLV 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  808 KYGSLRgflreSRKVGPGYLgsggsrnsssldhpderalTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNILV---AE 884
Cdd:cd14168   91 SGGELF-----DRIVEKGFY-------------------TEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYfsqDE 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  885 GRKMKISDFGLSRdvYEEDSYVKRSQGRIPvKWMAIESLFDHIYTTQSDVWSFGVLLWeIVTLGGNPYPGIPPERLF-NL 963
Cdd:cd14168  147 ESKIMISDFGLSK--MEGKGDVMSTACGTP-GYVAPEVLAQKPYSKAVDCWSIGVIAY-ILLCGYPPFYDENDSKLFeQI 222
                        250       260       270
                 ....*....|....*....|....*....|....
gi 10862703  964 LKTGHRMERP--DNCSEEMYRLMLQCWKQEPDKR 995
Cdd:cd14168  223 LKADYEFDSPywDDISDSAKDFIRNLMEKDPNKR 256
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
728-996 3.08e-11

Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle 1 (also called TTK); Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TTK/Mps1 is a spindle checkpoint kinase that was first discovered due to its necessity in centrosome duplication in budding yeast. It was later found to function in the spindle assembly checkpoint, which monitors the proper attachment of chromosomes to the mitotic spindle. In yeast, substrates of Mps1 include the spindle pole body components Spc98p, Spc110p, and Spc42p. The TTK/Mps1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271033 [Multi-domain]  Cd Length: 271  Bit Score: 65.31  E-value: 3.08e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  728 KTLGEGEFGKVVKATAfhlkgrAGYTTVAVKMLK-ENASPSELRDLLSEFNVLKQVNH-PHVIKLYGA--CSQDGPLLLI 803
Cdd:cd14131    7 KQLGKGGSSKVYKVLN------PKKKIYALKRVDlEGADEQTLQSYKNEIELLKKLKGsDRIIQLYDYevTDEDDYLYMV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  804 VEYAKYgSLRGFLRESRkvgpgylgsggsrnsssldhpdERALTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNILVA 883
Cdd:cd14131   81 MECGEI-DLATILKKKR----------------------PKPIDPNFIRYYWKQMLEAVHTIHEEGIVHSDLKPANFLLV 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  884 EGRkMKISDFGLSRDVYEEDSYVKRSQGRIPVKWMAIESLFDHIYTTQ----------SDVWSFGVLLWEIVtLGGNPYP 953
Cdd:cd14131  138 KGR-LKLIDFGIAKAIQNDTTSIVRDSQVGTLNYMSPEAIKDTSASGEgkpkskigrpSDVWSLGCILYQMV-YGKTPFQ 215
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 10862703  954 GIPP--ERLFNLLKTGHRMERPDNCSEEMYRLMLQCWKQEPDKRP 996
Cdd:cd14131  216 HITNpiAKLQAIIDPNHEIEFPDIPNPDLIDVMKRCLQRDPKKRP 260
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
726-951 4.10e-11

Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Aurora kinases are key regulators of mitosis and are essential for the accurate and equal division of genomic material from parent to daughter cells. Vertebrates contain at least 2 Aurora kinases (A and B); mammals contains a third Aurora kinase gene (C). This subfamily includes Aurora-B and Aurora-C. Aurora-B is most active at the transition during metaphase to the end of mitosis. It associates with centromeres, relocates to the midzone of the central spindle, and concentrates at the midbody during cell division. It is critical for accurate chromosomal segregation, cytokinesis, protein localization to the centrosome and kinetochore, correct microtubule-kinetochore attachments, and regulation of the mitotic checkpoint. Aurora-C is mainly expressed in meiotically dividing cells; it was originally discovered in mice as a testis-specific STK called Aie1. Both Aurora-B and -C are chromosomal passenger proteins that can form complexes with INCENP and survivin, and they may have redundant cellular functions. INCENP participates in the activation of Aurora-B in a two-step process: first by binding to form an intermediate state of activation and the phosphorylation of its C-terminal TSS motif to generate the fully active kinase. The Aurora-B subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271019 [Multi-domain]  Cd Length: 270  Bit Score: 64.89  E-value: 4.10e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  726 LGKTLGEGEFGKVVKAtafhlKGRAGYTTVAVKMLKENASPSE--LRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLI 803
Cdd:cd14117   10 IGRPLGKGKFGNVYLA-----REKQSKFIVALKVLFKSQIEKEgvEHQLRREIEIQSHLRHPNILRLYNYFHDRKRIYLI 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  804 VEYAKYGSLRGFLRESRKVGpgylgsggsrnsssldhpDERALTmgdlisFAWQISQGMQYLAEMKLVHRDLAARNILVA 883
Cdd:cd14117   85 LEYAPRGELYKELQKHGRFD------------------EQRTAT------FMEELADALHYCHEKKVIHRDIKPENLLMG 140
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 10862703  884 EGRKMKISDFGLSrdVYEEDSYVKRSQGRIpvKWMAIESLFDHIYTTQSDVWSFGVLLWEIvtLGGNP 951
Cdd:cd14117  141 YKGELKIADFGWS--VHAPSLRRRTMCGTL--DYLPPEMIEGRTHDEKVDLWCIGVLCYEL--LVGMP 202
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
716-957 4.57e-11

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 65.61  E-value: 4.57e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703   716 KWEFprKNLVLGKTLGEGEFGKVVKAtafHLKGRAGYttVAVKMLK--ENASPSELRDLLSEFNVLKQVNHPHVIKLYGA 793
Cdd:PTZ00263   14 SWKL--SDFEMGETLGTGSFGRVRIA---KHKGTGEY--YAIKCLKkrEILKMKQVQHVAQEKSILMELSHPFIVNMMCS 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703   794 CSQDGPLLLIVEYAKYGSLRGFLRESRKVgpgylgsggsrnsssldhPDERALTmgdlisFAWQISQGMQYLAEMKLVHR 873
Cdd:PTZ00263   87 FQDENRVYFLLEFVVGGELFTHLRKAGRF------------------PNDVAKF------YHAELVLAFEYLHSKDIIYR 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703   874 DLAARNILVAEGRKMKISDFGLSRDVYEEDSYVKRSQgripvKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTlggnpyp 953
Cdd:PTZ00263  143 DLKPENLLLDNKGHVKVTDFGFAKKVPDRTFTLCGTP-----EYLAPEVIQSKGHGKAVDWWTMGVLLYEFIA------- 210

                  ....
gi 10862703   954 GIPP 957
Cdd:PTZ00263  211 GYPP 214
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
720-996 5.22e-11

Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Human TAO2 is also known as prostate-derived Ste20-like kinase (PSK) and was identified in a screen for overexpressed RNAs in prostate cancer. TAO2 possesses mitogen-activated protein kinase (MAPK) kinase kinase activity and activates both p38 and c-Jun N-terminal kinase (JNK), by phosphorylating and activating their respective MAP/ERK kinases, MEK3/MEK6 and MKK4/MKK7. It contains a long C-terminal extension with autoinhibitory segments, and is activated by the release of this inhibition and the phosphorylation of its activation loop serine. TAO2 functions as a regulator of actin cytoskeletal and microtubule organization. In addition, it regulates the transforming growth factor-activated kinase 1 (TAK1), which is a MAPKKK that plays an essential role in the signaling pathways of tumor necrosis factor, interleukin 1, and Toll-like receptor. The TAO2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270804 [Multi-domain]  Cd Length: 308  Bit Score: 65.04  E-value: 5.22e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  720 PRKNLVLGKTLGEGEFGKVvkataFHLKGRAGYTTVAVKMLKENASPS--ELRDLLSEFNVLKQVNHPHVIKLYGACSQD 797
Cdd:cd06634   13 PEKLFSDLREIGHGSFGAV-----YFARDVRNNEVVAIKKMSYSGKQSneKWQDIIKEVKFLQKLRHPNTIEYRGCYLRE 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  798 GPLLLIVEYAkYGSLRGFLRESRKvgpgylgsggsrnssSLDHPDERALTMGDLisfawqisQGMQYLAEMKLVHRDLAA 877
Cdd:cd06634   88 HTAWLVMEYC-LGSASDLLEVHKK---------------PLQEVEIAAITHGAL--------QGLAYLHSHNMIHRDVKA 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  878 RNILVAEGRKMKISDFGLSRDVYEEDSYVKRSQgripvkWMAIESLF---DHIYTTQSDVWSFGVLLWEIVTLGGNPYPG 954
Cdd:cd06634  144 GNILLTEPGLVKLGDFGSASIMAPANSFVGTPY------WMAPEVILamdEGQYDGKVDVWSLGITCIELAERKPPLFNM 217
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 10862703  955 IPPERLFNLLKTGHRMERPDNCSEEMYRLMLQCWKQEPDKRP 996
Cdd:cd06634  218 NAMSALYHIAQNESPALQSGHWSEYFRNFVDSCLQKIPQDRP 259
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
732-952 5.39e-11

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type IV; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKIV is found predominantly in neurons and immune cells. It is activated by the binding of calcium/CaM and phosphorylation by CaMKK (alpha or beta). The CaMKK-CaMKIV cascade participates in regulating several transcription factors like CREB, MEF2, and retinoid orphan receptors. It also is implicated in T-cell development and signaling, cytokine secretion, and signaling through Toll-like receptors, and is thus, pivotal in immune response and inflammation. The CaMKIV subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270987 [Multi-domain]  Cd Length: 294  Bit Score: 64.85  E-value: 5.39e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  732 EGEFGKVVKATAFHLKGRAGYTTVAVKMLKENASPSELRdllSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVEYAKYGS 811
Cdd:cd14085    8 ESELGRGATSVVYRCRQKGTQKPYAVKKLKKTVDKKIVR---TEIGVLLRLSHPNIIKLKEIFETPTEISLVLELVTGGE 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  812 LRgflreSRKVGPGYLGsggsrnsssldhpdERaltmgDLISFAWQISQGMQYLAEMKLVHRDLAARNILVAEGRK---M 888
Cdd:cd14085   85 LF-----DRIVEKGYYS--------------ER-----DAADAVKQILEAVAYLHENGIVHRDLKPENLLYATPAPdapL 140
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 10862703  889 KISDFGLSRdVYEEDSYVKRSQGrIPvKWMAIESLFDHIYTTQSDVWSFGVLLWeIVTLGGNPY 952
Cdd:cd14085  141 KIADFGLSK-IVDQQVTMKTVCG-TP-GYCAPEILRGCAYGPEVDMWSVGVITY-ILLCGFEPF 200
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
726-995 5.63e-11

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called Doublecortin-like and CAM kinase-like 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL1 (or DCAMKL1) belongs to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. In addition, DCKL1 contains a serine, threonine, and proline rich domain (SP) and a C-terminal kinase domain with similarity to CAMKs. DCKL1 interacts with tubulin, glucocorticoid receptor, dynein, JIP1/2, caspases (3 and 8), and calpain, among others. It plays roles in neurogenesis, neuronal migration, retrograde transport, and neuronal apoptosis. The DCKL1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271085 [Multi-domain]  Cd Length: 268  Bit Score: 64.63  E-value: 5.63e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  726 LGKTLGEGEFGkVVKATAFHLKGRAgyttVAVKMLKENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVE 805
Cdd:cd14183   10 VGRTIGDGNFA-VVKECVERSTGRE----YALKIINKSKCRGKEHMIQNEVSILRRVKHPNIVLLIEEMDMPTELYLVME 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  806 YAKYGSLRGFLRESRKvgpgylgsggsrnsssldhpderaLTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNILVAE- 884
Cdd:cd14183   85 LVKGGDLFDAITSTNK------------------------YTERDASGMLYNLASAIKYLHSLNIVHRDIKPENLLVYEh 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  885 ---GRKMKISDFGLSRDVyeeDSYVKRSQGrIPVkWMAIESLFDHIYTTQSDVWSFGVLLWeIVTLGGNPYPGI--PPER 959
Cdd:cd14183  141 qdgSKSLKLGDFGLATVV---DGPLYTVCG-TPT-YVAPEIIAETGYGLKVDIWAAGVITY-ILLCGFPPFRGSgdDQEV 214
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 10862703  960 LFNLLKTGhRMERP----DNCSEEMYRLMLQCWKQEPDKR 995
Cdd:cd14183  215 LFDQILMG-QVDFPspywDNVSDSAKELITMMLQVDVDQR 253
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
726-1011 6.26e-11

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK3, also called DAP-like kinase (DLK) and zipper-interacting protein kinase (ZIPk), contains an N-terminal kinase domain and a C-terminal region with nuclear localization signals (NLS) and a leucine zipper motif that mediates homodimerization and interaction with other leucine zipper proteins. It interacts with Par-4, a protein that contains a death domain and interacts with actin filaments. DAPK3 is present in both the cytoplasm and nucleus. Its co-expression with Par-4 results in the co-localization of the two proteins to actin filaments. In addition to cell death, DAPK3 is also implicated in mediating cell motility and the contraction of smooth muscles. The DAPK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271097 [Multi-domain]  Cd Length: 271  Bit Score: 64.25  E-value: 6.26e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  726 LGKTLGEGEFGKVVKAtafhlKGRAGYTTVAVKMLKENASPSELR-----DLLSEFNVLKQVNHPHVIKLYGACSQDGPL 800
Cdd:cd14195    9 MGEELGSGQFAIVRKC-----REKGTGKEYAAKFIKKRRLSSSRRgvsreEIEREVNILREIQHPNIITLHDIFENKTDV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  801 LLIVEYAKYGSLRGFLREsrkvgpgylgsggsrnsssldhpdERALTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNI 880
Cdd:cd14195   84 VLILELVSGGELFDFLAE------------------------KESLTEEEATQFLKQILDGVHYLHSKRIAHFDLKPENI 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  881 LVAEGR----KMKISDFGLSRDVyEEDSYVKRSQGrIPvKWMAIESLFDHIYTTQSDVWSFGVLLWeIVTLGGNPYPG-I 955
Cdd:cd14195  140 MLLDKNvpnpRIKLIDFGIAHKI-EAGNEFKNIFG-TP-EFVAPEIVNYEPLGLEADMWSIGVITY-ILLSGASPFLGeT 215
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 10862703  956 PPERLFNLLKTGHRMERP--DNCSEEMYRLMLQCWKQEPDKRpvfADISKDLEKMMVK 1011
Cdd:cd14195  216 KQETLTNISAVNYDFDEEyfSNTSELAKDFIRRLLVKDPKKR---MTIAQSLEHSWIK 270
pknD PRK13184
serine/threonine-protein kinase PknD;
755-952 6.30e-11

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 66.72  E-value: 6.30e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703   755 VAVKMLKENASPSEL--RDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVEYAKYGSLRGFLRESRKvgpgylgsggs 832
Cdd:PRK13184   30 VALKKIREDLSENPLlkKRFLREAKIAADLIHPGIVPVYSICSDGDPVYYTMPYIEGYTLKSLLKSVWQ----------- 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703   833 rnSSSLDHPDERALTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNILVAEGRKMKISDFG--LSRDVYEED----SYV 906
Cdd:PRK13184   99 --KESLSKELAEKTSVGAFLSIFHKICATIEYVHSKGVLHRDLKPDNILLGLFGEVVILDWGaaIFKKLEEEDlldiDVD 176
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 10862703   907 KR----SQGRIPVK------WMAIESLFDHIYTTQSDVWSFGVLLWEIVTLgGNPY 952
Cdd:PRK13184  177 ERnicySSMTIPGKivgtpdYMAPERLLGVPASESTDIYALGVILYQMLTL-SFPY 231
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
723-1004 6.98e-11

Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase (also called MAK-V); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HUNK/MAK-V was identified from a mammary tumor in an MMTV-neu transgenic mouse. It is required for the metastasis of c-myc-induced mammary tumors, but is not necessary for c-myc-induced primary tumor formation or normal development. It is required for HER2/neu-induced tumor formation and maintenance of the cells' tumorigenic phenotype. It is over-expressed in aggressive subsets of ovary, colon, and breast carcinomas. HUNK interacts with synaptopodin, and may also play a role in synaptic plasticity. The HUNK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270972 [Multi-domain]  Cd Length: 262  Bit Score: 64.07  E-value: 6.98e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  723 NLVLGKTLGEGEFGKVVKAtafhLKGRAGyTTVAVKMLKENASPSE---LRDLLSEFNVLKQVNHPHVIKLYGACSQDGP 799
Cdd:cd14070    3 SYLIGRKLGEGSFAKVREG----LHAVTG-EKVAIKVIDKKKAKKDsyvTKNLRREGRIQQMIRHPNITQLLDILETENS 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  800 LLLIVEYAKYGSLRGFLRESRKvgpgylgsggsrnsssLDHPDERALTMgdlisfawQISQGMQYLAEMKLVHRDLAARN 879
Cdd:cd14070   78 YYLVMELCPGGNLMHRIYDKKR----------------LEEREARRYIR--------QLVSAVEHLHRAGVVHRDLKIEN 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  880 ILVAEGRKMKISDFGLSRDV----YEEDSYvkrSQGRIPVkWMAIESLFDHIYTTQSDVWSFGVLLWEIVTlGGNPYPGI 955
Cdd:cd14070  134 LLLDENDNIKLIDFGLSNCAgilgYSDPFS---TQCGSPA-YAAPELLARKKYGPKVDVWSIGVNMYAMLT-GTLPFTVE 208
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 10862703  956 PperlFNLLKTGHRM------ERPDNCSEEMYRLMLQCWKQEPDKRPVFADISKD 1004
Cdd:cd14070  209 P----FSLRALHQKMvdkemnPLPTDLSPGAISFLRSLLEPDPLKRPNIKQALAN 259
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
727-951 7.16e-11

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK3, also called Prk or Fnk (FGF-inducible kinase), regulates angiogenesis and responses to DNA damage. Activated PLK3 mediates Chk2 phosphorylation by ATM and the resulting checkpoint activation. PLK3 phosphorylates DNA polymerase delta and may be involved in DNA repair. It also inhibits Cdc25c, thereby regulating the onset of mitosis. The PLK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271091 [Multi-domain]  Cd Length: 255  Bit Score: 63.79  E-value: 7.16e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  727 GKTLGEGEFGKVVKATAFhlkgrAGYTTVAVKMLKEN--ASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIV 804
Cdd:cd14189    6 GRLLGKGGFARCYEMTDL-----ATNKTYAVKVIPHSrvAKPHQREKIVNEIELHRDLHHKHVVKFSHHFEDAENIYIFL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  805 EYAKYGSLrGFLRESRKVgpgylgsggsrnsssLDHPDERaltmgdliSFAWQISQGMQYLAEMKLVHRDLAARNILVAE 884
Cdd:cd14189   81 ELCSRKSL-AHIWKARHT---------------LLEPEVR--------YYLKQIISGLKYLHLKGILHRDLKLGNFFINE 136
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 10862703  885 GRKMKISDFGLSRDVYEEDSYVKRSQGrIPvKWMAIESLFDHIYTTQSDVWSFGVLLWEIvtLGGNP 951
Cdd:cd14189  137 NMELKVGDFGLAARLEPPEQRKKTICG-TP-NYLAPEVLLRQGHGPESDVWSLGCVMYTL--LCGNP 199
PTKc_Wee1 cd14051
Catalytic domain of the Protein Tyrosine Kinase, Wee1; PTKs catalyze the transfer of the ...
729-996 7.47e-11

Catalytic domain of the Protein Tyrosine Kinase, Wee1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Wee1 is a nuclear cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. There are two distinct Wee1 proteins in vertebrates showing different expression patterns, called Wee1a and Wee1b. They are functionally dstinct and are implicated in different steps of egg maturation and embryo development. The Wee1 subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270953 [Multi-domain]  Cd Length: 275  Bit Score: 64.35  E-value: 7.47e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  729 TLGEGEFGKVVKATAfHLKGragyttvAVKMLKENASPseLRDLLSEFNVLKQV-------NHPHVIKLYGACSQDGPLL 801
Cdd:cd14051    7 KIGSGEFGSVYKCIN-RLDG-------CVYAIKKSKKP--VAGSVDEQNALNEVyahavlgKHPHVVRYYSAWAEDDHMI 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  802 LIVEYAKYGSLRGFLRESRKVGpgylgsggsrnsssldhpdeRALTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNIL 881
Cdd:cd14051   77 IQNEYCNGGSLADAISENEKAG--------------------ERFSEAELKDLLLQVAQGLKYIHSQNLVHMDIKPGNIF 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  882 VA------------------EGRKM------KISDFGLSRDVyeEDSYVKRSQGRipvkWMAIESLF-DHIYTTQSDVWS 936
Cdd:cd14051  137 ISrtpnpvsseeeeedfegeEDNPEsnevtyKIGDLGHVTSI--SNPQVEEGDCR----FLANEILQeNYSHLPKADIFA 210
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  937 FGVLLWEIVtlGGNPYPGIPPErlFNLLKTGHrMERPDNCSEEMYRLMLQCWKQEPDKRP 996
Cdd:cd14051  211 LALTVYEAA--GGGPLPKNGDE--WHEIRQGN-LPPLPQCSPEFNELLRSMIHPDPEKRP 265
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
728-1025 8.89e-11

Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK7 (also called iodopsin kinase) belongs to the visual group of GRKs. It is primarily found in the retina and plays a role in the regulation of opsin light receptors. GRK7 is located in retinal cone outer segments and plays an important role in regulating photoresponse of the cones. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors, which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK7 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270758 [Multi-domain]  Cd Length: 286  Bit Score: 64.16  E-value: 8.89e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  728 KTLGEGEFGKVVKATAFHLKGRAGYTTVAVKMLKENASpsELRDLLsEFNVLKQVNHPHVIKLYGACSQDGPLLLIVEYA 807
Cdd:cd05607    8 RVLGKGGFGEVCAVQVKNTGQMYACKKLDKKRLKKKSG--EKMALL-EKEILEKVNSPFIVSLAYAFETKTHLCLVMSLM 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  808 KYGSLRgflresrkvgpgylgsggsrnsSSLDHPDERALTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNILVAEGRK 887
Cdd:cd05607   85 NGGDLK----------------------YHIYNVGERGIEMERVIFYSAQITCGILHLHSLKIVYRDMKPENVLLDDNGN 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  888 MKISDFGLSRDVYEEDSYVKRSQGRipvKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTlGGNPYpgipperlfnllktg 967
Cdd:cd05607  143 CRLSDLGLAVEVKEGKPITQRAGTN---GYMAPEILKEESYSYPVDWFAMGCSIYEMVA-GRTPF--------------- 203
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 10862703  968 hRMERPDNCSEEMYRLMLQcwKQEPDKRPVFADISKDLEKMMVKRRDYLDLAASTPSD 1025
Cdd:cd05607  204 -RDHKEKVSKEELKRRTLE--DEVKFEHQNFTEEAKDICRLFLAKKPENRLGSRTNDD 258
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
725-1001 9.59e-11

Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDKL2, also called p56 KKIAMRE, is expressed in testis, kidney, lung, and brain. It functions mainly in mature neurons and plays an important role in learning and memory. Inactivation of CDKL3, also called NKIAMRE (NKIATRE in rat), by translocation is associated with mild mental retardation. It has been reported that CDKL3 is lost in leukemic cells having a chromosome arm 5q deletion, and may contribute to the transformed phenotype. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL2/3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270836 [Multi-domain]  Cd Length: 286  Bit Score: 63.98  E-value: 9.59e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  725 VLGKtLGEGEFGKVVKAtafhlKGRAGYTTVAVKMLKENASPSELRDL-LSEFNVLKQVNHPHVIKLYGACSQDGPLLLI 803
Cdd:cd07846    5 NLGL-VGEGSYGMVMKC-----RHKETGQIVAIKKFLESEDDKMVKKIaMREIKMLKQLRHENLVNLIEVFRRKKRWYLV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  804 VEYAKygslRGFLRESRKVGPGylgsggsrnsssLDHPDERaltmgdliSFAWQISQGMQYLAEMKLVHRDLAARNILVA 883
Cdd:cd07846   79 FEFVD----HTVLDDLEKYPNG------------LDESRVR--------KYLFQILRGIDFCHSHNIIHRDIKPENILVS 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  884 EGRKMKISDFGLSR------DVYeeDSYVKRSQGRIPvkwmaiESLF-DHIYTTQSDVWSFGVLLWEIVTlgGNPY-PG- 954
Cdd:cd07846  135 QSGVVKLCDFGFARtlaapgEVY--TDYVATRWYRAP------ELLVgDTKYGKAVDVWAVGCLVTEMLT--GEPLfPGd 204
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 10862703  955 ----------------IPPER-LFNLLKTGHRMERPD------------NCSEEMYRLMLQCWKQEPDKRPVFADI 1001
Cdd:cd07846  205 sdidqlyhiikclgnlIPRHQeLFQKNPLFAGVRLPEvkeveplerrypKLSGVVIDLAKKCLHIDPDKRPSCSEL 280
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
856-1014 9.69e-11

Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase (also called MAPK14); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38alpha/MAPK14 is expressed in most tissues and is the major isoform involved in the immune and inflammatory response. It is the central p38 MAPK involved in myogenesis. It plays a role in regulating cell cycle check-point transition and promoting cell differentiation. p38alpha also regulates cell proliferation and death through crosstalk with the JNK pathway. Its substrates include MAPK activated protein kinase 2 (MK2), MK5, and the transcription factors ATF2 and Mitf. p38 kinases MAPKs, serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38alpha subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143382 [Multi-domain]  Cd Length: 345  Bit Score: 64.68  E-value: 9.69e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  856 WQISQGMQYLAEMKLVHRDLAARNILVAEGRKMKISDFGLSRDVYEE-DSYVKRSQGRIP---VKWMAieslfdhiYTTQ 931
Cdd:cd07877  127 YQILRGLKYIHSADIIHRDLKPSNLAVNEDCELKILDFGLARHTDDEmTGYVATRWYRAPeimLNWMH--------YNQT 198
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  932 SDVWSFGVLLWEIVTlGGNPYPG---IPPERLFNLLKTGHRMERPDNCSEEMYRLMLQCWKQEPDKRpvFADI------- 1001
Cdd:cd07877  199 VDIWSVGCIMAELLT-GRTLFPGtdhIDQLKLILRLVGTPGAELLKKISSESARNYIQSLTQMPKMN--FANVfiganpl 275
                        170
                 ....*....|....
gi 10862703 1002 SKD-LEKMMVKRRD 1014
Cdd:cd07877  276 AVDlLEKMLVLDSD 289
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
730-965 9.82e-11

Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase (IKK); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The IKK complex functions as a master regulator of Nuclear Factor-KappaB (NF-kB) proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. It is composed of two kinases, IKKalpha and IKKbeta, and the regulatory subunit IKKgamma or NEMO (NF-kB Essential MOdulator). IKKs facilitate the release of NF-kB dimers from an inactive state, allowing them to migrate to the nucleus where they regulate gene transcription. There are two IKK pathways that regulate NF-kB signaling, called the classical (involving IKKbeta and NEMO) and non-canonical (involving IKKalpha) pathways. The classical pathway regulates the majority of genes activated by NF-kB. The IKK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270891 [Multi-domain]  Cd Length: 289  Bit Score: 64.01  E-value: 9.82e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  730 LGEGEFGKVVKatafhLKGRAGYTTVAVKMLKENASPSE--LRDLLSEFNVLKQVNHPHVIKlygACSQDGPL------- 800
Cdd:cd13989    1 LGSGGFGYVTL-----WKHQDTGEYVAIKKCRQELSPSDknRERWCLEVQIMKKLNHPNVVS---ARDVPPELeklspnd 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  801 --LLIVEYAKYGSLRGFL-RESRKVGpgylgsggsrnsssldhpderaLTMGDLISFAWQISQGMQYLAEMKLVHRDLAA 877
Cdd:cd13989   73 lpLLAMEYCSGGDLRKVLnQPENCCG----------------------LKESEVRTLLSDISSAISYLHENRIIHRDLKP 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  878 RNI-LVAEGRKM--KISDFGLSRDVyEEDSYVKRSQGriPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTlGGNPY-P 953
Cdd:cd13989  131 ENIvLQQGGGRViyKLIDLGYAKEL-DQGSLCTSFVG--TLQYLAPELFESKKYTCTVDYWSFGTLAFECIT-GYRPFlP 206
                        250
                 ....*....|..
gi 10862703  954 GIPPERLFNLLK 965
Cdd:cd13989  207 NWQPVQWHGKVK 218
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
730-1035 1.13e-10

Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of fungal proteins with similarity to the AGC STKs, Saccharomyces cerevisiae YPK1 and Schizosaccharomyces pombe Gad8p. YPK1 is required for cell growth and acts as a downstream kinase in the sphingolipid-mediated signaling pathway of yeast. It also plays a role in efficient endocytosis and in the maintenance of cell wall integrity. Gad8p is a downstream target of Tor1p, the fission yeast homolog of mTOR. It plays a role in cell growth and sexual development. The YPK1-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270737 [Multi-domain]  Cd Length: 313  Bit Score: 64.13  E-value: 1.13e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  730 LGEGEFGKVVKatafhLKGRAGYTTVAVKMLKEN--ASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVEYA 807
Cdd:cd05585    2 IGKGSFGKVMQ-----VRKKDTSRIYALKTIRKAhiVSRSEVTHTLAERTVLAQVDCPFIVPLKFSFQSPEKLYLVLAFI 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  808 KYGSLRGFL-RESRkvgpgylgsggsrnsssLDHPDERALTMGDLISfawqisqgMQYLAEMKLVHRDLAARNILVAEGR 886
Cdd:cd05585   77 NGGELFHHLqREGR-----------------FDLSRARFYTAELLCA--------LECLHKFNVIYRDLKPENILLDYTG 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  887 KMKISDFGLSRDVYEEDSYVKRSQGrIPvKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTlggnpypGIPP-------ER 959
Cdd:cd05585  132 HIALCDFGLCKLNMKDDDKTNTFCG-TP-EYLAPELLLGHGYTKAVDWWTLGVLLYEMLT-------GLPPfydentnEM 202
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  960 LFNLLKTGHRMerPDNCSEEMYRLMLQCWKQEPDKR------------PVFADIskDLEKMMVKR---------RDYLD- 1017
Cdd:cd05585  203 YRKILQEPLRF--PDGFDRDAKDLLIGLLNRDPTKRlgyngaqeiknhPFFDQI--DWKRLLMKKiqppfkpavENAIDt 278
                        330       340
                 ....*....|....*....|....
gi 10862703 1018 ------LAASTPSDSLIYDDGLSE 1035
Cdd:cd05585  279 snfdeeFTREKPIDSVVDDSHLSE 302
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
728-957 1.17e-10

Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGK2 shows a more restricted distribution than SGK1 and is most abundantly expressed in epithelial tissues including kidney, liver, pancreas, and the choroid plexus of the brain. In vitro cellular assays show that SGK2 can stimulate the activity of ion channels, the glutamate transporter EEAT4, and the glutamate receptors, GluR6 and GLUR1. The SGK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270754 [Multi-domain]  Cd Length: 321  Bit Score: 64.22  E-value: 1.17e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  728 KTLGEGEFGKVVKAtafhlKGRAGYTTVAVKMLKENA--SPSELRDLLSEFNVL-KQVNHPHVIKLYGACSQDGPLLLIV 804
Cdd:cd05603    1 KVIGKGSFGKVLLA-----KRKCDGKFYAVKVLQKKTilKKKEQNHIMAERNVLlKNLKHPFLVGLHYSFQTSEKLYFVL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  805 EYAKYGSLRGFLRESRKvgpgylgsggsrnsssLDHPDERAltmgdlisFAWQISQGMQYLAEMKLVHRDLAARNILVAE 884
Cdd:cd05603   76 DYVNGGELFFHLQRERC----------------FLEPRARF--------YAAEVASAIGYLHSLNIIYRDLKPENILLDC 131
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 10862703  885 GRKMKISDFGLSRDVYEEDSYVKRSQGrIPvKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTlggnpypGIPP 957
Cdd:cd05603  132 QGHVVLTDFGLCKEGMEPEETTSTFCG-TP-EYLAPEVLRKEPYDRTVDWWCLGAVLYEMLY-------GLPP 195
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
731-995 1.26e-10

Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily contains uncharacterized STKs with similarity to the human protein designated as Yank1 or STK32A. The Yank1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270730 [Multi-domain]  Cd Length: 257  Bit Score: 63.04  E-value: 1.26e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  731 GEGEFGKVVKATAFHLKgragyTTVAVK-MLKENA-SPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVEYAK 808
Cdd:cd05578    9 GKGSFGKVCIVQKKDTK-----KMFAMKyMNKQKCiEKDSVRNVLNELEILQELEHPFLVNLWYSFQDEEDMYMVVDLLL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  809 YGSLRGFLRESRKVgpgylgsggsrnsssldhpDERALTMgdlisFAWQISQGMQYLAEMKLVHRDLAARNILVAEGRKM 888
Cdd:cd05578   84 GGDLRYHLQQKVKF-------------------SEETVKF-----YICEIVLALDYLHSKNIIHRDIKPDNILLDEQGHV 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  889 KISDFGLSRDVyEEDSYVKRSQGRIPvkWMAIESLFDHIYTTQSDVWSFGVLLWEIVTlGGNPYPGI---PPERLFNLLK 965
Cdd:cd05578  140 HITDFNIATKL-TDGTLATSTSGTKP--YMAPEVFMRAGYSFAVDWWSLGVTAYEMLR-GKRPYEIHsrtSIEEIRAKFE 215
                        250       260       270
                 ....*....|....*....|....*....|
gi 10862703  966 TgHRMERPDNCSEEMYRLMLQCWKQEPDKR 995
Cdd:cd05578  216 T-ASVLYPAGWSEEAIDLINKLLERDPQKR 244
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
730-946 1.29e-10

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK12 is also called Cdc2-related protein kinase 7 (CRK7) or Cdc2-related kinase arginine/serine-rich (CrkRS). It is a unique CDK that contains an RS domain, which is predominantly found in splicing factors. CDK12 is widely expressed in tissues. It interacts with cyclins L1 and L2, and plays roles in regulating transcription and alternative splicing. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK12 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270847 [Multi-domain]  Cd Length: 302  Bit Score: 63.67  E-value: 1.29e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  730 LGEGEFGKVVKATAFHLKGRAGYTTVAVKMLKENASPSELRdllsEFNVLKQVNHPHVIKLYGACSQD----------GP 799
Cdd:cd07864   15 IGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGFPITAIR----EIKILRQLNHRSVVNLKEIVTDKqdaldfkkdkGA 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  800 LLLIVEYAKYgSLRGFLrESRKVgpgylgsggsrnssslDHPDERaltmgdLISFAWQISQGMQYLAEMKLVHRDLAARN 879
Cdd:cd07864   91 FYLVFEYMDH-DLMGLL-ESGLV----------------HFSEDH------IKSFMKQLLEGLNYCHKKNFLHRDIKCSN 146
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 10862703  880 ILVAEGRKMKISDFGLSRdVYEEDSYVKRSQGRIPVKWMAIESLF-DHIYTTQSDVWSFGVLLWEIVT 946
Cdd:cd07864  147 ILLNNKGQIKLADFGLAR-LYNSEESRPYTNKVITLWYRPPELLLgEERYGPAIDVWSCGCILGELFT 213
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
728-954 1.94e-10

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK5 is widely expressed in many tissues. It associates with the membrane though an N-terminal PIP2 binding domain and also binds phospholipids via its C-terminus. GRK5 deficiency is associated with early Alzheimer's disease in humans and mouse models. GRK5 also plays a crucial role in the pathogenesis of sporadic Parkinson's disease. It participates in the regulation and desensitization of PDGFRbeta, a receptor tyrosine kinase involved in a variety of downstream cellular effects including cell growth, chemotaxis, apoptosis, and angiogenesis. GRK5 also regulates Toll-like receptor 4, which is involved in innate and adaptive immunity. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270780 [Multi-domain]  Cd Length: 313  Bit Score: 63.45  E-value: 1.94e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  728 KTLGEGEFGKVVKATAfhlkgRAGYTTVAVKMLKENASPSELRD--LLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVE 805
Cdd:cd05632    8 RVLGKGGFGEVCACQV-----RATGKMYACKRLEKKRIKKRKGEsmALNEKQILEKVNSQFVVNLAYAYETKDALCLVLT 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  806 YAKYGSLRGFLRESRKvgPGYlgsggsrnsssldhPDERALTmgdlisFAWQISQGMQYLAEMKLVHRDLAARNILVAEG 885
Cdd:cd05632   83 IMNGGDLKFHIYNMGN--PGF--------------EEERALF------YAAEILCGLEDLHRENTVYRDLKPENILLDDY 140
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  886 RKMKISDFGLSRDVYEEDSYvkrsQGRI-PVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTlGGNPYPG 954
Cdd:cd05632  141 GHIRISDLGLAVKIPEGESI----RGRVgTVGYMAPEVLNNQRYTLSPDYWGLGCLIYEMIE-GQSPFRG 205
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
853-951 1.95e-10

Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the MAPKs MPK1 from Saccharomyces cerevisiae, Pmk1 from Schizosaccharomyces pombe, and similar proteins. MPK1 (also called Slt2) and Pmk1 (also called Spm1) are stress-activated MAPKs that regulate the cell wall integrity pathway, and are therefore important in the maintainance of cell shape, cell wall construction, morphogenesis, and ion homeostasis. MPK1 is activated in response to cell wall stress including heat stimulation, osmotic shock, UV irradiation, and any agents that interfere with cell wall biogenesis such as chitin antagonists, caffeine, or zymolase. MPK1 is regulated by the MAP2Ks Mkk1/2, which are regulated by the MAP3K Bck1. Pmk1 is also activated by multiple stresses including elevated temperatures, hyper- or hypotonic stress, glucose deprivation, exposure to cell-wall damaging compounds, and oxidative stress. It is regulated by the MAP2K Pek1, which is regulated by the MAP3K Mkh1. MAPKs are important mediators of cellular responses to extracellular signals. The MPK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173750 [Multi-domain]  Cd Length: 332  Bit Score: 63.58  E-value: 1.95e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  853 SFAWQISQGMQYLAEMKLVHRDLAARNILVAEGRKMKISDFGLSR----DVYEEDSYVKrsqGRIPVKWM-AIESLFDHI 927
Cdd:cd07857  109 SFIYQILCGLKYIHSANVLHRDLKPGNLLVNADCELKICDFGLARgfseNPGENAGFMT---EYVATRWYrAPEIMLSFQ 185
                         90       100
                 ....*....|....*....|....*
gi 10862703  928 -YTTQSDVWSFGVLLWEIvtLGGNP 951
Cdd:cd07857  186 sYTKAIDVWSVGCILAEL--LGRKP 208
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
708-965 1.95e-10

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK4 regulates cell morphology and cytoskeletal organization. It is essential for embryonic viability and proper neural development. Mice lacking PAK4 die due to defects in the fetal heart. In addition, their spinal cord motor neurons showed failure to differentiate and migrate. PAK4 also plays a role in cell survival and tumorigenesis. It is overexpressed in many primary tumors including colon, esophageal, and mammary tumors. PAK4 has also been implicated in viral and bacterial infection pathways. PAK4 belongs to the group II PAKs, which contain a PBD (p21-binding domain) and a C-terminal catalytic domain, but do not harbor an AID (autoinhibitory domain) or SH3 binding sites. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132988 [Multi-domain]  Cd Length: 292  Bit Score: 63.12  E-value: 1.95e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  708 AFKILEDPKweFPRKNLVLGKTLGEGEFGKVVKATAfhlkgRAGYTTVAVKmlKENASPSELRDLL-SEFNVLKQVNHPH 786
Cdd:cd06657    8 ALQMVVDPG--DPRTYLDNFIKIGEGSTGIVCIATV-----KSSGKLVAVK--KMDLRKQQRRELLfNEVVIMRDYQHEN 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  787 VIKLYGACSQDGPLLLIVEYAKYGSLRGFLRESRkvgpgylgsggsrnsssldhpderaLTMGDLISFAWQISQGMQYLA 866
Cdd:cd06657   79 VVEMYNSYLVGDELWVVMEFLEGGALTDIVTHTR-------------------------MNEEQIAAVCLAVLKALSVLH 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  867 EMKLVHRDLAARNILVAEGRKMKISDFGLSRDVYEEdsyVKRSQGRIPVK-WMAIESLFDHIYTTQSDVWSFGVLLWEIV 945
Cdd:cd06657  134 AQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKE---VPRRKSLVGTPyWMAPELISRLPYGPEVDIWSLGIMVIEMV 210
                        250       260
                 ....*....|....*....|
gi 10862703  946 TlGGNPYPGIPPERLFNLLK 965
Cdd:cd06657  211 D-GEPPYFNEPPLKAMKMIR 229
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
728-949 2.33e-10

Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKDs are important regulators of many intracellular signaling pathways such as ERK and JNK, and cellular processes including the organization of the trans-Golgi network, membrane trafficking, cell proliferation, migration, and apoptosis. They contain N-terminal cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. Mammals harbor three types of PKDs: PKD1 (or PKCmu), PKD2, and PKD3 (or PKCnu). PKDs are activated in a PKC-dependent manner by many agents including diacylglycerol (DAG), PDGF, neuropeptides, oxidative stress, and tumor-promoting phorbol esters, among others. The PKD subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270984 [Multi-domain]  Cd Length: 260  Bit Score: 62.43  E-value: 2.33e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  728 KTLGEGEFGKVVKATAFHlKGRAgyttVAVKML-KENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVEY 806
Cdd:cd14082    9 EVLGSGQFGIVYGGKHRK-TGRD----VAIKVIdKLRFPTKQESQLRNEVAILQQLSHPGVVNLECMFETPERVFVVMEK 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  807 AKYGSLRGFLRESRkvgpGYLgsggsrnsssldhpDERALTMgdLISfawQISQGMQYLAEMKLVHRDLAARNILVAEGR 886
Cdd:cd14082   84 LHGDMLEMILSSEK----GRL--------------PERITKF--LVT---QILVALRYLHSKNIVHCDLKPENVLLASAE 140
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 10862703  887 ---KMKISDFGLSRdVYEEDSYvKRSQGRIPVkWMAIESLFDHIYTTQSDVWSFGVLLWeiVTLGG 949
Cdd:cd14082  141 pfpQVKLCDFGFAR-IIGEKSF-RRSVVGTPA-YLAPEVLRNKGYNRSLDMWSVGVIIY--VSLSG 201
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
721-995 2.45e-10

Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related Apoptosis-inducing protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DRAKs were named based on their similarity (around 50% identity) to the kinase domain of DAPKs. They contain an N-terminal kinase domain and a C-terminal regulatory domain. Vertebrates contain two subfamily members, DRAK1 (also called STK17A) and DRAK2. Both DRAKs are localized to the nucleus, autophosphorylate themselves, and phosphorylate myosin light chain as a substrate. Rabbit DRAK1 has been shown to induce apoptosis in osteoclasts and overexpressio of human DRAK1 induces apoptosis in cultured fibroblast cells. DRAK1 may be involved in apoptotic signaling. The DRAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271099 [Multi-domain]  Cd Length: 271  Bit Score: 62.65  E-value: 2.45e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  721 RKNLVLGKTLGEGEFGKVVKAtafhLKGRAGYTTVAVKMLKENASPSELRDLLSEFNVLKQVN-HPHVIKLYGACSQDGP 799
Cdd:cd14197    8 RYSLSPGRELGRGKFAVVRKC----VEKDSGKEFAAKFMRKRRKGQDCRMEIIHEIAVLELAQaNPWVINLHEVYETASE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  800 LLLIVEYAKYGSLRGFLRESRkvgpgylgsggsrnsssldhpdERALTMGDLISFAWQISQGMQYLAEMKLVHRDLAARN 879
Cdd:cd14197   84 MILVLEYAAGGEIFNQCVADR----------------------EEAFKEKDVKRLMKQILEGVSFLHNNNVVHLDLKPQN 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  880 ILVAEGRKM---KISDFGLSRDVyeEDSYVKRSQGRIPvKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTlGGNPYPGIP 956
Cdd:cd14197  142 ILLTSESPLgdiKIVDFGLSRIL--KNSEELREIMGTP-EYVAPEILSYEPISTATDMWSIGVLAYVMLT-GISPFLGDD 217
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 10862703  957 PERLF---NLLKTGHRMERPDNCSEEMYRLMLQCWKQEPDKR 995
Cdd:cd14197  218 KQETFlniSQMNVSYSEEEFEHLSESAIDFIKTLLIKKPENR 259
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
717-951 2.62e-10

Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase (also called MAPK12); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38gamma/MAPK12 is predominantly expressed in skeletal muscle. Unlike p38alpha and p38beta, p38gamma is insensitive to pyridinylimidazoles. It displays an antagonizing function compared to p38alpha. p38gamma inhibits, while p38alpha stimulates, c-Jun phosphorylation and AP-1 mediated transcription. p38gamma also plays a role in the signaling between Ras and the estrogen receptor and has been implicated to increase cell invasion and breast cancer progression. In Xenopus, p38gamma is critical in the meiotic maturation of oocytes. p38 kinases are MAPKs, serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38gamma subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143385 [Multi-domain]  Cd Length: 343  Bit Score: 63.43  E-value: 2.62e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  717 WEFPRKNLVLgKTLGEGEFGKVVKAtafhLKGRAGyTTVAVKMLKENASpSEL--RDLLSEFNVLKQVNHPHVIKLYGAC 794
Cdd:cd07880   11 WEVPDRYRDL-KQVGSGAYGTVCSA----LDRRTG-AKVAIKKLYRPFQ-SELfaKRAYRELRLLKHMKHENVIGLLDVF 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  795 SQDGPL------LLIVEYAkyGSLRGFLRESRKVGPgylgsggsrnsssldhpderaltmgDLISF-AWQISQGMQYLAE 867
Cdd:cd07880   84 TPDLSLdrfhdfYLVMPFM--GTDLGKLMKHEKLSE-------------------------DRIQFlVYQMLKGLKYIHA 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  868 MKLVHRDLAARNILVAEGRKMKISDFGLSRDVYEE-DSYVKRSQGRIP---VKWMAieslfdhiYTTQSDVWSFGVLLWE 943
Cdd:cd07880  137 AGIIHRDLKPGNLAVNEDCELKILDFGLARQTDSEmTGYVVTRWYRAPeviLNWMH--------YTQTVDIWSVGCIMAE 208

                 ....*...
gi 10862703  944 IVTlgGNP 951
Cdd:cd07880  209 MLT--GKP 214
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
725-954 2.74e-10

Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MOK, also called Renal tumor antigen 1 (RAGE-1), is widely expressed and is enriched in testis, kidney, lung, and brain. It is expressed in approximately 50% of renal cell carcinomas (RCC) and is a potential target for immunotherapy. MOK is stabilized by its association with the HSP90 molecular chaperone. It is induced by the transcription factor Cdx2 and may be involved in regulating intestinal epithelial development and differentiation. The MOK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270825 [Multi-domain]  Cd Length: 282  Bit Score: 62.67  E-value: 2.74e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  725 VLGKtLGEGEFGKVVKATAFhlkgRAGyTTVAVKMLKENASPSELRDLLSEFNVLKQVN-HPHVIKL----YGACSqdGP 799
Cdd:cd07831    3 ILGK-IGEGTFSEVLKAQSR----KTG-KYYAIKCMKKHFKSLEQVNNLREIQALRRLSpHPNILRLievlFDRKT--GR 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  800 LLLIVEYAKyGSLRGFLRESRKvgpgYLgsggsrnsssldhPDERALtmgdliSFAWQISQGMQYLAEMKLVHRDLAARN 879
Cdd:cd07831   75 LALVFELMD-MNLYELIKGRKR----PL-------------PEKRVK------NYMYQLLKSLDHMHRNGIFHRDIKPEN 130
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 10862703  880 ILVAEGRkMKISDFGLSRDVYEEDSYVKrsqgRIPVKWM-AIESLF-DHIYTTQSDVWSFGVLLWEIVTLggNP-YPG 954
Cdd:cd07831  131 ILIKDDI-LKLADFGSCRGIYSKPPYTE----YISTRWYrAPECLLtDGYYGPKMDIWAVGCVFFEILSL--FPlFPG 201
STKc_BMPR1 cd14144
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type I Receptor; ...
728-1008 2.80e-10

Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type I Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR1 functions as a receptor for morphogenetic proteins (BMPs), which are involved in the regulation of cell proliferation, survival, differentiation, and apoptosis. BMPs are able to induce bone, cartilage, ligament, and tendon formation, and may play roles in bone diseases and tumors. Vertebrates contain two type I BMP receptors, BMPR1a and BMPR1b. BMPR1 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that also includes TGFbeta, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like BMPR1, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The BMPR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271046 [Multi-domain]  Cd Length: 287  Bit Score: 62.49  E-value: 2.80e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  728 KTLGEGEFGKVVKAtafhlKGRAGYttVAVKMLKENASPSELRD-------LLSEFNVLKQVNHPhvIKLYGACSQdgpL 800
Cdd:cd14144    1 RSVGKGRYGEVWKG-----KWRGEK--VAVKIFFTTEEASWFREteiyqtvLMRHENILGFIAAD--IKGTGSWTQ---L 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  801 LLIVEYAKYGSLRGFLRESrkvgpgylgsggsrnsssldhpderALTMGDLISFAWQISQGMQYL-AEM-------KLVH 872
Cdd:cd14144   69 YLITDYHENGSLYDFLRGN-------------------------TLDTQSMLKLAYSAACGLAHLhTEIfgtqgkpAIAH 123
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  873 RDLAARNILVAEGRKMKISDFGLSRDVYEEDSYVKRSQG-RIPVK-WMAIESL--------FDHIytTQSDVWSFGVLLW 942
Cdd:cd14144  124 RDIKSKNILVKKNGTCCIADLGLAVKFISETNEVDLPPNtRVGTKrYMAPEVLdeslnrnhFDAY--KMADMYSFGLVLW 201
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  943 EI----VTLG-----GNPY-PGIPPERLFNLLKTGHRME--RP--------DNCSEEMYRLMLQCWKQEPDKRPVFADIS 1002
Cdd:cd14144  202 EIarrcISGGiveeyQLPYyDAVPSDPSYEDMRRVVCVErrRPsipnrwssDEVLRTMSKLMSECWAHNPAARLTALRVK 281

                 ....*.
gi 10862703 1003 KDLEKM 1008
Cdd:cd14144  282 KTLGKL 287
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
727-946 3.47e-10

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK3 is a MAPK kinase kinase (MAPKKK or MKKK), that phosphorylates and activates the MAPK kinase MEK5 (or MKK5), which in turn phosphorylates and activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK3 plays an essential role in embryonic angiogenesis and early heart development. In addition, MEKK3 is involved in interleukin-1 receptor and Toll-like receptor 4 signaling. It is also a specific regulator of the proinflammatory cytokines IL-6 and GM-CSF in some immune cells. MEKK3 also regulates calcineurin, which plays a critical role in T cell activation, apoptosis, skeletal myocyte differentiation, and cardiac hypertrophy. The MEKK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270817 [Multi-domain]  Cd Length: 271  Bit Score: 62.02  E-value: 3.47e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  727 GKTLGEGEFGKVvkatafHL--KGRAGYTTVAVKMLKENASPS---ELRDLLSEFNVLKQVNHPHVIKLYGACSQDG--P 799
Cdd:cd06651   12 GKLLGQGAFGRV------YLcyDVDTGRELAAKQVQFDPESPEtskEVSALECEIQLLKNLQHERIVQYYGCLRDRAekT 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  800 LLLIVEYAKYGSLRGFLRESRkvgpgylgsggsrnsssldhpderALTMGDLISFAWQISQGMQYLAEMKLVHRDLAARN 879
Cdd:cd06651   86 LTIFMEYMPGGSVKDQLKAYG------------------------ALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGAN 141
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 10862703  880 ILVAEGRKMKISDFGLSRDVYE--EDSYVKRSQGRIPVkWMAIESLFDHIYTTQSDVWSFGVLLWEIVT 946
Cdd:cd06651  142 ILRDSAGNVKLGDFGASKRLQTicMSGTGIRSVTGTPY-WMSPEVISGEGYGRKADVWSLGCTVVEMLT 209
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
730-995 3.63e-10

Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Schizosaccharomyces pombe Pat1 (also called Ran1), Saccharomyces cerevisiae VHS1 and KSP1, and similar fungal STKs. Pat1 blocks Mei2, an RNA-binding protein which is indispensable in the initiation of meiosis. Pat1 is inactivated and Mei2 activated, which initiates meiosis, under nutrient-deprived conditions through a signaling cascade involving Ste11. Meiosis induced by Pat1 inactivation may show different characteristics than normal meiosis including aberrant positioning of centromeres. VHS1 was identified in a screen for suppressors of cell cycle arrest at the G1/S transition, while KSP1 may be involved in regulating PRP20, which is required for mRNA export and maintenance of nuclear structure. The Pat1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270895 [Multi-domain]  Cd Length: 267  Bit Score: 61.98  E-value: 3.63e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  730 LGEGEFGKVVKATAFHLKgragyTTVAVKMLK------ENASPSELRDLLSEFNVLKQV-NHPHVIKLYGACSQDGPLLL 802
Cdd:cd13993    8 IGEGAYGVVYLAVDLRTG-----RKYAIKCLYksgpnsKDGNDFQKLPQLREIDLHRRVsRHPNIITLHDVFETEVAIYI 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  803 IVEYAKYGSLRGFLRESRkvgpgylgsggsrnsssldhpdeRALTMGDLI-SFAWQISQGMQYLAEMKLVHRDLAARNIL 881
Cdd:cd13993   83 VLEYCPNGDLFEAITENR-----------------------IYVGKTELIkNVFLQLIDAVKHCHSLGIYHRDIKPENIL 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  882 VA-EGRKMKISDFGLSrdvyeEDSYVKRSQGRIPVKWMAIEsLFDHI-------YTTQSDVWSFGVLLWEIvTLGGNPYP 953
Cdd:cd13993  140 LSqDEGTVKLCDFGLA-----TTEKISMDFGVGSEFYMAPE-CFDEVgrslkgyPCAAGDIWSLGIILLNL-TFGRNPWK 212
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 10862703  954 GIPPERLFNLLKTGHRMERPD---NCSEEMYRLMLQCWKQEPDKR 995
Cdd:cd13993  213 IASESDPIFYDYYLNSPNLFDvilPMSDDFYNLLRQIFTVNPNNR 257
STKc_TGFbR2_like cd14055
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II ...
728-995 3.76e-10

Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TGFbR2 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. Type II receptors, such as TGFbR2, are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. TGFbR2 acts as the receptor for TGFbeta, which is crucial in growth control and homeostasis in many different tissues. It plays roles in regulating apoptosis and in maintaining the balance between self renewal and cell loss. It also plays a key role in maintaining vascular integrity and in regulating responses to genotoxic stress. Mutations in TGFbR2 can cause aortic aneurysm disorders such as Loeys-Dietz and Marfan syndromes. The TGFbR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270957 [Multi-domain]  Cd Length: 295  Bit Score: 62.39  E-value: 3.76e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  728 KTLGEGEFGKVVKAtafHLKGRAG--YTTVAVKM--LKENASPSELRDLLSEFNVlkqvNHPHVIKLYGA----CSQDGP 799
Cdd:cd14055    1 KLVGKGRFAEVWKA---KLKQNASgqYETVAVKIfpYEEYASWKNEKDIFTDASL----KHENILQFLTAeergVGLDRQ 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  800 LLLIVEYAKYGSLRGFLREsrkvgpgylgsggsrnsssldhpdeRALTMGDLISFAWQISQGMQYL---------AEMKL 870
Cdd:cd14055   74 YWLITAYHENGSLQDYLTR-------------------------HILSWEDLCKMAGSLARGLAHLhsdrtpcgrPKIPI 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  871 VHRDLAARNILVAEGRKMKISDFGLSRDV---YEEDSYVKRSQGRIPvKWMAIESLFDHIYTT------QSDVWSFGVLL 941
Cdd:cd14055  129 AHRDLKSSNILVKNDGTCVLADFGLALRLdpsLSVDELANSGQVGTA-RYMAPEALESRVNLEdlesfkQIDVYSMALVL 207
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 10862703  942 WEIVT---LGGNPYPGIPP-----------ERLFNLLKtgHRMERPD-----NCSEEMYRL---MLQCWKQEPDKR 995
Cdd:cd14055  208 WEMASrceASGEVKPYELPfgskvrerpcvESMKDLVL--RDRGRPEipdswLTHQGMCVLcdtITECWDHDPEAR 281
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
728-952 4.14e-10

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK4 has a limited tissue distribution. It is mainly found in the testis, but is also present in the cerebellum and kidney. It is expressed as multiple splice variants with different domain architectures and is post-translationally palmitoylated and localized in the membrane. GRK4 polymorphisms are associated with hypertension and salt sensitivity, as they cause hyperphosphorylation, desensitization, and internalization of the dopamine 1 (D1) receptor while increasing the expression of the angiotensin II type 1 receptor. GRK4 plays a crucial role in the D1 receptor regulation of sodium excretion and blood pressure. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173720 [Multi-domain]  Cd Length: 285  Bit Score: 61.93  E-value: 4.14e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  728 KTLGEGEFGKV----VKATafhlkgraGYTTVAVKMLKENASPSELRDL-LSEFNVLKQVNHPHVIKLYGACSQDGPLLL 802
Cdd:cd05631    6 RVLGKGGFGEVcacqVRAT--------GKMYACKKLEKKRIKKRKGEAMaLNEKRILEKVNSRFVVSLAYAYETKDALCL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  803 IVEYAKYGSLRGFLRESRKvgPGYlgsggsrnsssldhPDERAltmgdlISFAWQISQGMQYLAEMKLVHRDLAARNILV 882
Cdd:cd05631   78 VLTIMNGGDLKFHIYNMGN--PGF--------------DEQRA------IFYAAELCCGLEDLQRERIVYRDLKPENILL 135
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 10862703  883 AEGRKMKISDFGLSRDVYEEDsyvkRSQGRI-PVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTlGGNPY 952
Cdd:cd05631  136 DDRGHIRISDLGLAVQIPEGE----TVRGRVgTVGYMAPEVINNEKYTFSPDWWGLGCLIYEMIQ-GQSPF 201
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
728-961 6.46e-10

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-eta is predominantly expressed in squamous epithelia, where it plays a crucial role in the signaling of cell-type specific differentiation. It is also expressed in pro-B cells and early-stage thymocytes, and acts as a key regulator in early B-cell development. PKC-eta increases glioblastoma multiforme (GBM) proliferation and resistance to radiation, and is being developed as a therapeutic target for the management of GBM. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC-eta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270742 [Multi-domain]  Cd Length: 323  Bit Score: 61.85  E-value: 6.46e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  728 KTLGEGEFGKVVKAtafhlKGRAGYTTVAVKMLKENA--SPSELRDLLSEFNVLKQV-NHPHVIKLYGACSQDGPLLLIV 804
Cdd:cd05590    1 RVLGKGSFGKVMLA-----RLKESGRLYAVKVLKKDVilQDDDVECTMTEKRILSLArNHPFLTQLYCCFQTPDRLFFVM 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  805 EYAKYGSLRGFLRESRKvgpgylgsggsrnsssLDHPDERAltmgdlisFAWQISQGMQYLAEMKLVHRDLAARNILVAE 884
Cdd:cd05590   76 EFVNGGDLMFHIQKSRR----------------FDEARARF--------YAAEITSALMFLHDKGIIYRDLKLDNVLLDH 131
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 10862703  885 GRKMKISDFGLSRDVYEEDSYVKRSQGrIPvKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTlGGNPYPGIPPERLF 961
Cdd:cd05590  132 EGHCKLADFGMCKEGIFNGKTTSTFCG-TP-DYIAPEILQEMLYGPSVDWWAMGVLLYEMLC-GHAPFEAENEDDLF 205
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
728-995 6.51e-10

Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PKC beta isoforms (I and II), generated by alternative splicing of a single gene, are preferentially activated by hyperglycemia-induced DAG (1,2-diacylglycerol) in retinal tissues. This is implicated in diabetic microangiopathy such as ischemia, neovascularization, and abnormal vasodilator function. PKC-beta also plays an important role in VEGF signaling. In addition, glucose regulates proliferation in retinal endothelial cells via PKC-betaI. PKC-beta is also being explored as a therapeutic target in cancer. It contributes to tumor formation and is involved in the tumor host mechanisms of inflammation and angiogenesis. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. PKCs undergo three phosphorylations in order to take mature forms. In addition, cPKCs depend on calcium, DAG, and in most cases, phosphatidylserine (PS) for activation. The cPKC-beta subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270767 [Multi-domain]  Cd Length: 323  Bit Score: 61.94  E-value: 6.51e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  728 KTLGEGEFGKVVkatafhLKGRAGYTTV-AVKMLKENA--SPSELRDLLSEFNVLKQVNHPHVIKLYGACSQD-GPLLLI 803
Cdd:cd05616    6 MVLGKGSFGKVM------LAERKGTDELyAVKILKKDVviQDDDVECTMVEKRVLALSGKPPFLTQLHSCFQTmDRLYFV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  804 VEYAKYGSLrgfLRESRKVGpgylgsggsrnssSLDHPDEraltmgdlISFAWQISQGMQYLAEMKLVHRDLAARNILVA 883
Cdd:cd05616   80 MEYVNGGDL---MYHIQQVG-------------RFKEPHA--------VFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLD 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  884 EGRKMKISDFGLSRDVYEEDSYVKRSQGrIPvKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTlGGNPYPGIPPERLFNL 963
Cdd:cd05616  136 SEGHIKIADFGMCKENIWDGVTTKTFCG-TP-DYIAPEIIAYQPYGKSVDWWAFGVLLYEMLA-GQAPFEGEDEDELFQS 212
                        250       260       270
                 ....*....|....*....|....*....|..
gi 10862703  964 LKTgHRMERPDNCSEEMYRLMLQCWKQEPDKR 995
Cdd:cd05616  213 IME-HNVAYPKSMSKEAVAICKGLMTKHPGKR 243
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
728-1004 6.76e-10

Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein kinase subfamily 2, group 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The SnRKs form three different subfamilies designated SnRK1-3. SnRK2 is represented in this cd. SnRK2s are involved in plant response to abiotic stresses and abscisic acid (ABA)-dependent plant development. The SnRK2s subfamily is in turn classed into three subgroups, all 3 of which are represented in this CD. Group 1 comprises kinases not activated by ABA, group 2 - kinases not activated or activated very weakly by ABA (depending on plant species), and group 3 - kinases strongly activated by ABA. The SnRKs belong to a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271135 [Multi-domain]  Cd Length: 257  Bit Score: 61.15  E-value: 6.76e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  728 KTLGEGEFGkvvkaTAFHLKGRAGYTTVAVKMLKENASPSE--LRDLLSEfnvlKQVNHPHVIKLYGACSQDGPLLLIVE 805
Cdd:cd14665    6 KDIGSGNFG-----VARLMRDKQTKELVAVKYIERGEKIDEnvQREIINH----RSLRHPNIVRFKEVILTPTHLAIVME 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  806 YAKYGSLRgflreSRKVGPGYLGSggsrnsssldhpDERALTMGDLISfawqisqGMQYLAEMKLVHRDLAARNILV--A 883
Cdd:cd14665   77 YAAGGELF-----ERICNAGRFSE------------DEARFFFQQLIS-------GVSYCHSMQICHRDLKLENTLLdgS 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  884 EGRKMKISDFGLSRdvyeedSYVKRSQGRIPV---KWMAIESLFDHIYTTQ-SDVWSFGVLLWeiVTLGGnPYPGIPPER 959
Cdd:cd14665  133 PAPRLKICDFGYSK------SSVLHSQPKSTVgtpAYIAPEVLLKKEYDGKiADVWSCGVTLY--VMLVG-AYPFEDPEE 203
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 10862703  960 LFNLLKTGHRM-----ERPD--NCSEEMYRLMLQCWKQEPDKRPVFADISKD 1004
Cdd:cd14665  204 PRNFRKTIQRIlsvqySIPDyvHISPECRHLISRIFVADPATRITIPEIRNH 255
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
728-966 7.24e-10

Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PFTAIRE-1 is widely expressed except in the spleen and thymus. It is highly expressed in the brain, heart, pancreas, testis, and ovary, and is localized in the cytoplasm. It is regulated by cyclin D3 and is inhibited by the p21 cell cycle inhibitor. It has also been shown to interact with the membrane-associated cyclin Y, which recruits the protein to the plasma membrane. PFTAIRE-1 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PFTAIRE-1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143374 [Multi-domain]  Cd Length: 303  Bit Score: 61.63  E-value: 7.24e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  728 KTLGEGEFgkvvkATAFHLKGRAGYTTVAVKMLKENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVEYA 807
Cdd:cd07869   11 EKLGEGSY-----ATVYKGKSKVNGKLVALKVIRLQEEEGTPFTAIREASLLKGLKHANIVLLHDIIHTKETLTLVFEYV 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  808 kYGSLRGFLRESrkvgPGYLgsggsrnsssldHPDERALtmgdlisFAWQISQGMQYLAEMKLVHRDLAARNILVAEGRK 887
Cdd:cd07869   86 -HTDLCQYMDKH----PGGL------------HPENVKL-------FLFQLLRGLSYIHQRYILHRDLKPQNLLISDTGE 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  888 MKISDFGLSR-DVYEEDSYvkrSQGRIPVKWMAIESLFDHI-YTTQSDVWSFGVLLWEIVTlGGNPYPGIPP-----ERL 960
Cdd:cd07869  142 LKLADFGLARaKSVPSHTY---SNEVVTLWYRPPDVLLGSTeYSTCLDMWGVGCIFVEMIQ-GVAAFPGMKDiqdqlERI 217

                 ....*.
gi 10862703  961 FNLLKT 966
Cdd:cd07869  218 FLVLGT 223
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
731-945 9.01e-10

Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of receptors for the TGFbeta family of secreted signaling molecules including TGFbeta, bone morphogenetic proteins (BMPs), activins, growth and differentiation factors (GDFs), and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. There are two types of TGFbeta receptors included in this subfamily, I and II, that play different roles in signaling. For signaling to occur, the ligand first binds to the high-affinity type II receptor, which is followed by the recruitment of the low-affinity type I receptor to the complex and its activation through trans-phosphorylation by the type II receptor. The active type I receptor kinase starts intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. Different ligands interact with various combinations of types I and II receptors to elicit a specific signaling pathway. Activins primarily signal through combinations of ACVR1b/ALK7 and ACVR2a/b; myostatin and GDF11 through TGFbR1/ALK4 and ACVR2a/b; BMPs through ACVR1/ALK1 and BMPR2; and TGFbeta through TGFbR1 and TGFbR2. The TGFbR-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270900 [Multi-domain]  Cd Length: 289  Bit Score: 61.30  E-value: 9.01e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  731 GEGEFGKVVKATafhLKGRagytTVAVKMLkenaSPSELRDLLSEFNVLKQVN--HPHVIKLYGACSQDGP----LLLIV 804
Cdd:cd13998    4 GKGRFGEVWKAS---LKNE----PVAVKIF----SSRDKQSWFREKEIYRTPMlkHENILQFIAADERDTAlrteLWLVT 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  805 EYAKYGSLRGFLRESrkvgpgylgsggsrnsssldhpderALTMGDLISFAWQISQGMQYLAE---------MKLVHRDL 875
Cdd:cd13998   73 AFHPNGSL*DYLSLH-------------------------TIDWVSLCRLALSVARGLAHLHSeipgctqgkPAIAHRDL 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  876 AARNILVAEGRKMKISDFGLS----RDVYEEDsyvKRSQGRIPVK-WMAIESL-----FDHIYT-TQSDVWSFGVLLWEI 944
Cdd:cd13998  128 KSKNILVKNDGTCCIADFGLAvrlsPSTGEED---NANNGQVGTKrYMAPEVLegainLRDFESfKRVDIYAMGLVLWEM 204

                 .
gi 10862703  945 V 945
Cdd:cd13998  205 A 205
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
730-952 9.23e-10

Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. A splice variant of TLK1, called TLK1B, is expressed in the presence of double strand breaks (DSBs). It lacks the N-terminal part of TLK1, but is expected to phosphorylate the same substrates. TLK1/1B interacts with Rad9, which is critical in DNA damage-activated checkpoint response, and plays a role in the repair of linearized DNA with incompatible ends. TLKs play important functions during the cell cycle and are implicated in chromatin remodeling, DNA replication and repair, and mitosis. The TLK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270942 [Multi-domain]  Cd Length: 299  Bit Score: 61.23  E-value: 9.23e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  730 LGEGEFGKVVKATAFHlkgRAGYTTVAVKML--------KENASPSELRdllsEFNVLKQVNHPHVIKLYGACSQD-GPL 800
Cdd:cd14040   14 LGRGGFSEVYKAFDLY---EQRYAAVKIHQLnkswrdekKENYHKHACR----EYRIHKELDHPRIVKLYDYFSLDtDTF 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  801 LLIVEYAKYGSLRGFLRESRkvgpgylgsggsrnssSLDHPDERALTMgdlisfawQISQGMQYLAEMK--LVHRDLAAR 878
Cdd:cd14040   87 CTVLEYCEGNDLDFYLKQHK----------------LMSEKEARSIVM--------QIVNALRYLNEIKppIIHYDLKPG 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  879 NILVAEGR---KMKISDFGLSR----DVYEEDSYVKRSQGR-----IPVKWMAIESLFDHIyTTQSDVWSFGVLLWEIVt 946
Cdd:cd14040  143 NILLVDGTacgEIKITDFGLSKimddDSYGVDGMDLTSQGAgtywyLPPECFVVGKEPPKI-SNKVDVWSVGVIFFQCL- 220

                 ....*.
gi 10862703  947 LGGNPY 952
Cdd:cd14040  221 YGRKPF 226
PKc_CLK cd14134
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity ...
728-946 1.17e-09

Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on S/T residues. In Drosophila, the CLK homolog DOA (Darkener of apricot) is essential for embryogenesis and its mutation leads to defects in sexual differentiation, eye formation, and neuronal development. In fission yeast, the CLK homolog Lkh1 is a negative regulator of filamentous growth and asexual flocculation, and is also involved in oxidative stress response. Vertebrates contain mutliple CLK proteins and mammals have four (CLK1-4). The CLK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271036 [Multi-domain]  Cd Length: 332  Bit Score: 61.04  E-value: 1.17e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  728 KTLGEGEFGKVVKAtaFHLKGRAgytTVAVKMLKenASPSELRDLLSEFNVLKQVNH------PHVIKLYGACSQDGPLL 801
Cdd:cd14134   18 RLLGEGTFGKVLEC--WDRKRKR---YVAVKIIR--NVEKYREAAKIEIDVLETLAEkdpngkSHCVQLRDWFDYRGHMC 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  802 LIVEyaKYG-SLRGFLRESRKVGpgylgsggsrnsssldhpderaLTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNI 880
Cdd:cd14134   91 IVFE--LLGpSLYDFLKKNNYGP----------------------FPLEHVQHIAKQLLEAVAFLHDLKLTHTDLKPENI 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  881 LVAEGR-------------------KMKISDFGLSRDVYEEDSYV--KRsQGRIP-----VKWMaieslfdhiYTtqSDV 934
Cdd:cd14134  147 LLVDSDyvkvynpkkkrqirvpkstDIKLIDFGSATFDDEYHSSIvsTR-HYRAPevilgLGWS---------YP--CDV 214
                        250
                 ....*....|..
gi 10862703  935 WSFGVLLWEIVT 946
Cdd:cd14134  215 WSIGCILVELYT 226
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
730-995 1.17e-09

Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Mammals have two cGK isoforms from different genes, cGKI and cGKII. cGKI exists as two splice variants, cGKI-alpha and cGKI-beta. cGK consists of an N-terminal regulatory domain containing a dimerization and an autoinhibitory pseudosubstrate region, two cGMP-binding domains, and a C-terminal catalytic domain. Binding of cGMP to both binding sites releases the inhibition of the catalytic center by the pseudosubstrate region, allowing autophosphorylation and activation of the kinase. cGKI is a soluble protein expressed in all smooth muscles, platelets, cerebellum, and kidney. It is also expressed at lower concentrations in other tissues. cGKII is a membrane-bound protein that is most abundantly expressed in the intestine. It is also present in the brain nuclei, adrenal cortex, kidney, lung, and prostate. cGKI is involved in the regulation of smooth muscle tone, smooth cell proliferation, and platelet activation. cGKII plays a role in the regulation of secretion, such as renin secretion by the kidney and aldosterone secretion by the adrenal. It also regulates bone growth and the circadian rhythm. The cGK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270724 [Multi-domain]  Cd Length: 262  Bit Score: 60.32  E-value: 1.17e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  730 LGEGEFGKV--VKATAfhlKGRagytTVAVKMLKENA--SPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVE 805
Cdd:cd05572    1 LGVGGFGRVelVQLKS---KGR----TFALKCVKKRHivQTRQQEHIFSEKEILEECNSPFIVKLYRTFKDKKYLYMLME 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  806 YAKYGSLRGFLREsrkvgpgylgsggsrnSSSLDHPDERALTMgdlisfawQISQGMQYLAEMKLVHRDLAARNILVAEG 885
Cdd:cd05572   74 YCLGGELWTILRD----------------RGLFDEYTARFYTA--------CVVLAFEYLHSRGIIYRDLKPENLLLDSN 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  886 RKMKISDFGLSRDVYeedSYVKrsqgripvKW--------MAIESLFDHIYTTQSDVWSFGVLLWEIVTlGGNPYPGI-- 955
Cdd:cd05572  130 GYVKLVDFGFAKKLG---SGRK--------TWtfcgtpeyVAPEIILNKGYDFSVDYWSLGILLYELLT-GRPPFGGDde 197
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 10862703  956 PPERLFNL-LKTGHRMERPDNCSEEMYRLMLQCWKQEPDKR 995
Cdd:cd05572  198 DPMKIYNIiLKGIDKIEFPKYIDKNAKNLIKQLLRRNPEER 238
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
723-952 1.19e-09

N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK1 plays a role in the regulation of translational control and transcriptional activation. It phosphorylates the transcription factors, CREB and NFkB. It also phosphorylates the nucleosomal proteins H3 and HMG-14. Increased phosphorylation of MSK1 is associated with the development of cerebral ischemic/hypoxic preconditioning. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270764 [Multi-domain]  Cd Length: 290  Bit Score: 60.78  E-value: 1.19e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  723 NLVLGKTLGEGEFGKV--VKATAFHLKGRagytTVAVKMLK-----ENASPSElrDLLSEFNVLKQVNH-PHVIKLYGAC 794
Cdd:cd05613    1 NFELLKVLGTGAYGKVflVRKVSGHDAGK----LYAMKVLKkativQKAKTAE--HTRTERQVLEHIRQsPFLVTLHYAF 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  795 SQDGPLLLIVEYAKYGSLRGFLRESRKvgpgylgsggsrnsssldhpderaLTMGDLISFAWQISQGMQYLAEMKLVHRD 874
Cdd:cd05613   75 QTDTKLHLILDYINGGELFTHLSQRER------------------------FTENEVQIYIGEIVLALEHLHKLGIIYRD 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  875 LAARNILVAEGRKMKISDFGLSRD-VYEEDSYVKRSQGRIpvKWMAIESLF--DHIYTTQSDVWSFGVLLWEIVTlGGNP 951
Cdd:cd05613  131 IKLENILLDSSGHVVLTDFGLSKEfLLDENERAYSFCGTI--EYMAPEIVRggDSGHDKAVDWWSLGVLMYELLT-GASP 207

                 .
gi 10862703  952 Y 952
Cdd:cd05613  208 F 208
PHA02988 PHA02988
hypothetical protein; Provisional
747-1001 1.30e-09

hypothetical protein; Provisional


Pssm-ID: 165291 [Multi-domain]  Cd Length: 283  Bit Score: 60.53  E-value: 1.30e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703   747 KGRAGYTTVAVKMLK--ENASPSELRDLLSEFNVLKQVNHPHVIKLYG---ACSQDGP-LLLIVEYAKYGSLRGFLREsr 820
Cdd:PHA02988   38 KGIFNNKEVIIRTFKkfHKGHKVLIDITENEIKNLRRIDSNNILKIYGfiiDIVDDLPrLSLILEYCTRGYLREVLDK-- 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703   821 kvgpgylgsggsrnsssldhpdERALTMGDLISFAWQISQGMQYLAE-MKLVHRDLAARNILVAEGRKMKISDFGLSRdV 899
Cdd:PHA02988  116 ----------------------EKDLSFKTKLDMAIDCCKGLYNLYKyTNKPYKNLTSVSFLVTENYKLKIICHGLEK-I 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703   900 YEEDSYVKrsqgripVKWMAIES--LFDHI---YTTQSDVWSFGVLLWEIVTlGGNPYPGIPPERLFNLLKTGHRMER-P 973
Cdd:PHA02988  173 LSSPPFKN-------VNFMVYFSykMLNDIfseYTIKDDIYSLGVVLWEIFT-GKIPFENLTTKEIYDLIINKNNSLKlP 244
                         250       260
                  ....*....|....*....|....*...
gi 10862703   974 DNCSEEMYRLMLQCWKQEPDKRPVFADI 1001
Cdd:PHA02988  245 LDCPLEIKCIVEACTSHDSIKRPNIKEI 272
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
717-954 1.60e-09

Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase (also called MAPK11); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38beta/MAPK11 is widely expressed in tissues and shows more similarity with p38alpha than with the other isoforms. Both are sensitive to pyridinylimidazoles and share some common substrates such as MAPK activated protein kinase 2 (MK2) and the transcription factors ATF2, c-Fos and, ELK-1. p38beta is involved in regulating the activation of the cyclooxygenase-2 promoter and the expression of TGFbeta-induced alpha-smooth muscle cell actin. p38 kinases are mitogen-activated protein kinases (MAPKs), serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38beta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143383 [Multi-domain]  Cd Length: 343  Bit Score: 60.83  E-value: 1.60e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  717 WEFPRKNLVLgKTLGEGEFGKVvkATAFHLKGRagyTTVAVKML-KENASPSELRDLLSEFNVLKQVNHPHVIKLYGACS 795
Cdd:cd07878   11 WEVPERYQNL-TPVGSGAYGSV--CSAYDTRLR---QKVAVKKLsRPFQSLIHARRTYRELRLLKHMKHENVIGLLDVFT 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  796 QDGPLLLIVEYAKYGSLRGflresrkvgpGYLGSGGSRNSSSLDHpderaltmgdlISF-AWQISQGMQYLAEMKLVHRD 874
Cdd:cd07878   85 PATSIENFNEVYLVTNLMG----------ADLNNIVKCQKLSDEH-----------VQFlIYQLLRGLKYIHSAGIIHRD 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  875 LAARNILVAEGRKMKISDFGLSRDVYEE-DSYVKRSQGRIP---VKWMaieslfdHiYTTQSDVWSFGVLLWEIVTlGGN 950
Cdd:cd07878  144 LKPSNVAVNEDCELRILDFGLARQADDEmTGYVATRWYRAPeimLNWM-------H-YNQTVDIWSVGCIMAELLK-GKA 214

                 ....
gi 10862703  951 PYPG 954
Cdd:cd07878  215 LFPG 218
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
730-983 1.61e-09

Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TBK1 is also called T2K and NF-kB-activating kinase. It is widely expressed in most cell types and acts as an IkappaB kinase (IKK)-activating kinase responsible for NF-kB activation in response to growth factors. It plays a role in modulating inflammatory responses through the NF-kB pathway. TKB1 is also a major player in innate immune responses since it functions as a virus-activated kinase necessary for establishing an antiviral state. It phosphorylates IRF-3 and IRF-7, which are important transcription factors for inducing type I interferon during viral infection. In addition, TBK1 may also play roles in cell transformation and oncogenesis. The TBK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270890 [Multi-domain]  Cd Length: 316  Bit Score: 60.58  E-value: 1.61e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  730 LGEGefgkvvkATAFHLKGRAGYT--TVAVKMLKenaSPSELRDL---LSEFNVLKQVNHPHVIKLYgACSQDGPL---L 801
Cdd:cd13988    1 LGQG-------ATANVFRGRHKKTgdLYAVKVFN---NLSFMRPLdvqMREFEVLKKLNHKNIVKLF-AIEEELTTrhkV 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  802 LIVEYAKYGSLrgflresrkvgpgylgsggsrnSSSLDHPDER-ALTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNI 880
Cdd:cd13988   70 LVMELCPCGSL----------------------YTVLEEPSNAyGLPESEFLIVLRDVVAGMNHLRENGIVHRDIKPGNI 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  881 LVAEGRK----MKISDFGLSRDVYEEDSYV--------------KRSQGRIPVKWMaieslfdhiYTTQSDVWSFGVLLW 942
Cdd:cd13988  128 MRVIGEDgqsvYKLTDFGAARELEDDEQFVslygteeylhpdmyERAVLRKDHQKK---------YGATVDLWSIGVTFY 198
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 10862703  943 EIVTlggnpypGIPPERLFnllktghrmERPDNCSEEMYRL 983
Cdd:cd13988  199 HAAT-------GSLPFRPF---------EGPRRNKEVMYKI 223
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
728-1010 1.87e-09

Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases Sty1 and Hog1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the MAPKs Sty1 from Schizosaccharomyces pombe, Hog1 from Saccharomyces cerevisiae, and similar proteins. Sty1 and Hog1 are stress-activated MAPKs that partipate in transcriptional regulation in response to stress. Sty1 is activated in response to oxidative stress, osmotic stress, and UV radiation. It is regulated by the MAP2K Wis1, which is activated by the MAP3Ks Wis4 and Win1, which receive signals of the stress condition from membrane-spanning histidine kinases Mak1-3. Activated Sty1 stabilizes the Atf1 transcription factor and induces transcription of Atf1-dependent genes of the core environmetal stress response. Hog1 is the key element in the high osmolarity glycerol (HOG) pathway and is activated upon hyperosmotic stress. Activated Hog1 accumulates in the nucleus and regulates stress-induced transcription. The HOG pathway is mediated by two transmembrane osmosensors, Sln1 and Sho1. MAPKs are important mediators of cellular responses to extracellular signals. The Sty1/Hog1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270843 [Multi-domain]  Cd Length: 328  Bit Score: 60.66  E-value: 1.87e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  728 KTLGEGEFGKVVKATAfHLKGRagytTVAVK-MLKENASPSELRDLLSEFNVLKQVNHPHVIKL---YGACSQDgpLLLI 803
Cdd:cd07856   16 QPVGMGAFGLVCSARD-QLTGQ----NVAVKkIMKPFSTPVLAKRTYRELKLLKHLRHENIISLsdiFISPLED--IYFV 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  804 VEYakYGSLRGFLRESRKVGPGYLGSggsrnsssldhpderaltmgdlisFAWQISQGMQYLAEMKLVHRDLAARNILVA 883
Cdd:cd07856   89 TEL--LGTDLHRLLTSRPLEKQFIQY------------------------FLYQILRGLKYVHSAGVIHRDLKPSNILVN 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  884 EGRKMKISDFGLSR-DVYEEDSYVKRSQGRIP---VKWMAieslfdhiYTTQSDVWSFGVLLWEIvtLGGNP-YP----- 953
Cdd:cd07856  143 ENCDLKICDFGLARiQDPQMTGYVSTRYYRAPeimLTWQK--------YDVEVDIWSAGCIFAEM--LEGKPlFPgkdhv 212
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 10862703  954 ----------GIPPERLFNLLktghrmerpdnCSEEMYRLMLQCWKQE--------PDKRPVFADIskdLEKMMV 1010
Cdd:cd07856  213 nqfsiitellGTPPDDVINTI-----------CSENTLRFVQSLPKRErvpfsekfKNADPDAIDL---LEKMLV 273
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
718-946 1.88e-09

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK9, together with a cyclin partner (cyclin T1, T2a, T2b, or K), is the main component of distinct positive transcription elongation factors (P-TEFb), which function as Ser2 C-terminal domain kinases of RNA polymerase II. P-TEFb participates in multiple steps of gene expression including transcription elongation, mRNA synthesis, processing, export, and translation. It also plays a role in mediating cytokine induced transcription networks such as IL6-induced STAT3 signaling. In addition, the CDK9/cyclin T2a complex promotes muscle differentiation and enhances the function of some myogenic regulatory factors. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK9 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270848 [Multi-domain]  Cd Length: 310  Bit Score: 60.46  E-value: 1.88e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  718 EFPRKNLV-----LGKtLGEGEFGKVVKAtafhlKGRAGYTTVAVKM-LKENASPSELRDLLSEFNVLKQVNHPHVIKLY 791
Cdd:cd07865    4 EFPFCDEVskyekLAK-IGQGTFGEVFKA-----RHRKTGQIVALKKvLMENEKEGFPITALREIKILQLLKHENVVNLI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  792 GACSQD--------GPLLLIVEYAKYgSLRGFLrESRKVgpgylgsggsrnsssldhpderALTMGDLISFAWQISQGMQ 863
Cdd:cd07865   78 EICRTKatpynrykGSIYLVFEFCEH-DLAGLL-SNKNV----------------------KFTLSEIKKVMKMLLNGLY 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  864 YLAEMKLVHRDLAARNILVAEGRKMKISDFGLSRD-VYEEDSYVKRSQGRIPVKWM-AIESLF-DHIYTTQSDVWSFGVL 940
Cdd:cd07865  134 YIHRNKILHRDMKAANILITKDGVLKLADFGLARAfSLAKNSQPNRYTNRVVTLWYrPPELLLgERDYGPPIDMWGAGCI 213

                 ....*.
gi 10862703  941 LWEIVT 946
Cdd:cd07865  214 MAEMWT 219
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
717-954 2.05e-09

Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38 kinases are mitogen-activated protein kinases (MAPKs), serving as important mediators of cellular responses to extracellular signals. They function in the regulation of the cell cycle, cell development, cell differentiation, senescence, tumorigenesis, apoptosis, pain development and pain progression, and immune responses. p38 kinases are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. p38 substrates include other protein kinases and factors that regulate transcription, nuclear export, mRNA stability and translation. p38 kinases are drug targets for the inflammatory diseases psoriasis, rheumatoid arthritis, and chronic pulmonary disease. Vertebrates contain four isoforms of p38, named alpha, beta, gamma, and delta, which show varying substrate specificity and expression patterns. p38alpha and p38beta are ubiquitously expressed, p38gamma is predominantly found in skeletal muscle, and p38delta is found in the heart, lung, testis, pancreas, and small intestine. The p38 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143356 [Multi-domain]  Cd Length: 343  Bit Score: 60.38  E-value: 2.05e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  717 WEFPRKNLVLgKTLGEGEFGKVVKATAfhlkgRAGYTTVAVKMLKEN-ASPSELRDLLSEFNVLKQVNHPHVIKLYGACS 795
Cdd:cd07851   11 WEVPDRYQNL-SPVGSGAYGQVCSAFD-----TKTGRKVAIKKLSRPfQSAIHAKRTYRELRLLKHMKHENVIGLLDVFT 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  796 QDGPL------LLIVEYAKyGSLRGFLReSRKVGpgylgsggsrnsssldhpDERaltmgdlISF-AWQISQGMQYLAEM 868
Cdd:cd07851   85 PASSLedfqdvYLVTHLMG-ADLNNIVK-CQKLS------------------DDH-------IQFlVYQILRGLKYIHSA 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  869 KLVHRDLAARNILVAEGRKMKISDFGLSRDVYEE-DSYVKRSQGRIP---VKWMaieslfdHiYTTQSDVWSFGVLLWEI 944
Cdd:cd07851  138 GIIHRDLKPSNLAVNEDCELKILDFGLARHTDDEmTGYVATRWYRAPeimLNWM-------H-YNQTVDIWSVGCIMAEL 209
                        250
                 ....*....|.
gi 10862703  945 VTlgGNP-YPG 954
Cdd:cd07851  210 LT--GKTlFPG 218
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
730-946 2.15e-09

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 60.22  E-value: 2.15e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703   730 LGEGEFGKVVKAtafhlKGRAGYTTVAVKMLK----ENASPSELrdlLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVE 805
Cdd:PLN00009   10 IGEGTYGVVYKA-----RDRVTNETIALKKIRleqeDEGVPSTA---IREISLLKEMQHGNIVRLQDVVHSEKRLYLVFE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703   806 YAKYgSLRGFLRESrkvgpgylgsggsrnsssldhPD-ERALTMgdLISFAWQISQGMQYLAEMKLVHRDLAARNILVAE 884
Cdd:PLN00009   82 YLDL-DLKKHMDSS---------------------PDfAKNPRL--IKTYLYQILRGIAYCHSHRVLHRDLKPQNLLIDR 137
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 10862703   885 GRK-MKISDFGLSRDVyeedsyvkrsqgRIPVK----------WMAIESLF-DHIYTTQSDVWSFGVLLWEIVT 946
Cdd:PLN00009  138 RTNaLKLADFGLARAF------------GIPVRtfthevvtlwYRAPEILLgSRHYSTPVDIWSVGCIFAEMVN 199
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
730-1012 2.16e-09

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK1 (or MYLK1) phosphorylates myosin regulatory light chain and controls the contraction of smooth muscles. The MLCK1 gene expresses three transcripts in a cell-specific manner: a short MLCK1 which contains three immunoglobulin (Ig)-like and one fibronectin type III (FN3) domains, PEVK and actin-binding regions, and a kinase domain near the C-terminus followed by a regulatory segment containing an autoinhibitory Ca2+/calmodulin binding site; a long MLCK1 containing six additional Ig-like domains at the N-terminus compared to the short MLCK1; and the C-terminal Ig module which results in the expression of telokin in phasic smooth muscles, leading to Ca2+ desensitization by cyclic nucleotides of smooth muscle force. MLCK1 is also responsible for myosin regulatory light chain phosphorylation in nonmuscle cells and may play a role in regulating myosin II ATPase activity. The MLCK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271093 [Multi-domain]  Cd Length: 259  Bit Score: 59.63  E-value: 2.16e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  730 LGEGEFGKVvkataFHLKGRAGYTTVAVKMLKEnASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVEYAKY 809
Cdd:cd14191   10 LGSGKFGQV-----FRLVEKKTKKVWAGKFFKA-YSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEMVSG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  810 GSLrgFLResrkvgpgylgsggsrnssSLDHPDEraLTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNILVAE--GRK 887
Cdd:cd14191   84 GEL--FER-------------------IIDEDFE--LTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNktGTK 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  888 MKISDFGLSRDVyeedsyvkRSQGRIPV-----KWMAIESLFDHIYTTQSDVWSFGVLLWEIVTlGGNPYPGipperlfn 962
Cdd:cd14191  141 IKLIDFGLARRL--------ENAGSLKVlfgtpEFVAPEVINYEPIGYATDMWSIGVICYILVS-GLSPFMG-------- 203
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 10862703  963 llktghrmerpDNCSEEMYRLMLQCWKQEPDKRPVFADISKDLEKMMVKR 1012
Cdd:cd14191  204 -----------DNDNETLANVTSATWDFDDEAFDEISDDAKDFISNLLKK 242
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
728-1007 2.31e-09

Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes cyclin G-Associated Kinase (GAK), Drosophila melanogaster Numb-Associated Kinase (NAK)-like proteins, and similar protein kinases. GAK plays regulatory roles in clathrin-mediated membrane trafficking, the maintenance of centrosome integrity and chromosome congression, neural patterning, survival of neurons, and immune responses. NAK plays a role in asymmetric cell division through its association with Numb. It also regulates the localization of Dlg, a protein essential for septate junction formation. The GAK-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270887 [Multi-domain]  Cd Length: 272  Bit Score: 59.66  E-value: 2.31e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  728 KTLGEGEFGKVVKATAFHLKGRagyttVAVKMLKENASPSeLRDLLSEFNVLKQV-NHPHVIKLYG-ACSQDGPL---LL 802
Cdd:cd13985    6 KQLGEGGFSYVYLAHDVNTGRR-----YALKRMYFNDEEQ-LRVAIKEIEIMKRLcGHPNIVQYYDsAILSSEGRkevLL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  803 IVEYAKyGSLRGFLResrKVGPGYLGsggsrnsssldhpDERALTMGDlisfawQISQGMQYLAEMK--LVHRDLAARNI 880
Cdd:cd13985   80 LMEYCP-GSLVDILE---KSPPSPLS-------------EEEVLRIFY------QICQAVGHLHSQSppIIHRDIKIENI 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  881 LVAEGRKMKISDFGlsrDVYEEDsYVKRSQGRIPV------KWM-----AIESLFDHIY---TTQSDVWSFGVLLWEIVT 946
Cdd:cd13985  137 LFSNTGRFKLCDFG---SATTEH-YPLERAEEVNIieeeiqKNTtpmyrAPEMIDLYSKkpiGEKADIWALGCLLYKLCF 212
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 10862703  947 LgGNPYPGIPPERLFNLlktGHRMERPDNCSEE---MYRLMLQcwkQEPDKRPVFADISKDLEK 1007
Cdd:cd13985  213 F-KLPFDESSKLAIVAG---KYSIPEQPRYSPElhdLIRHMLT---PDPAERPDIFQVINIITK 269
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
730-995 2.50e-09

Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-alpha is expressed in many tissues and is associated with cell proliferation, apoptosis, and cell motility. It plays a role in the signaling of the growth factors PDGF, VEGF, EGF, and FGF. Abnormal levels of PKC-alpha have been detected in many transformed cell lines and several human tumors. In addition, PKC-alpha is required for HER2 dependent breast cancer invasion. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. PKCs undergo three phosphorylations in order to take mature forms. In addition, cPKCs depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. The cPKC-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270766 [Multi-domain]  Cd Length: 341  Bit Score: 60.40  E-value: 2.50e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  730 LGEGEFGKVVKAtafhlKGRAGYTTVAVKMLKENA--SPSELRDLLSEFNVLKQVNHPHVIKLYGACSQD-GPLLLIVEY 806
Cdd:cd05615   18 LGKGSFGKVMLA-----ERKGSDELYAIKILKKDVviQDDDVECTMVEKRVLALQDKPPFLTQLHSCFQTvDRLYFVMEY 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  807 AKYGSLRGFLRESRKvgpgylgsggsrnsssLDHPDEraltmgdlISFAWQISQGMQYLAEMKLVHRDLAARNILVAEGR 886
Cdd:cd05615   93 VNGGDLMYHIQQVGK----------------FKEPQA--------VFYAAEISVGLFFLHKKGIIYRDLKLDNVMLDSEG 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  887 KMKISDFGLSRDvYEEDSYVKRSQGRIPvKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTlGGNPYPGIPPERLFNLLKT 966
Cdd:cd05615  149 HIKIADFGMCKE-HMVEGVTTRTFCGTP-DYIAPEIIAYQPYGRSVDWWAYGVLLYEMLA-GQPPFDGEDEDELFQSIME 225
                        250       260
                 ....*....|....*....|....*....
gi 10862703  967 gHRMERPDNCSEEMYRLMLQCWKQEPDKR 995
Cdd:cd05615  226 -HNVSYPKSLSKEAVSICKGLMTKHPAKR 253
PTKc_Wee1b cd14139
Catalytic domain of the Protein Tyrosine Kinase, Wee1b; PTKs catalyze the transfer of the ...
730-905 2.59e-09

Catalytic domain of the Protein Tyrosine Kinase, Wee1b; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of human Wee1b (also called Wee2), Xenopus laevis Wee1a (XeWee1a) and similar vertebrate proteins. XeWee1a accumulates after exiting the metaphase II stage in oocytes and in early mitotic cells. It functions during the first zygotic cell division and not during subsequent divisions. Mammalian Wee2/Wee1b is an oocyte-specific inhibitor of meiosis that functions downstream of cAMP. Wee1 is a cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. The Wee1b subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271041 [Multi-domain]  Cd Length: 274  Bit Score: 59.56  E-value: 2.59e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  730 LGEGEFGKVVKATAfHLKGragyttvAVKMLKENASPseLRDLLSEFNVLKQV-------NHPHVIKLYGACSQDGPLLL 802
Cdd:cd14139    8 IGVGEFGSVYKCIK-RLDG-------CVYAIKRSMRP--FAGSSNEQLALHEVyahavlgHHPHVVRYYSAWAEDDHMII 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  803 IVEYAKYGSLRGFLRESRKVGPGYlgsggsrnsssldhpderalTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNILV 882
Cdd:cd14139   78 QNEYCNGGSLQDAISENTKSGNHF--------------------EEPELKDILLQVSMGLKYIHNSGLVHLDIKPSNIFI 137
                        170       180
                 ....*....|....*....|...
gi 10862703  883 AegRKMKISDFGLSRDVYEEDSY 905
Cdd:cd14139  138 C--HKMQSSSGVGEEVSNEEDEF 158
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
861-1001 2.62e-09

Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMP-activated protein kinase (AMPK). CaMKK1, also called CaMKK alpha, is involved in the regulation of glucose uptake in skeletal muscles, independently of AMPK and PKB activation. It also play roles in learning and memory. Studies on CaMKK1 knockout mice reveal deficits in fear conditioning. The CaMKK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271102 [Multi-domain]  Cd Length: 284  Bit Score: 59.58  E-value: 2.62e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  861 GMQYLAEMKLVHRDLAARNILVAEGRKMKISDFGLSRDVYEEDSYVKRSQGrIPVkWMAIESLFDhiyTTQS------DV 934
Cdd:cd14200  136 GIEYLHYQKIVHRDIKPSNLLLGDDGHVKIADFGVSNQFEGNDALLSSTAG-TPA-FMAPETLSD---SGQSfsgkalDV 210
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 10862703  935 WSFGVLLWEIVtLGGNPYPGIPPERLFNLLKTgHRMERPD--NCSEEMYRLMLQCWKQEPDKRPVFADI 1001
Cdd:cd14200  211 WAMGVTLYCFV-YGKCPFIDEFILALHNKIKN-KPVEFPEepEISEELKDLILKMLDKNPETRITVPEI 277
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
730-952 3.19e-09

C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide Exchange Factor, Triple functional domain protein; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Triple functional domain protein (Trio), also called PTPRF-interacting protein, is a large multidomain protein containing a series of spectrin-like repeats, two each of RhoGEF and SH3 domains, an immunoglobulin-like (Ig) domain and a C-terminal kinase. Trio plays important roles in neuronal cell migration and axon guidance. It was originally identified as an interacting partner of the of the receptor-like tyrosine phosphatase (RPTP) LAR (leukocyte-antigen-related protein), a family of receptors that function in the signaling to the actin cytoskeleton during development. Trio functions as a GEF for Rac1, RhoG, and RhoA, and is involved in the regulation of lamellipodia formation, mediating Rac1-dependent cell spreading and migration. The Trio subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271015 [Multi-domain]  Cd Length: 263  Bit Score: 59.22  E-value: 3.19e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  730 LGEGEFGKVVKATAfhlkgRAGYTTVAVKMLKENASPselRDLLS-EFNVLKQVNHPHVIKLYGACSQDGPLLLIVEYAK 808
Cdd:cd14113   15 LGRGRFSVVKKCDQ-----RGTKRAVATKFVNKKLMK---RDQVThELGVLQSLQHPQLVGLLDTFETPTSYILVLEMAD 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  809 YGSLRGFLresrkVGPGylgsggsrnsssldhpderALTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNILVAEGRK- 887
Cdd:cd14113   87 QGRLLDYV-----VRWG-------------------NLTEEKIRFYLREILEALQYLHNCRIAHLDLKPENILVDQSLSk 142
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 10862703  888 --MKISDFGlsrDVYEEDS--YVKRSQGRipVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTlGGNPY 952
Cdd:cd14113  143 ptIKLADFG---DAVQLNTtyYIHQLLGS--PEFAAPEIILGNPVSLTSDLWSIGVLTYVLLS-GVSPF 205
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
730-952 3.49e-09

Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TLKs play important functions during the cell cycle and are implicated in chromatin remodeling, DNA replication and repair, and mitosis. They phosphorylate and regulate Anti-silencing function 1 protein (Asf1), a histone H3/H4 chaperone that helps facilitate the assembly of chromatin following DNA replication during S phase. TLKs also phosphorylate the H3 histone tail and are essential in transcription. Vertebrates contain two subfamily members, TLK1 and TLK2. The TLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270943 [Multi-domain]  Cd Length: 309  Bit Score: 59.69  E-value: 3.49e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  730 LGEGEFGKVVKAtaFHLKGRAgYTTVAVKMLKENASPSELRDL----LSEFNVLKQVNHPHVIKLYGACSQD-GPLLLIV 804
Cdd:cd14041   14 LGRGGFSEVYKA--FDLTEQR-YVAVKIHQLNKNWRDEKKENYhkhaCREYRIHKELDHPRIVKLYDYFSLDtDSFCTVL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  805 EYAKYGSLRGFLRESRkvgpgylgsggsrnssSLDHPDERALTMgdlisfawQISQGMQYLAEMK--LVHRDLAARNILV 882
Cdd:cd14041   91 EYCEGNDLDFYLKQHK----------------LMSEKEARSIIM--------QIVNALKYLNEIKppIIHYDLKPGNILL 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  883 AEGR---KMKISDFGLSRdVYEEDSYVK------RSQGR-----IPVKWMAIESLFDHIyTTQSDVWSFGVLLWEIVtLG 948
Cdd:cd14041  147 VNGTacgEIKITDFGLSK-IMDDDSYNSvdgmelTSQGAgtywyLPPECFVVGKEPPKI-SNKVDVWSVGVIFYQCL-YG 223

                 ....
gi 10862703  949 GNPY 952
Cdd:cd14041  224 RKPF 227
STKc_TGFbR1_ACVR1b_ACVR1c cd14143
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta Type I ...
730-1008 4.26e-09

Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta Type I Receptor and Activin Type IB/IC Receptors; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TGFbR1, also called Activin receptor-Like Kinase 5 (ALK5), functions as a receptor for TGFbeta and phoshorylates SMAD2/3. TGFbeta proteins are cytokines that regulate cell growth, differentiation, and survival, and are critical in the development and progression of many human cancers. Mutations in TGFbR1 (and TGFbR2) can cause aortic aneurysm disorders such as Loeys-Dietz and Marfan syndromes. ACVR1b (also called ALK4) and ACVR1c (also called ALK7) act as receptors for activin A and B, respectively. TGFbR1, ACVR1b, and ACVR1c belong to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like TGFbR1, ACVR1b, and ACVR1c, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The TGFbR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271045 [Multi-domain]  Cd Length: 288  Bit Score: 58.99  E-value: 4.26e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  730 LGEGEFGKVvkatafhLKGRAGYTTVAVKMLkenaSPSELRDLLSEFNVLKQV--NHPHVIKLYGACSQDG----PLLLI 803
Cdd:cd14143    3 IGKGRFGEV-------WRGRWRGEDVAVKIF----SSREERSWFREAEIYQTVmlRHENILGFIAADNKDNgtwtQLWLV 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  804 VEYAKYGSLRGFLRESRkvgpgylgsggsrnsssldhpderaLTMGDLISFAWQISQGMQYLaEMKLV---------HRD 874
Cdd:cd14143   72 SDYHEHGSLFDYLNRYT-------------------------VTVEGMIKLALSIASGLAHL-HMEIVgtqgkpaiaHRD 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  875 LAARNILVAEGRKMKISDFGLS-RDVYEEDSYVKRSQGRIPVK-WMAIESLFDHIYTT------QSDVWSFGVLLWEIV- 945
Cdd:cd14143  126 LKSKNILVKKNGTCCIADLGLAvRHDSATDTIDIAPNHRVGTKrYMAPEVLDDTINMKhfesfkRADIYALGLVFWEIAr 205
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  946 --TLGGNP-------YPGIPPERLFNLLK--TGHRMERP--------DNCSEEMYRLMLQCWKQEPDKRPVFADISKDLE 1006
Cdd:cd14143  206 rcSIGGIHedyqlpyYDLVPSDPSIEEMRkvVCEQKLRPnipnrwqsCEALRVMAKIMRECWYANGAARLTALRIKKTLS 285

                 ..
gi 10862703 1007 KM 1008
Cdd:cd14143  286 QL 287
PTKc_Wee1a cd14138
Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the ...
730-996 4.91e-09

Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of human Wee1a, Xenopus laevis Wee1b (XeWee1b) and similar vertebrate proteins. Members of this subfamily show a wide expression pattern. XeWee1b functions after the first zygotic cell divisions. It is expressed in all tissues and is also present after the gastrulation stage of embryos. Wee1 is a cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. The Wee1a subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271040 [Multi-domain]  Cd Length: 276  Bit Score: 58.88  E-value: 4.91e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  730 LGEGEFGKVVKATAfHLKGragyttvAVKMLKENASPseLRDLLSEFNVLKQV-------NHPHVIKLYGACSQDGPLLL 802
Cdd:cd14138   13 IGSGEFGSVFKCVK-RLDG-------CIYAIKRSKKP--LAGSVDEQNALREVyahavlgQHSHVVRYYSAWAEDDHMLI 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  803 IVEYAKYGSLRGFLRESRKVgpgylgsggsrnsssldhpdERALTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNILV 882
Cdd:cd14138   83 QNEYCNGGSLADAISENYRI--------------------MSYFTEPELKDLLLQVARGLKYIHSMSLVHMDIKPSNIFI 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  883 ------------------AEGRKM-KISDFG-----LSRDVYEEDSyvkrsqgripvKWMAIESLF-DHIYTTQSDVWSF 937
Cdd:cd14138  143 srtsipnaaseegdedewASNKVIfKIGDLGhvtrvSSPQVEEGDS-----------RFLANEVLQeNYTHLPKADIFAL 211
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 10862703  938 GVLLWeiVTLGGNPYPGIPPErlFNLLKTGHRMERPDNCSEEMYRLMLQCWKQEPDKRP 996
Cdd:cd14138  212 ALTVV--CAAGAEPLPTNGDQ--WHEIRQGKLPRIPQVLSQEFLDLLKVMIHPDPERRP 266
STKc_BMPR1a cd14220
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IA Receptor; ...
728-1008 7.33e-09

Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IA Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR1a, also called Activin receptor-Like Kinase 3 (ALK3), functions as a receptor for bone morphogenetic proteins (BMPs), which are involved in the regulation of cell proliferation, survival, differentiation, and apoptosis. BMPs are able to induce bone, cartilage, ligament, and tendon formation, and may play roles in bone diseases and tumors. Germline mutations in BMPR1a are associated with an increased risk to Juvenile Polyposis Syndrome, a hamartomatous disorder that may lead to gastrointestinal cancer. BMPR1a may also play an indirect role in the development of hematopoietic stem cells (HSCs) as osteoblasts are a major component of the HSC niche within the bone marrow. BMPR1a belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like BMPR1a, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The BMPR1a subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271122 [Multi-domain]  Cd Length: 287  Bit Score: 58.51  E-value: 7.33e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  728 KTLGEGEFGKVvkatafhLKGRAGYTTVAVKMLKENASPSELRD-------LLSEFNVLKQVNHPhvIKLYGACSQdgpL 800
Cdd:cd14220    1 RQIGKGRYGEV-------WMGKWRGEKVAVKVFFTTEEASWFREteiyqtvLMRHENILGFIAAD--IKGTGSWTQ---L 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  801 LLIVEYAKYGSLRGFLRESRKvgpgylgsggsrnsssldhpDERALtmgdlISFAWQISQGMQYL--------AEMKLVH 872
Cdd:cd14220   69 YLITDYHENGSLYDFLKCTTL--------------------DTRAL-----LKLAYSAACGLCHLhteiygtqGKPAIAH 123
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  873 RDLAARNILVAEGRKMKISDFGLS----RDVYEEDSYVKRSQGriPVKWMAIESLFDHIYTTQ------SDVWSFGVLLW 942
Cdd:cd14220  124 RDLKSKNILIKKNGTCCIADLGLAvkfnSDTNEVDVPLNTRVG--TKRYMAPEVLDESLNKNHfqayimADIYSFGLIIW 201
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  943 EIV---TLGG-------NPYPGIPPERLFNLLKTGHRME--RP--------DNCSEEMYRLMLQCWKQEPDKRPVFADIS 1002
Cdd:cd14220  202 EMArrcVTGGiveeyqlPYYDMVPSDPSYEDMREVVCVKrlRPtvsnrwnsDECLRAVLKLMSECWAHNPASRLTALRIK 281

                 ....*.
gi 10862703 1003 KDLEKM 1008
Cdd:cd14220  282 KTLAKM 287
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
730-945 7.40e-09

Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PDIK1L is also called STK35 or CLIK-1. It is predominantly a nuclear protein which is capable of autophosphorylation. Through its interaction with the PDZ-LIM protein CLP-36, it is localized to actin stress fibers. The PDIK1L subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270879 [Multi-domain]  Cd Length: 322  Bit Score: 58.72  E-value: 7.40e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  730 LGEGEFGKVVKATAfhlkGRAGyTTVAVKMLKENAsPSELRDLLSEFNVLK--QVNHPHVIKLYGACSQDGPL------- 800
Cdd:cd13977    8 VGRGSYGVVYEAVV----RRTG-ARVAVKKIRCNA-PENVELALREFWALSsiQRQHPNVIQLEECVLQRDGLaqrmshg 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  801 -------LLIVEyakyGSLRGflreSRKVGP----------GYLGSGGSRNSSSLDHPDERALTmgdliSFAWQISQGMQ 863
Cdd:cd13977   82 ssksdlyLLLVE----TSLKG----ERCFDPrsacylwfvmEFCDGGDMNEYLLSRRPDRQTNT-----SFMLQLSSALA 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  864 YLAEMKLVHRDLAARNILVAEGRK---MKISDFGLSRdvyeedsyVKRSQGRIPVK-----------------WMAIESL 923
Cdd:cd13977  149 FLHRNQIVHRDLKPDNILISHKRGepiLKVADFGLSK--------VCSGSGLNPEEpanvnkhflssacgsdfYMAPEVW 220
                        250       260
                 ....*....|....*....|..
gi 10862703  924 FDHiYTTQSDVWSFGVLLWEIV 945
Cdd:cd13977  221 EGH-YTAKADIFALGIIIWAMV 241
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
856-952 7.99e-09

Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. This subfamily is composed of the catalytically inactive kinases with similarity to yeast Scy1. It includes four mammalian proteins called SCY1-like protein 1 (SCYL1), SCYL2, SCYL3, as well as Testis-EXpressed protein 14 (TEX14). SCYL1 binds to and co-localizes with the membrane trafficking coatomer I (COPI) complex, and regulates COPI-mediated vesicle trafficking. Null mutations in the SCYL1 gene are responsible for the pathology in mdf (muscle-deficient) mice which display progressive motor neuropathy. SCYL2, also called coated vesicle-associated kinase of 104 kDa (CVAK104), is involved in the trafficking of clathrin-coated vesicles. It also binds the HIV-1 accessory protein Vpu and acts as a regulatory factor that promotes the dephosphorylation of Vpu, facilitating the restriction of HIV-1 release. SCYL3, also called ezrin-binding protein PACE-1, may be involved in regulating cell adhesion and migration. TEX14 is required for spermatogenesis and male fertility. It localizes to kinetochores (KT) during mitosis and is a target of the mitotic kinase PLK1. It regulates the maturation of the outer KT and the KT-microtubule attachment. The SCY1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270913 [Multi-domain]  Cd Length: 287  Bit Score: 58.10  E-value: 7.99e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  856 WQISQGMQYL-AEMKLVHRDLAARNILVAEGRKMKISDFGLSRDV----YEEDSYVKRSQGRIPVK-----WMAIESLFD 925
Cdd:cd14011  121 LQISEALSFLhNDVKLVHGNICPESVVINSNGEWKLAGFDFCISSeqatDQFPYFREYDPNLPPLAqpnlnYLAPEYILS 200
                         90       100
                 ....*....|....*....|....*..
gi 10862703  926 HIYTTQSDVWSFGVLLWEIVTLGGNPY 952
Cdd:cd14011  201 KTCDPASDMFSLGVLIYAIYNKGKPLF 227
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
854-952 8.78e-09

Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of the GRK4-like group include GRK4, GRK5, GRK6, and similar GRKs. They contain an N-terminal RGS homology (RH) domain and a catalytic domain, but lack a G protein betagamma-subunit binding domain. They are localized to the plasma membrane through post-translational lipid modification or direct binding to PIP2. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK4-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270756 [Multi-domain]  Cd Length: 285  Bit Score: 58.14  E-value: 8.78e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  854 FAWQISQGMQYLAEMKLVHRDLAARNILVAEGRKMKISDFGLSRDVYEEDSyVKrsqGRI-PVKWMAIESLFDHIYTTQS 932
Cdd:cd05605  107 YAAEITCGLEHLHSERIVYRDLKPENILLDDHGHVRISDLGLAVEIPEGET-IR---GRVgTVGYMAPEVVKNERYTFSP 182
                         90       100
                 ....*....|....*....|
gi 10862703  933 DVWSFGVLLWEIVTlGGNPY 952
Cdd:cd05605  183 DWWGLGCLIYEMIE-GQAPF 201
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
854-946 8.88e-09

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPKs serve as important mediators of cellular responses to extracellular signals. They control critical cellular functions including differentiation, proliferation, migration, and apoptosis. They are also implicated in the pathogenesis of many diseases including multiple types of cancer, stroke, diabetes, and chronic inflammation. Typical MAPK pathways involve a triple kinase core cascade comprising of the MAPK, which is phosphorylated and activated by a MAPK kinase (MAP2K or MKK), which itself is phosphorylated and activated by a MAPK kinase kinase (MAP3K or MKKK). Each cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAP3K to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. There are three typical MAPK subfamilies: Extracellular signal-Regulated Kinase (ERK), c-Jun N-terminal Kinase (JNK), and p38. Some MAPKs are atypical in that they are not regulated by MAP2Ks. These include MAPK4, MAPK6, NLK, and ERK7. The MAPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270828 [Multi-domain]  Cd Length: 329  Bit Score: 58.31  E-value: 8.88e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  854 FAWQISQGMQYLAEMKLVHRDLAARNILVAEGRKMKISDFGLSRDVYEEDS------YVkrsqgripV-KWM-AIESLFD 925
Cdd:cd07834  108 FLYQILRGLKYLHSAGVIHRDLKPSNILVNSNCDLKICDFGLARGVDPDEDkgflteYV--------VtRWYrAPELLLS 179
                         90       100
                 ....*....|....*....|..
gi 10862703  926 -HIYTTQSDVWSFGVLLWEIVT 946
Cdd:cd07834  180 sKKYTKAIDIWSVGCIFAELLT 201
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
730-966 1.07e-08

Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-like proteins show unusual expression patterns with high levels in post-mitotic tissues, suggesting that they may be involved in regulating post-mitotic cellular events. They share sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The association of PCTAIRE-like proteins with cyclins has not been widely studied, although PFTAIRE-1 has been shown to function as a CDK which is regulated by cyclin D3 as well as the membrane-associated cyclin Y. The PCTAIRE-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270835 [Multi-domain]  Cd Length: 286  Bit Score: 57.78  E-value: 1.07e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  730 LGEGEFGKVVKAtafhlKGRAGYTTVAVKMLK----ENASPSELRdllsEFNVLKQVNHPHVIKLYGACSQDGPLLLIVE 805
Cdd:cd07844    8 LGEGSYATVYKG-----RSKLTGQLVALKEIRleheEGAPFTAIR----EASLLKDLKHANIVTLHDIIHTKKTLTLVFE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  806 YakygsLRGFLREsrkvgpgYLGsggsrnssslDHPdeRALTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNILVAEG 885
Cdd:cd07844   79 Y-----LDTDLKQ-------YMD----------DCG--GGLSMHNVRLFLFQLLRGLAYCHQRRVLHRDLKPQNLLISER 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  886 RKMKISDFGLSRdvyeedsyvKRSqgrIPVKWMAIES-----------LFDHIYTTQSDVWSFGVLLWEIVTlgGNP-YP 953
Cdd:cd07844  135 GELKLADFGLAR---------AKS---VPSKTYSNEVvtlwyrppdvlLGSTEYSTSLDMWGVGCIFYEMAT--GRPlFP 200
                        250
                 ....*....|....*...
gi 10862703  954 GIPP-----ERLFNLLKT 966
Cdd:cd07844  201 GSTDvedqlHKIFRVLGT 218
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
730-996 1.09e-08

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 2 or Heme-Regulated Inhibitor kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HRI (or EIF2AK1) contains an N-terminal regulatory heme-binding domain and a C-terminal catalytic kinase domain. It is suppressed under normal conditions by binding of the heme iron, and is activated during heme deficiency. It functions as a critical regulator that ensures balanced synthesis of globins and heme, in order to form stable hemoglobin during erythroid differentiation and maturation. HRI also protects cells and enhances survival under iron-deficient conditions. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. The HRI subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270951 [Multi-domain]  Cd Length: 284  Bit Score: 57.90  E-value: 1.09e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  730 LGEGEFGKVVKATAfHLKGRagYTTVAvKMLKENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVEYAK- 808
Cdd:cd14049   14 LGKGGYGKVYKVRN-KLDGQ--YYAIK-KILIKKVTKRDCMKVLREVKVLAGLQHPNIVGYHTAWMEHVQLMLYIQMQLc 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  809 YGSLRGFLRESRKVGPGYLGSGGSRNSSSLDHpderaltmgdLISFAWQISQGMQYLAEMKLVHRDLAARNILV-AEGRK 887
Cdd:cd14049   90 ELSLWDWIVERNKRPCEEEFKSAPYTPVDVDV----------TTKILQQLLEGVTYIHSMGIVHRDLKPRNIFLhGSDIH 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  888 MKISDFGLS-RDVYEEDS-YVKRSQGRIP--------VKWMAIESLFDHIYTTQSDVWSFGVLLWEIVtlggNPYpGIPP 957
Cdd:cd14049  160 VRIGDFGLAcPDILQDGNdSTTMSRLNGLthtsgvgtCLYAAPEQLEGSHYDFKSDMYSIGVILLELF----QPF-GTEM 234
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 10862703  958 ER--LFNLLKTGHRMERPDNCSEEMYRLMLQCWKQEPDKRP 996
Cdd:cd14049  235 ERaeVLTQLRNGQIPKSLCKRWPVQAKYIKLLTSTEPSERP 275
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
728-1001 1.23e-08

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 3 or PKR-like Endoplasmic Reticulum Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PERK (or EIF2AK3) is a type-I ER transmembrane protein containing a luminal domain bound with the chaperone BiP under unstressed conditions and a cytoplasmic catalytic kinase domain. In response to the accumulation of misfolded or unfolded proteins in the ER, PERK is activated through the release of BiP, allowing it to dimerize and autophosphorylate. It functions as the central regulator of translational control during the Unfolded Protein Response (UPR) pathway. In addition to the eIF-2 alpha subunit, PERK also phosphorylates Nrf2, a leucine zipper transcription factor which regulates cellular redox status and promotes cell survival during the UPR. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. The PERK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270950 [Multi-domain]  Cd Length: 281  Bit Score: 57.58  E-value: 1.23e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  728 KTLGEGEFGKVVKAtafhlKGRAGYTTVAVKMLKENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGP-------- 799
Cdd:cd14048   12 QCLGRGGFGVVFEA-----KNKVDDCNYAVKRIRLPNNELAREKVLREVRALAKLDHPGIVRYFNAWLERPPegwqekmd 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  800 ---LLLIVEYAKYGSLRGFLRESRKVgpgylgsggsrnsssldhpDERAL-TMGDLISfawQISQGMQYLAEMKLVHRDL 875
Cdd:cd14048   87 evyLYIQMQLCRKENLKDWMNRRCTM-------------------ESRELfVCLNIFK---QIASAVEYLHSKGLIHRDL 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  876 AARNILVAEGRKMKISDFGL--SRDVYEE--------DSYVKRSqGRIPVK-WMAIESLFDHIYTTQSDVWSFGVLLWEI 944
Cdd:cd14048  145 KPSNVFFSLDDVVKVGDFGLvtAMDQGEPeqtvltpmPAYAKHT-GQVGTRlYMSPEQIHGNQYSEKVDIFALGLILFEL 223
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 10862703  945 VtlggnpYP-GIPPERLFNLLKTgHRMERP---DNCSEEMYRLMLQCWKQEPDKRPVFADI 1001
Cdd:cd14048  224 I------YSfSTQMERIRTLTDV-RKLKFPalfTNKYPEERDMVQQMLSPSPSERPEAHEV 277
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
730-954 1.33e-08

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK10, also called PISSLRE, is essential for cell growth and proliferation, and acts through the G2/M phase of the cell cycle. CDK10 has also been identified as an important factor in endocrine therapy resistance in breast cancer. CDK10 silencing increases the transcription of c-RAF and the activation of the p42/p44 MAPK pathway, which leads to antiestrogen resistance. Patients who express low levels of CDK10 relapse early on tamoxifen. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK10 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173742 [Multi-domain]  Cd Length: 309  Bit Score: 57.76  E-value: 1.33e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  730 LGEGEFGKVVKAtafhlKGRAGYTTVAVKML-----KENASPSELRdllsEFNVLKQVNHPHVIKLYG--ACSQDGPLLL 802
Cdd:cd07845   15 IGEGTYGIVYRA-----RDTTSGEIVALKKVrmdneRDGIPISSLR----EITLLLNLRHPNIVELKEvvVGKHLDSIFL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  803 IVEYAKY--GSLrgflresrkvgpgylgsggsrnsssLDHpDERALTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNI 880
Cdd:cd07845   86 VMEYCEQdlASL-------------------------LDN-MPTPFSESQVKCLMLQLLRGLQYLHENFIIHRDLKVSNL 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  881 LVAEGRKMKISDFGLSRdVYEedsyvkrsqgrIPVKWM----------AIESLF-DHIYTTQSDVWSFGVLLWEIvtLGG 949
Cdd:cd07845  140 LLTDKGCLKIADFGLAR-TYG-----------LPAKPMtpkvvtlwyrAPELLLgCTTYTTAIDMWAVGCILAEL--LAH 205

                 ....*.
gi 10862703  950 NP-YPG 954
Cdd:cd07845  206 KPlLPG 211
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
728-949 1.49e-08

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK1 (also called rhodopsin kinase) belongs to the visual group of GRKs and is expressed in retinal cells. It phosphorylates rhodopsin in rod cells, which leads to termination of the phototransduction cascade. Mutations in GRK1 are associated to a recessively inherited form of stationary nightblindness called Oguchi disease. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors, which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270759 [Multi-domain]  Cd Length: 288  Bit Score: 57.58  E-value: 1.49e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  728 KTLGEGEFGKV----VKATAF----------HLKGRAGYTTVAVkmlkenaspselrdllsEFNVLKQVNHPHVIKLYGA 793
Cdd:cd05608    7 RVLGKGGFGEVsacqMRATGKlyackklnkkRLKKRKGYEGAMV-----------------EKRILAKVHSRFIVSLAYA 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  794 CSQDGPLLLIVEYAKYGSLRGFLRESRKVGPGYlgsggsrnsssldhPDERAltmgdlISFAWQISQGMQYLAEMKLVHR 873
Cdd:cd05608   70 FQTKTDLCLVMTIMNGGDLRYHIYNVDEENPGF--------------QEPRA------CFYTAQIISGLEHLHQRRIIYR 129
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 10862703  874 DLAARNILVAEGRKMKISDFGLSRDVYEEDSYVKRSQGrIPvKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLGG 949
Cdd:cd05608  130 DLKPENVLLDDDGNVRISDLGLAVELKDGQTKTKGYAG-TP-GFMAPELLLGEEYDYSVDYFTLGVTLYEMIAARG 203
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
730-945 1.56e-08

Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The plant-specific B-type CDKs are expressed from the late S to the M phase of the cell cycle. They are characterized by the cyclin binding motif PPT[A/T]LRE. They play a role in controlling mitosis and integrating developmental pathways, such as stomata and leaf development. CdkB has been shown to associate with both cyclin B, which controls G2/M transition, and cyclin D, which acts as a mediator in linking extracellular signals to the cell cycle. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CdkB subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270830 [Multi-domain]  Cd Length: 294  Bit Score: 57.54  E-value: 1.56e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  730 LGEGEFGKVVKAtafhlKGRAGYTTVAVK-----MLKENASPSELRdllsEFNVLKQVNH-PHVIKLYGA--CSQDG-PL 800
Cdd:cd07837    9 IGEGTYGKVYKA-----RDKNTGKLVALKktrleMEEEGVPSTALR----EVSLLQMLSQsIYIVRLLDVehVEENGkPL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  801 L-LIVEYAKyGSLRGFLRESRKvGPGylgsggsrnsssldHPDERALTMgdliSFAWQISQGMQYLAEMKLVHRDLAARN 879
Cdd:cd07837   80 LyLVFEYLD-TDLKKFIDSYGR-GPH--------------NPLPAKTIQ----SFMYQLCKGVAHCHSHGVMHRDLKPQN 139
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 10862703  880 ILVAEGRK-MKISDFGLSRDVYEEdsyVKRSQGRIPVKWM-AIESLFDHI-YTTQSDVWSFGVLLWEIV 945
Cdd:cd07837  140 LLVDKQKGlLKIADLGLGRAFTIP---IKSYTHEIVTLWYrAPEVLLGSThYSTPVDMWSVGCIFAEMS 205
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
756-951 1.59e-08

Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phosphorylase kinase (PhK) catalyzes the phosphorylation of inactive phosphorylase b to form the active phosphorylase a. It coordinates hormonal, metabolic, and neuronal signals to initiate the breakdown of glycogen stores, which enables the maintenance of blood-glucose homeostasis during fasting, and is also used as a source of energy for muscle contraction. PhK is one of the largest and most complex protein kinases, composed of a heterotetramer containing four molecules each of four subunit types: one catalytic (gamma) and three regulatory (alpha, beta, and delta). The gamma 2 subunit (PhKG2) is also referred to as the testis/liver gamma isoform. Mutations in its gene cause autosomal-recessive glycogenosis of the liver. The gamma subunit, when isolated, is constitutively active and does not require phosphorylation of the A-loop for activity. The regulatory subunits restrain this kinase activity until signals are received to relieve this inhibition. For example, the kinase is activated in response to hormonal stimulation, after autophosphorylation or phosphorylation by cAMP-dependent kinase of the alpha and beta subunits. The high-affinity binding of ADP to the beta subunit also stimulates kinase activity, whereas calcium relieves inhibition by binding to the delta (calmodulin) subunit. The PhKG2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271083 [Multi-domain]  Cd Length: 279  Bit Score: 57.29  E-value: 1.59e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  756 AVKMLK---ENASPSELRDL----LSEFNVLKQV-NHPHVIKLYGACSQDGPLLLIVEYAKYGSLRGFLREsrKVgpgyl 827
Cdd:cd14181   39 AVKIIEvtaERLSPEQLEEVrsstLKEIHILRQVsGHPSIITLIDSYESSTFIFLVFDLMRRGELFDYLTE--KV----- 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  828 gsggsrnssSLDHPDERALtMGDLIsfawqisQGMQYLAEMKLVHRDLAARNILVAEGRKMKISDFGLSrdVYEEDSYVK 907
Cdd:cd14181  112 ---------TLSEKETRSI-MRSLL-------EAVSYLHANNIVHRDLKPENILLDDQLHIKLSDFGFS--CHLEPGEKL 172
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 10862703  908 RSQGRIPvKWMAIESL---FDHI---YTTQSDVWSFGVLLWEIvtLGGNP 951
Cdd:cd14181  173 RELCGTP-GYLAPEILkcsMDEThpgYGKEVDLWACGVILFTL--LAGSP 219
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
728-946 1.70e-08

Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. Myt1 is a cytoplasmic cell cycle checkpoint kinase that can keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of N-terminal thr (T14) and tyr (Y15) residues, leading to the delay of meiosis I entry. Meiotic progression is ensured by a two-step inhibition and downregulation of Myt1 by CDK1/XRINGO and p90Rsk during oocyte maturation. In addition, Myt1 targets cyclin B1/B2 and is essential for Golgi and ER assembly during telophase. In Drosophila, Myt1 may be a downstream target of Notch during eye development. The Myt1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270952 [Multi-domain]  Cd Length: 249  Bit Score: 56.55  E-value: 1.70e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  728 KTLGEGEFGKVVKAtafhlKGRAGYTTVAVKMLKEN-ASPSELRDLLSEFNVLKQVN-HPHVIKLYGACSQDGPLLLIVE 805
Cdd:cd14050    7 SKLGEGSFGEVFKV-----RSREDGKLYAVKRSRSRfRGEKDRKRKLEEVERHEKLGeHPNCVRFIKAWEEKGILYIQTE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  806 YAKyGSLRGFLRESRKVgpgylgsggsrnsssldhPDERaltmgdLISFAWQISQGMQYLAEMKLVHRDLAARNILVAEG 885
Cdd:cd14050   82 LCD-TSLQQYCEETHSL------------------PESE------VWNILLDLLKGLKHLHDHGLIHLDIKPANIFLSKD 136
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 10862703  886 RKMKISDFGLSRDVYEEDS-YVKRSQGRipvkWMAIEsLFDHIYTTQSDVWSFGVLLWEIVT 946
Cdd:cd14050  137 GVCKLGDFGLVVELDKEDIhDAQEGDPR----YMAPE-LLQGSFTKAADIFSLGITILELAC 193
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
728-960 1.74e-08

Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PFTAIRE-2 is also referred to as ALS2CR7 (amyotrophic lateral sclerosis 2 (juvenile) chromosome region candidate 7). It may be associated with amyotrophic lateral sclerosis 2 (ALS2), an autosomal recessive form of juvenile ALS. The function of PFTAIRE-2 is not yet known. It shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PFTAIRE-2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270852 [Multi-domain]  Cd Length: 286  Bit Score: 57.28  E-value: 1.74e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  728 KTLGEGEFGKVVKATAfhlkgRAGYTTVAVKMLKENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVEYA 807
Cdd:cd07870    6 EKLGEGSYATVYKGIS-----RINGQLVALKVISMKTEEGVPFTAIREASLLKGLKHANIVLLHDIIHTKETLTFVFEYM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  808 kYGSLRGFLRESrkvgPGYLgsggsrnsssldHPDERALtmgdlisFAWQISQGMQYLAEMKLVHRDLAARNILVAEGRK 887
Cdd:cd07870   81 -HTDLAQYMIQH----PGGL------------HPYNVRL-------FMFQLLRGLAYIHGQHILHRDLKPQNLLISYLGE 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  888 MKISDFGLSR------DVYEedSYVKRSQGRIPVKWMAIESlfdhiYTTQSDVWSFGVLLWEIVTlgGNP-YPGIP--PE 958
Cdd:cd07870  137 LKLADFGLARaksipsQTYS--SEVVTLWYRPPDVLLGATD-----YSSALDIWGAGCIFIEMLQ--GQPaFPGVSdvFE 207

                 ..
gi 10862703  959 RL 960
Cdd:cd07870  208 QL 209
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
728-945 1.91e-08

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 57.58  E-value: 1.91e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703   728 KTLGEGEFGKVVKATafhlkgRAGYTTVAVkmLKENASPSELRDLLsefnVLKQVNHPHVIKLYGACSQdGPLLLIVEYA 807
Cdd:PHA03209   72 KTLTPGSEGRVFVAT------KPGQPDPVV--LKIGQKGTTLIEAM----LLQNVNHPSVIRMKDTLVS-GAITCMVLPH 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703   808 KYGSLRGFLreSRKVGPgylgsggsrnsssldhpderaLTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNILVAEGRK 887
Cdd:PHA03209  139 YSSDLYTYL--TKRSRP---------------------LPIDQALIIEKQILEGLRYLHAQRIIHRDVKTENIFINDVDQ 195
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 10862703   888 MKISDFGLSR-DVYEEDSYVKRSQgripVKWMAIESLFDHIYTTQSDVWSFGVLLWEIV 945
Cdd:PHA03209  196 VCIGDLGAAQfPVVAPAFLGLAGT----VETNAPEVLARDKYNSKADIWSAGIVLFEML 250
PK_IRAK3 cd14160
Pseudokinase domain of Interleukin-1 Receptor Associated Kinase 3; The pseudokinase domain ...
730-946 2.14e-08

Pseudokinase domain of Interleukin-1 Receptor Associated Kinase 3; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain (a pseudokinase in the case of IRAK3), and a C-terminal domain; IRAK-4 lacks the C-terminal domain. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK3 (or IRAK-M) is the only IRAK that does not show kinase activity. It is found only in monocytes and macrophages in humans, and functions as a negative regulator of TLR signaling including TLR-2 induced p38 activation. It also negatively regulates the alternative NFkB pathway in a TLR-2 specific manner. IRAK3 is downregulated in the monocytes of obese people, and is associated with high SOD2, a marker of mitochondrial oxidative stress. It is an important inhibitor of inflammation in association with obesity and metabolic syndrome. The IRAK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271062 [Multi-domain]  Cd Length: 276  Bit Score: 56.82  E-value: 2.14e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  730 LGEGEFGKVvkatafhLKGRAGYTTVAVKMLKENAS---PSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVEY 806
Cdd:cd14160    1 IGEGEIFEV-------YRVRIGNRSYAVKLFKQEKKmqwKKHWKRFLSELEVLLLFQHPNILELAAYFTETEKFCLVYPY 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  807 AKYGSLRGFLREsrkvgpgylgsggsrnsssldHPDERALTMGDLISFAWQISQGMQYLAEMK---LVHRDLAARNILVA 883
Cdd:cd14160   74 MQNGTLFDRLQC---------------------HGVTKPLSWHERINILIGIAKAIHYLHNSQpctVICGNISSANILLD 132
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 10862703  884 EGRKMKISDFGLSR----DVYEEDSYVKRSQGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVT 946
Cdd:cd14160  133 DQMQPKLTDFALAHfrphLEDQSCTINMTTALHKHLWYMPEEYIRQGKLSVKTDVYSFGIVIMEVLT 199
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
726-967 2.17e-08

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type II; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKs contain an N-terminal catalytic domain followed by a regulatory domain that harbors a CaM binding site. In addition, CaMKII contains a C-terminal association domain that facilitates oligomerization. There are four CaMKII proteins (alpha, beta, gamma, delta) encoded by different genes; each gene undergoes alternative splicing to produce more than 30 isoforms. CaMKII-alpha and -beta are enriched in neurons while CaMKII-gamma and -delta are predominant in myocardium. CaMKII is a signaling molecule that translates upstream calcium and reactive oxygen species (ROS) signals into downstream responses that play important roles in synaptic function and cardiovascular physiology. It is a major component of the postsynaptic density and is critical in regulating synaptic plasticity including long-term potentiation. It is critical in regulating ion channels and proteins involved in myocardial excitation-contraction and excitation-transcription coupling. Excessive CaMKII activity promotes processes that contribute to heart failure and arrhythmias. The CaMKII subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270988 [Multi-domain]  Cd Length: 292  Bit Score: 57.05  E-value: 2.17e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  726 LGKTLGEGEFGKVVKAtafhLKGRAGYTtVAVKMLK-ENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIV 804
Cdd:cd14086    5 LKEELGKGAFSVVRRC----VQKSTGQE-FAAKIINtKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGFHYLVF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  805 EYAKYGSL------RGFLRESrkvgpgylgsggsrnsssldhpderaltmgDLISFAWQISQGMQYLAEMKLVHRDLAAR 878
Cdd:cd14086   80 DLVTGGELfedivaREFYSEA------------------------------DASHCIQQILESVNHCHQNGIVHRDLKPE 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  879 NILVA---EGRKMKISDFGLSRDVyEEDSYVKRSQGRIPVkWMAIESLFDHIYTTQSDVWSFGVLLWeIVTLGGNPYPGI 955
Cdd:cd14086  130 NLLLAsksKGAAVKLADFGLAIEV-QGDQQAWFGFAGTPG-YLSPEVLRKDPYGKPVDIWACGVILY-ILLVGYPPFWDE 206
                        250
                 ....*....|..
gi 10862703  956 PPERLFNLLKTG 967
Cdd:cd14086  207 DQHRLYAQIKAG 218
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
728-1004 2.23e-08

Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PASK (or PASKIN) is a nutrient and energy sensor and thus, plays an important role in maintaining cellular energy homeostasis. It coordinates the utilization of glucose in response to metabolic demand. It contains an N-terminal PAS domain which directly interacts and inhibits a C-terminal catalytic kinase domain. The PAS domain serves as a sensory module for different environmental signals such as light, redox state, and various metabolites. Binding of ligands to the PAS domain causes structural changes which leads to kinase activation and the phosphorylation of substrates to trigger the appropriate cellular response. The PASK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270906 [Multi-domain]  Cd Length: 256  Bit Score: 56.63  E-value: 2.23e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  728 KTLGEGEFGKVvkATAFHLKGRagyTTVAVKMLKENA--SPSELRD-----LLSEFNVLKQVN---HPHVIKLYGACSQD 797
Cdd:cd14004    6 KEMGEGAYGQV--NLAIYKSKG---KEVVIKFIFKERilVDTWVRDrklgtVPLEIHILDTLNkrsHPNIVKLLDFFEDD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  798 GPLLLIVEyaKYGS-LRGFLRESRKVGpgylgsggsrnsssLDHPDERALTMgdlisfawQISQGMQYLAEMKLVHRDLA 876
Cdd:cd14004   81 EFYYLVME--KHGSgMDLFDFIERKPN--------------MDEKEAKYIFR--------QVADAVKHLHDQGIVHRDIK 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  877 ARNILVAEGRKMKISDFGLSrdvyeedSYVKRSQ-----GRIpvKWMAIESLFDHIYTTQS-DVWSFGVLLWEIVtLGGN 950
Cdd:cd14004  137 DENVILDGNGTIKLIDFGSA-------AYIKSGPfdtfvGTI--DYAAPEVLRGNPYGGKEqDIWALGVLLYTLV-FKEN 206
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 10862703  951 PYpgipperlFNLLKTGHRMERPDNC-SEEMYRLMLQCWKQEPDKRPVFADISKD 1004
Cdd:cd14004  207 PF--------YNIEEILEADLRIPYAvSEDLIDLISRMLNRDVGDRPTIEELLTD 253
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
774-1011 2.34e-08

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 57.70  E-value: 2.34e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703   774 SEFNVLKQVNHPHVIKLYGACSQDGPLLLIVEYAKyGSLRGFLresrkvgpgylgsggsrnsssldhPDERALTMGDLIS 853
Cdd:PHA03212  132 TEAHILRAINHPSIIQLKGTFTYNKFTCLILPRYK-TDLYCYL------------------------AAKRNIAICDILA 186
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703   854 FAWQISQGMQYLAEMKLVHRDLAARNILVAEGRKMKISDFGLSrdVYEEDSYVKRSQGripvkWM------AIESLFDHI 927
Cdd:PHA03212  187 IERSVLRAIQYLHENRIIHRDIKAENIFINHPGDVCLGDFGAA--CFPVDINANKYYG-----WAgtiatnAPELLARDP 259
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703   928 YTTQSDVWSFGVLLWEIVT----------LGGNpypgIPPERLFNLL--KTG-HRMERPDNCS---EEMYRLMLQCWKQE 991
Cdd:PHA03212  260 YGPAVDIWSAGIVLFEMATchdslfekdgLDGD----CDSDRQIKLIirRSGtHPNEFPIDAQanlDEIYIGLAKKSSRK 335
                         250       260
                  ....*....|....*....|...
gi 10862703   992 PDKRPVFADISK---DLEKMMVK 1011
Cdd:PHA03212  336 PGSRPLWTNLYElpiDLEYLICK 358
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
726-954 2.40e-08

Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDKL1, also called p42 KKIALRE, is a glial protein that is upregulated in gliosis. It is present in neuroblastoma and A431 human carcinoma cells, and may be implicated in neoplastic transformation. The function of CDKL4 is unknown. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL1/4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270837 [Multi-domain]  Cd Length: 286  Bit Score: 56.61  E-value: 2.40e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  726 LGKtLGEGEFGKVVKAtafhlKGRAGYTTVAVKMLKENASPSELRDL-LSEFNVLKQVNHPHVIKLYGACSQDGPLLLIV 804
Cdd:cd07847    6 LSK-IGEGSYGVVFKC-----RNRETGQIVAIKKFVESEDDPVIKKIaLREIRMLKQLKHPNLVNLIEVFRRKRKLHLVF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  805 EYAKYGSLRgflresrkvgpgylgsggsrnssSLD-HPdeRALTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNILVA 883
Cdd:cd07847   80 EYCDHTVLN-----------------------ELEkNP--RGVPEHLIKKIIWQTLQAVNFCHKHNCIHRDVKPENILIT 134
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 10862703  884 EGRKMKISDFGLSR------DVYEEdsYVKRSQGRIPvkwmaiESLF-DHIYTTQSDVWSFGVLLWEIVTlgGNP-YPG 954
Cdd:cd07847  135 KQGQIKLCDFGFARiltgpgDDYTD--YVATRWYRAP------ELLVgDTQYGPPVDVWAIGCVFAELLT--GQPlWPG 203
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
854-945 2.45e-08

Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NLK is an atypical mitogen-activated protein kinase (MAPK) that is not regulated by a MAPK kinase. It functions downstream of the MAPK kinase kinase Tak1, which also plays a role in activating the JNK and p38 MAPKs. The Tak1/NLK pathways are regulated by Wnts, a family of secreted proteins that is critical in the control of asymmetric division and cell polarity. NLK can phosphorylate transcription factors from the TCF/LEF family, inhibiting their ability to activate the transcription of target genes. In prostate cancer cells, NLK is involved in regulating androgen receptor-mediated transcription and its expression is altered during cancer progression. MAPKs are important mediators of cellular responses to extracellular signals. The NLK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173748 [Multi-domain]  Cd Length: 372  Bit Score: 57.45  E-value: 2.45e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  854 FAWQISQGMQYLAEMKLVHRDLAARNILVAEGRKMKISDFGLSRdVYEEDSYVKRSQGRIPVKWMAIESLF--DHiYTTQ 931
Cdd:cd07853  108 FLYQILRGLKYLHSAGILHRDIKPGNLLVNSNCVLKICDFGLAR-VEEPDESKHMTQEVVTQYYRAPEILMgsRH-YTSA 185
                         90
                 ....*....|....
gi 10862703  932 SDVWSFGVLLWEIV 945
Cdd:cd07853  186 VDIWSVGCIFAELL 199
PKc_YAK1 cd14212
Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze ...
729-964 2.76e-08

Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. This subfamily is composed of proteins with similarity to Saccharomyces cerevisiae YAK1 (or Yak1p), a dual-specificity kinase that autophosphorylates at tyrosine residues and phosphorylates substrates on S/T residues. YAK1 phosphorylates and activates the transcription factors Hsf1 and Msn2, which play important roles in cellular homeostasis during stress conditions including heat shock, oxidative stress, and nutrient deficiency. It also phosphorylates the protein POP2, a component of a complex that regulates transcription, under glucose-deprived conditions. It functions as a part of a glucose-sensing system that is involved in controlling growth in yeast. The YAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271114 [Multi-domain]  Cd Length: 330  Bit Score: 56.87  E-value: 2.76e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  729 TLGEGEFGKVVKATAfHLKGRagytTVAVKMLKENasPSELRDLLSEFNVLKQVN-------HPHVIKLYGACSQDGPLL 801
Cdd:cd14212    6 LLGQGTFGQVVKCQD-LKTNK----LVAVKVLKNK--PAYFRQAMLEIAILTLLNtkydpedKHHIVRLLDHFMHHGHLC 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  802 LIVEyakygsLRG-----FLRESRKvgpgylgsggsrnsssldhpdeRALTMGDLISFAWQISQGMQYLAEMKLVHRDLA 876
Cdd:cd14212   79 IVFE------LLGvnlyeLLKQNQF----------------------RGLSLQLIRKFLQQLLDALSVLKDARIIHCDLK 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  877 ARNILV--AEGRKMKISDFGLS----RDVYeedSYVkrsQGRIpvkWMAIESLFDHIYTTQSDVWSFGVLLWEIVtLGgn 950
Cdd:cd14212  131 PENILLvnLDSPEIKLIDFGSAcfenYTLY---TYI---QSRF---YRSPEVLLGLPYSTAIDMWSLGCIAAELF-LG-- 198
                        250
                 ....*....|....
gi 10862703  951 pYPGIPPERLFNLL 964
Cdd:cd14212  199 -LPLFPGNSEYNQL 211
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
717-1042 3.18e-08

Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase (also called MAPK13); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38delta/MAPK13 is found in skeletal muscle, heart, lung, testis, pancreas, and small intestine. It regulates microtubule function by phosphorylating Tau. It activates the c-jun promoter and plays a role in G2 cell cycle arrest. It also controls the degration of c-Myb, which is associated with myeloid leukemia and poor prognosis in colorectal cancer. p38delta is the main isoform involved in regulating the differentiation and apoptosis of keratinocytes. p38 kinases are MAPKs, serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38delta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143384 [Multi-domain]  Cd Length: 342  Bit Score: 56.83  E-value: 3.18e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  717 WEFPRKNLVLgKTLGEGEFGKVVKAtafhLKGRAGyTTVAVKMLKENASpSEL--RDLLSEFNVLKQVNHPHVIKLY--- 791
Cdd:cd07879   11 WELPERYTSL-KQVGSGAYGSVCSA----IDKRTG-EKVAIKKLSRPFQ-SEIfaKRAYRELTLLKHMQHENVIGLLdvf 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  792 -GACS----QDGPLLLIVEYAKYGSLRGFLRESRKVGpgYLgsggsrnsssldhpderaltmgdlisfAWQISQGMQYLA 866
Cdd:cd07879   84 tSAVSgdefQDFYLVMPYMQTDLQKIMGHPLSEDKVQ--YL---------------------------VYQMLCGLKYIH 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  867 EMKLVHRDLAARNILVAEGRKMKISDFGLSRDV-YEEDSYVKRSQGRIP---VKWMaieslfdHiYTTQSDVWSFGVLLW 942
Cdd:cd07879  135 SAGIIHRDLKPGNLAVNEDCELKILDFGLARHAdAEMTGYVVTRWYRAPeviLNWM-------H-YNQTVDIWSVGCIMA 206
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  943 EIVT----LGGNPYpgipPERLFNLLK-TGHR----MERPDNCSEEMYrlmLQCWKQEPDKR-----PVFADISKD-LEK 1007
Cdd:cd07879  207 EMLTgktlFKGKDY----LDQLTQILKvTGVPgpefVQKLEDKAAKSY---IKSLPKYPRKDfstlfPKASPQAVDlLEK 279
                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 10862703 1008 MM---VKRRDYLDLAASTPSDSLIYDDGLSEEETPLVD 1042
Cdd:cd07879  280 MLeldVDKRLTATEALEHPYFDSFRDADEETEQQPYDD 317
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
697-1001 3.38e-08

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase Kinase 7; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK7 is a dual-specificity PK that phosphorylates and activates its downstream target, c-Jun N-terminal kinase (JNK), on specific threonine and tyrosine residues. Although MKK7 is capable of dual phosphorylation, it prefers to phosphorylate the threonine residue of JNK. Thus, optimal activation of JNK requires both MKK4 and MKK7. MKK7 is primarily activated by cytokines. MKK7 is essential for liver formation during embryogenesis. It plays roles in G2/M cell cycle arrest and cell growth. In addition, it is involved in the control of programmed cell death, which is crucial in oncogenesis, cancer chemoresistance, and antagonism to TNFalpha-induced killing, through its inhibition by Gadd45beta and the subsequent suppression of the JNK cascade. The MKK7 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270791 [Multi-domain]  Cd Length: 295  Bit Score: 56.23  E-value: 3.38e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  697 LDSMENQVSVDAFKILEDpkwefprknlvlgktLGEGEFGKVVKATafHLKGRagyTTVAVKMLKENASPSELRDLLSEF 776
Cdd:cd06618    5 IDGKKYKADLNDLENLGE---------------IGSGTCGQVYKMR--HKKTG---HVMAVKQMRRSGNKEENKRILMDL 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  777 NV-LKQVNHPHVIKLYGACSQDGPLLLIVEYAKyGSLRGFLRESRKVGPgylgsggsrnsssldhpdERALtmGDLisfA 855
Cdd:cd06618   65 DVvLKSHDCPYIVKCYGYFITDSDVFICMELMS-TCLDKLLKRIQGPIP------------------EDIL--GKM---T 120
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  856 WQISQGMQYLAEMK-LVHRDLAARNILVAEGRKMKISDFGLS-RDVyeeDSYVK-RSQGRIPvkWMAIESL----FDHiY 928
Cdd:cd06618  121 VSIVKALHYLKEKHgVIHRDVKPSNILLDESGNVKLCDFGISgRLV---DSKAKtRSAGCAA--YMAPERIdppdNPK-Y 194
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 10862703  929 TTQSDVWSFGVLLWEIVTlGGNPYPGIPPErlFNLLKTGHRMERP-----DNCSEEMYRLMLQCWKQEPDKRPVFADI 1001
Cdd:cd06618  195 DIRADVWSLGISLVELAT-GQFPYRNCKTE--FEVLTKILNEEPPslppnEGFSPDFCSFVDLCLTKDHRYRPKYREL 269
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
720-996 3.59e-08

Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase kinase kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP4K3 plays a role in the nutrient-responsive pathway of mTOR (mammalian target of rapamycin) signaling. MAP4K3 is required in the activation of S6 kinase by amino acids and for the phosphorylation of the mTOR-regulated inhibitor of eukaryotic initiation factor 4E. mTOR regulates ribosome biogenesis and protein translation, and is frequently deregulated in cancer. MAP4Ks are involved in MAPK signaling pathways by activating a MAPK kinase kinase. Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAP3K to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Members of this subfamily contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. The MAP4K3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270812 [Multi-domain]  Cd Length: 272  Bit Score: 56.21  E-value: 3.59e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  720 PRKNLVLGKTLGEGEFGKVVKATAFHLKGRAgyttvAVKMLKenASPSELRDLLS-EFNVLKQVNHPHVIKLYGACSQDG 798
Cdd:cd06645    9 PQEDFELIQRIGSGTYGDVYKARNVNTGELA-----AIKVIK--LEPGEDFAVVQqEIIMMKDCKHSNIVAYFGSYLRRD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  799 PLLLIVEYAKYGSLRGFLRESrkvGPgylgsggsrnsssldhpderaLTMGDLISFAWQISQGMQYLAEMKLVHRDLAAR 878
Cdd:cd06645   82 KLWICMEFCGGGSLQDIYHVT---GP---------------------LSESQIAYVSRETLQGLYYLHSKGKMHRDIKGA 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  879 NILVAEGRKMKISDFGLSRDVyeEDSYVKRSQGRIPVKWMAIESLFDHI---YTTQSDVWSFGVLLWEIVTLGGNPYPGI 955
Cdd:cd06645  138 NILLTDNGHVKLADFGVSAQI--TATIAKRKSFIGTPYWMAPEVAAVERkggYNQLCDIWAVGITAIELAELQPPMFDLH 215
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 10862703  956 PPERLFNLLKTGH---RMERPDNCSEEMYRLMLQCWKQEPDKRP 996
Cdd:cd06645  216 PMRALFLMTKSNFqppKLKDKMKWSNSFHHFVKMALTKNPKKRP 259
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
730-995 3.85e-08

Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CASK belongs to the MAGUK (membrane-associated guanylate kinase) protein family, which functions as multiple domain adaptor proteins and is characterized by the presence of a core of three domains: PDZ, SH3, and guanylate kinase (GuK). The enzymatically inactive GuK domain in MAGUK proteins mediates protein-protein interactions and associates intramolecularly with the SH3 domain. In addition, CASK contains a catalytic kinase and two L27 domains. It is highly expressed in the nervous system and plays roles in synaptic protein targeting, neural development, and regulation of gene expression. Binding partners include parkin (a Parkinson's disease molecule), neurexin (adhesion molecule), syndecans, calcium channel proteins, CINAP (nucleosome assembly protein), transcription factor Tbr-1, and the cytoplasmic adaptor proteins Mint1, Veli/mLIN-7/MALS, SAP97, caskin, and CIP98. Deletion or mutations in the CASK gene have been implicated in X-linked mental retardation. The CASK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270996 [Multi-domain]  Cd Length: 300  Bit Score: 56.40  E-value: 3.85e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  730 LGEGEFGKVVKAtaFHLKGRAGYTTVAVKMLKENASPS-ELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVEYAK 808
Cdd:cd14094   11 IGKGPFSVVRRC--IHRETGQQFAVKIVDVAKFTSSPGlSTEDLKREASICHMLKHPHIVELLETYSSDGMLYMVFEFMD 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  809 YGSL---------RGFLReSRKVGPGYLGsggsrnsssldhpderaltmgdlisfawQISQGMQYLAEMKLVHRDLAARN 879
Cdd:cd14094   89 GADLcfeivkradAGFVY-SEAVASHYMR----------------------------QILEALRYCHDNNIIHRDVKPHC 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  880 ILVAE---GRKMKISDFGLSRDVYEEDSYvkrSQGRIPV-KWMAIESLFDHIYTTQSDVWSFGVLLWeiVTLGGN-PYPG 954
Cdd:cd14094  140 VLLASkenSAPVKLGGFGVAIQLGESGLV---AGGRVGTpHFMAPEVVKREPYGKPVDVWGCGVILF--ILLSGClPFYG 214
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 10862703  955 iPPERLFN-LLKTGHRMERP--DNCSEEMYRLMLQCWKQEPDKR 995
Cdd:cd14094  215 -TKERLFEgIIKGKYKMNPRqwSHISESAKDLVRRMLMLDPAER 257
STKc_ACVR1_ALK1 cd14142
Catalytic domain of the Serine/Threonine Kinases, Activin Type I Receptor and Activin ...
722-1008 4.14e-08

Catalytic domain of the Serine/Threonine Kinases, Activin Type I Receptor and Activin receptor-Like Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ACVR1, also called Activin receptor-Like Kinase 2 (ALK2), and ALK1 act as receptors for bone morphogenetic proteins (BMPs) and they activate SMAD1/5/8. ACVR1 is widely expressed while ALK1 is limited mainly to endothelial cells. The specificity of BMP binding to type I receptors is affected by type II receptors. ACVR1 binds BMP6/7/9/10 and can also bind anti-Mullerian hormone (AMH) in the presence of AMHR2. ALK1 binds BMP9/10 as well as TGFbeta in endothelial cells. A missense mutation in the GS domain of ACVR1 causes fibrodysplasia ossificans progressiva, a complex and disabling disease characterized by congenital skeletal malformations and extraskeletal bone formation. ACVR1 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors, and AMH, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like ACVR1 and ALK1, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The ACVR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271044 [Multi-domain]  Cd Length: 298  Bit Score: 56.29  E-value: 4.14e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  722 KNLVLGKTLGEGEFGKVvkatafhLKGRAGYTTVAVKMLKENASPSELRDLLSEFNVLkqVNHPHVIKLYGA-------C 794
Cdd:cd14142    5 RQITLVECIGKGRYGEV-------WRGQWQGESVAVKIFSSRDEKSWFRETEIYNTVL--LRHENILGFIASdmtsrnsC 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  795 SQdgpLLLIVEYAKYGSLRGFLRESrkvgpgylgsggsrnsssldhpderALTMGDLISFAWQISQGMQYL--------A 866
Cdd:cd14142   76 TQ---LWLITHYHENGSLYDYLQRT-------------------------TLDHQEMLRLALSAASGLVHLhteifgtqG 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  867 EMKLVHRDLAARNILVAEGRKMKISDFGLSRDVYEEDSYVKRSQG-RIPVK-WMAIESLFDHIYTT------QSDVWSFG 938
Cdd:cd14142  128 KPAIAHRDLKSKNILVKSNGQCCIADLGLAVTHSQETNQLDVGNNpRVGTKrYMAPEVLDETINTDcfesykRVDIYAFG 207
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  939 VLLWEIV---TLGG-----NP--YPGIPPERLFNLLKT-----GHRMERPDNCSEE-----MYRLMLQCWKQEPDKRPVF 998
Cdd:cd14142  208 LVLWEVArrcVSGGiveeyKPpfYDVVPSDPSFEDMRKvvcvdQQRPNIPNRWSSDptltaMAKLMKECWYQNPSARLTA 287
                        330
                 ....*....|
gi 10862703  999 ADISKDLEKM 1008
Cdd:cd14142  288 LRIKKTLLKI 297
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
728-1003 4.67e-08

Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein kinase subfamily 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The SnRKs form three different subfamilies designated SnRK1-3. SnRK2 is represented in this cd. SnRK2s are involved in plant response to abiotic stresses and abscisic acid (ABA)-dependent plant development. The SnRK2s subfamily is in turn classed into three subgroups, all 3 of which are represented in this CD. Group 1 comprises kinases not activated by ABA, group 2 - kinases not activated or activated very weakly by ABA (depending on plant species), and group 3 - kinases strongly activated by ABA. The SnRKs belong to a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271132 [Multi-domain]  Cd Length: 257  Bit Score: 55.55  E-value: 4.67e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  728 KTLGEGEFGkvvkaTAFHLKGRAGYTTVAVKMLKENASPSE--LRDLLSEfnvlKQVNHPHVIKLYGACSQDGPLLLIVE 805
Cdd:cd14662    6 KDIGSGNFG-----VARLMRNKETKELVAVKYIERGLKIDEnvQREIINH----RSLRHPNIIRFKEVVLTPTHLAIVME 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  806 YAKYGSLRGflresRKVGPGYLgsggsrnsssldHPDERALTMGDLISfawqisqGMQYLAEMKLVHRDLAARNILV--A 883
Cdd:cd14662   77 YAAGGELFE-----RICNAGRF------------SEDEARYFFQQLIS-------GVSYCHSMQICHRDLKLENTLLdgS 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  884 EGRKMKISDFGLSRdvyeedSYVKRSQGRIPV---KWMAIESLFDHIYTTQ-SDVWSFGVLLWeiVTLGGnPYPGIPPER 959
Cdd:cd14662  133 PAPRLKICDFGYSK------SSVLHSQPKSTVgtpAYIAPEVLSRKEYDGKvADVWSCGVTLY--VMLVG-AYPFEDPDD 203
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 10862703  960 LFNLLKTGHRMER-----PDNC--SEEMYRLMLQCWKQEPDKRPVFADISK 1003
Cdd:cd14662  204 PKNFRKTIQRIMSvqykiPDYVrvSQDCRHLLSRIFVANPAKRITIPEIKN 254
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
728-951 4.72e-08

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-epsilon has been shown to behave as an oncoprotein. Its overexpression contributes to neoplastic transformation depending on the cell type. It contributes to oncogenesis by inducing disordered cell growth and inhibiting cell death. It also plays a role in tumor invasion and metastasis. PKC-epsilon has also been found to confer cardioprotection against ischemia and reperfusion-mediated damage. Other cellular functions include the regulation of gene expression, cell adhesion, and cell motility. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC-epsilon subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270743 [Multi-domain]  Cd Length: 321  Bit Score: 56.35  E-value: 4.72e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  728 KTLGEGEFGKVVkatafhLKGRAGYTTV-AVKMLKENA--SPSELRDLLSEFNVLK-QVNHPHVIKLYGACSQDGPLLLI 803
Cdd:cd05591    1 KVLGKGSFGKVM------LAERKGTDEVyAIKVLKKDVilQDDDVDCTMTEKRILAlAAKHPFLTALHSCFQTKDRLFFV 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  804 VEYAKYGSLRGFLRESRKvgpgylgsggsrnsssLDHPDERAltmgdlisFAWQISQGMQYLAEMKLVHRDLAARNILV- 882
Cdd:cd05591   75 MEYVNGGDLMFQIQRARK----------------FDEPRARF--------YAAEVTLALMFLHRHGVIYRDLKLDNILLd 130
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 10862703  883 AEGRkMKISDFGLSRDVYEEDSYVKRSQGrIPvKWMAIESLFDHIYTTQSDVWSFGVLLWEIvtLGGNP 951
Cdd:cd05591  131 AEGH-CKLADFGMCKEGILNGKTTTTFCG-TP-DYIAPEILQELEYGPSVDWWALGVLMYEM--MAGQP 194
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
695-996 5.43e-08

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 56.80  E-value: 5.43e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703   695 PSLDSMENQVS---VDAFKILEDPKWEfPRKNLVLGKTLGEGEFGKVVKATafhlKGRAGYTtVAVKMLK-ENASPSELR 770
Cdd:PTZ00283    3 ASGDAMIGRVCrtfPDTFAKDEATAKE-QAKKYWISRVLGSGATGTVLCAK----RVSDGEP-FAVKVVDmEGMSEADKN 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703   771 DLLSEFNVLKQVNHPHVIKLYGACSQDGP--------LLLIVEYAKYGSLRGFLRESRKVGPGYLgsggsrnssslDHpd 842
Cdd:PTZ00283   77 RAQAEVCCLLNCDFFSIVKCHEDFAKKDPrnpenvlmIALVLDYANAGDLRQEIKSRAKTNRTFR-----------EH-- 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703   843 ERALTMgdlisfaWQISQGMQYLAEMKLVHRDLAARNILVAEGRKMKISDFGLSR---DVYEEDsyVKRSQGRIPVkWMA 919
Cdd:PTZ00283  144 EAGLLF-------IQVLLAVHHVHSKHMIHRDIKSANILLCSNGLVKLGDFGFSKmyaATVSDD--VGRTFCGTPY-YVA 213
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 10862703   920 IESLFDHIYTTQSDVWSFGVLLWEIVTLgGNPYPGIPPERLFNLLKTGHRMERPDNCSEEMYRLMLQCWKQEPDKRP 996
Cdd:PTZ00283  214 PEIWRRKPYSKKADMFSLGVLLYELLTL-KRPFDGENMEEVMHKTLAGRYDPLPPSISPEMQEIVTALLSSDPKRRP 289
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
854-946 6.62e-08

Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also called ERK4) and 6 (also called ERK3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK4 (also called ERK4 or p63MAPK) and MAPK6 (also called ERK3 or p97MAPK) are atypical MAPKs that are not regulated by MAPK kinases. MAPK6 is expressed ubiquitously with highest amounts in brain and skeletal muscle. It may be involved in the control of cell differentiation by negatively regulating cell cycle progression in certain conditions. It may also play a role in glucose-induced insulin secretion. MAPK6 and MAPK4 cooperate to regulate the activity of MAPK-activated protein kinase 5 (MK5), leading to its relocation to the cytoplasm and exclusion from the nucleus. The MAPK6/MK5 and MAPK4/MK5 pathways may play critical roles in embryonic and post-natal development. MAPKs are important mediators of cellular responses to extracellular signals. The MAPK4/6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143359 [Multi-domain]  Cd Length: 342  Bit Score: 55.94  E-value: 6.62e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  854 FAWQISQGMQYLAEMKLVHRDLAARNILV-AEGRKMKISDFGLSRDV---YEEDSYVkrSQGrIPVKWMAIESLFDHI-- 927
Cdd:cd07854  119 FMYQLLRGLKYIHSANVLHRDLKPANVFInTEDLVLKIGDFGLARIVdphYSHKGYL--SEG-LVTKWYRSPRLLLSPnn 195
                         90
                 ....*....|....*....
gi 10862703  928 YTTQSDVWSFGVLLWEIVT 946
Cdd:cd07854  196 YTKAIDMWAAGCIFAEMLT 214
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
850-952 1.04e-07

Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle preferentially expressed protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Striated muscle preferentially expressed gene (SPEG) generates 4 different isoforms through alternative promoter use and splicing in a tissue-specific manner: SPEGalpha and SPEGbeta are expressed in cardiac and skeletal striated muscle; Aortic Preferentially Expressed Protein-1 (APEG-1) is expressed in vascular smooth muscle; and Brain preferentially expressed gene (BPEG) is found in the brain and aorta. SPEG proteins have mutliple immunoglobulin (Ig), 2 fibronectin type III (FN3), and two kinase domains. They are necessary for cardiac development and survival. The SPEG subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271013 [Multi-domain]  Cd Length: 257  Bit Score: 54.44  E-value: 1.04e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  850 DLISFAWQISQGMQYLAEMKLVHRDLAARNILVAEGRKMKISDFGlSRDVYEEDSYVKRSQGRIPVKWMAIESLFDHIYT 929
Cdd:cd14111  100 DVVGYLVQILQGLEYLHGRRVLHLDIKPDNIMVTNLNAIKIVDFG-SAQSFNPLSLRQLGRRTGTLEYMAPEMVKGEPVG 178
                         90       100
                 ....*....|....*....|...
gi 10862703  930 TQSDVWSFGVLLWeIVTLGGNPY 952
Cdd:cd14111  179 PPADIWSIGVLTY-IMLSGRSPF 200
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
854-954 1.31e-07

Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Plant MAPKs are typed based on the conserved phosphorylation motif present in the activation loop, TEY and TDY. This subfamily represents the TEY subtype of plant MAPKs and is further subdivided into three groups (A, B, and C). Group A is represented by AtMPK3, AtMPK6, Nicotiana tabacum BTF4 (NtNTF4), among others. They are mostly involved in environmental and hormonal responses. AtMPK3 and AtMPK6 are also key regulators for stomatal development and patterning. Group B is represented by AtMPK4, AtMPK13, and NtNTF6, among others. They may be involved in both cell division and environmental stress response. AtMPK4 also participates in regulating innate immunity. Group C is represented by AtMPK1, AtMPK2, NtNTF3, Oryza sativa MAPK4 (OsMAPK4), among others. They may also be involved in stress responses. AtMPK1 and AtMPK2 are activated following mechanical injury and in the presence of stress chemicals such as jasmonic acid, hydrogen peroxide and abscisic acid. OsMAPK4 is also called OsMSRMK3 for Multiple Stress-Responsive MAPK3. In plants, MAPKs are associated with physiological, developmental, hormonal, and stress responses. Some plants show numerous gene duplications of MAPKs; Arabidopsis thaliana harbors at least 20 MAPKs, named AtMPK1-20. The TEY MAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143363 [Multi-domain]  Cd Length: 337  Bit Score: 55.07  E-value: 1.31e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  854 FAWQISQGMQYLAEMKLVHRDLAARNILVAEGRKMKISDFGLSRDVYEED----SYVKRSQGRIPvkwmaiESLFD-HIY 928
Cdd:cd07858  113 FLYQLLRGLKYIHSANVLHRDLKPSNLLLNANCDLKICDFGLARTTSEKGdfmtEYVVTRWYRAP------ELLLNcSEY 186
                         90       100
                 ....*....|....*....|....*..
gi 10862703  929 TTQSDVWSFGVLLWEIvtLGGNP-YPG 954
Cdd:cd07858  187 TTAIDVWSVGCIFAEL--LGRKPlFPG 211
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
729-949 1.57e-07

C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. Mammals possess four RSK isoforms (RSK1-4) from distinct genes. RSK proteins are also referred to as MAP kinase-activated protein kinases (MAPKAPKs), 90 kDa ribosomal protein S6 kinases (p90-RSKs), or p90S6Ks. The RSK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270993 [Multi-domain]  Cd Length: 291  Bit Score: 54.18  E-value: 1.57e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  729 TLGEGEFGKVVKAtaFHLKGRAGYttvAVKML-KENASPSELRDLLsefnvLKQVNHPHVIKLYGACSQDGPLLLIVEYA 807
Cdd:cd14091    7 EIGKGSYSVCKRC--IHKATGKEY---AVKIIdKSKRDPSEEIEIL-----LRYGQHPNIITLRDVYDDGNSVYLVTELL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  808 KYGSL------RGFLRESrkvgpgylgsggsrnsssldhpdERALTMGDLISfawqisqGMQYLAEMKLVHRDLAARNIL 881
Cdd:cd14091   77 RGGELldrilrQKFFSER-----------------------EASAVMKTLTK-------TVEYLHSQGVVHRDLKPSNIL 126
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 10862703  882 VA-EGRK---MKISDFGLSRDVYEEDS------YVKrsqgripvKWMAIESLFDHIYTTQSDVWSFGVLLWeiVTLGG 949
Cdd:cd14091  127 YAdESGDpesLRICDFGFAKQLRAENGllmtpcYTA--------NFVAPEVLKKQGYDAACDIWSLGVLLY--TMLAG 194
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
854-954 2.37e-07

Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ERK5 (also called Big MAPK1 (BMK1) or MAPK7) has a unique C-terminal extension, making it approximately twice as big as other MAPKs. This extension contains transcriptional activation capability which is inhibited by the N-terminal half. ERK5 is activated in response to growth factors and stress by a cascade that leads to its phosphorylation by the MAP2K MEK5, which in turn is regulated by the MAP3Ks MEKK2 and MEKK3. Activated ERK5 phosphorylates its targets including myocyte enhancer factor 2 (MEF2), Sap1a, c-Myc, and RSK. It plays a role in EGF-induced cell proliferation during the G1/S phase transition. Studies on knockout mice revealed that ERK5 is essential for cardiovascular development and plays an important role in angiogenesis. It is also critical for neural differentiation and survival. The ERK5 pathway has been implicated in the pathogenesis of many diseases including cancer, cardiac hypertrophy, and atherosclerosis. MAPKs are important mediators of cellular responses to extracellular signals. The ERK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270842 [Multi-domain]  Cd Length: 336  Bit Score: 53.91  E-value: 2.37e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  854 FAWQISQGMQYLAEMKLVHRDLAARNILVAEGRKMKISDFGLSRDV--------YEEDSYVKRSQGRIPvkwmaiESLFD 925
Cdd:cd07855  114 FLYQLLRGLKYIHSANVIHRDLKPSNLLVNENCELKIGDFGMARGLctspeehkYFMTEYVATRWYRAP------ELMLS 187
                         90       100       110
                 ....*....|....*....|....*....|.
gi 10862703  926 -HIYTTQSDVWSFGVLLWEIvtLGGNP-YPG 954
Cdd:cd07855  188 lPEYTQAIDMWSVGCIFAEM--LGRRQlFPG 216
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
854-954 2.40e-07

Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Plant MAPKs are typed based on the conserved phosphorylation motif present in the activation loop, TEY and TDY. This subfamily represents the TDY subtype and is composed of Group D plant MAPKs including Arabidopsis thaliana MPK18 (AtMPK18), Oryza sativa Blast- and Wound-induced MAPK1 (OsBWMK1), OsWJUMK1 (Wound- and JA-Uninducible MAPK1), Zea mays MPK6, and the Medicago sativa TDY1 gene product. OsBWMK1 enhances resistance to pathogenic infections. It mediates stress-activated defense responses by activating a transcription factor that affects the expression of stress-related genes. AtMPK18 is involved in microtubule-related functions. In plants, MAPKs are associated with physiological, developmental, hormonal, and stress responses. Some plants show numerous gene duplications of MAPKs; Arabidopsis thaliana harbors at least 20 MAPKs, named AtMPK1-20 while Oryza sativa contains at least 17 MAPKs. Arabidopsis thaliana contains more TEY-type MAPKs than TDY-type, whereas the reverse is true for Oryza sativa. The TDY MAPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143364 [Multi-domain]  Cd Length: 338  Bit Score: 54.02  E-value: 2.40e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  854 FAWQISQGMQYLAEMKLVHRDLAARNILVAEGRKMKISDFGLSRDVYEEDSYVKRSQGRIPVKWMAIESL---FDHIYTT 930
Cdd:cd07859  108 FLYQLLRALKYIHTANVFHRDLKPKNILANADCKLKICDFGLARVAFNDTPTAIFWTDYVATRWYRAPELcgsFFSKYTP 187
                         90       100
                 ....*....|....*....|....*
gi 10862703  931 QSDVWSFGVLLWEIVTlgGNP-YPG 954
Cdd:cd07859  188 AIDIWSIGCIFAEVLT--GKPlFPG 210
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
855-954 2.42e-07

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and similar MAPKs; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Human MAPK15 is also called Extracellular signal Regulated Kinase 8 (ERK8) while the rat protein is called ERK7. ERK7 and ERK8 display both similar and different biochemical properties. They autophosphorylate and activate themselves and do not require upstream activating kinases. ERK7 is constitutively active and is not affected by extracellular stimuli whereas ERK8 shows low basal activity and is activated by DNA-damaging agents. ERK7 and ERK8 also have different substrate profiles. Genome analysis shows that they are orthologs with similar gene structures. ERK7 and ERK 8 may be involved in the signaling of some nuclear receptor transcription factors. ERK7 regulates hormone-dependent degradation of estrogen receptor alpha while ERK8 down-regulates the transcriptional co-activation androgen and glucocorticoid receptors. MAPKs are important mediators of cellular responses to extracellular signals. The MAPK15 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270841 [Multi-domain]  Cd Length: 337  Bit Score: 54.10  E-value: 2.42e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  855 AWQISQGMQYLAEMKLVHRDLAARNILVAEGRKMKISDFGLSRDVYEEDSYVKrsqgrIPV-------KWM-AIESLF-D 925
Cdd:cd07852  113 MYQLLKALKYLHSGGVIHRDLKPSNILLNSDCRVKLADFGLARSLSQLEEDDE-----NPVltdyvatRWYrAPEILLgS 187
                         90       100       110
                 ....*....|....*....|....*....|
gi 10862703  926 HIYTTQSDVWSFGVLLWEIvtLGGNP-YPG 954
Cdd:cd07852  188 TRYTKGVDMWSVGCILGEM--LLGKPlFPG 215
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
730-954 2.49e-07

The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. Twitchin and Projectin are both associated with thick filaments. Twitchin is localized in the outer parts of A-bands and is involved in regulating muscle contraction. It interacts with the myofibrillar proteins myosin and actin in a phosphorylation-dependent manner, and may be involved in regulating the myosin cross-bridge cycle. The kinase activity of Twitchen is activated by Ca2+ and the Ca2+ binding protein S100A1. Projectin is associated with the end of thick filaments and is a component of flight muscle connecting filaments. The kinase domain of Projectin may play roles in autophosphorylation and transphosphorylation, which impact the formation of myosin filaments. The Twitchin-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271016 [Multi-domain]  Cd Length: 259  Bit Score: 53.36  E-value: 2.49e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  730 LGEGEFGKVVKATAfhlkgRAGYTTVAVKMLKeNASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVEYAKY 809
Cdd:cd14114   10 LGTGAFGVVHRCTE-----RATGNNFAAKFIM-TPHESDKETVRKEIQIMNQLHHPKLINLHDAFEDDNEMVLILEFLSG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  810 GSLRgflreSRKVGPGYlgsggsrnsssldhpderALTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNILVAEGR--K 887
Cdd:cd14114   84 GELF-----ERIAAEHY------------------KMSEAEVINYMRQVCEGLCHMHENNIVHLDIKPENIMCTTKRsnE 140
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 10862703  888 MKISDFGLSRDVyEEDSYVKRSQGriPVKWMAIESLFDHIYTTQSDVWSFGVLLWeIVTLGGNPYPG 954
Cdd:cd14114  141 VKLIDFGLATHL-DPKESVKVTTG--TAEFAAPEIVEREPVGFYTDMWAVGVLSY-VLLSGLSPFAG 203
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
854-954 3.68e-07

Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the mitogen-activated protein kinases (MAPKs) ERK1, ERK2, baker's yeast Fus3, and similar proteins. MAPK pathways are important mediators of cellular responses to extracellular signals. ERK1/2 activation is preferentially by mitogenic factors, differentiation stimuli, and cytokines, through a kinase cascade involving the MAPK kinases MEK1/2 and a MAPK kinase kinase from the Raf family. ERK1/2 have numerous substrates, many of which are nuclear and participate in transcriptional regulation of many cellular processes. They regulate cell growth, cell proliferation, and cell cycle progression from G1 to S phase. Although the distinct roles of ERK1 and ERK2 have not been fully determined, it is known that ERK2 can maintain most functions in the absence of ERK1, and that the deletion of ERK2 is embryonically lethal. The MAPK, Fus3, regulates yeast mating processes including mating-specific gene expression, G1 arrest, mating projection, and cell fusion. This ERK1/2-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270839 [Multi-domain]  Cd Length: 336  Bit Score: 53.46  E-value: 3.68e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  854 FAWQISQGMQYLAEMKLVHRDLAARNILVAEGRKMKISDFGLSR-DVYEEDS------YVKRSQGRIPvKWMaiesLFDH 926
Cdd:cd07849  111 FLYQILRGLKYIHSANVLHRDLKPSNLLLNTNCDLKICDFGLARiADPEHDHtgflteYVATRWYRAP-EIM----LNSK 185
                         90       100
                 ....*....|....*....|....*....
gi 10862703  927 IYTTQSDVWSFGVLLWEIvtLGGNP-YPG 954
Cdd:cd07849  186 GYTKAIDIWSVGCILAEM--LSNRPlFPG 212
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
854-979 4.97e-07

Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. cPKCs are potent kinases for histones, myelin basic protein, and protamine. They depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. cPKCs contain a calcium-binding C2 region in their regulatory domain. There are four cPKC isoforms, named alpha, betaI, betaII, and gamma. PKC-gamma is mainly expressed in neuronal tissues. It plays a role in protection from ischemia. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. The cPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270739 [Multi-domain]  Cd Length: 320  Bit Score: 53.16  E-value: 4.97e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  854 FAWQISQGMQYLAEMKLVHRDLAARNILV-AEGRkMKISDFGLSRDVYEEDSYVKRSQGrIPvKWMAIESLFDHIYTTQS 932
Cdd:cd05587  102 YAAEIAVGLFFLHSKGIIYRDLKLDNVMLdAEGH-IKIADFGMCKEGIFGGKTTRTFCG-TP-DYIAPEIIAYQPYGKSV 178
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 10862703  933 DVWSFGVLLWEIVTlGGNPYPGIPPERLFNLLkTGHRMERPDNCSEE 979
Cdd:cd05587  179 DWWAYGVLLYEMLA-GQPPFDGEDEDELFQSI-MEHNVSYPKSLSKE 223
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
730-955 5.17e-07

Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein 89; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. The nematode Unc-89 gene, through alternative promoter use and splicing, encodes at least six major isoforms (Unc-89A to Unc-89F) of giant muscle proteins that are homologs for the vetebrate obscurin. In flies, five isoforms of Unc-89 have been detected: four in the muscles of adult flies (two in the indirect flight muscle and two in other muscles) and another isoform in the larva. Unc-89 in nematodes is required for normal muscle cell architecture. In flies, it is necessary for the development of a symmetrical sarcomere in the flight muscles. Unc-89 proteins contain several adhesion and signaling domains including multiple copies of the immunoglobulin (Ig) domain, as well as fibronectin type III (FN3), SH3, RhoGEF, and PH domains. The nematode Unc-89 isoforms D, C, D, and F contain two kinase domain with B and F having two complete kinase domains while the first repeat of C and D are partial domains. Homology modeling suggests that the first kinase repeat of Unc-89 may be catalytically inactive, a pseudokinase, while the second kinase repeat may be active. The pseudokinase domain may function as a regulatory domain or a protein interaction domain. The Unc-89 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271011 [Multi-domain]  Cd Length: 255  Bit Score: 52.13  E-value: 5.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  730 LGEGEFGKVVKATAFHLKGRAGYTTVAVKMLKenASPSelrdLLSEFNVLKQVNHPHVIKLYGACSQDG-PLLLIVEYAK 808
Cdd:cd14109    7 IGEEDEKRAAQGAPFHVTERSTGRNFLAQLRY--GDPF----LMREVDIHNSLDHPNIVQMHDAYDDEKlAVTVIDNLAS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  809 YGSLrgflresrkvgpgylgsggsrnSSSLDHPDERALTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNILVAEGrKM 888
Cdd:cd14109   81 TIEL----------------------VRDNLLPGKDYYTERQVAVFVRQLLLALKHMHDLGIAHLDLRPEDILLQDD-KL 137
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 10862703  889 KISDFGLSRDVyeEDSYVKRSQGRIPvKWMAIESLFDHIYTTQSDVWSFGVLLWeiVTLGG-NPYPGI 955
Cdd:cd14109  138 KLADFGQSRRL--LRGKLTTLIYGSP-EFVSPEIVNSYPVTLATDMWSVGVLTY--VLLGGiSPFLGD 200
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
726-1001 6.20e-07

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3); each gene may result in mutliple protein isoforms. There are two PIM1 and three PIM2 isoforms as a result of alternative translation initiation sites, while there is only one PIM3 protein. Compound knockout mice deficient of all three PIM kinases that survive the perinatal period show a profound reduction in body size, indicating that PIMs are important for body growth. The PIM subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270907 [Multi-domain]  Cd Length: 255  Bit Score: 51.85  E-value: 6.20e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  726 LGKTLGEGEFGKVVkaTAFHLKGRAgytTVAVK-MLKEN----ASPSELRDLLSEFNVLKQVN---HPHVIKLYGACSQD 797
Cdd:cd14005    4 VGDLLGKGGFGTVY--SGVRIRDGL---PVAVKfVPKSRvtewAMINGPVPVPLEIALLLKASkpgVPGVIRLLDWYERP 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  798 GPLLLIVEYAK-------YGSLRGFLRE--SRKvgpgylgsggsrnsssldhpderaltmgdlisFAWQISQGMQYLAEM 868
Cdd:cd14005   79 DGFLLIMERPEpcqdlfdFITERGALSEnlARI--------------------------------IFRQVVEAVRHCHQR 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  869 KLVHRDLAARNILVAEGR-KMKISDFGlSRDVYEEDSYVKRSQGRI--PVKWMaiesLFDHIYTTQSDVWSFGVLLWEIV 945
Cdd:cd14005  127 GVLHRDIKDENLLINLRTgEVKLIDFG-CGALLKDSVYTDFDGTRVysPPEWI----RHGRYHGRPATVWSLGILLYDML 201
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 10862703  946 TlggnpypGIPP-----ERLFNLLKTGHRMerpdncSEEMYRLMLQCWKQEPDKRPVFADI 1001
Cdd:cd14005  202 C-------GDIPfendeQILRGNVLFRPRL------SKECCDLISRCLQFDPSKRPSLEQI 249
STKc_PIM1 cd14100
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
853-1001 7.84e-07

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3); each gene may result in mutliple protein isoforms. There are two PIM1 isoforms resulting from alternative translation initiation sites. PIM1 is the founding member of the PIM subfamily. It is involved in regulating cell growth, differentiation, and apoptosis. It promotes cancer development when overexpressed by inhibiting apoptosis, promoting cell proliferation, and promoting genomic instability. The PIM1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271002 [Multi-domain]  Cd Length: 254  Bit Score: 51.89  E-value: 7.84e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  853 SFAWQISQGMQYLAEMKLVHRDLAARNILVAEGR-KMKISDFGlSRDVYEEDSYVKRSQGRI--PVKWMAieslFDHIYT 929
Cdd:cd14100  110 SFFRQVLEAVRHCHNCGVLHRDIKDENILIDLNTgELKLIDFG-SGALLKDTVYTDFDGTRVysPPEWIR----FHRYHG 184
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 10862703  930 TQSDVWSFGVLLWEIVTlgGNpypgIPPERLFNLLKtGHRMERpDNCSEEMYRLMLQCWKQEPDKRPVFADI 1001
Cdd:cd14100  185 RSAAVWSLGILLYDMVC--GD----IPFEHDEEIIR-GQVFFR-QRVSSECQHLIKWCLALRPSDRPSFEDI 248
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
720-1027 8.31e-07

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 52.73  E-value: 8.31e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703   720 PRKNLVLGKTLGEGEFGKVVKATAFHLKGRagyttVAVKMLKENASPSElRDLLsefnVLKQVNHPHVIKL----YGACS 795
Cdd:PTZ00036   64 PNKSYKLGNIIGNGSFGVVYEAICIDTSEK-----VAIKKVLQDPQYKN-RELL----IMKNLNHINIIFLkdyyYTECF 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703   796 QDGP----LLLIVEYAKYGSLRGFLRESRkvgpgylgsggsrnsssldhpDERALTMGDLISFAWQISQGMQYLAEMKLV 871
Cdd:PTZ00036  134 KKNEknifLNVVMEFIPQTVHKYMKHYAR---------------------NNHALPLFLVKLYSYQLCRALAYIHSKFIC 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703   872 HRDLAARNILV-AEGRKMKISDFGLSRDVY---EEDSYVKRSQGRIPVKWMAIESlfdhiYTTQSDVWSFGVLLWEIVtL 947
Cdd:PTZ00036  193 HRDLKPQNLLIdPNTHTLKLCDFGSAKNLLagqRSVSYICSRFYRAPELMLGATN-----YTTHIDLWSLGCIIAEMI-L 266
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703   948 GgnpYPGIPPE-------RLFNLLKTghrmerPdncSEEMYRLMlqcwkqepdkRPVFADI------SKDLEKMMVKrrd 1014
Cdd:PTZ00036  267 G---YPIFSGQssvdqlvRIIQVLGT------P---TEDQLKEM----------NPNYADIkfpdvkPKDLKKVFPK--- 321
                         330
                  ....*....|...
gi 10862703  1015 yldlaaSTPSDSL 1027
Cdd:PTZ00036  322 ------GTPDDAI 328
STKc_PRP4 cd14135
Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze ...
729-987 8.48e-07

Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PRP4 phosphorylates a number of factors involved in the formation of active spliceosomes, which catalyze pre-mRNA splicing. It phosphorylates PRP6 and PRP31, components of the U4/U6-U5 tri-small nuclear ribonucleoprotein (snRNP), during spliceosomal complex formation. In fission yeast, PRP4 phosphorylates the splicing factor PRP1 (U5-102 kD in mammals). Thus, PRP4 plays a key role in regulating spliceosome assembly and pre-mRNA splicing. It also plays an important role in mitosis by acting as a spindle assembly checkpoint kinase that is required for chromosome alignment and the recruitment of the checkpoint proteins MPS1, MAD1, and MAD2 at kinetochores. The PRP4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271037 [Multi-domain]  Cd Length: 318  Bit Score: 52.22  E-value: 8.48e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  729 TLGEGEFGKVVKATafhlKGRAGYTTVAVKMLKENasPSELRDLLSEFNVLKQVNHP------HVIKLYGACSQDGPLLL 802
Cdd:cd14135    7 YLGKGVFSNVVRAR----DLARGNQEVAIKIIRNN--ELMHKAGLKELEILKKLNDAdpddkkHCIRLLRHFEHKNHLCL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  803 IVEyakygSLRGFLRE-----SRKVGpgylgsggsrnsssldhpderaLTMGDLISFAWQISQGMQYLAEMKLVHRDLAA 877
Cdd:cd14135   81 VFE-----SLSMNLREvlkkyGKNVG----------------------LNIKAVRSYAQQLFLALKHLKKCNILHADIKP 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  878 RNILVAEGRKM-KISDFGLSRDVYEED--SY-VKRSQgRIPvkwmaiESLFDHIYTTQSDVWSFGVLLWEIVTlGGNPYP 953
Cdd:cd14135  134 DNILVNEKKNTlKLCDFGSASDIGENEitPYlVSRFY-RAP------EIILGLPYDYPIDMWSVGCTLYELYT-GKILFP 205
                        250       260       270
                 ....*....|....*....|....*....|....
gi 10862703  954 GipperlfnllktghrmeRPDNcseEMYRLMLQC 987
Cdd:cd14135  206 G-----------------KTNN---HMLKLMMDL 219
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
850-954 1.00e-06

Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and -Regulated Kinase; Protein Kinases (PKs), Dual-specificity tYrosine-phosphorylated and -Regulated Kinase (DYRK) subfamily, catalytic (c) domain. Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. The DYRK subfamily is part of a larger superfamily that includes the catalytic domains of other protein S/T PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K). DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. They play important roles in cell proliferation, differentiation, survival, and development. Vertebrates contain multiple DYRKs (DYRK1-4) and mammals contain two types of DYRK1 proteins, DYRK1A and DYRK1B. DYRK1A is involved in neuronal differentiation and is implicated in the pathogenesis of DS (Down syndrome). DYRK1B plays a critical role in muscle differentiation by regulating transcription, cell motility, survival, and cell cycle progression. It is overexpressed in many solid tumors where it acts as a tumor survival factor. DYRK2 promotes apoptosis in response to DNA damage by phosphorylating the tumor suppressor p53, while DYRK3 promotes cell survival by phosphorylating SIRT1 and promoting p53 deacetylation. DYRK4 is a testis-specific kinase that may function during spermiogenesis.


Pssm-ID: 271112 [Multi-domain]  Cd Length: 311  Bit Score: 51.78  E-value: 1.00e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  850 DLI-SFAWQISQGMQYLAEMKLVHRDLAARNILVAEGRKM--KISDFGLS----RDVYEedsYVkrsQGRIpvkWMAIES 922
Cdd:cd14210  116 SLIrKFAKQILQALQFLHKLNIIHCDLKPENILLKQPSKSsiKVIDFGSScfegEKVYT---YI---QSRF---YRAPEV 186
                         90       100       110
                 ....*....|....*....|....*....|...
gi 10862703  923 LFDHIYTTQSDVWSFGVLLWEIVTlgGNP-YPG 954
Cdd:cd14210  187 ILGLPYDTAIDMWSLGCILAELYT--GYPlFPG 217
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
730-954 1.01e-06

Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Titin, also called connectin, is a muscle-specific elastic protein and is the largest known protein to date. It contains multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains, and a single kinase domain near the C-terminus. It spans half of the sarcomere, the repeating contractile unit of striated muscle, and performs mechanical and catalytic functions. Titin contributes to the passive force generated when muscle is stretched during relaxation. Its kinase domain phosphorylates and regulates the muscle protein telethonin, which is required for sarcomere formation in differentiating myocytes. In addition, titin binds many sarcomere proteins and acts as a molecular scaffold for filament formation during myofibrillogenesis. The Titin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271006 [Multi-domain]  Cd Length: 277  Bit Score: 51.78  E-value: 1.01e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  730 LGEGEFGKVVKATAfhlkgRAGYTTVAVKMLKENASPSELrdLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVEYAKY 809
Cdd:cd14104    8 LGRGQFGIVHRCVE-----TSSKKTYMAKFVKVKGADQVL--VKKEISILNIARHRNILRLHESFESHEELVMIFEFISG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  810 GSLrgFLRESrkvgpgylgsggsrnssslDHPDEraLTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNIL--VAEGRK 887
Cdd:cd14104   81 VDI--FERIT-------------------TARFE--LNEREIVSYVRQVCEALEFLHSKNIGHFDIRPENIIycTRRGSY 137
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 10862703  888 MKISDFGLSRDVYEEDSYvkRSQGRIPvKWMAIESLFDHIYTTQSDVWSFGVLLWeiVTLGG-NPYPG 954
Cdd:cd14104  138 IKIIEFGQSRQLKPGDKF--RLQYTSA-EFYAPEVHQHESVSTATDMWSLGCLVY--VLLSGiNPFEA 200
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
730-953 1.16e-06

Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK4 shows a restricted expression pattern and is usually found in epithelial cells. It is expressed in nephrons and in extrarenal tissues including intestine, eye, mammary glands, and prostate. WNK4 regulates a variety of ion transport proteins including apical or basolateral ion transporters, ion channels in the transcellular pathway, and claudins in the paracellular pathway. Mutations in WNK4 cause PseudoHypoAldosteronism type II (PHAII), characterized by hypertension and hyperkalemia. WNK4 inhibits the activity of the thiazide-sensitive Na-Cl cotransporter (NCC), which is responsible for about 15% of NaCl reabsorption in the kidney. It also inhibits the renal outer medullary potassium channel (ROMK) and decreases its surface expression. Hypertension and hyperkalemia in PHAII patients with WNK4 mutations may be partly due to increased NaCl reabsorption through NCC and impaired renal potassium secretion by ROMK, respectively. The WNK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270935 [Multi-domain]  Cd Length: 261  Bit Score: 51.16  E-value: 1.16e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  730 LGEGEFGKVvkatafhLKGRAGYTTVAV---KMLKENASPSELRDLLSEFNVLKQVNHPHVIKLYGA--CSQDGP--LLL 802
Cdd:cd14033    9 IGRGSFKTV-------YRGLDTETTVEVawcELQTRKLSKGERQRFSEEVEMLKGLQHPNIVRFYDSwkSTVRGHkcIIL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  803 IVEYAKYGSLRGFLRESRKVGPGYLGsggsrnsssldhpderaltmgdliSFAWQISQGMQYLAEM--KLVHRDLAARNI 880
Cdd:cd14033   82 VTELMTSGTLKTYLKRFREMKLKLLQ------------------------RWSRQILKGLHFLHSRcpPILHRDLKCDNI 137
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 10862703  881 LV-AEGRKMKISDFGLSrdVYEEDSYVKRSQGrIPvKWMAIEsLFDHIYTTQSDVWSFGVLLWEIVTlggNPYP 953
Cdd:cd14033  138 FItGPTGSVKIGDLGLA--TLKRASFAKSVIG-TP-EFMAPE-MYEEKYDEAVDVYAFGMCILEMAT---SEYP 203
CA smart00112
Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. ...
198-270 1.35e-06

Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. Cadherin domains occur as repeats in the extracellular regions which are thought to mediate cell-cell contact when bound to calcium.


Pssm-ID: 214520 [Multi-domain]  Cd Length: 81  Bit Score: 47.34  E-value: 1.35e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 10862703     198 PNISVAYRLLEG-EGLPFRCAPDSLEVSTRWALDREQREKYELVAVCTVHaGAREEVVMVPFPVTVYDEDDSAP 270
Cdd:smart00112    9 ENGKVTYSILSGnDDGLFSIDPETGEITTTKPLDREEQPEYTLTVEATDG-GGPPLSSTATVTITVLDVNDNAP 81
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
726-954 1.37e-06

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 52.49  E-value: 1.37e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703   726 LGKTLGEGEFGKVVKATAfHLKGRagytTVAVKMLKenaspSEL-RDllSEFnVLK---------QVNHPHVIKLY--Ga 793
Cdd:NF033483   11 IGERIGRGGMAEVYLAKD-TRLDR----DVAVKVLR-----PDLaRD--PEF-VARfrreaqsaaSLSHPNIVSVYdvG- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703   794 csQDGPLLLIV-EYAKYGSLRGFLRESRKVGPgylgsggsrnsssldhpdERALTMGDlisfawQISQGMQYLAEMKLVH 872
Cdd:NF033483   77 --EDGGIPYIVmEYVDGRTLKDYIREHGPLSP------------------EEAVEIMI------QILSALEHAHRNGIVH 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703   873 RDLAARNILVAEGRKMKISDFGLSRDVYEED-----------SYVKRSQGR-IPVkwmaieslfdhiyTTQSDVWSFGVL 940
Cdd:NF033483  131 RDIKPQNILITKDGRVKVTDFGIARALSSTTmtqtnsvlgtvHYLSPEQARgGTV-------------DARSDIYSLGIV 197
                         250
                  ....*....|....
gi 10862703   941 LWEIVTlGGNPYPG 954
Cdd:NF033483  198 LYEMLT-GRPPFDG 210
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
720-996 1.40e-06

Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase kinase kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP4K5, also called germinal center kinase-related enzyme (GCKR), has been shown to activate the MAPK c-Jun N-terminal kinase (JNK). MAP4K5 also facilitates Wnt signaling in B cells, and may therefore be implicated in the control of cell fate, proliferation, and polarity. MAP4Ks are involved in some MAPK signaling pathways by activating a MAPK kinase kinase. Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAP3K to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Members of this subfamily contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. The MAP4K5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270813 [Multi-domain]  Cd Length: 268  Bit Score: 51.18  E-value: 1.40e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  720 PRKNLVLGKTLGEGEFGKVVKATAFHLKGRAgyttvAVKMLKenASPSELRDLLS-EFNVLKQVNHPHVIKLYGACSQDG 798
Cdd:cd06646    7 PQHDYELIQRVGSGTYGDVYKARNLHTGELA-----AVKIIK--LEPGDDFSLIQqEIFMVKECKHCNIVAYFGSYLSRE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  799 PLLLIVEYAKYGSLRGFLRESrkvGPgylgsggsrnsssldhpderaLTMGDLISFAWQISQGMQYLAEMKLVHRDLAAR 878
Cdd:cd06646   80 KLWICMEYCGGGSLQDIYHVT---GP---------------------LSELQIAYVCRETLQGLAYLHSKGKMHRDIKGA 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  879 NILVAEGRKMKISDFGLSRDVYEedSYVKRSQGRIPVKWMAIESLF---DHIYTTQSDVWSFGVLLWEIVTLGGNPYPGI 955
Cdd:cd06646  136 NILLTDNGDVKLADFGVAAKITA--TIAKRKSFIGTPYWMAPEVAAvekNGGYNQLCDIWAVGITAIELAELQPPMFDLH 213
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 10862703  956 PPERLFNLLKTGH---RMERPDNCSEEMYRLMLQCWKQEPDKRP 996
Cdd:cd06646  214 PMRALFLMSKSNFqppKLKDKTKWSSTFHNFVKISLTKNPKKRP 257
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
173-267 1.41e-06

Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. The cadherin repeat domains occur as tandem repeats in the extracellular regions, which are thought to mediate cell-cell contact when bound to calcium. They play numerous roles in cell fate, signalling, proliferation, differentiation, and migration; members include E-, N-, P-, T-, VE-, CNR-, proto-, and FAT-family cadherin, desmocollin, and desmoglein, a large variety of domain architectures with varying repeat copy numbers. Cadherin-repeat containing proteins exist as monomers, homodimers, or heterodimers.


Pssm-ID: 206637 [Multi-domain]  Cd Length: 98  Bit Score: 47.69  E-value: 1.41e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  173 SFRIRENRPPGTfhqfrllPVQFLC-------PNISVAYRLLEG-EGLPFRCAPDSLEVSTRWALDREQREKYELVAVCT 244
Cdd:cd11304    3 EVSVPENAPPGT-------VVLTVSatdpdsgENGEVTYSIVSGnEDGLFSIDPSTGEITTAKPLDREEQSSYTLTVTAT 75
                         90       100
                 ....*....|....*....|...
gi 10862703  245 VHAGAREEVVmVPFPVTVYDEDD 267
Cdd:cd11304   76 DGGGPPLSST-ATVTITVLDVND 97
STKc_BMPR1b cd14219
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IB; STKs ...
722-1008 1.65e-06

Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IB; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR1b, also called Activin receptor-Like Kinase 6 (ALK6), functions as a receptor for bone morphogenetic proteins (BMPs), which are involved in the regulation of cell proliferation, survival, differentiation, and apoptosis. BMPs are able to induce bone, cartilage, ligament, and tendon formation, and may play roles in bone diseases and tumors. Mutations in BMPR1b that led to inhibition of chondrogenesis can cause Brachydactyly (BD) type A2, a dominant hand malformation characterized by shortening and lateral deviation of the index fingers. A point mutation in the BMPR1b kinase domain is also associated with the Booroola phenotype, characterized by precocious differentiation of ovarian follicles. BMPR1b belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like BMPR1b, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The BMPR1b subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271121 [Multi-domain]  Cd Length: 305  Bit Score: 51.20  E-value: 1.65e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  722 KNLVLGKTLGEGEFGKVvkatafhLKGRAGYTTVAVKMLKENASPSELRD-------LLSEFNVLKQVNHPhvIKLYGAC 794
Cdd:cd14219    5 KQIQMVKQIGKGRYGEV-------WMGKWRGEKVAVKVFFTTEEASWFREteiyqtvLMRHENILGFIAAD--IKGTGSW 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  795 SQdgpLLLIVEYAKYGSLRGFLRESrkvgpgylgsggsrnsssldhpderALTMGDLISFAWQISQGMQYL--------A 866
Cdd:cd14219   76 TQ---LYLITDYHENGSLYDYLKST-------------------------TLDTKAMLKLAYSSVSGLCHLhteifstqG 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  867 EMKLVHRDLAARNILVAEGRKMKISDFGLS----RDVYEEDSYVKRSQGriPVKWMAIESLFDHIYTTQ------SDVWS 936
Cdd:cd14219  128 KPAIAHRDLKSKNILVKKNGTCCIADLGLAvkfiSDTNEVDIPPNTRVG--TKRYMPPEVLDESLNRNHfqsyimADMYS 205
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  937 FGVLLWEI---VTLGGN------PY----PGIPPERLFNLLKTGHRMeRP--------DNCSEEMYRLMLQCWKQEPDKR 995
Cdd:cd14219  206 FGLILWEVarrCVSGGIveeyqlPYhdlvPSDPSYEDMREIVCIKRL-RPsfpnrwssDECLRQMGKLMTECWAHNPASR 284
                        330
                 ....*....|...
gi 10862703  996 PVFADISKDLEKM 1008
Cdd:cd14219  285 LTALRVKKTLAKM 297
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
730-954 2.81e-06

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase signal-integrating kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK signal-integrating kinases (Mnks) are MAPK-activated protein kinases and is comprised by a group of four proteins, produced by alternative splicing from two genes (Mnk1 and Mnk2). The isoforms of Mnk1 (1a/1b) and Mnk2 (2a/2b) differ at their C-termini, with the a-form having a longer C-terminus containing a MAPK-binding region. All Mnks contain a catalytic kinase domain and a polybasic region at the N-terminus which binds importin and the eukaryotic initiation factor eIF4G. The best characterized Mnk substrate is eIF4G, whose phosphorylation may promote the export of certain mRNAs from the nucleus. Mnk also phosphorylate substrates that bind to AU-rich elements that regulate mRNA stability and translation. Mnks have also been implicated in tyrosine kinase receptor signaling, inflammation, and cell prolieration or survival. The Mnk subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271076 [Multi-domain]  Cd Length: 289  Bit Score: 50.41  E-value: 2.81e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  730 LGEGEFGKVVKATAfhLKGRAGYttvAVKMLKENASPSELRdLLSEFNVLKQVN-HPHVIKLYGACSQDGPLLLIVEYAK 808
Cdd:cd14174   10 LGEGAYAKVQGCVS--LQNGKEY---AVKIIEKNAGHSRSR-VFREVETLYQCQgNKNILELIEFFEDDTRFYLVFEKLR 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  809 YGSLRGFLrESRKvgpgylgsggsrnsssldHPDERALTmgdliSFAWQISQGMQYLAEMKLVHRDLAARNILVAEGRK- 887
Cdd:cd14174   84 GGSILAHI-QKRK------------------HFNEREAS-----RVVRDIASALDFLHTKGIAHRDLKPENILCESPDKv 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  888 --MKISDFGLSrdvyeedSYVKRSQGRIPV------------KWMA---IESLFDH--IYTTQSDVWSFGVLLWeIVTLG 948
Cdd:cd14174  140 spVKICDFDLG-------SGVKLNSACTPIttpelttpcgsaEYMApevVEVFTDEatFYDKRCDLWSLGVILY-IMLSG 211

                 ....*.
gi 10862703  949 GNPYPG 954
Cdd:cd14174  212 YPPFVG 217
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
774-951 2.95e-06

Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to Calcium/calmodulin-dependent protein kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of uncharacterized STKs with similarity to CaMKs, which are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). CaMKs contain an N-terminal catalytic domain followed by a regulatory domain that harbors a CaM binding site. This uncharacterized subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270990 [Multi-domain]  Cd Length: 265  Bit Score: 50.02  E-value: 2.95e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  774 SEFNVLKQVNHPHVIKLYGACSQDGPLLLIVEYAKygslrgflreSRKVGPGYLgsggsrnsssldhpDERALTMGDLIS 853
Cdd:cd14088   48 NEINILKMVKHPNILQLVDVFETRKEYFIFLELAT----------GREVFDWIL--------------DQGYYSERDTSN 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  854 FAWQISQGMQYLAEMKLVHRDLAARNILV---AEGRKMKISDFGLSRdvyEEDSYVKRSQGrIPvKWMAIESLFDHIYTT 930
Cdd:cd14088  104 VIRQVLEAVAYLHSLKIVHRNLKLENLVYynrLKNSKIVISDFHLAK---LENGLIKEPCG-TP-EYLAPEVVGRQRYGR 178
                        170       180
                 ....*....|....*....|.
gi 10862703  931 QSDVWSFGVLLWeiVTLGGNP 951
Cdd:cd14088  179 PVDCWAIGVIMY--ILLSGNP 197
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
726-952 3.08e-06

Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-iota is directly implicated in carcinogenesis. It is critical to oncogenic signaling mediated by Ras and Bcr-Abl. The PKC-iota gene is the target of tumor-specific gene amplification in many human cancers, and has been identified as a human oncogene. In addition to its role in transformed growth, PKC-iota also promotes invasion, chemoresistance, and tumor cell survival. Expression profiling of PKC-iota is a prognostic marker of poor clinical outcome in several human cancers. PKC-iota also plays a role in establishing cell polarity, and has critical embryonic functions. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. aPKCs only require phosphatidylserine (PS) for activation. The aPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270769 [Multi-domain]  Cd Length: 364  Bit Score: 50.80  E-value: 3.08e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  726 LGKTLGEGEFGKVVKATAfhLKGRAGYTTVAVKmlKENASPSELRDLL-SEFNVLKQV-NHPHVIKLYGACSQDGPLLLI 803
Cdd:cd05618   24 LLRVIGRGSYAKVLLVRL--KKTERIYAMKVVK--KELVNDDEDIDWVqTEKHVFEQAsNHPFLVGLHSCFQTESRLFFV 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  804 VEYAKYGSLRGFLRESRKVgpgylgsggsrnsssldhPDERALTmgdlisFAWQISQGMQYLAEMKLVHRDLAARNILVA 883
Cdd:cd05618  100 IEYVNGGDLMFHMQRQRKL------------------PEEHARF------YSAEISLALNYLHERGIIYRDLKLDNVLLD 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 10862703  884 EGRKMKISDFGLSRDVYEEDSYVKRSQGriPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTlGGNPY 952
Cdd:cd05618  156 SEGHIKLTDYGMCKEGLRPGDTTSTFCG--TPNYIAPEILRGEDYGFSVDWWALGVLMFEMMA-GRSPF 221
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
756-967 3.27e-06

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called 90kDa ribosomal protein S6 kinase 3 or Ribosomal protein S6 kinase alpha-3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK2 is also called p90RSK3, RPS6KA3, S6K-alpha-3, or MAPK-activated protein kinase 1b (MAPKAPK-1b). RSK2 is expressed highly in the regions of the brain with high synaptic activity. It plays a role in the maintenance and consolidation of excitatory synapses. It is a specific modulator of phospholipase D in calcium-regulated exocytosis. Mutations in the RSK2 gene, RPS6KA3, cause Coffin-Lowry syndrome (CLS), a rare syndromic form of X-linked mental retardation characterized by growth and psychomotor retardation and skeletal abnormalities. RSK2 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271078 [Multi-domain]  Cd Length: 339  Bit Score: 50.40  E-value: 3.27e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  756 AVKML-KENASPSELRDLLsefnvLKQVNHPHVIKLYGACSQDGPLLLIVEYAKYGSL-RGFLREsrkvgpgylgsggsr 833
Cdd:cd14176   48 AVKIIdKSKRDPTEEIEIL-----LRYGQHPNIITLKDVYDDGKYVYVVTELMKGGELlDKILRQ--------------- 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  834 nsssldhpdeRALTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNILVAEG----RKMKISDFGLSRDVYEEDSYVKRS 909
Cdd:cd14176  108 ----------KFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDEsgnpESIRICDFGFAKQLRAENGLLMTP 177
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 10862703  910 QgrIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTlGGNPYPGIP---PERLFNLLKTG 967
Cdd:cd14176  178 C--YTANFVAPEVLERQGYDAACDIWSLGVLLYTMLT-GYTPFANGPddtPEEILARIGSG 235
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
705-946 3.52e-06

Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDC2L1, also called PITSLRE, exists in different isoforms which are named using the alias CDK11(p). The CDC2L1 gene produces two protein products, CDK11(p110) and CDK11(p58). CDC2L1 is also represented by the caspase-processed CDK11(p46). CDK11(p110), the major isoform, associates with cyclin L and is expressed throughout the cell cycle. It is involved in RNA processing and the regulation of transcription. CDK11(p58) associates with cyclin D3 and is expressed during the G2/M phase of the cell cycle. It plays roles in spindle morphogenesis, centrosome maturation, sister chromatid cohesion, and the completion of mitosis. CDK11(p46) is formed from the larger isoforms by caspases during TNFalpha- and Fas-induced apoptosis. It functions as a downstream effector kinase in apoptotic signaling pathways and interacts with eukaryotic initiation factor 3f (eIF3f), p21-activated kinase (PAK1), and Ran-binding protein (RanBPM). CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDC2L1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173741 [Multi-domain]  Cd Length: 293  Bit Score: 50.30  E-value: 3.52e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  705 SVDAFKILEdpkwefprknlvlgkTLGEGEFGKVVKAtafhlKGRAGYTTVAVKMLK-----ENASPSELRdllsEFNVL 779
Cdd:cd07843    3 SVDEYEKLN---------------RIEEGTYGVVYRA-----RDKKTGEIVALKKLKmekekEGFPITSLR----EINIL 58
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  780 KQVNHPHVIKL----YGACSQDgpLLLIVEYAKYgSLRGFLRESRKvgpgylgsggsrnsssldhpderALTMGDLISFA 855
Cdd:cd07843   59 LKLQHPNIVTVkevvVGSNLDK--IYMVMEYVEH-DLKSLMETMKQ-----------------------PFLQSEVKCLM 112
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  856 WQISQGMQYLAEMKLVHRDLAARNILVAEGRKMKISDFGLSRDvYEEdsyVKRSQGRIPVK-WM-AIESLFD-HIYTTQS 932
Cdd:cd07843  113 LQLLSGVAHLHDNWILHRDLKTSNLLLNNRGILKICDFGLARE-YGS---PLKPYTQLVVTlWYrAPELLLGaKEYSTAI 188
                        250
                 ....*....|....
gi 10862703  933 DVWSFGVLLWEIVT 946
Cdd:cd07843  189 DMWSVGCIFAELLT 202
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
861-961 3.74e-06

Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine/threonine kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAST kinases contain an N-terminal domain of unknown function, a central catalytic domain, and a C-terminal PDZ domain that mediates protein-protein interactions. There are four mammalian MAST kinases, named MAST1-MAST4. MAST1 is also called syntrophin-associated STK (SAST) while MAST2 is also called MAST205. MAST kinases are cytoskeletal associated kinases of unknown function that are also expressed at neuromuscular junctions and postsynaptic densities. MAST1, MAST2, and MAST3 bind and phosphorylate the tumor suppressor PTEN, and may contribute to the regulation and stabilization of PTEN. MAST2 is involved in the regulation of the Fc-gamma receptor of the innate immune response in macrophages, and may also be involved in the regulation of the Na+/H+ exchanger NHE3. The MAST kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270760 [Multi-domain]  Cd Length: 280  Bit Score: 50.10  E-value: 3.74e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  861 GMQYLAEMKLVHRDLAARNILVAEGRKMKISDFGLSR--------DVYE----EDS--YVKRSQGRIPvKWMAIESLFDH 926
Cdd:cd05609  112 ALEYLHSYGIVHRDLKPDNLLITSMGHIKLTDFGLSKiglmslttNLYEghieKDTreFLDKQVCGTP-EYIAPEVILRQ 190
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 10862703  927 IYTTQSDVWSFGVLLWEIVtLGGNPYPGIPPERLF 961
Cdd:cd05609  191 GYGKPVDWWAMGIILYEFL-VGCVPFFGDTPEELF 224
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
728-995 4.86e-06

C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK1 plays a role in the regulation of translational control and transcriptional activation. It phosphorylates the transcription factors, CREB and NFkB. It also phosphorylates the nucleosomal proteins H3 and HMG-14. Increased phosphorylation of MSK1 is associated with the development of cerebral ischemic/hypoxic preconditioning. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271081 [Multi-domain]  Cd Length: 310  Bit Score: 49.65  E-value: 4.86e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  728 KTLGEGEFGKVVKATafHLKGRAGYttvAVKMLKENASPSELRdllsEFNVLKQVN-HPHVIKLYGACSQDGPLLLIVEY 806
Cdd:cd14179   13 KPLGEGSFSICRKCL--HKKTNQEY---AVKIVSKRMEANTQR----EIAALKLCEgHPNIVKLHEVYHDQLHTFLVMEL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  807 AKYGSLrgFLRESRKvgpgylgsggsrnssSLDHPDERALTMGDLISfawqisqGMQYLAEMKLVHRDLAARNILV---A 883
Cdd:cd14179   84 LKGGEL--LERIKKK---------------QHFSETEASHIMRKLVS-------AVSHMHDVGVVHRDLKPENLLFtdeS 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  884 EGRKMKISDFGLSRDVYEEDSYVKRSQgrIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTlGGNPYPG-------IP 956
Cdd:cd14179  140 DNSEIKIIDFGFARLKPPDNQPLKTPC--FTLHYAAPELLNYNGYDESCDLWSLGVILYTMLS-GQVPFQChdksltcTS 216
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 10862703  957 PERLFNLLKTGH---RMERPDNCSEEMYRLMLQCWKQEPDKR 995
Cdd:cd14179  217 AEEIMKKIKQGDfsfEGEAWKNVSQEAKDLIQGLLTVDPNKR 258
STKc_Unc-89_rpt2 cd14112
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated ...
720-996 4.86e-06

Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein 89; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The nematode Unc-89 gene, through alternative promoter use and splicing, encodes at least six major isoforms (Unc-89A to Unc-89F) of giant muscle proteins that are homologs for the vetebrate obscurin. In flies, five isoforms of Unc-89 have been detected: four in the muscles of adult flies (two in the indirect flight muscle and two in other muscles) and another isoform in the larva. Unc-89 in nematodes is required for normal muscle cell architecture. In flies, it is necessary for the development of a symmetrical sarcomere in the flight muscles. Unc-89 proteins contain several adhesion and signaling domains including multiple copies of the immunoglobulin (Ig) domain, as well as fibronectin type III (FN3), SH3, RhoGEF, and PH domains. The nematode Unc-89 isoforms D, C, D, and F contain two kinase domain with B and F having two complete kinase domains while the first repeat of C and D are partial domains. Homology modeling suggests that the first kinase repeat of Unc-89 may be catalytically inactive, a pseudokinase, while the second kinase repeat may be active. The Unc-89 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271014 [Multi-domain]  Cd Length: 259  Bit Score: 49.45  E-value: 4.86e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  720 PRKNLVLGKTLGEGEFGKVVKATAfhlKGRAGYTTVAVKMLKENASPSELrdlLSEFNVLKQVNHPHVIKLYGACSQDGP 799
Cdd:cd14112    1 PTGRFSFGSEIFRGRFSVIVKAVD---STTETDAHCAVKIFEVSDEASEA---VREFESLRTLQHENVQRLIAAFKPSNF 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  800 LLLIVE--YA---KYGSLRGFLREsrkvgpgylgsggsrnsssldhpDERALTMGdlisfawQISQGMQYLAEMKLVHRD 874
Cdd:cd14112   75 AYLVMEklQEdvfTRFSSNDYYSE-----------------------EQVATTVR-------QILDALHYLHFKGIAHLD 124
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  875 LAARNILVAEGR--KMKISDFGLSRDVYEEDSyvKRSQGRipVKWMAIESLFDH-IYTTQSDVWSFGVLLWEIVTlGGNP 951
Cdd:cd14112  125 VQPDNIMFQSVRswQVKLVDFGRAQKVSKLGK--VPVDGD--TDWASPEFHNPEtPITVQSDIWGLGVLTFCLLS-GFHP 199
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 10862703  952 YPGIPP---ERLFNLLKTGHRMER-PDNCSEEMYRLMLQCWKQEPDKRP 996
Cdd:cd14112  200 FTSEYDdeeETKENVIFVKCRPNLiFVEATQEALRFATWALKKSPTRRM 248
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
730-953 4.94e-06

Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK3 shows a restricted expression pattern; it is found at high levels in the pituary glands and is also expressed in the kidney and brain. It has been shown to regulate many ion transporters including members of the SLC12A family of cation-chloride cotransporters such as NCC and NKCC2, the renal potassium channel ROMK, and the epithelial calcium channels TRPV5 and TRPV6. WNK3 appears to sense low-chloride hypotonic stress and under these conditions, it activates SPAK, which directly interacts and phosphorylates cation-chloride cotransporters. WNK3 has also been shown to promote cell survival, possibly through interaction with procaspase-3 and HSP70. WNKs comprise a subfamily of STKs with an unusual placement of the catalytic lysine relative to all other protein kinases. The WNK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270933 [Multi-domain]  Cd Length: 275  Bit Score: 49.72  E-value: 4.94e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  730 LGEGEFGKVVKAtafhLKGRAGYTTVAVKMLKENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQ----DGPLLLIVE 805
Cdd:cd14031   18 LGRGAFKTVYKG----LDTETWVEVAWCELQDRKLTKAEQQRFKEEAEMLKGLQHPNIVRFYDSWESvlkgKKCIVLVTE 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  806 YAKYGSLRGFLRESRKVGPGYLGsggsrnsssldhpderaltmgdliSFAWQISQGMQYLAEMK--LVHRDLAARNILV- 882
Cdd:cd14031   94 LMTSGTLKTYLKRFKVMKPKVLR------------------------SWCRQILKGLQFLHTRTppIIHRDLKCDNIFIt 149
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 10862703  883 AEGRKMKISDFGLSrdVYEEDSYVKRSQGrIPvKWMAIESLFDHiYTTQSDVWSFGVLLWEIVTlggNPYP 953
Cdd:cd14031  150 GPTGSVKIGDLGLA--TLMRTSFAKSVIG-TP-EFMAPEMYEEH-YDESVDVYAFGMCMLEMAT---SEYP 212
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
726-952 4.96e-06

Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-zeta plays a critical role in activating the glucose transport response. It is activated by glucose, insulin, and exercise through diverse pathways. PKC-zeta also plays a central role in maintaining cell polarity in yeast and mammalian cells. In addition, it affects actin remodeling in muscle cells. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. aPKCs only require phosphatidylserine (PS) for activation. The aPKC-zeta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270768 [Multi-domain]  Cd Length: 357  Bit Score: 50.02  E-value: 4.96e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  726 LGKTLGEGEFGKVVKatafhLKGRAGYTTVAVKMLKENA--SPSELRDLLSEFNVLKQVN-HPHVIKLYGACSQDGPLLL 802
Cdd:cd05617   19 LIRVIGRGSYAKVLL-----VRLKKNDQIYAMKVVKKELvhDDEDIDWVQTEKHVFEQASsNPFLVGLHSCFQTTSRLFL 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  803 IVEYAKYGSLRGFLRESRKVgpgylgsggsrnsssldhPDERALTmgdlisFAWQISQGMQYLAEMKLVHRDLAARNILV 882
Cdd:cd05617   94 VIEYVNGGDLMFHMQRQRKL------------------PEEHARF------YAAEICIALNFLHERGIIYRDLKLDNVLL 149
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  883 AEGRKMKISDFGLSRDVYEEDSYVKRSQGriPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTlGGNPY 952
Cdd:cd05617  150 DADGHIKLTDYGMCKEGLGPGDTTSTFCG--TPNYIAPEILRGEEYGFSVDWWALGVLMFEMMA-GRSPF 216
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
858-995 5.58e-06

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated protein kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK-activated protein kinase 3 (MAPKAP3 or MK3) contains an N-terminal proline-rich region that can bind to SH3 domains, a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. MK3 is a bonafide substrate for the MAPK p38. It is closely related to MK2 and thus far, MK2/3 show indistinguishable substrate specificity. They are mainly involved in the regulation of gene expression and they participate in diverse cellular processes such as endocytosis, cytokine production, cytoskeletal reorganization, cell migration, cell cycle control and chromatin remodeling. They are implicated in inflammation and cance and their substrates include mRNA-AU-rich-element (ARE)-binding proteins (TTP and hnRNP A0), Hsp proteins (Hsp27 and Hsp25) and RSK, among others. MK2/3 are both expressed ubiquitously but MK2 is expressed at significantly higher levels. MK3 activity is only significant when MK2 is absent. The MK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271074 [Multi-domain]  Cd Length: 267  Bit Score: 49.22  E-value: 5.58e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  858 ISQGMQYLAEMKLVHRDLAARNILVAEGRK---MKISDFGLSRDVYEEDSYvkRSQGRIPVkWMAIESLFDHIYTTQSDV 934
Cdd:cd14172  112 IGTAIQYLHSMNIAHRDVKPENLLYTSKEKdavLKLTDFGFAKETTVQNAL--QTPCYTPY-YVAPEVLGPEKYDKSCDM 188
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  935 WSFGVLLWeIVTLGGNPY---------PGIppERLFNLLKTGHRMERPDNCSEEMYRLMLQCWKQEPDKR 995
Cdd:cd14172  189 WSLGVIMY-ILLCGFPPFysntgqaisPGM--KRRIRMGQYGFPNPEWAEVSEEAKQLIRHLLKTDPTER 255
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
749-967 5.84e-06

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called Ribosomal protein S6 kinase alpha-2 or 90kDa ribosomal protein S6 kinase 2); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK3 is also called S6K-alpha-2, RPS6KA2, p90RSK2 or MAPK-activated protein kinase 1c (MAPKAPK-1c). RSK3 binds muscle A-kinase anchoring protein (mAKAP)-b directly and regulates concentric cardiac myocyte growth. The RSK3 gene, RPS6KA2, is a putative tumor suppressor gene in sporadic epithelial ovarian cancer and variations to the gene may be associated with rectal cancer risk. RSK3 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271080 [Multi-domain]  Cd Length: 293  Bit Score: 49.63  E-value: 5.84e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  749 RAGYTTVAVKML-KENASPSELRDLLsefnvLKQVNHPHVIKLYGACSQDGPLLLIVEYAKYGSLRG-FLREsrkvgpgy 826
Cdd:cd14178   25 KATSTEYAVKIIdKSKRDPSEEIEIL-----LRYGQHPNIITLKDVYDDGKFVYLVMELMRGGELLDrILRQ-------- 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  827 lgsggsrnsssldhpdeRALTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNILVAEG----RKMKISDFGLSRDVYEE 902
Cdd:cd14178   92 -----------------KCFSEREASAVLCTITKTVEYLHSQGVVHRDLKPSNILYMDEsgnpESIRICDFGFAKQLRAE 154
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 10862703  903 DSYVKRSQgrIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTlGGNPYPGIP---PERLFNLLKTG 967
Cdd:cd14178  155 NGLLMTPC--YTANFVAPEVLKRQGYDAACDIWSLGILLYTMLA-GFTPFANGPddtPEEILARIGSG 219
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
730-1005 7.49e-06

Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Schizosaccharomyces pombe Sck1 and similar fungal proteins. Sck1 plays a role in trehalase activation triggered by glucose and a nitrogen source. Trehalase catalyzes the cleavage of the disaccharide trehalose to glucose. Trehalose, as a carbohydrate reserve and stress metabolite, plays an important role in the response of yeast to environmental changes. The Sck1-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270738 [Multi-domain]  Cd Length: 330  Bit Score: 49.49  E-value: 7.49e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  730 LGEGEFGKVvkataFHLKGRAGYTTVAVKML--KENASPSELRDLLSEFNVLKQV---NHPHVIKLYGACSQDGPLLLIV 804
Cdd:cd05586    1 IGKGTFGQV-----YQVRKKDTRRIYAMKVLskKVIVAKKEVAHTIGERNILVRTaldESPFIVGLKFSFQTPTDLYLVT 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  805 EYAKYGSLRGFLRESRKVgpgylgsggsrnsssldhPDERA-LTMGDLIsfawqisQGMQYLAEMKLVHRDLAARNILVA 883
Cdd:cd05586   76 DYMSGGELFWHLQKEGRF------------------SEDRAkFYIAELV-------LALEHLHKNDIVYRDLKPENILLD 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  884 EGRKMKISDFGLSRDVYEEDSYVKRSQGriPVKWMAIESLFDHI-YTTQSDVWSFGVLLWEIVTlGGNPYPGIPPERLFN 962
Cdd:cd05586  131 ANGHIALCDFGLSKADLTDNKTTNTFCG--TTEYLAPEVLLDEKgYTKMVDFWSLGVLVFEMCC-GWSPFYAEDTQQMYR 207
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 10862703  963 LLKTGHRMERPDNCSEEMYRLMLQCWKQEPDKR-------------PVFADISKDL 1005
Cdd:cd05586  208 NIAFGKVRFPKDVLSDEGRSFVKGLLNRNPKHRlgahddavelkehPFFADIDWDL 263
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
768-951 1.02e-05

Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phosphorylase kinase (PhK) catalyzes the phosphorylation of inactive phosphorylase b to form the active phosphorylase a. It coordinates hormonal, metabolic, and neuronal signals to initiate the breakdown of glycogen stores, which enables the maintenance of blood-glucose homeostasis during fasting, and is also used as a source of energy for muscle contraction. PhK is one of the largest and most complex protein kinases, composed of a heterotetramer containing four molecules each of four subunit types: one catalytic (gamma) and three regulatory (alpha, beta, and delta). The gamma 1 subunit (PhKG1) is also referred to as the muscle gamma isoform. The gamma subunit, when isolated, is constitutively active and does not require phosphorylation of the A-loop for activity. The regulatory subunits restrain this kinase activity until signals are received to relieve this inhibition. For example, the kinase is activated in response to hormonal stimulation, after autophosphorylation or phosphorylation by cAMP-dependent kinase of the alpha and beta subunits. The high-affinity binding of ADP to the beta subunit also stimulates kinase activity, whereas calcium relieves inhibition by binding to the delta (calmodulin) subunit. The PhKG1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271084 [Multi-domain]  Cd Length: 276  Bit Score: 48.76  E-value: 1.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  768 ELRD-LLSEFNVLKQVN-HPHVIKLYGACSQDGPLLLIVEYAKYGSLRGFLREsrKVgpgylgsggsrnssSLDHPDERA 845
Cdd:cd14182   51 ELREaTLKEIDILRKVSgHPNIIQLKDTYETNTFFFLVFDLMKKGELFDYLTE--KV--------------TLSEKETRK 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  846 LtMGDLISFawqisqgMQYLAEMKLVHRDLAARNILVAEGRKMKISDFGLSRDVYEEDSyVKRSQGrIPvKWMAIE---- 921
Cdd:cd14182  115 I-MRALLEV-------ICALHKLNIVHRDLKPENILLDDDMNIKLTDFGFSCQLDPGEK-LREVCG-TP-GYLAPEiiec 183
                        170       180       190
                 ....*....|....*....|....*....|..
gi 10862703  922 SLFDHI--YTTQSDVWSFGVLLWEIvtLGGNP 951
Cdd:cd14182  184 SMDDNHpgYGKEVDMWSTGVIMYTL--LAGSP 213
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
858-967 1.29e-05

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called Ribosomal protein S6 kinase alpha-1 or 90kDa ribosomal protein S6 kinase 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK1 is also called S6K-alpha-1, RPS6KA1, p90RSK1 or MAPK-activated protein kinase 1a (MAPKAPK-1a). It is a component of the insulin transduction pathway, regulating the function of IRS1. It also interacts with PKA and promotes its inactivation. RSK1 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271077 [Multi-domain]  Cd Length: 291  Bit Score: 48.48  E-value: 1.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  858 ISQGMQYLAEMKLVHRDLAARNIL-VAEG---RKMKISDFGLSRDVYEEDSYVKRSQgrIPVKWMAIESLFDHIYTTQSD 933
Cdd:cd14175  104 ICKTVEYLHSQGVVHRDLKPSNILyVDESgnpESLRICDFGFAKQLRAENGLLMTPC--YTANFVAPEVLKRQGYDEGCD 181
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 10862703  934 VWSFGVLLWEIVTlGGNPY---PGIPPERLFNLLKTG 967
Cdd:cd14175  182 IWSLGILLYTMLA-GYTPFangPSDTPEEILTRIGSG 217
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
730-1001 1.84e-05

Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK1 is widely expressed and is most abundant in the testis. In hyperosmotic or hypotonic low-chloride stress conditions, WNK1 is activated and it phosphorylates its substrates including SPAK and OSR1 kinases, which regulate the activity of cation-chloride cotransporters through direct interaction and phosphorylation. Mutations in WNK1 cause PseudoHypoAldosteronism type II (PHAII), characterized by hypertension and hyperkalemia. WNK1 negates WNK4-mediated inhibition of the sodium-chloride cotransporter NCC and activates the epithelial sodium channel ENaC by activating SGK1. WNK1 also decreases the surface expression of renal outer medullary potassium channel (ROMK) by stimulating their endocytosis. Hypertension and hyperkalemia in PHAII patients with WNK1 mutations may be due partly to increased activity of NCC and ENaC, and impaired renal potassium secretion by ROMK, respectively. In addition, WNK1 interacts with MEKK2/3 and acts as an activator of extracellular signal-regulated kinase (ERK) 5. It also negatively regulates TGFbeta signaling. WNKs comprise a subfamily of STKs with an unusual placement of the catalytic lysine relative to all other protein kinases. The WNK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270932 [Multi-domain]  Cd Length: 289  Bit Score: 47.74  E-value: 1.84e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  730 LGEGEFGKVvkatafhLKGRAGYTTVAV---KMLKENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGP----LLL 802
Cdd:cd14030   33 IGRGSFKTV-------YKGLDTETTVEVawcELQDRKLSKSERQRFKEEAGMLKGLQHPNIVRFYDSWESTVKgkkcIVL 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  803 IVEYAKYGSLRGFLRESRkvgpgylgsggsrnsssldhpderALTMGDLISFAWQISQGMQYLAEMK--LVHRDLAARNI 880
Cdd:cd14030  106 VTELMTSGTLKTYLKRFK------------------------VMKIKVLRSWCRQILKGLQFLHTRTppIIHRDLKCDNI 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  881 LV-AEGRKMKISDFGLSrdVYEEDSYVKRSQGriPVKWMAIEsLFDHIYTTQSDVWSFGVLLWEIVTlGGNPYPGIP-PE 958
Cdd:cd14030  162 FItGPTGSVKIGDLGLA--TLKRASFAKSVIG--TPEFMAPE-MYEEKYDESVDVYAFGMCMLEMAT-SEYPYSECQnAA 235
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 10862703  959 RLFNLLKTGHRMERPDNCS-EEMYRLMLQCWKQEPDKRPVFADI 1001
Cdd:cd14030  236 QIYRRVTSGVKPASFDKVAiPEVKEIIEGCIRQNKDERYAIKDL 279
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
722-957 2.15e-05

Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear Dbf2-Related (NDR)-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily include ROCK and ROCK-like proteins such as DMPK, MRCK, and CRIK, as well as NDR and NDR-like proteins such as LATS, CBK1 and Sid2p. ROCK and CRIK are effectors of the small GTPase Rho, while MRCK is an effector of the small GTPase Cdc42. NDR and NDR-like kinases contain an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Proteins in this subfamily are involved in regulating many cellular functions including contraction, motility, division, proliferation, apoptosis, morphogenesis, and cytokinesis. The ROCK/NDR-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270725 [Multi-domain]  Cd Length: 350  Bit Score: 48.05  E-value: 2.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  722 KNLVLGKTLGEGEFGKVvkATAFHLKGRAGYttvAVK------MLKENaspsELRDLLSEFNVLKQVNHPHVIKLYGACS 795
Cdd:cd05573    1 DDFEVIKVIGRGAFGEV--WLVRDKDTGQVY---AMKilrksdMLKRE----QIAHVRAERDILADADSPWIVRLHYAFQ 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  796 QDGPLLLIVEYAKYGSLRGFLreSRKvgpgylgsggsrnssslDHPDEraltmgDLISFawqisqgmqYLAEMKL----- 870
Cdd:cd05573   72 DEDHLYLVMEYMPGGDLMNLL--IKY-----------------DVFPE------ETARF---------YIAELVLaldsl 117
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  871 -----VHRDLAARNILVAEGRKMKISDFGLS--------RDVYEEDSYVKRSQGRIPVK-------------------WM 918
Cdd:cd05573  118 hklgfIHRDIKPDNILLDADGHIKLADFGLCtkmnksgdRESYLNDSVNTLFQDNVLARrrphkqrrvraysavgtpdYI 197
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 10862703  919 AIESLFDHIYTTQSDVWSFGVLLWEIVTlggnpypGIPP 957
Cdd:cd05573  198 APEVLRGTGYGPECDWWSLGVILYEMLY-------GFPP 229
STKc_CDK8 cd07868
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 8; STKs ...
727-964 2.16e-05

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 8; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK8 can act as a negative or positive regulator of transcription, depending on the scenario. Together with its regulator, cyclin C, it reversibly associates with the multi-subunit core Mediator complex, a cofactor that is involved in regulating RNA polymerase II (RNAP II)-dependent transcription. CDK8 phosphorylates cyclin H, a subunit of the general transcription factor TFIIH, which results in the inhibition of TFIIH-dependent phosphorylation of the C-terminal domain of RNAP II, facilitating the inhibition of transcription. It has also been shown to promote transcription by a mechanism that is likely to involve RNAP II phosphorylation. CDK8 also functions as a stimulus-specific positive coregulator of p53 transcriptional responses. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK8 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270851 [Multi-domain]  Cd Length: 333  Bit Score: 48.13  E-value: 2.16e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  727 GKTLGEGEFGKVVKATAFHLKGRAGYttvAVKMLKENA-SPSELRdllsEFNVLKQVNHPHVIKLYGA--CSQDGPLLLI 803
Cdd:cd07868   22 GCKVGRGTYGHVYKAKRKDGKDDKDY---ALKQIEGTGiSMSACR----EIALLRELKHPNVISLQKVflSHADRKVWLL 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  804 VEYAKYG--SLRGFLRESRKvgpgylgsggsrnsssldHPDERALTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNIL 881
Cdd:cd07868   95 FDYAEHDlwHIIKFHRASKA------------------NKKPVQLPRGMVKSLLYQILDGIHYLHANWVLHRDLKPANIL 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  882 V----AEGRKMKISDFGLSRDVyeeDSYVKRSQGRIPVK---WMAIESLF--DHIYTTQSDVWSFGVLLWEIVT------ 946
Cdd:cd07868  157 VmgegPERGRVKIADMGFARLF---NSPLKPLADLDPVVvtfWYRAPELLlgARHYTKAIDIWAIGCIFAELLTsepifh 233
                        250       260
                 ....*....|....*....|....
gi 10862703  947 ------LGGNPYPGIPPERLFNLL 964
Cdd:cd07868  234 crqediKTSNPYHHDQLDRIFNVM 257
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
728-945 2.22e-05

Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LATS was originally identified in Drosophila using a screen for genes whose inactivation led to overproliferation of cells. In tetrapods, there are two LATS isoforms, LATS1 and LATS2. Inactivation of LATS1 in mice results in the development of various tumors, including sarcomas and ovarian cancer. LATS functions as a tumor suppressor and is implicated in cell cycle regulation. The LATS subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270749 [Multi-domain]  Cd Length: 333  Bit Score: 47.70  E-value: 2.22e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  728 KTLGEGEFGKVV---KATAFHLkgragYttvAVKMLKEN--------ASPSELRDLLSEfnvlkqVNHPHVIKLYGACSQ 796
Cdd:cd05598    7 KTIGVGAFGEVSlvrKKDTNAL-----Y---AMKTLRKKdvlkrnqvAHVKAERDILAE------ADNEWVVKLYYSFQD 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  797 DGPLLLIVEYAkygslrgflresrkvgPGylgsggsrnsssldhpderaltmGDLISFAwqISQGM-------QYLAE-- 867
Cdd:cd05598   73 KENLYFVMDYI----------------PG-----------------------GDLMSLL--IKKGIfeedlarFYIAElv 111
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  868 --------MKLVHRDLAARNILVAEGRKMKISDFGLS---RDVYEEDSYVKRSQGRIPvKWMAIESLFDHIYTTQSDVWS 936
Cdd:cd05598  112 caiesvhkMGFIHRDIKPDNILIDRDGHIKLTDFGLCtgfRWTHDSKYYLAHSLVGTP-NYIAPEVLLRTGYTQLCDWWS 190

                 ....*....
gi 10862703  937 FGVLLWEIV 945
Cdd:cd05598  191 VGVILYEML 199
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
858-995 2.41e-05

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated protein kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK-activated protein kinase 2 (MAPKAP2 or MK2) contains an N-terminal proline-rich region that can bind to SH3 domains, a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. MK2 is a bonafide substrate for the MAPK p38. It is closely related to MK3 and thus far, MK2/3 show indistinguishable substrate specificity. They are mainly involved in the regulation of gene expression and they participate in diverse cellular processes such as endocytosis, cytokine production, cytoskeletal reorganization, cell migration, cell cycle control and chromatin remodeling. They are implicated in inflammation and cance and their substrates include mRNA-AU-rich-element (ARE)-binding proteins (TTP and hnRNP A0), Hsp proteins (Hsp27 and Hsp25) and RSK, among others. MK2/3 are both expressed ubiquitously but MK2 is expressed at significantly higher levels. The MK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271072 [Multi-domain]  Cd Length: 303  Bit Score: 47.72  E-value: 2.41e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  858 ISQGMQYLAEMKLVHRDLAARNILVAEGRK---MKISDFGLSRDVYEEDSYVkrSQGRIPVkWMAIESLFDHIYTTQSDV 934
Cdd:cd14170  110 IGEAIQYLHSINIAHRDVKPENLLYTSKRPnaiLKLTDFGFAKETTSHNSLT--TPCYTPY-YVAPEVLGPEKYDKSCDM 186
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 10862703  935 WSFGVLLWeIVTLGGNPYPGIPPERLFNLLKTGHRM---ERPD----NCSEEMYRLMLQCWKQEPDKR 995
Cdd:cd14170  187 WSLGVIMY-ILLCGYPPFYSNHGLAISPGMKTRIRMgqyEFPNpewsEVSEEVKMLIRNLLKTEPTQR 253
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
856-954 2.51e-05

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNK1 is expressed in every cell and tissue type. It specifically binds with JAMP (JNK1-associated membrane protein), which regulates the duration of JNK1 activity in response to stimuli. Specific JNK1 substrates include Itch and SG10, which are implicated in Th2 responses and airway inflammation, and microtubule dynamics and axodendritic length, respectively. Mice deficient in JNK1 are protected against arthritis, obesity, type 2 diabetes, cardiac cell death, and non-alcoholic liver disease, suggesting that JNK1 may play roles in the pathogenesis of these diseases. Initially, it was thought that JNK1 and JNK2 were functionally redundant as mice deficient in either genes could survive but disruption of both genes resulted in lethality. However, recent studies have shown that JNK1 and JNK2 perform distinct functions through specific binding partners and substrates. JNKs are mitogen-activated protein kinases that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. The JNK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143380 [Multi-domain]  Cd Length: 364  Bit Score: 47.73  E-value: 2.51e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  856 WQISQGMQYLAEMKLVHRDLAARNILVAEGRKMKISDFGLSRDV---YEEDSYVKRSQGRIPvkwmaiESLFDHIYTTQS 932
Cdd:cd07875  133 YQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTAgtsFMMTPYVVTRYYRAP------EVILGMGYKENV 206
                         90       100
                 ....*....|....*....|..
gi 10862703  933 DVWSFGVLLWEIVTlGGNPYPG 954
Cdd:cd07875  207 DIWSVGCIMGEMIK-GGVLFPG 227
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
854-1001 2.56e-05

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3); each gene may result in mutliple protein isoforms. There are three PIM2 isoforms resulting from alternative translation initiation sites. PIM2 is highly expressed in leukemia and lymphomas and has been shown to promote the survival and proliferation of tumor cells. The PIM2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271003 [Multi-domain]  Cd Length: 257  Bit Score: 47.15  E-value: 2.56e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  854 FAWQISQGMQYLAEMKLVHRDLAARNILVAEGR-KMKISDFGlSRDVYEEDSYVKRSQGRI--PVKWMaiesLFDHIYTT 930
Cdd:cd14101  113 FFKQVVEAVQHCHSKGVVHRDIKDENILVDLRTgDIKLIDFG-SGATLKDSMYTDFDGTRVysPPEWI----LYHQYHAL 187
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 10862703  931 QSDVWSFGVLLWEIVTlgGNpypgIPPERLFNLLKTghRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADI 1001
Cdd:cd14101  188 PATVWSLGILLYDMVC--GD----IPFERDTDILKA--KPSFNKRVSNDCRSLIRSCLAYNPSDRPSLEQI 250
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
730-952 2.80e-05

N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, in response to various stimuli such as growth factors, hormones, neurotransmitters, cellular stress, and pro-inflammatory cytokines. This triggers phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) in the C-terminal extension of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. MSKs are predominantly nuclear proteins. They are widely expressed in many tissues including heart, brain, lung, liver, kidney, and pancreas. There are two isoforms of MSK, called MSK1 and MSK2. The MSK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270735 [Multi-domain]  Cd Length: 268  Bit Score: 47.00  E-value: 2.80e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  730 LGEGEFGKVvkataFHLKGRAGY---TTVAVKMLKENASPSELRDL---LSEFNVLKQVNH-PHVIKLYGACSQDGPLLL 802
Cdd:cd05583    2 LGTGAYGKV-----FLVRKVGGHdagKLYAMKVLKKATIVQKAKTAehtMTERQVLEAVRQsPFLVTLHYAFQTDAKLHL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  803 IVEYAKYGSLRGFLRESrkvgpgylgsggsrnssslDHPDERALTMgdlisFAWQISQGMQYLAEMKLVHRDLAARNILV 882
Cdd:cd05583   77 ILDYVNGGELFTHLYQR-------------------EHFTESEVRI-----YIGEIVLALEHLHKLGIIYRDIKLENILL 132
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 10862703  883 AEGRKMKISDFGLSRDVYEEDSYVKRSQ-GRIpvKWMAIESLF--DHIYTTQSDVWSFGVLLWEIVTlGGNPY 952
Cdd:cd05583  133 DSEGHVVLTDFGLSKEFLPGENDRAYSFcGTI--EYMAPEVVRggSDGHDKAVDWWSLGVLTYELLT-GASPF 202
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
856-945 2.96e-05

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNK2 is expressed in every cell and tissue type. It is specifically translocated to the mitochondria during dopaminergic cell death. Specific substrates include the microtubule-associated proteins DCX and Tau, as well as TIF-IA which is involved in ribosomal RNA synthesis regulation. Mice deficient in Jnk2 show protection against arthritis, type 1 diabetes, atherosclerosis, abdominal aortic aneurysm, cardiac cell death, TNF-induced liver damage, and tumor growth, indicating that JNK2 may play roles in the pathogenesis of these diseases. Initially it was thought that JNK1 and JNK2 were functionally redundant as mice deficient in either genes could survive but disruption of both genes resulted in lethality. However, recent studies have shown that JNK1 and JNK2 perform distinct functions through specific binding partners and substrates. JNKs are mitogen-activated protein kinases (MAPKs) that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. The JNK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143381 [Multi-domain]  Cd Length: 359  Bit Score: 47.72  E-value: 2.96e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  856 WQISQGMQYLAEMKLVHRDLAARNILVAEGRKMKISDFGLSRDV---YEEDSYVKRSQGRIPvkwmaiESLFDHIYTTQS 932
Cdd:cd07876  130 YQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTActnFMMTPYVVTRYYRAP------EVILGMGYKENV 203
                         90
                 ....*....|...
gi 10862703  933 DVWSFGVLLWEIV 945
Cdd:cd07876  204 DIWSVGCIMGELV 216
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
856-967 2.96e-05

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called Ribosomal protein S6 kinase alpha-6 or 90kDa ribosomal protein S6 kinase 6); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK4 is also called S6K-alpha-6, RPS6KA6, p90RSK6 or pp90RSK4. RSK4 is a substrate of ERK and is a modulator of p53-dependent proliferation arrest in human cells. Deletion of the RSK4 gene, RPS6KA6, frequently occurs in patients of X-linked deafness type 3, mental retardation and choroideremia. Studies of RSK4 in cancer cells and tissues suggest that it may be oncogenic or tumor suppressive depending on many factors. RSK4 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271079 [Multi-domain]  Cd Length: 295  Bit Score: 47.32  E-value: 2.96e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  856 WQISQGMQYLAEMKLVHRDLAARNILV----AEGRKMKISDFGLSRDVYEEDSYVKRSQgrIPVKWMAIESLFDHIYTTQ 931
Cdd:cd14177  105 YTITKTVDYLHCQGVVHRDLKPSNILYmddsANADSIRICDFGFAKQLRGENGLLLTPC--YTANFVAPEVLMRQGYDAA 182
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 10862703  932 SDVWSFGVLLWEIVTlGGNPY---PGIPPERLfnLLKTG 967
Cdd:cd14177  183 CDIWSLGVLLYTMLA-GYTPFangPNDTPEEI--LLRIG 218
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
728-952 3.89e-05

Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ROCK1 is preferentially expressed in the liver, lung, spleen, testes, and kidney. It mediates signaling from Rho to the actin cytoskeleton. It is implicated in the development of cardiac fibrosis, cardiomyocyte apoptosis, and hyperglycemia. Mice deficient with ROCK1 display eyelids open at birth (EOB) and omphalocele phenotypes due to the disorganization of actin filaments in the eyelids and the umbilical ring. ROCK contains an N-terminal extension, a catalytic kinase domain, and a C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD) and a pleckstrin homology (PH) domain. ROCK is auto-inhibited by the RBD and PH domain interacting with the catalytic domain, and is activated via interaction with Rho GTPases. The ROCK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270772 [Multi-domain]  Cd Length: 405  Bit Score: 47.31  E-value: 3.89e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  728 KTLGEGEFGKVvkATAFHLKGRAGYttvAVKMLK--ENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVE 805
Cdd:cd05622   79 KVIGRGAFGEV--QLVRHKSTRKVY---AMKLLSkfEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVME 153
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  806 YAKYGSLRGFLREsrkvgpgylgsggsrnsssLDHPDERALTmgdlisFAWQISQGMQYLAEMKLVHRDLAARNILVAEG 885
Cdd:cd05622  154 YMPGGDLVNLMSN-------------------YDVPEKWARF------YTAEVVLALDAIHSMGFIHRDVKPDNMLLDKS 208
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 10862703  886 RKMKISDFGLSRDVyEEDSYVKRSQGRIPVKWMAIESLF----DHIYTTQSDVWSFGVLLWEIVtLGGNPY 952
Cdd:cd05622  209 GHLKLADFGTCMKM-NKEGMVRCDTAVGTPDYISPEVLKsqggDGYYGRECDWWSVGVFLYEML-VGDTPF 277
STKc_ACVR2a cd14141
Catalytic domain of the Serine/Threonine Kinase, Activin Type IIA Receptor; STKs catalyze the ...
733-946 4.19e-05

Catalytic domain of the Serine/Threonine Kinase, Activin Type IIA Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ACVR2a (or ActRIIA) belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins (BMPs), activins, growth and differentiation factors (GDFs), and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. ACVR2b is one of two ACVR2 receptors found in vertebrates. Type II receptors are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. ACVR2 acts primarily as the receptors for activins, nodal, myostatin, GDF11, and a subset of BMPs. ACVR2 signaling impacts many cellular and physiological processes including reproductive and gonadal functions, myogenesis, bone remodeling and tooth development, kidney organogenesis, apoptosis, fibrosis, inflammation, and neurogenesis. The ACVR2a subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271043 [Multi-domain]  Cd Length: 290  Bit Score: 46.96  E-value: 4.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  733 GEFGKVVKATAFHlkgragyTTVAVKMLKenaspseLRDLLS---EFNV--LKQVNHPHVIKLYGA----CSQDGPLLLI 803
Cdd:cd14141    6 GRFGCVWKAQLLN-------EYVAVKIFP-------IQDKLSwqnEYEIysLPGMKHENILQFIGAekrgTNLDVDLWLI 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  804 VEYAKYGSLRGFLRESrkvgpgylgsggsrnsssldhpderALTMGDLISFAWQISQGMQYLAE----------MKLVHR 873
Cdd:cd14141   72 TAFHEKGSLTDYLKAN-------------------------VVSWNELCHIAQTMARGLAYLHEdipglkdghkPAIAHR 126
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 10862703  874 DLAARNILVAEGRKMKISDFGLSRDvYEEDSYVKRSQGRIPV-KWMAIESL-----FDHIYTTQSDVWSFGVLLWEIVT 946
Cdd:cd14141  127 DIKSKNVLLKNNLTACIADFGLALK-FEAGKSAGDTHGQVGTrRYMAPEVLegainFQRDAFLRIDMYAMGLVLWELAS 204
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
730-1000 4.72e-05

Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Obscurin, approximately 800 kDa in size, is one of three giant proteins expressed in vetebrate striated muscle, together with titin and nebulin. It is a multidomain protein composed of tandem adhesion and signaling domains, including 49 immunoglobulin (Ig) and 2 fibronectin type III (FN3) domains at the N-terminus followed by a more complex region containing more Ig domains, a conserved SH3 domain near a RhoGEF and PH domains, non-modular regions, as well as IQ and phosphorylation motifs. The obscurin gene also encode two kinase domains, which are not expressed as part of the 800 kDa protein, but as a smaller, alternatively spliced product present mainly in the heart muscle, also called obscurin-MLCK. Obscurin is localized at the peripheries of Z-disks and M-lines, where it is able to communicate with the surrounding myoplasm. It interacts with diverse proteins including sAnk1, myosin, titin, and MyBP-C. It may act as a scaffold for the assembly of elements of the contractile apparatus. The obscurin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271009 [Multi-domain]  Cd Length: 257  Bit Score: 46.42  E-value: 4.72e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  730 LGEGEFGKVVKATafHlkgRAGYTTVAVKML----KENASPSELRDLLSefnvlkQVNHPHVIKLYGACSQDGPLLLIVE 805
Cdd:cd14107   10 IGRGTFGFVKRVT--H---KGNGECCAAKFIplrsSTRARAFQERDILA------RLSHRRLTCLLDQFETRKTLILILE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  806 YAKYGSLrgflresrkvgpgylgsggsrnsssLDHPDERA-LTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNILVA- 883
Cdd:cd14107   79 LCSSEEL-------------------------LDRLFLKGvVTEAEVKLYIQQVLEGIGYLHGMNILHLDIKPDNILMVs 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  884 -EGRKMKISDFGLSRDVyeEDSYVKRSQGRIPvKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLgGNPYPGiPPER--L 960
Cdd:cd14107  134 pTREDIKICDFGFAQEI--TPSEHQFSKYGSP-EFVAPEIVHQEPVSAATDIWALGVIAYLSLTC-HSPFAG-ENDRatL 208
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 10862703  961 FNLLKTGHRMERPD--NCSEEMYRLMLQCWKQEPDKRPVFAD 1000
Cdd:cd14107  209 LNVAEGVVSWDTPEitHLSEDAKDFIKRVLQPDPEKRPSASE 250
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
856-945 6.84e-05

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNK3 is expressed primarily in the brain, and to a lesser extent in the heart and testis. Mice deficient in JNK3 are protected against kainic acid-induced seizures, stroke, sciatic axotomy neural death, and neuronal death due to NGF deprivation, oxidative stress, or exposure to beta-amyloid peptide. This suggests that JNK3 may play roles in the pathogenesis of these diseases. JNKs are mitogen-activated protein kinases (MAPKs) that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. The JNK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143379 [Multi-domain]  Cd Length: 355  Bit Score: 46.62  E-value: 6.84e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  856 WQISQGMQYLAEMKLVHRDLAARNILVAEGRKMKISDFGLSRDV---YEEDSYVKRSQGRIPvkwmaiESLFDHIYTTQS 932
Cdd:cd07874  126 YQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTAgtsFMMTPYVVTRYYRAP------EVILGMGYKENV 199
                         90
                 ....*....|...
gi 10862703  933 DVWSFGVLLWEIV 945
Cdd:cd07874  200 DIWSVGCIMGEMV 212
PKc_DYRK4 cd14225
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
854-954 9.11e-05

Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and -Regulated Kinase 4; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. DYRK4 is a testis-specific kinase with restricted expression to postmeiotic spermatids. It may function during spermiogenesis, however, it is not required for male fertility. DYRK4 has also been detected in a human teratocarcinoma cell line induced to produce postmitotic neurons. It may have a role in neuronal differentiation. DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. They play important roles in cell proliferation, differentiation, survival, and development. The DYRK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271127 [Multi-domain]  Cd Length: 341  Bit Score: 45.85  E-value: 9.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  854 FAWQISQGMQYLAEMKLVHRDLAARNILVAEGRK--MKISDFGLSrdVYEEDSYVKRSQGRIpvkWMAIESLFDHIYTTQ 931
Cdd:cd14225  151 FAISLLQCLRLLYRERIIHCDLKPENILLRQRGQssIKVIDFGSS--CYEHQRVYTYIQSRF---YRSPEVILGLPYSMA 225
                         90       100
                 ....*....|....*....|....
gi 10862703  932 SDVWSFGVLLWEIVTlgGNP-YPG 954
Cdd:cd14225  226 IDMWSLGCILAELYT--GYPlFPG 247
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
728-952 9.69e-05

Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ROCK2 was the first identified target of activated RhoA, and was found to play a role in stress fiber and focal adhesion formation. It is prominently expressed in the brain, heart, and skeletal muscles. It is implicated in vascular and neurological disorders, such as hypertension and vasospasm of the coronary and cerebral arteries. ROCK2 is also activated by caspase-2 cleavage, resulting in thrombin-induced microparticle generation in response to cell activation. Mice deficient in ROCK2 show intrauterine growth retardation and embryonic lethality because of placental dysfunction. ROCK contains an N-terminal extension, a catalytic kinase domain, and a C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD) and a pleckstrin homology (PH) domain. ROCK is auto-inhibited by the RBD and PH domain interacting with the catalytic domain, and is activated via interaction with Rho GTPases. The ROCK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270771 [Multi-domain]  Cd Length: 379  Bit Score: 46.15  E-value: 9.69e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  728 KTLGEGEFGKVVKatafhLKGRAGYTTVAVKMLK--ENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVE 805
Cdd:cd05621   58 KVIGRGAFGEVQL-----VRHKASQKVYAMKLLSkfEMIKRSDSAFFWEERDIMAFANSPWVVQLFCAFQDDKYLYMVME 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  806 YAKYGSLRGFLresrkvgpgylgsggsrnsSSLDHPDERALTmgdlisFAWQISQGMQYLAEMKLVHRDLAARNILVAEG 885
Cdd:cd05621  133 YMPGGDLVNLM-------------------SNYDVPEKWAKF------YTAEVVLALDAIHSMGLIHRDVKPDNMLLDKY 187
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 10862703  886 RKMKISDFGLSRDVyEEDSYVKRSQGRIPVKWMAIESLF----DHIYTTQSDVWSFGVLLWEIVtLGGNPY 952
Cdd:cd05621  188 GHLKLADFGTCMKM-DETGMVHCDTAVGTPDYISPEVLKsqggDGYYGRECDWWSVGVFLFEML-VGDTPF 256
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
730-936 1.16e-04

Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NIK, also called mitogen activated protein kinase kinase kinase 14 (MAP3K14), phosphorylates and activates Inhibitor of NF-KappaB Kinase (IKK) alpha, which is a regulator of NF-kB proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. NIK is essential in the IKKalpha-mediated non-canonical NF-kB signaling pathway, in which IKKalpha processes the IkB-like C-terminus of NF-kB2/p100 to produce p52, allowing the p52/RelB dimer to migrate to the nucleus where it regulates gene transcription. NIK also plays an important role in Toll-like receptor 7/9 signaling cascades. The NIK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270893 [Multi-domain]  Cd Length: 268  Bit Score: 45.19  E-value: 1.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  730 LGEGEFGKVVKA----TAFhlkgragytTVAVKMLKENASPSElrdllsEFNVLKQVNHPHVIKLYGACsQDGPLLLI-V 804
Cdd:cd13991   14 IGRGSFGEVHRMedkqTGF---------QCAVKKVRLEVFRAE------ELMACAGLTSPRVVPLYGAV-REGPWVNIfM 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  805 EYAKYGSLRGFLRESrkvgpGYLgsggsrnsssldhPDERALtmgdliSFAWQISQGMQYLAEMKLVHRDLAARNILVAE 884
Cdd:cd13991   78 DLKEGGSLGQLIKEQ-----GCL-------------PEDRAL------HYLGQALEGLEYLHSRKILHGDVKADNVLLSS 133
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 10862703  885 -GRKMKISDF---------GLSRDVYEEDsYVKRSQGRipvkwMAIESLFDHIYTTQSDVWS 936
Cdd:cd13991  134 dGSDAFLCDFghaecldpdGLGKSLFTGD-YIPGTETH-----MAPEVVLGKPCDAKVDVWS 189
PKc_DYRK2_3 cd14224
Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and ...
854-958 1.38e-04

Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and -Regulated Kinases 2 and 3; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. This subfamily is composed of DYRK2 and DYRK3, and similar proteins. Drosophila DYRK2 interacts and phosphorylates the chromatin remodelling factor, SNR1 (Snf5-related 1), and also interacts with the essential chromatin component, trithorax. It may play a role in chromatin remodelling. Vertebrate DYRK2 phosphorylates and regulates the tumor suppressor p53 to induce apoptosis in response to DNA damage. It can also phosphorylate the transcription factor, nuclear factor of activated T cells (NFAT). DYRK2 is overexpressed in lung adenocarcinoma and esophageal carcinomas, and is a predictor for favorable prognosis in lung adenocarcinoma. DYRK3, also called regulatory erythroid kinase (REDK), is highly expressed in erythroid cells and the testis, and is also present in adult kidney and liver. It promotes cell survival by phosphorylating and activating SIRT1, an NAD(+)-dependent protein deacetylase, which promotes p53 deacetylation, resulting in the inhibition of apoptosis. DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. The DYRK2/3 subfamily is part of a larger superfamily that includes the catalytic domains of other S/T kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271126 [Multi-domain]  Cd Length: 380  Bit Score: 45.51  E-value: 1.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  854 FAWQISQGMQYLAEMKLVHRDLAARNILVAE-GRK-MKISDFGLSrdVYEEDSYVKRSQGRIpvkWMAIESLFDHIYTTQ 931
Cdd:cd14224  173 FAHSILQCLDALHRNKIIHCDLKPENILLKQqGRSgIKVIDFGSS--CYEHQRIYTYIQSRF---YRAPEVILGARYGMP 247
                         90       100
                 ....*....|....*....|....*..
gi 10862703  932 SDVWSFGVLLWEIVTlggnPYPGIPPE 958
Cdd:cd14224  248 IDMWSFGCILAELLT----GYPLFPGE 270
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
856-946 1.49e-04

C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK2 and MSK1 play nonredundant roles in activating histone H3 kinases, which play pivotal roles in compaction of the chromatin fiber. MSK2 is the required H3 kinase in response to stress stimuli and activation of the p38 MAPK pathway. MSK2 also plays a role in the pathogenesis of psoriasis. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family, similar to 90 kDa ribosomal protein S6 kinases (RSKs). MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271082 [Multi-domain]  Cd Length: 309  Bit Score: 45.25  E-value: 1.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  856 WQISQGMQ-------YLAEMKLVHRDLAARNILVA---EGRKMKISDFGLSRdvyeedsyvKRSQGRIP-------VKWM 918
Cdd:cd14180  101 SEASQLMRslvsavsFMHEAGVVHRDLKPENILYAdesDGAVLKVIDFGFAR---------LRPQGSRPlqtpcftLQYA 171
                         90       100
                 ....*....|....*....|....*...
gi 10862703  919 AIESLFDHIYTTQSDVWSFGVLLWEIVT 946
Cdd:cd14180  172 APELFSNQGYDESCDLWSLGVILYTMLS 199
STKc_WNK2_like cd14032
Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the ...
730-953 1.49e-04

Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK2 is widely expressed and has been shown to be epigenetically silenced in gliomas. It inhibits cell growth by acting as a negative regulator of MEK1-ERK1/2 signaling. WNK2 modulates growth factor-induced cancer cell proliferation, suggesting that it may be a tumor suppressor gene. WNKs comprise a subfamily of STKs with an unusual placement of the catalytic lysine relative to all other protein kinases. They are critical in regulating ion balance and are thus, important components in the control of blood pressure. The WNK2-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270934 [Multi-domain]  Cd Length: 266  Bit Score: 45.07  E-value: 1.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  730 LGEGEFGKVVKAtafhLKGRAGYTTVAVKMLKENASPSELRDLLSEFNVLKQVNHPHVIKLYG--ACSQDGP--LLLIVE 805
Cdd:cd14032    9 LGRGSFKTVYKG----LDTETWVEVAWCELQDRKLTKVERQRFKEEAEMLKGLQHPNIVRFYDfwESCAKGKrcIVLVTE 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  806 YAKYGSLRGFLRESRKVGPGYLGsggsrnsssldhpderaltmgdliSFAWQISQGMQYLAEMK--LVHRDLAARNILV- 882
Cdd:cd14032   85 LMTSGTLKTYLKRFKVMKPKVLR------------------------SWCRQILKGLLFLHTRTppIIHRDLKCDNIFIt 140
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 10862703  883 AEGRKMKISDFGLSrdVYEEDSYVKRSQGriPVKWMAIESLFDHiYTTQSDVWSFGVLLWEIVTlggNPYP 953
Cdd:cd14032  141 GPTGSVKIGDLGLA--TLKRASFAKSVIG--TPEFMAPEMYEEH-YDESVDVYAFGMCMLEMAT---SEYP 203
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
728-945 1.82e-04

Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CRIK (also called citron kinase) is an effector of the small GTPase Rho. It plays an important function during cytokinesis and affects its contractile process. CRIK-deficient mice show severe ataxia and epilepsy as a result of abnormal cytokinesis and massive apoptosis in neuronal precursors. A Down syndrome critical region protein TTC3 interacts with CRIK and inhibits CRIK-dependent neuronal differentiation and neurite extension. CRIK contains a catalytic domain, a central coiled-coil domain, and a C-terminal region containing a Rho-binding domain (RBD), a zinc finger, and a pleckstrin homology (PH) domain, in addition to other motifs. The CRIK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270752 [Multi-domain]  Cd Length: 328  Bit Score: 44.99  E-value: 1.82e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  728 KTLGEGEFGKVvkatafHL-KGRAGYTTVAVKMLKENASPS--------ELRDLLSefnvlkQVNHPHVIKLYGACSQDG 798
Cdd:cd05601    7 NVIGRGHFGEV------QVvKEKATGDIYAMKVLKKSETLAqeevsffeEERDIMA------KANSPWITKLQYAFQDSE 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  799 PLLLIVEYAKYGSLRGFLreSRKVGPgylgsggsrnsssLDHpderaltmgDLISFawqisqgmqYLAEMKL-------- 870
Cdd:cd05601   75 NLYLVMEYHPGGDLLSLL--SRYDDI-------------FEE---------SMARF---------YLAELVLaihslhsm 121
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  871 --VHRDLAARNILVAEGRKMKISDFG----LSRDvyeedsyvKRSQGRIPV---KWMAIESL------FDHIYTTQSDVW 935
Cdd:cd05601  122 gyVHRDIKPENILIDRTGHIKLADFGsaakLSSD--------KTVTSKMPVgtpDYIAPEVLtsmnggSKGTYGVECDWW 193
                        250
                 ....*....|
gi 10862703  936 SFGVLLWEIV 945
Cdd:cd05601  194 SLGIVAYEML 203
STKc_PIM3 cd14102
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
854-1001 1.99e-04

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3). PIM3 can inhibit apoptosis and promote cell survival and protein translation, therefore, it can enhance the proliferation of normal and cancer cells. Mice deficient with PIM3 show minimal effects, suggesting that PIM3 msy not be essential. Since its expression is enhanced in several cancers, it may make a good molecular target for cancer drugs. The PIM3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271004 [Multi-domain]  Cd Length: 253  Bit Score: 44.56  E-value: 1.99e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  854 FAWQISQGMQYLAEMKLVHRDLAARNILV-AEGRKMKISDFGlSRDVYEEDSYVKRSQGRI--PVKWMAIeslfdHIYTT 930
Cdd:cd14102  110 FFRQVLEAVRHCYSCGVVHRDIKDENLLVdLRTGELKLIDFG-SGALLKDTVYTDFDGTRVysPPEWIRY-----HRYHG 183
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 10862703  931 QS-DVWSFGVLLWEIVtlggnpYPGIPPERLFNLLKTghRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADI 1001
Cdd:cd14102  184 RSaTVWSLGVLLYDMV------CGDIPFEQDEEILRG--RLYFRRRVSPECQQLIKWCLSLRPSDRPTLEQI 247
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
727-951 2.12e-04

Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase signal-integrating kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK signal-integrating kinases (Mnks) are MAPK-activated protein kinases and is comprised by a group of four proteins, produced by alternative splicing from two genes (Mnk1 and Mnk2). The isoforms of Mnk1 (1a/1b) and Mnk2 (2a/2b) differ at their C-termini, with the a-form having a longer C-terminus containing a MAPK-binding region. All Mnks contain a catalytic kinase domain and a polybasic region at the N-terminus which binds importin and the eukaryotic initiation factor eIF4G. The best characterized Mnk substrate is eIF4G, whose phosphorylation may promote the export of certain mRNAs from the nucleus. Mnk also phosphorylate substrates that bind to AU-rich elements that regulate mRNA stability and translation. Mnks have also been implicated in tyrosine kinase receptor signaling, inflammation, and cell prolieration or survival. The Mnk subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270992 [Multi-domain]  Cd Length: 289  Bit Score: 44.71  E-value: 2.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  727 GKTLGEGEFGKVvkATAFHLKGRAGYttvAVKMLKENASPSELRdLLSEFNVLKQV-NHPHVIKLYGACSQDGPLLLIVE 805
Cdd:cd14090    7 GELLGEGAYASV--QTCINLYTGKEY---AVKIIEKHPGHSRSR-VFREVETLHQCqGHPNILQLIEYFEDDERFYLVFE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  806 YAKYGSL------RGFLRESrkvgpgylgsggsrnsssldhpdERALTMGDlisfawqISQGMQYLAEMKLVHRDLAARN 879
Cdd:cd14090   81 KMRGGPLlshiekRVHFTEQ-----------------------EASLVVRD-------IASALDFLHDKGIAHRDLKPEN 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  880 ILVAEGRKM---KISDFGLS---RDVYEEDSYVKRSQGRIPV---KWMAIE--SLF---DHIYTTQSDVWSFGVLLWeiV 945
Cdd:cd14090  131 ILCESMDKVspvKICDFDLGsgiKLSSTSMTPVTTPELLTPVgsaEYMAPEvvDAFvgeALSYDKRCDLWSLGVILY--I 208

                 ....*.
gi 10862703  946 TLGGNP 951
Cdd:cd14090  209 MLCGYP 214
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
838-954 2.39e-04

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNKs are mitogen-activated protein kinases (MAPKs) that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. They are also essential regulators of physiological and pathological processes and are involved in the pathogenesis of several diseases such as diabetes, atherosclerosis, stroke, Parkinson's and Alzheimer's. Vetebrates harbor three different JNK genes (Jnk1, Jnk2, and Jnk3) that are alternatively spliced to produce at least 10 isoforms. JNKs are specifically activated by the MAPK kinases MKK4 and MKK7, which are in turn activated by upstream MAPK kinase kinases as a result of different stimuli including stresses such as ultraviolet (UV) irradiation, hyperosmolarity, heat shock, or cytokines. JNKs activate a large number of different substrates based on specific stimulus, cell type, and cellular condition, and may be implicated in seemingly contradictory functions. The JNK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270840 [Multi-domain]  Cd Length: 337  Bit Score: 44.71  E-value: 2.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  838 LDHpdERaltmgdLISFAWQISQGMQYLAEMKLVHRDLAARNILVAEGRKMKISDFGLSRDVYEE---DSYVKRSQGRIP 914
Cdd:cd07850   99 LDH--ER------MSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTAGTSfmmTPYVVTRYYRAP 170
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 10862703  915 vkwmaiESLFDHIYTTQSDVWSFGVLLWEIVtLGGNPYPG 954
Cdd:cd07850  171 ------EVILGMGYKENVDIWSVGCIMGEMI-RGTVLFPG 203
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
725-951 2.80e-04

Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated protein kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the MAPK-activated protein kinases MK2, MK3, MK5 (also called PRAK for p38-regulated/activated protein kinase), and related proteins. These proteins contain a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. In addition, MK2 and MK3 contain an N-terminal proline-rich region that can bind to SH3 domains. MK2 and MK3 are bonafide substrates for the MAPK p38, while MK5 plays a functional role in the p38 MAPK pathway although their direct interaction has been difficult to detect. MK2 and MK3 are closely related and show, thus far, indistinguishable substrate specificity, while MK5 shows a distinct spectrum of substrates. MK2 and MK3 are mainly involved in the regulation of gene expression and they participate in diverse cellular processes such as endocytosis, cytokine production, cytoskeletal reorganization, cell migration, cell cycle control and chromatin remodeling. They are implicated in inflammation and cance and their substrates include mRNA-AU-rich-element (ARE)-binding proteins (TTP and hnRNP A0), Hsp proteins (Hsp27 and Hsp25) and RSK, among others. MK2/3 are both expressed ubiquitously but MK2 is expressed at significantly higher levels. MK5 is a ubiquitous protein that is implicated in neuronal morphogenesis, cell migration, and tumor angiogenesis. It interacts with PKA, which induces cytoplasmic translocation of MK5. Its substrates includes p53, ERK3/4, Hsp27, and cytosolic phospholipase A2 (cPLA2). The MAPKAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270991 [Multi-domain]  Cd Length: 263  Bit Score: 43.82  E-value: 2.80e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  725 VLGKTLGEGEFGKVVKAtaFHLKGRAGYttvAVKMLKENasPSELRDLLSEFnvlKQVNHPHVIKL---YGACSQDGPLL 801
Cdd:cd14089    4 ISKQVLGLGINGKVLEC--FHKKTGEKF---ALKVLRDN--PKARREVELHW---RASGCPHIVRIidvYENTYQGRKCL 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  802 LIV-EYAKYGSLrgFLRESRKVgpgylgsggsrnsssldhpdERALTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNI 880
Cdd:cd14089   74 LVVmECMEGGEL--FSRIQERA--------------------DSAFTEREAAEIMRQIGSAVAHLHSMNIAHRDLKPENL 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  881 LVAE---GRKMKISDFGLSRDVYEEDS---------YVkrsqgripvkwmAIESLFDHIYTTQSDVWSFGVLLWeiVTLG 948
Cdd:cd14089  132 LYSSkgpNAILKLTDFGFAKETTTKKSlqtpcytpyYV------------APEVLGPEKYDKSCDMWSLGVIMY--ILLC 197

                 ...
gi 10862703  949 GNP 951
Cdd:cd14089  198 GYP 200
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
730-951 3.47e-04

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase signal-integrating kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK signal-integrating kinases (Mnks) are MAPK-activated protein kinases and is comprised by a group of four proteins, produced by alternative splicing from two genes (Mnk1 and Mnk2). The isoforms of Mnk1 (1a/1b) and Mnk2 (2a/2b) differ at their C-termini, with the a-form having a longer C-terminus containing a MAPK-binding region. All Mnks contain a catalytic kinase domain and a polybasic region at the N-terminus which binds importin and the eukaryotic initiation factor eIF4G. The best characterized Mnk substrate is eIF4G, whose phosphorylation may promote the export of certain mRNAs from the nucleus. Mnk also phosphorylate substrates that bind to AU-rich elements that regulate mRNA stability and translation. Mnks have also been implicated in tyrosine kinase receptor signaling, inflammation, and cell prolieration or survival. The Mnk subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271075 [Multi-domain]  Cd Length: 288  Bit Score: 43.86  E-value: 3.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  730 LGEGEFGKVvkATAFHLKGRAGYttvAVKMLKENASPSELRdLLSEFNVLKQVN-HPHVIKLYGACSQDGPLLLIVEYAK 808
Cdd:cd14173   10 LGEGAYARV--QTCINLITNKEY---AVKIIEKRPGHSRSR-VFREVEMLYQCQgHRNVLELIEFFEEEDKFYLVFEKMR 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  809 YGSLRGFLRESRkvgpgylgsggsrnsssldHPDERAltmgdlISFAWQ-ISQGMQYLAEMKLVHRDLAARNILVAEGRK 887
Cdd:cd14173   84 GGSILSHIHRRR-------------------HFNELE------ASVVVQdIASALDFLHNKGIAHRDLKPENILCEHPNQ 138
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 10862703  888 M---KISDFGLSRDVY--EEDSYVKRSQGRIP---VKWMAIESL--FDH---IYTTQSDVWSFGVLLWeiVTLGGNP 951
Cdd:cd14173  139 VspvKICDFDLGSGIKlnSDCSPISTPELLTPcgsAEYMAPEVVeaFNEeasIYDKRCDLWSLGVILY--IMLSGYP 213
STKc_CDC2L6 cd07867
Catalytic domain of Serine/Threonine Kinase, Cell Division Cycle 2-like 6; STKs catalyze the ...
727-946 3.59e-04

Catalytic domain of Serine/Threonine Kinase, Cell Division Cycle 2-like 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDC2L6 is also called CDK8-like and was previously referred to as CDK11. However, this is a confusing nomenclature as CDC2L6 is distinct from CDC2L1, which is represented by the two protein products from its gene, called CDK11(p110) and CDK11(p58), as well as the caspase-processed CDK11(p46). CDK11(p110), CDK11(p58), and CDK11(p46)do not belong to this subfamily. CDC2L6 is an associated protein of Mediator, a multiprotein complex that provides a platform to connect transcriptional and chromatin regulators and cofactors, in order to activate and mediate RNA polymerase II transcription. CDC2L6 is localized mainly in the nucleus amd exerts an opposing effect to CDK8 in VP16-dependent transcriptional activation by being a negative regulator. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDC2L6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270850 [Multi-domain]  Cd Length: 318  Bit Score: 43.90  E-value: 3.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  727 GKTLGEGEFGKVVKATAFHLKGRAGYttvAVKMLKENA-SPSELRdllsEFNVLKQVNHPHVIKLYGA--CSQDGPLLLI 803
Cdd:cd07867    7 GCKVGRGTYGHVYKAKRKDGKDEKEY---ALKQIEGTGiSMSACR----EIALLRELKHPNVIALQKVflSHSDRKVWLL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  804 VEYAKYG--SLRGFLRESRKvgpgylgsggsrnsssldHPDERALTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNIL 881
Cdd:cd07867   80 FDYAEHDlwHIIKFHRASKA------------------NKKPMQLPRSMVKSLLYQILDGIHYLHANWVLHRDLKPANIL 141
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 10862703  882 V----AEGRKMKISDFGLSRDVyeeDSYVKRSQGRIPVK---WMAIESLF--DHIYTTQSDVWSFGVLLWEIVT 946
Cdd:cd07867  142 VmgegPERGRVKIADMGFARLF---NSPLKPLADLDPVVvtfWYRAPELLlgARHYTKAIDIWAIGCIFAELLT 212
PK_TRB2 cd14022
Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein ...
856-995 4.46e-04

Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. TRB2 binds and negatively regulates the mitogen activated protein kinase (MAPK) kinases, MKK7 and MEK1, which are activators of the MAPKs, ERK and JNK. It controls the activation of inflammatory monocytes, which is essential in innate immune responses and the pathogenesis of inflammatory diseases such as atherosclerosis. TRB2 expression is down-regulated in human acute myeloid leukaemia (AML), which may lead to enhanced cell survival and pathogenesis of the disease. TRB2 is one of three Tribbles Homolog (TRB) proteins present in vertebrates that are encoded by three separate genes. TRB proteins interact with many proteins involved in signalling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, and gene expression. The TRB2 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270924 [Multi-domain]  Cd Length: 242  Bit Score: 43.10  E-value: 4.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  856 WQISQGMQYLAEMKLVHRDLAARNILVAEGRKMKISDFGLsrdvyeEDSYVKRSQGripvkwmaiESLFD---------- 925
Cdd:cd14022   91 YQIASAVAHCHDGGLVLRDLKLRKFVFKDEERTRVKLESL------EDAYILRGHD---------DSLSDkhgcpayvsp 155
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 10862703  926 HIYTTQ-------SDVWSFGVLLWEIVtLGGNPYPGIPPERLFNLLKTGHrMERPDNCSEEMYRLMLQCWKQEPDKR 995
Cdd:cd14022  156 EILNTSgsysgkaADVWSLGVMLYTML-VGRYPFHDIEPSSLFSKIRRGQ-FNIPETLSPKAKCLIRSILRREPSER 230
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
853-954 5.94e-04

Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle preferentially expressed protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Striated muscle preferentially expressed gene (SPEG) generates 4 different isoforms through alternative promoter use and splicing in a tissue-specific manner: SPEGalpha and SPEGbeta are expressed in cardiac and skeletal striated muscle; Aortic Preferentially Expressed Protein-1 (APEG-1) is expressed in vascular smooth muscle; and Brain preferentially expressed gene (BPEG) is found in the brain and aorta. SPEG proteins have mutliple immunoglobulin (Ig), 2 fibronectin type III (FN3), and two kinase domains. They are necessary for cardiac development and survival. The SPEG subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271010 [Multi-domain]  Cd Length: 255  Bit Score: 42.97  E-value: 5.94e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  853 SFAWQISQGMQYLAEMKLVHRDLAARNILVAEGR--KMKISDFGLSRDVY-EEDSYVKRSqgrIPvKWMAIESLFDHIYT 929
Cdd:cd14108  101 SYMRQLLEGIEYLHQNDVLHLDLKPENLLMADQKtdQVRICDFGNAQELTpNEPQYCKYG---TP-EFVAPEIVNQSPVS 176
                         90       100
                 ....*....|....*....|....*
gi 10862703  930 TQSDVWSFGVLLWEIVTlGGNPYPG 954
Cdd:cd14108  177 KVTDIWPVGVIAYLCLT-GISPFVG 200
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
724-1012 7.59e-04

Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GAK, also called auxilin-2, contains an N-terminal kinase domain that phosphorylates the mu subunits of adaptor protein (AP) 1 and AP2. In addition, it contains an auxilin-1-like domain structure consisting of PTEN-like, clathrin-binding, and J domains. Like auxilin-1, GAK facilitates Hsc70-mediated dissociation of clathrin from clathrin-coated vesicles. GAK is expressed ubiquitously and is enriched in the Golgi, unlike auxilin-1 which is nerve-specific. GAK also plays regulatory roles outside of clathrin-mediated membrane traffic including the maintenance of centrosome integrity and chromosome congression, neural patterning, survival of neurons, and immune responses through interaction with the interleukin 12 receptor. It also interacts with the androgen receptor, acting as a transcriptional coactivator, and its expression is significantly increased with the progression of prostate cancer. The GAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270938 [Multi-domain]  Cd Length: 282  Bit Score: 42.88  E-value: 7.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  724 LVLGKTLGEGEFGKVVKATafhlKGRAGyTTVAVKMLKENASpSELRDLLSEFNVLKQVN-HPHVIKLYGACS------- 795
Cdd:cd14036    2 LRIKRVIAEGGFAFVYEAQ----DVGTG-KEYALKRLLSNEE-EKNKAIIQEINFMKKLSgHPNIVQFCSAASigkeesd 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  796 -QDGPLLLIVEYAKyGSLRGFLRESRKVGPgylgsggsrnsssldhpderaLTMGDLISFAWQISQGMQYLAEMK--LVH 872
Cdd:cd14036   76 qGQAEYLLLTELCK-GQLVDFVKKVEAPGP---------------------FSPDTVLKIFYQTCRAVQHMHKQSppIIH 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  873 RDLAARNILVAEGRKMKISDFGLSRDV--YEEDSYV--KRSQG------------RIPvkwMAIESLFDHIYTTQSDVWS 936
Cdd:cd14036  134 RDLKIENLLIGNQGQIKLCDFGSATTEahYPDYSWSaqKRSLVedeitrnttpmyRTP---EMIDLYSNYPIGEKQDIWA 210
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 10862703  937 FGVLLWeIVTLGGNPYPGIPPERLFNLLKTGHRMERPDNCSEEMYRLMLQCwkqEPDKRPVFADISKDLEKMMVKR 1012
Cdd:cd14036  211 LGCILY-LLCFRKHPFEDGAKLRIINAKYTIPPNDTQYTVFHDLIRSTLKV---NPEERLSITEIVEQLQELAAAR 282
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
849-995 1.26e-03

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK2, also called beta-adrenergic receptor kinase (beta-ARK) or beta-ARK1, is important in regulating several cardiac receptor responses. It plays a role in cardiac development and in hypertension. Deletion of GRK2 in mice results in embryonic lethality, caused by hypoplasia of the ventricular myocardium. GRK2 also plays important roles in the liver (as a regulator of portal blood pressure), in immune cells, and in the nervous system. Altered GRK2 expression has been reported in several disorders including major depression, schizophrenia, bipolar disorder, and Parkinsonism. GRK2 contains an N-terminal RGS homology (RH) domain, a central catalytic domain, and C-terminal pleckstrin homology (PH) domain that mediates PIP2 and G protein betagamma-subunit translocation to the membrane. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. TheGRK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271125 [Multi-domain]  Cd Length: 321  Bit Score: 42.34  E-value: 1.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  849 GDLISFAWQISQGMQYLAEMKLVHRDLAARNILVAEGRKMKISDFGLSRDVYEEDSYVK-RSQGripvkWMAIESLFDHI 927
Cdd:cd14223  103 AEMRFYAAEIILGLEHMHSRFVVYRDLKPANILLDEFGHVRISDLGLACDFSKKKPHASvGTHG-----YMAPEVLQKGV 177
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 10862703  928 -YTTQSDVWSFGVLLWEIVTlGGNPYP--GIPPERLFNLLKTGHRMERPDNCSEEMYRLMLQCWKQEPDKR 995
Cdd:cd14223  178 aYDSSADWFSLGCMLFKLLR-GHSPFRqhKTKDKHEIDRMTLTMAVELPDSFSPELRSLLEGLLQRDVNRR 247
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
854-995 1.45e-03

Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The beta-ARK group is composed of GRK2, GRK3, and similar proteins. GRK2 and GRK3 are both widely expressed in many tissues, although GRK2 is present at higher levels. They contain an N-terminal RGS homology (RH) domain, a central catalytic domain, and C-terminal pleckstrin homology (PH) domain that mediates PIP2 and G protein betagamma-subunit translocation to the membrane. GRK2 (also called beta-ARK or beta-ARK1) is important in regulating several cardiac receptor responses. It plays a role in cardiac development and in hypertension. Deletion of GRK2 in mice results in embryonic lethality, caused by hypoplasia of the ventricular myocardium. GRK2 also plays important roles in the liver (as a regulator of portal blood pressure), in immune cells, and in the nervous system. Altered GRK2 expression has been reported in several disorders including major depression, schizophrenia, bipolar disorder, and Parkinsonism. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The beta-ARK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270757 [Multi-domain]  Cd Length: 279  Bit Score: 42.04  E-value: 1.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  854 FAWQISQGMQYLAEMKLVHRDLAARNILVAEGRKMKISDFGLSRDVyeedSYVKRSQGRIPVKWMAIESLFDHI-YTTQS 932
Cdd:cd05606  103 YAAEVILGLEHMHNRFIVYRDLKPANILLDEHGHVRISDLGLACDF----SKKKPHASVGTHGYMAPEVLQKGVaYDSSA 178
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 10862703  933 DVWSFGVLLWEIVTlggnpypGIPPERLFNlLKTGHRMER---------PDNCSEEMYRLMLQCWKQEPDKR 995
Cdd:cd05606  179 DWFSLGCMLYKLLK-------GHSPFRQHK-TKDKHEIDRmtltmnvelPDSFSPELKSLLEGLLQRDVSKR 242
STKc_SHIK cd13974
Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs ...
865-1006 1.60e-03

Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SHIK, also referred to as STK40 or LYK4, is a cytoplasmic and nuclear protein that is involved in the negative regulation of NF-kappaB- and p53-mediated transcription. It was identified as a protein related to SINK, a p65-interacting protein that inhibits p65 phosphorylation by the catalytic subunit of PKA, thereby inhibiting transcriptional competence of NF-kappaB. The SHIK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270876 [Multi-domain]  Cd Length: 290  Bit Score: 42.01  E-value: 1.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  865 LAEMKLVHRDLAARNI-LVAEGRKMKISDFGLSRDVYEEDSYVKRSQGRiPVkWMAIESLFDHIYTTQ-SDVWSFGVLLW 942
Cdd:cd13974  148 LHKKNIVHRDLKLGNMvLNKRTRKITITNFCLGKHLVSEDDLLKDQRGS-PA-YISPDVLSGKPYLGKpSDMWALGVVLF 225
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 10862703  943 EIVtLGGNPYPGIPPERLFNLLKTG-HRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADISKDLE 1006
Cdd:cd13974  226 TML-YGQFPFYDSIPQELFRKIKAAeYTIPEDGRVSENTVCLIRKLLVLNPQKRLTASEVLDSLE 289
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
728-952 1.81e-03

Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. aPKCs only require phosphatidylserine (PS) for activation. They contain a C2-like region, instead of a calcium-binding (C2) region found in classical PKCs, in their regulatory domain. There are two aPKC isoforms, zeta and iota. aPKCs are involved in many cellular functions including proliferation, migration, apoptosis, polarity maintenance and cytoskeletal regulation. They also play a critical role in the regulation of glucose metabolism and in the pathogenesis of type 2 diabetes. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. The aPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270740 [Multi-domain]  Cd Length: 328  Bit Score: 41.64  E-value: 1.81e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  728 KTLGEGEFGKVVKATafHLKGRAGYTTVAVKmlKENASPSELRDLL-SEFNVLKQV-NHPHVIKLYGACSQDGPLLLIVE 805
Cdd:cd05588    1 RVIGRGSYAKVLMVE--LKKTKRIYAMKVIK--KELVNDDEDIDWVqTEKHVFETAsNHPFLVGLHSCFQTESRLFFVIE 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  806 YAKYGSLRGFLRESRKVgpgylgsggsrnsssldhPDERALTmgdlisFAWQISQGMQYLAEMKLVHRDLAARNILVAEG 885
Cdd:cd05588   77 FVNGGDLMFHMQRQRRL------------------PEEHARF------YSAEISLALNFLHEKGIIYRDLKLDNVLLDSE 132
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 10862703  886 RKMKISDFGLSRDVYEEDSYVKRSQGrIPvKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTlGGNPY 952
Cdd:cd05588  133 GHIKLTDYGMCKEGLRPGDTTSTFCG-TP-NYIAPEILRGEDYGFSVDWWALGVLMFEMLA-GRSPF 196
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
730-946 3.56e-03

Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Cdc7 kinase (or Hsk1 in fission yeast) is a critical regulator in the initiation of DNA replication. It forms a complex with a Dbf4-related regulatory subunit, a cyclin-like molecule that activates the kinase in late G1 phase, and is also referred to as Dbf4-dependent kinase (DDK). Its main targets are mini-chromosome maintenance (MCM) proteins. Cdc7 kinase may also have additional roles in meiosis, checkpoint responses, the maintenance and repair of chromosome structures, and cancer progression. The Cdc7 kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270921 [Multi-domain]  Cd Length: 252  Bit Score: 40.67  E-value: 3.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  730 LGEGEFGKVVKATA--FHLKGRAGYTTVAVKMLKENASPSELrdlLSEFNVLKQVN-HPHVIKLYGACSQDGPLLLIVEY 806
Cdd:cd14019    9 IGEGTFSSVYKAEDklHDLYDRNKGRLVALKHIYPTSSPSRI---LNELECLERLGgSNNVSGLITAFRNEDQVVAVLPY 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  807 AKYGSLRGFLREsrkvgpgylgsggsrnsssldhpderaLTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNILV-AEG 885
Cdd:cd14019   86 IEHDDFRDFYRK---------------------------MSLTDIRIYLRNLFKALKHVHSFGIIHRDVKPGNFLYnRET 138
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 10862703  886 RKMKISDFGLSRdvYEEDSYVKRS-----QG-RIPvkwmaiESLFDHIY-TTQSDVWSFGVLLWEIVT 946
Cdd:cd14019  139 GKGVLVDFGLAQ--REEDRPEQRApragtRGfRAP------EVLFKCPHqTTAIDIWSAGVILLSILS 198
STKc_PINK1 cd14018
Catalytic domain of the Serine/Threonine protein kinase, Pten INduced Kinase 1; STKs catalyze ...
857-996 5.00e-03

Catalytic domain of the Serine/Threonine protein kinase, Pten INduced Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PINK1 contains an N-terminal mitochondrial targeting sequence, a catalytic domain, and a C-terminal regulatory region. It plays an important role in maintaining mitochondrial homeostasis. It protects cells against oxidative stress-induced apoptosis by phosphorylating the chaperone TNFR-associated protein 1 (TRAP1), also called Hsp75. Phosphorylated TRAP1 prevents cytochrome c release and peroxide-induced apoptosis. PINK1 interacts with Omi/HtrA2, a serine protease, and Parkin, an E3 ubiquitin ligase, in different pathways to promote mitochondrial health. The parkin gene is the most commonly mutated gene in autosomal recessive familial parkinsonism. Mutations within the catalytic domain of PINK1 are also associated with Parkinson's disease. The PINK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270920 [Multi-domain]  Cd Length: 313  Bit Score: 40.56  E-value: 5.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  857 QISQGMQYLAEMKLVHRDLAARNILV----AEGRKMKISDFG--LSRDVYE-----EDSYVKR---SQGRIPVKWMAIES 922
Cdd:cd14018  146 QLLEGVDHLVRHGIAHRDLKSDNILLeldfDGCPWLVIADFGccLADDSIGlqlpfSSWYVDRggnACLMAPEVSTAVPG 225
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 10862703  923 LFDHIYTTQSDVWSFGVLLWEIVTLgGNPYPGIPPERLFNllkTGHRMER----PDNCSEEMYRLMLQCWKQEPDKRP 996
Cdd:cd14018  226 PGVVINYSKADAWAVGAIAYEIFGL-SNPFYGLGDTMLES---RSYQESQlpalPSAVPPDVRQVVKDLLQRDPNKRV 299
STKc_Bub1_BubR1 cd13981
Catalytic domain of the Serine/Threonine kinases, Spindle assembly checkpoint proteins Bub1 ...
728-898 5.16e-03

Catalytic domain of the Serine/Threonine kinases, Spindle assembly checkpoint proteins Bub1 and BubR1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Bub1 (Budding uninhibited by benzimidazoles 1), BubR1, and similar proteins. They contain an N-terminal Bub1/Mad3 homology domain essential for Cdc20 binding and a C-terminal kinase domain. Bub1 and BubR1 are involved in SAC, a surveillance system that delays metaphase to anaphase transition by blocking the activity of APC/C (the anaphase promoting complex) until all chromosomes achieve proper attachments to the mitotic spindle, to avoid chromosome missegregation. Impaired SAC leads to genomic instabilities and tumor development. Bub1 and BubR1 facilitate the localization of SAC proteins to kinetochores and regulate kinetochore-microtubule (K-MT) attachments. Repression studies of Bub1 and BubR1 show that they exert an additive effect in misalignment phenotypes and may function cooperatively or in parallel pathways in regulating K-MT attachments. The Bub1/BubR1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270883 [Multi-domain]  Cd Length: 298  Bit Score: 40.42  E-value: 5.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  728 KTLGEGEFGKVVKATafHLKGRAGYTTVAVKMLKEnASP------SELRDLLSEFNVLKQVNHPHVIKLYGACSqdgplL 801
Cdd:cd13981    6 KELGEGGYASVYLAK--DDDEQSDGSLVALKVEKP-PSIwefyicDQLHSRLKNSRLRESISGAHSAHLFQDES-----I 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10862703  802 LIVEYAKYGSLRGFLRESRKVGPGylgsggsrnsssldhPDERALTMgdliSFAWQISQGMQYLAEMKLVHRDLAARNIL 881
Cdd:cd13981   78 LVMDYSSQGTLLDVVNKMKNKTGG---------------GMDEPLAM----FFTIELLKVVEALHEVGIIHGDIKPDNFL 138
                        170       180       190
                 ....*....|....*....|....*....|..
gi 10862703  882 V---------------AEGRKMKISDFGLSRD 898
Cdd:cd13981  139 LrleicadwpgegengWLSKGLKLIDFGRSID 170
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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