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Conserved domains on  [gi|41349437|ref|NP_004320|]
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bone morphogenetic protein receptor type-1A isoform 3 precursor [Homo sapiens]

Protein Classification

bone morphogenetic protein receptor type-1A( domain architecture ID 19229609)

bone morphogenetic protein receptor type-1A is a receptor serine/threonine-protein kinase that catalyzes the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates; functions as a receptor for bone morphogenetic proteins (BMPs)

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
STKc_BMPR1a cd14220
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IA Receptor; ...
238-524 0e+00

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: 635.16  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 238 RQVGKGRYGEVWMGKWRGEKVAVKVFFTTEEASWFRETEIYQTVLMRHENILGFIAADIKGTGSWTQLYLITDYHENGSL 317
Cdd:cd14220   1 RQIGKGRYGEVWMGKWRGEKVAVKVFFTTEEASWFRETEIYQTVLMRHENILGFIAADIKGTGSWTQLYLITDYHENGSL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 318 YDFLKCATLDTRALLKLAYSAACGLCHLHTEIYGTQGKPAIAHRDLKSKNILIKKNGSCCIADLGLAVKFNSDTNEVDVP 397
Cdd:cd14220  81 YDFLKCTTLDTRALLKLAYSAACGLCHLHTEIYGTQGKPAIAHRDLKSKNILIKKNGTCCIADLGLAVKFNSDTNEVDVP 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 398 LNTRVGTKRYMAPEVLDESLNKNHFQPYIMADIYSFGLIIWEMARRCITGGIVEEYQLPYYNMVPSDPSYEDMREVVCVK 477
Cdd:cd14220 161 LNTRVGTKRYMAPEVLDESLNKNHFQAYIMADIYSFGLIIWEMARRCVTGGIVEEYQLPYYDMVPSDPSYEDMREVVCVK 240
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 41349437 478 RLRPIVSNRWNSDECLRAVLKLMSECWAHNPASRLTALRIKKTLAKM 524
Cdd:cd14220 241 RLRPTVSNRWNSDECLRAVLKLMSECWAHNPASRLTALRIKKTLAKM 287
TFP_LU_ECD_BMPR1A cd23612
extracellular domain (ECD) found in bone morphogenetic protein receptor type-1A (BMPR-1A) and ...
57-140 3.12e-60

extracellular domain (ECD) found in bone morphogenetic protein receptor type-1A (BMPR-1A) and similar proteins; BMPR-1A (EC 2.7.11.30, also called BMP type-1A receptor, or activin receptor-like kinase 3 (ALK-3), or serine/threonine-protein kinase receptor R5 (SKR5), or CD292) on ligand binding, forms a receptor complex consisting of two type II, and two type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators. BMPR-1A is the receptor for BMP2, BMP4, GDF5, and GDF6. It positively regulates chondrocyte differentiation through GDF5 interaction and mediates induction of adipogenesis by GDF6. This model corresponds to extracellular domain (ECD) of BMPR-1A, which belongs to Ly-6 antigen/uPA receptor-like (LU) superfamily and exhibits a snake toxin-like fold (also known as three-finger toxin/3FTx fold or three-fingered protein/TFP domain fold).


:

Pssm-ID: 467132  Cd Length: 84  Bit Score: 193.12  E-value: 3.12e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437  57 PFLKCYCSGHCPDDAINNTCITNGHCFAIIEEDDQGETTLASGCMKYEGSDFQCKDSPKAQLRRTIECCRTNLCNQYLQP 136
Cdd:cd23612   1 PFLKCYCSGHCPDDAINNTCITNGHCFAIIEEDDQGETTLASGCMKYEGSDFQCKDSPKAQLRRTIECCRTNLCNQYLQP 80

                ....
gi 41349437 137 TLPP 140
Cdd:cd23612  81 TLPP 84
TGF_beta_GS pfam08515
Transforming growth factor beta type I GS-motif; This motif is found in the transforming ...
205-232 6.04e-03

Transforming growth factor beta type I GS-motif; This motif is found in the transforming growth factor beta (TGF-beta) type I which regulates cell growth and differentiation. The name of the GS motif comes from its highly conserved GSGSGLP signature in the cytoplasmic juxtamembrane region immediately preceding the protein's kinase domain. Point mutations in the GS motif modify the signaling ability of the type I receptor.


:

Pssm-ID: 462503  Cd Length: 28  Bit Score: 34.49  E-value: 6.04e-03
                          10        20
                  ....*....|....*....|....*...
gi 41349437   205 SLKDLIDQSQSSGSGSGLPLLVQRTIAK 232
Cdd:pfam08515   1 TLKDLIDESCTSGSGSGLPLLVQRTIAR 28
 
Name Accession Description Interval E-value
STKc_BMPR1a cd14220
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IA Receptor; ...
238-524 0e+00

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: 635.16  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 238 RQVGKGRYGEVWMGKWRGEKVAVKVFFTTEEASWFRETEIYQTVLMRHENILGFIAADIKGTGSWTQLYLITDYHENGSL 317
Cdd:cd14220   1 RQIGKGRYGEVWMGKWRGEKVAVKVFFTTEEASWFRETEIYQTVLMRHENILGFIAADIKGTGSWTQLYLITDYHENGSL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 318 YDFLKCATLDTRALLKLAYSAACGLCHLHTEIYGTQGKPAIAHRDLKSKNILIKKNGSCCIADLGLAVKFNSDTNEVDVP 397
Cdd:cd14220  81 YDFLKCTTLDTRALLKLAYSAACGLCHLHTEIYGTQGKPAIAHRDLKSKNILIKKNGTCCIADLGLAVKFNSDTNEVDVP 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 398 LNTRVGTKRYMAPEVLDESLNKNHFQPYIMADIYSFGLIIWEMARRCITGGIVEEYQLPYYNMVPSDPSYEDMREVVCVK 477
Cdd:cd14220 161 LNTRVGTKRYMAPEVLDESLNKNHFQAYIMADIYSFGLIIWEMARRCVTGGIVEEYQLPYYDMVPSDPSYEDMREVVCVK 240
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 41349437 478 RLRPIVSNRWNSDECLRAVLKLMSECWAHNPASRLTALRIKKTLAKM 524
Cdd:cd14220 241 RLRPTVSNRWNSDECLRAVLKLMSECWAHNPASRLTALRIKKTLAKM 287
TFP_LU_ECD_BMPR1A cd23612
extracellular domain (ECD) found in bone morphogenetic protein receptor type-1A (BMPR-1A) and ...
57-140 3.12e-60

extracellular domain (ECD) found in bone morphogenetic protein receptor type-1A (BMPR-1A) and similar proteins; BMPR-1A (EC 2.7.11.30, also called BMP type-1A receptor, or activin receptor-like kinase 3 (ALK-3), or serine/threonine-protein kinase receptor R5 (SKR5), or CD292) on ligand binding, forms a receptor complex consisting of two type II, and two type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators. BMPR-1A is the receptor for BMP2, BMP4, GDF5, and GDF6. It positively regulates chondrocyte differentiation through GDF5 interaction and mediates induction of adipogenesis by GDF6. This model corresponds to extracellular domain (ECD) of BMPR-1A, which belongs to Ly-6 antigen/uPA receptor-like (LU) superfamily and exhibits a snake toxin-like fold (also known as three-finger toxin/3FTx fold or three-fingered protein/TFP domain fold).


Pssm-ID: 467132  Cd Length: 84  Bit Score: 193.12  E-value: 3.12e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437  57 PFLKCYCSGHCPDDAINNTCITNGHCFAIIEEDDQGETTLASGCMKYEGSDFQCKDSPKAQLRRTIECCRTNLCNQYLQP 136
Cdd:cd23612   1 PFLKCYCSGHCPDDAINNTCITNGHCFAIIEEDDQGETTLASGCMKYEGSDFQCKDSPKAQLRRTIECCRTNLCNQYLQP 80

                ....
gi 41349437 137 TLPP 140
Cdd:cd23612  81 TLPP 84
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
234-521 2.45e-43

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: 154.63  E-value: 2.45e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437    234 IQMVRQVGKGRYGEVWMGKWRG------EKVAVKVF----FTTEEASWFRETEIYQTvlMRHENILGFIAADIKGTgswt 303
Cdd:smart00221   1 LTLGKKLGEGAFGEVYKGTLKGkgdgkeVEVAVKTLkedaSEQQIEEFLREARIMRK--LDHPNIVKLLGVCTEEE---- 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437    304 QLYLITDYHENGSLYDFLK---CATLDTRALLKLAYSAACGLCHLHTeiygtqgKPAIaHRDLKSKNILIKKNGSCCIAD 380
Cdd:smart00221  75 PLMIVMEYMPGGDLLDYLRknrPKELSLSDLLSFALQIARGMEYLES-------KNFI-HRDLAARNCLVGENLVVKISD 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437    381 LGLAVKFNSDtnEVDVPLNTRVgTKRYMAPevldESLNKNHFqpYIMADIYSFGLIIWEMarrcITGGiveeyQLPYYNM 460
Cdd:smart00221 147 FGLSRDLYDD--DYYKVKGGKL-PIRWMAP----ESLKEGKF--TSKSDVWSFGVLLWEI----FTLG-----EEPYPGM 208
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41349437    461 VPsdpsyEDMREVVCVKRLRPIVSNrwnsdeCLRAVLKLMSECWAHNPASRLTALRIKKTL 521
Cdd:smart00221 209 SN-----AEVLEYLKKGYRLPKPPN------CPPELYKLMLQCWAEDPEDRPTFSELVEIL 258
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
234-521 2.37e-41

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: 149.18  E-value: 2.37e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437   234 IQMVRQVGKGRYGEVWMGKWRGE------KVAVKVF--FTTEE--ASWFRETEIYQTVlmRHENILGFIAADIKGTgswt 303
Cdd:pfam07714   1 LTLGEKLGEGAFGEVYKGTLKGEgentkiKVAVKTLkeGADEEerEDFLEEASIMKKL--DHPNIVKLLGVCTQGE---- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437   304 QLYLITDYHENGSLYDFLKC--ATLDTRALLKLAYSAACGLCHLHteiygtqGKPAIaHRDLKSKNILIKKNGSCCIADL 381
Cdd:pfam07714  75 PLYIVTEYMPGGDLLDFLRKhkRKLTLKDLLSMALQIAKGMEYLE-------SKNFV-HRDLAARNCLVSENLVVKISDF 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437   382 GLA-VKFNSDTNEVDVPLNTRVgtkRYMAPevldESLNKNHFqpYIMADIYSFGLIIWEMarrcITGGiveeyQLPYYNM 460
Cdd:pfam07714 147 GLSrDIYDDDYYRKRGGGKLPI---KWMAP----ESLKDGKF--TSKSDVWSFGVLLWEI----FTLG-----EQPYPGM 208
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41349437   461 VPSD--PSYEDMRevvcvkRL-RPivsnrwnsDECLRAVLKLMSECWAHNPASRLTALRIKKTL 521
Cdd:pfam07714 209 SNEEvlEFLEDGY------RLpQP--------ENCPDELYDLMKQCWAYDPEDRPTFSELVEDL 258
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
235-511 7.55e-26

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 110.49  E-value: 7.55e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 235 QMVRQVGKGRYGEVWMGKWR--GEKVAVKVFF-----TTEEASWF-RETEIYQTVlmRHENILGFIAADIKGTgswtQLY 306
Cdd:COG0515  10 RILRLLGRGGMGVVYLARDLrlGRPVALKVLRpelaaDPEARERFrREARALARL--NHPNIVRVYDVGEEDG----RPY 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 307 LITDYHENGSLYDFLK-CATLDTRALLKLAYSAACGLCHLHTeiygtQGkpaIAHRDLKSKNILIKKNGSCCIADLGLAV 385
Cdd:COG0515  84 LVMEYVEGESLADLLRrRGPLPPAEALRILAQLAEALAAAHA-----AG---IVHRDIKPANILLTPDGRVKLIDFGIAR 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 386 KFNSDTNEVDvplNTRVGTKRYMAPEVL-----DESlnknhfqpyimADIYSFGLIIWEMarrcITGgiveeyQLPYynm 460
Cdd:COG0515 156 ALGGATLTQT---GTVVGTPGYMAPEQArgepvDPR-----------SDVYSLGVTLYEL----LTG------RPPF--- 208
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 41349437 461 vPSDPSYEDMREVVCVKRLRPIVSNRWNSDECLRAVLKLMsecwAHNPASR 511
Cdd:COG0515 209 -DGDSPAELLRAHLREPPPPPSELRPDLPPALDAIVLRAL----AKDPEER 254
Activin_recp pfam01064
Activin types I and II receptor domain; This Pfam entry consists of both TGF-beta receptor ...
59-131 4.67e-17

Activin types I and II receptor domain; This Pfam entry consists of both TGF-beta receptor types. This is an alignment of the hydrophilic cysteine-rich ligand-binding domains, Both receptor types, (type I and II) posses a 9 amino acid cysteine box, with the the consensus CCX{4-5}CN. The type I receptors also possess 7 extracellular residues preceding the cysteine box.


Pssm-ID: 460048  Cd Length: 78  Bit Score: 76.00  E-value: 4.67e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41349437    59 LKCYCSGH-CPDDAINNTCITNGHCFAIIEEDDQGETTL-ASGCMKYEGSDFQCKDSPKAQLRRTIECCRTNLCN 131
Cdd:pfam01064   1 LKCYCNPLkCNDDNVNFTCETDGQCFSSWELDTDGFIECvKKGCLSPEDDPFECKTSNKPHSLYRIECCKTDFCN 75
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
233-439 7.79e-15

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 76.02  E-value: 7.79e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437  233 QIQMVRQVGKGRYGEVWMGKWR--GEKVAVKVFFTTEEAS----WFRETEIYQTVlmRHENILGfiAADIKGTGSWTQLY 306
Cdd:PLN00034  75 ELERVNRIGSGAGGTVYKVIHRptGRLYALKVIYGNHEDTvrrqICREIEILRDV--NHPNVVK--CHDMFDHNGEIQVL 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437  307 LitDYHENGSLyDFLKCAtlDTRALLKLAYSAACGLCHLHteiygtqgKPAIAHRDLKSKNILIKKNGSCCIADLGLAVK 386
Cdd:PLN00034 151 L--EFMDGGSL-EGTHIA--DEQFLADVARQILSGIAYLH--------RRHIVHRDIKPSNLLINSAKNVKIADFGVSRI 217
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 41349437  387 FNSDTNevdvPLNTRVGTKRYMAPEVLDESLNKNHFQPYiMADIYSFGLIIWE 439
Cdd:PLN00034 218 LAQTMD----PCNSSVGTIAYMSPERINTDLNHGAYDGY-AGDIWSLGVSILE 265
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
358-457 4.12e-06

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 49.41  E-value: 4.12e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437  358 IAHRDLKSKNILIKKNGSCCIADLGLAVKFNS----DTNEVdvplntrVGTKRYMAPE-----VLDESlnknhfqpyimA 428
Cdd:NF033483 128 IVHRDIKPQNILITKDGRVKVTDFGIARALSSttmtQTNSV-------LGTVHYLSPEqarggTVDAR-----------S 189
                         90       100
                 ....*....|....*....|....*....
gi 41349437  429 DIYSFGLIIWEMarrcITGgiveeyQLPY 457
Cdd:NF033483 190 DIYSLGIVLYEM----LTG------RPPF 208
TGF_beta_GS pfam08515
Transforming growth factor beta type I GS-motif; This motif is found in the transforming ...
205-232 6.04e-03

Transforming growth factor beta type I GS-motif; This motif is found in the transforming growth factor beta (TGF-beta) type I which regulates cell growth and differentiation. The name of the GS motif comes from its highly conserved GSGSGLP signature in the cytoplasmic juxtamembrane region immediately preceding the protein's kinase domain. Point mutations in the GS motif modify the signaling ability of the type I receptor.


Pssm-ID: 462503  Cd Length: 28  Bit Score: 34.49  E-value: 6.04e-03
                          10        20
                  ....*....|....*....|....*...
gi 41349437   205 SLKDLIDQSQSSGSGSGLPLLVQRTIAK 232
Cdd:pfam08515   1 TLKDLIDESCTSGSGSGLPLLVQRTIAR 28
 
Name Accession Description Interval E-value
STKc_BMPR1a cd14220
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IA Receptor; ...
238-524 0e+00

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: 635.16  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 238 RQVGKGRYGEVWMGKWRGEKVAVKVFFTTEEASWFRETEIYQTVLMRHENILGFIAADIKGTGSWTQLYLITDYHENGSL 317
Cdd:cd14220   1 RQIGKGRYGEVWMGKWRGEKVAVKVFFTTEEASWFRETEIYQTVLMRHENILGFIAADIKGTGSWTQLYLITDYHENGSL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 318 YDFLKCATLDTRALLKLAYSAACGLCHLHTEIYGTQGKPAIAHRDLKSKNILIKKNGSCCIADLGLAVKFNSDTNEVDVP 397
Cdd:cd14220  81 YDFLKCTTLDTRALLKLAYSAACGLCHLHTEIYGTQGKPAIAHRDLKSKNILIKKNGTCCIADLGLAVKFNSDTNEVDVP 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 398 LNTRVGTKRYMAPEVLDESLNKNHFQPYIMADIYSFGLIIWEMARRCITGGIVEEYQLPYYNMVPSDPSYEDMREVVCVK 477
Cdd:cd14220 161 LNTRVGTKRYMAPEVLDESLNKNHFQAYIMADIYSFGLIIWEMARRCVTGGIVEEYQLPYYDMVPSDPSYEDMREVVCVK 240
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 41349437 478 RLRPIVSNRWNSDECLRAVLKLMSECWAHNPASRLTALRIKKTLAKM 524
Cdd:cd14220 241 RLRPTVSNRWNSDECLRAVLKLMSECWAHNPASRLTALRIKKTLAKM 287
STKc_BMPR1 cd14144
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type I Receptor; ...
238-524 0e+00

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: 624.89  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 238 RQVGKGRYGEVWMGKWRGEKVAVKVFFTTEEASWFRETEIYQTVLMRHENILGFIAADIKGTGSWTQLYLITDYHENGSL 317
Cdd:cd14144   1 RSVGKGRYGEVWKGKWRGEKVAVKIFFTTEEASWFRETEIYQTVLMRHENILGFIAADIKGTGSWTQLYLITDYHENGSL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 318 YDFLKCATLDTRALLKLAYSAACGLCHLHTEIYGTQGKPAIAHRDLKSKNILIKKNGSCCIADLGLAVKFNSDTNEVDVP 397
Cdd:cd14144  81 YDFLRGNTLDTQSMLKLAYSAACGLAHLHTEIFGTQGKPAIAHRDIKSKNILVKKNGTCCIADLGLAVKFISETNEVDLP 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 398 LNTRVGTKRYMAPEVLDESLNKNHFQPYIMADIYSFGLIIWEMARRCITGGIVEEYQLPYYNMVPSDPSYEDMREVVCVK 477
Cdd:cd14144 161 PNTRVGTKRYMAPEVLDESLNRNHFDAYKMADMYSFGLVLWEIARRCISGGIVEEYQLPYYDAVPSDPSYEDMRRVVCVE 240
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 41349437 478 RLRPIVSNRWNSDECLRAVLKLMSECWAHNPASRLTALRIKKTLAKM 524
Cdd:cd14144 241 RRRPSIPNRWSSDEVLRTMSKLMSECWAHNPAARLTALRVKKTLGKL 287
STKc_BMPR1b cd14219
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IB; STKs ...
228-532 0e+00

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: 588.94  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 228 RTIAKQIQMVRQVGKGRYGEVWMGKWRGEKVAVKVFFTTEEASWFRETEIYQTVLMRHENILGFIAADIKGTGSWTQLYL 307
Cdd:cd14219   1 RTIAKQIQMVKQIGKGRYGEVWMGKWRGEKVAVKVFFTTEEASWFRETEIYQTVLMRHENILGFIAADIKGTGSWTQLYL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 308 ITDYHENGSLYDFLKCATLDTRALLKLAYSAACGLCHLHTEIYGTQGKPAIAHRDLKSKNILIKKNGSCCIADLGLAVKF 387
Cdd:cd14219  81 ITDYHENGSLYDYLKSTTLDTKAMLKLAYSSVSGLCHLHTEIFSTQGKPAIAHRDLKSKNILVKKNGTCCIADLGLAVKF 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 388 NSDTNEVDVPLNTRVGTKRYMAPEVLDESLNKNHFQPYIMADIYSFGLIIWEMARRCITGGIVEEYQLPYYNMVPSDPSY 467
Cdd:cd14219 161 ISDTNEVDIPPNTRVGTKRYMPPEVLDESLNRNHFQSYIMADMYSFGLILWEVARRCVSGGIVEEYQLPYHDLVPSDPSY 240
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41349437 468 EDMREVVCVKRLRPIVSNRWNSDECLRAVLKLMSECWAHNPASRLTALRIKKTLAKMVESQDVKI 532
Cdd:cd14219 241 EDMREIVCIKRLRPSFPNRWSSDECLRQMGKLMTECWAHNPASRLTALRVKKTLAKMSESQDIKL 305
STKc_TGFbR_I cd14056
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type ...
239-524 0e+00

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: 553.03  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 239 QVGKGRYGEVWMGKWRGEKVAVKVFFTTEEASWFRETEIYQTVLMRHENILGFIAADIKGTGSWTQLYLITDYHENGSLY 318
Cdd:cd14056   2 TIGKGRYGEVWLGKYRGEKVAVKIFSSRDEDSWFRETEIYQTVMLRHENILGFIAADIKSTGSWTQLWLITEYHEHGSLY 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 319 DFLKCATLDTRALLKLAYSAACGLCHLHTEIYGTQGKPAIAHRDLKSKNILIKKNGSCCIADLGLAVKFNSDTNEVDVPL 398
Cdd:cd14056  82 DYLQRNTLDTEEALRLAYSAASGLAHLHTEIVGTQGKPAIAHRDLKSKNILVKRDGTCCIADLGLAVRYDSDTNTIDIPP 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 399 NTRVGTKRYMAPEVLDESLNKNHFQPYIMADIYSFGLIIWEMARRCITGGIVEEYQLPYYNMVPSDPSYEDMREVVCVKR 478
Cdd:cd14056 162 NPRVGTKRYMAPEVLDDSINPKSFESFKMADIYSFGLVLWEIARRCEIGGIAEEYQLPYFGMVPSDPSFEEMRKVVCVEK 241
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 41349437 479 LRPIVSNRWNSDECLRAVLKLMSECWAHNPASRLTALRIKKTLAKM 524
Cdd:cd14056 242 LRPPIPNRWKSDPVLRSMVKLMQECWSENPHARLTALRVKKTLAKL 287
STKc_TGFbR1_ACVR1b_ACVR1c cd14143
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta Type I ...
240-524 0e+00

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: 512.37  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 240 VGKGRYGEVWMGKWRGEKVAVKVFFTTEEASWFRETEIYQTVLMRHENILGFIAADIKGTGSWTQLYLITDYHENGSLYD 319
Cdd:cd14143   3 IGKGRFGEVWRGRWRGEDVAVKIFSSREERSWFREAEIYQTVMLRHENILGFIAADNKDNGTWTQLWLVSDYHEHGSLFD 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 320 FLKCATLDTRALLKLAYSAACGLCHLHTEIYGTQGKPAIAHRDLKSKNILIKKNGSCCIADLGLAVKFNSDTNEVDVPLN 399
Cdd:cd14143  83 YLNRYTVTVEGMIKLALSIASGLAHLHMEIVGTQGKPAIAHRDLKSKNILVKKNGTCCIADLGLAVRHDSATDTIDIAPN 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 400 TRVGTKRYMAPEVLDESLNKNHFQPYIMADIYSFGLIIWEMARRCITGGIVEEYQLPYYNMVPSDPSYEDMREVVCVKRL 479
Cdd:cd14143 163 HRVGTKRYMAPEVLDDTINMKHFESFKRADIYALGLVFWEIARRCSIGGIHEDYQLPYYDLVPSDPSIEEMRKVVCEQKL 242
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 41349437 480 RPIVSNRWNSDECLRAVLKLMSECWAHNPASRLTALRIKKTLAKM 524
Cdd:cd14143 243 RPNIPNRWQSCEALRVMAKIMRECWYANGAARLTALRIKKTLSQL 287
STKc_ACVR1_ALK1 cd14142
Catalytic domain of the Serine/Threonine Kinases, Activin Type I Receptor and Activin ...
228-524 5.72e-179

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: 505.05  E-value: 5.72e-179
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 228 RTIAKQIQMVRQVGKGRYGEVWMGKWRGEKVAVKVFFTTEEASWFRETEIYQTVLMRHENILGFIAADIKGTGSWTQLYL 307
Cdd:cd14142   1 RTVARQITLVECIGKGRYGEVWRGQWQGESVAVKIFSSRDEKSWFRETEIYNTVLLRHENILGFIASDMTSRNSCTQLWL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 308 ITDYHENGSLYDFLKCATLDTRALLKLAYSAACGLCHLHTEIYGTQGKPAIAHRDLKSKNILIKKNGSCCIADLGLAVKF 387
Cdd:cd14142  81 ITHYHENGSLYDYLQRTTLDHQEMLRLALSAASGLVHLHTEIFGTQGKPAIAHRDLKSKNILVKSNGQCCIADLGLAVTH 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 388 NSDTNEVDVPLNTRVGTKRYMAPEVLDESLNKNHFQPYIMADIYSFGLIIWEMARRCITGGIVEEYQLPYYNMVPSDPSY 467
Cdd:cd14142 161 SQETNQLDVGNNPRVGTKRYMAPEVLDETINTDCFESYKRVDIYAFGLVLWEVARRCVSGGIVEEYKPPFYDVVPSDPSF 240
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 41349437 468 EDMREVVCVKRLRPIVSNRWNSDECLRAVLKLMSECWAHNPASRLTALRIKKTLAKM 524
Cdd:cd14142 241 EDMRKVVCVDQQRPNIPNRWSSDPTLTAMAKLMKECWYQNPSARLTALRIKKTLLKI 297
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
240-524 7.17e-155

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: 443.42  E-value: 7.17e-155
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 240 VGKGRYGEVWMGKWRGEKVAVKVFFTTEEASWFRETEIYQTVLMRHENILGFIAADIKGTGSWTQLYLITDYHENGSLYD 319
Cdd:cd13998   3 IGKGRFGEVWKASLKNEPVAVKIFSSRDKQSWFREKEIYRTPMLKHENILQFIAADERDTALRTELWLVTAFHPNGSL*D 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 320 FLKCATLDTRALLKLAYSAACGLCHLHTEIYG-TQGKPAIAHRDLKSKNILIKKNGSCCIADLGLAVKFNSDTNEVDVPL 398
Cdd:cd13998  83 YLSLHTIDWVSLCRLALSVARGLAHLHSEIPGcTQGKPAIAHRDLKSKNILVKNDGTCCIADFGLAVRLSPSTGEEDNAN 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 399 NTRVGTKRYMAPEVLDESLNKNHFQPYIMADIYSFGLIIWEMARRC-ITGGIVEEYQLPYYNMVPSDPSYEDMREVVCVK 477
Cdd:cd13998 163 NGQVGTKRYMAPEVLEGAINLRDFESFKRVDIYAMGLVLWEMASRCtDLFGIVEEYKPPFYSEVPNHPSFEDMQEVVVRD 242
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 41349437 478 RLRPIVSNRWNSDECLRAVLKLMSECWAHNPASRLTALRIKKTLAKM 524
Cdd:cd13998 243 KQRPNIPNRWLSHPGLQSLAETIEECWDHDAEARLTAQCIEERLSEF 289
STKc_ACVR2 cd14053
Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the ...
242-514 1.37e-106

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: 320.43  E-value: 1.37e-106
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 242 KGRYGEVWMGKWRGEKVAVKVFFTTEEASWFRETEIYQTVLMRHENILGFIAADIKGTGSWTQLYLITDYHENGSLYDFL 321
Cdd:cd14053   5 RGRFGAVWKAQYLNRLVAVKIFPLQEKQSWLTEREIYSLPGMKHENILQFIGAEKHGESLEAEYWLITEFHERGSLCDYL 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 322 KCATLDTRALLKLAYSAACGLCHLHTEIYGTQG--KPAIAHRDLKSKNILIKKNGSCCIADLGLAVKFNSDTNEVDvpLN 399
Cdd:cd14053  85 KGNVISWNELCKIAESMARGLAYLHEDIPATNGghKPSIAHRDFKSKNVLLKSDLTACIADFGLALKFEPGKSCGD--TH 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 400 TRVGTKRYMAPEVLDESLNknhFQP--YIMADIYSFGLIIWEMARRC-ITGGIVEEYQLPYYNMVPSDPSYEDMREVVCV 476
Cdd:cd14053 163 GQVGTRRYMAPEVLEGAIN---FTRdaFLRIDMYAMGLVLWELLSRCsVHDGPVDEYQLPFEEEVGQHPTLEDMQECVVH 239
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 41349437 477 KRLRPIVSNRWNSDECLRAVLKLMSECWAHNPASRLTA 514
Cdd:cd14053 240 KKLRPQIRDEWRKHPGLAQLCETIEECWDHDAEARLSA 277
STKc_TGFbR2_like cd14055
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II ...
239-514 1.24e-93

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: 287.35  E-value: 1.24e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 239 QVGKGRYGEVWMGKWRG------EKVAVKVFFTTEEASWFRETEIYQTVLMRHENILGFIAADIKGTGSWTQLYLITDYH 312
Cdd:cd14055   2 LVGKGRFAEVWKAKLKQnasgqyETVAVKIFPYEEYASWKNEKDIFTDASLKHENILQFLTAEERGVGLDRQYWLITAYH 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 313 ENGSLYDFLKCATLDTRALLKLAYSAACGLCHLHTEIYGtQGKP--AIAHRDLKSKNILIKKNGSCCIADLGLAVKFNSD 390
Cdd:cd14055  82 ENGSLQDYLTRHILSWEDLCKMAGSLARGLAHLHSDRTP-CGRPkiPIAHRDLKSSNILVKNDGTCVLADFGLALRLDPS 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 391 TNEVDVPLNTRVGTKRYMAPEVLDESLNKNHFQPYIMADIYSFGLIIWEMARRCITGGIVEEYQLPYYNMVPSDPSYEDM 470
Cdd:cd14055 161 LSVDELANSGQVGTARYMAPEALESRVNLEDLESFKQIDVYSMALVLWEMASRCEASGEVKPYELPFGSKVRERPCVESM 240
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 41349437 471 REVVCVKRLRPIVSNRWNSDECLRAVLKLMSECWAHNPASRLTA 514
Cdd:cd14055 241 KDLVLRDRGRPEIPDSWLTHQGMCVLCDTITECWDHDPEARLTA 284
STKc_BMPR2_AMHR2 cd14054
Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and ...
240-524 1.61e-85

Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and Anti-Muellerian Hormone Type II Receptors; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR2 and AMHR2 belong to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors (GDFs), and AMH, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. Type II receptors are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. BMPR2 and AMHR2 act primarily as a receptor for BMPs and AMH, respectively. BMPs induce bone and cartilage formation, as well as regulate tooth, kidney, skin, hair, haematopoietic, and neuronal development. Mutations in BMPR2A is associated with familial pulmonary arterial hypertension. AMH is mainly responsible for the regression of Mullerian ducts during male sex differentiation. It is expressed exclusively by somatic cells of the gonads. Mutations in either AMH or AMHR2 cause persistent Mullerian duct syndrome (PMDS), a rare form of male pseudohermaphroditism characterized by the presence of Mullerian derivatives (ovary and tubes) in otherwise normally masculine males. The BMPR2/AMHR2 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: 270956 [Multi-domain]  Cd Length: 300  Bit Score: 266.53  E-value: 1.61e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 240 VGKGRYGEVWMGKWRGEKVAVKVFFTTEEASWFRETEIYQTVLMRHENILGFIAADIKGTG-SWTQLYLITDYHENGSLY 318
Cdd:cd14054   3 IGQGRYGTVWKGSLDERPVAVKVFPARHRQNFQNEKDIYELPLMEHSNILRFIGADERPTAdGRMEYLLVLEYAPKGSLC 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 319 DFLKCATLDTRALLKLAYSAACGLCHLHTEIY-GTQGKPAIAHRDLKSKNILIKKNGSCCIADLGLAVKFNSDT------ 391
Cdd:cd14054  83 SYLRENTLDWMSSCRMALSLTRGLAYLHTDLRrGDQYKPAIAHRDLNSRNVLVKADGSCVICDFGLAMVLRGSSlvrgrp 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 392 NEVDVPLNTRVGTKRYMAPEVLDESLNKNHFQPYIM-ADIYSFGLIIWEMARRC---ITGGIVEEYQLPYYNMVPSDPSY 467
Cdd:cd14054 163 GAAENASISEVGTLRYMAPEVLEGAVNLRDCESALKqVDVYALGLVLWEIAMRCsdlYPGESVPPYQMPYEAELGNHPTF 242
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 41349437 468 EDMREVVCVKRLRPIVSNRWNS-DECLRAVLKLMSECWAHNPASRLTALRIKKTLAKM 524
Cdd:cd14054 243 EDMQLLVSREKARPKFPDAWKEnSLAVRSLKETIEDCWDQDAEARLTALCVEERLAEL 300
STKc_ACVR2a cd14141
Catalytic domain of the Serine/Threonine Kinase, Activin Type IIA Receptor; STKs catalyze the ...
241-524 2.45e-80

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: 253.04  E-value: 2.45e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 241 GKGRYGEVWMGKWRGEKVAVKVFFTTEEASWFRETEIYQTVLMRHENILGFIAADIKGTGSWTQLYLITDYHENGSLYDF 320
Cdd:cd14141   4 ARGRFGCVWKAQLLNEYVAVKIFPIQDKLSWQNEYEIYSLPGMKHENILQFIGAEKRGTNLDVDLWLITAFHEKGSLTDY 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 321 LKCATLDTRALLKLAYSAACGLCHLHTEIYGTQG--KPAIAHRDLKSKNILIKKNGSCCIADLGLAVKFNSDTNEVDVpl 398
Cdd:cd14141  84 LKANVVSWNELCHIAQTMARGLAYLHEDIPGLKDghKPAIAHRDIKSKNVLLKNNLTACIADFGLALKFEAGKSAGDT-- 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 399 NTRVGTKRYMAPEVLDESLNknhFQ--PYIMADIYSFGLIIWEMARRCITG-GIVEEYQLPYYNMVPSDPSYEDMREVVC 475
Cdd:cd14141 162 HGQVGTRRYMAPEVLEGAIN---FQrdAFLRIDMYAMGLVLWELASRCTASdGPVDEYMLPFEEEVGQHPSLEDMQEVVV 238
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 41349437 476 VKRLRPIVSNRWNSDECLRAVLKLMSECWAHNPASRLTALRIKKTLAKM 524
Cdd:cd14141 239 HKKKRPVLRECWQKHAGMAMLCETIEECWDHDAEARLSAGCVEERIIQM 287
STKc_ACVR2b cd14140
Catalytic domain of the Serine/Threonine Kinase, Activin Type IIB Receptor; STKs catalyze the ...
242-527 1.68e-76

Catalytic domain of the Serine/Threonine Kinase, Activin Type IIB Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ACVR2b (or ActRIIB) 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 ACVR2b 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: 271042 [Multi-domain]  Cd Length: 291  Bit Score: 243.01  E-value: 1.68e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 242 KGRYGEVWMGKWRGEKVAVKVFFTTEEASWFRETEIYQTVLMRHENILGFIAADIKGTGSWTQLYLITDYHENGSLYDFL 321
Cdd:cd14140   5 RGRFGCVWKAQLMNEYVAVKIFPIQDKQSWQSEREIFSTPGMKHENLLQFIAAEKRGSNLEMELWLITAFHDKGSLTDYL 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 322 KCATLDTRALLKLAYSAACGLCHLHTEIYGTQG---KPAIAHRDLKSKNILIKKNGSCCIADLGLAVKFNSDTNEVDVpl 398
Cdd:cd14140  85 KGNIVSWNELCHIAETMARGLSYLHEDVPRCKGeghKPAIAHRDFKSKNVLLKNDLTAVLADFGLAVRFEPGKPPGDT-- 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 399 NTRVGTKRYMAPEVLDESLNknhFQ--PYIMADIYSFGLIIWEMARRCITG-GIVEEYQLPYYNMVPSDPSYEDMREVVC 475
Cdd:cd14140 163 HGQVGTRRYMAPEVLEGAIN---FQrdSFLRIDMYAMGLVLWELVSRCKAAdGPVDEYMLPFEEEIGQHPSLEDLQEVVV 239
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 41349437 476 VKRLRPIVSNRWNSDECLRAVLKLMSECWAHNPASRLTALRIKKTLAKMVES 527
Cdd:cd14140 240 HKKMRPVFKDHWLKHPGLAQLCVTIEECWDHDAEARLSAGCVEERISQIRRS 291
TFP_LU_ECD_BMPR1A cd23612
extracellular domain (ECD) found in bone morphogenetic protein receptor type-1A (BMPR-1A) and ...
57-140 3.12e-60

extracellular domain (ECD) found in bone morphogenetic protein receptor type-1A (BMPR-1A) and similar proteins; BMPR-1A (EC 2.7.11.30, also called BMP type-1A receptor, or activin receptor-like kinase 3 (ALK-3), or serine/threonine-protein kinase receptor R5 (SKR5), or CD292) on ligand binding, forms a receptor complex consisting of two type II, and two type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators. BMPR-1A is the receptor for BMP2, BMP4, GDF5, and GDF6. It positively regulates chondrocyte differentiation through GDF5 interaction and mediates induction of adipogenesis by GDF6. This model corresponds to extracellular domain (ECD) of BMPR-1A, which belongs to Ly-6 antigen/uPA receptor-like (LU) superfamily and exhibits a snake toxin-like fold (also known as three-finger toxin/3FTx fold or three-fingered protein/TFP domain fold).


Pssm-ID: 467132  Cd Length: 84  Bit Score: 193.12  E-value: 3.12e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437  57 PFLKCYCSGHCPDDAINNTCITNGHCFAIIEEDDQGETTLASGCMKYEGSDFQCKDSPKAQLRRTIECCRTNLCNQYLQP 136
Cdd:cd23612   1 PFLKCYCSGHCPDDAINNTCITNGHCFAIIEEDDQGETTLASGCMKYEGSDFQCKDSPKAQLRRTIECCRTNLCNQYLQP 80

                ....
gi 41349437 137 TLPP 140
Cdd:cd23612  81 TLPP 84
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
240-511 1.60e-57

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: 191.98  E-value: 1.60e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 240 VGKGRYGEVWMGKWRGEKVAVKVF----FTTEEASWFREtEIYQTVLMRHENILGFIAADIKGTgswtQLYLITDYHENG 315
Cdd:cd13999   1 IGSGSFGEVYKGKWRGTDVAIKKLkvedDNDELLKEFRR-EVSILSKLRHPNIVQFIGACLSPP----PLCIVTEYMPGG 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 316 SLYDFLKCA--TLDTRALLKLAYSAACGLCHLHTeiygtqgkPAIAHRDLKSKNILIKKNGSCCIADLGLAVKFNSDTNE 393
Cdd:cd13999  76 SLYDLLHKKkiPLSWSLRLKIALDIARGMNYLHS--------PPIIHRDLKSLNILLDENFTVKIADFGLSRIKNSTTEK 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 394 vdvpLNTRVGTKRYMAPEVLDEslnknhfQPY-IMADIYSFGLIIWEMarrcITGgiveeyQLPYYNMVPSdpsyEDMRE 472
Cdd:cd13999 148 ----MTGVVGTPRWMAPEVLRG-------EPYtEKADVYSFGIVLWEL----LTG------EVPFKELSPI----QIAAA 202
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 41349437 473 VVCVKRLRPIVSNrwnsdeCLRAVLKLMSECWAHNPASR 511
Cdd:cd13999 203 VVQKGLRPPIPPD------CPPELSKLIKRCWNEDPEKR 235
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
234-521 2.45e-43

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: 154.63  E-value: 2.45e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437    234 IQMVRQVGKGRYGEVWMGKWRG------EKVAVKVF----FTTEEASWFRETEIYQTvlMRHENILGFIAADIKGTgswt 303
Cdd:smart00221   1 LTLGKKLGEGAFGEVYKGTLKGkgdgkeVEVAVKTLkedaSEQQIEEFLREARIMRK--LDHPNIVKLLGVCTEEE---- 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437    304 QLYLITDYHENGSLYDFLK---CATLDTRALLKLAYSAACGLCHLHTeiygtqgKPAIaHRDLKSKNILIKKNGSCCIAD 380
Cdd:smart00221  75 PLMIVMEYMPGGDLLDYLRknrPKELSLSDLLSFALQIARGMEYLES-------KNFI-HRDLAARNCLVGENLVVKISD 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437    381 LGLAVKFNSDtnEVDVPLNTRVgTKRYMAPevldESLNKNHFqpYIMADIYSFGLIIWEMarrcITGGiveeyQLPYYNM 460
Cdd:smart00221 147 FGLSRDLYDD--DYYKVKGGKL-PIRWMAP----ESLKEGKF--TSKSDVWSFGVLLWEI----FTLG-----EEPYPGM 208
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41349437    461 VPsdpsyEDMREVVCVKRLRPIVSNrwnsdeCLRAVLKLMSECWAHNPASRLTALRIKKTL 521
Cdd:smart00221 209 SN-----AEVLEYLKKGYRLPKPPN------CPPELYKLMLQCWAEDPEDRPTFSELVEIL 258
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
234-521 2.35e-42

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 151.91  E-value: 2.35e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437    234 IQMVRQVGKGRYGEVWMGKWRG------EKVAVKVF----FTTEEASWFRETEIYQTvlMRHENILGFIAADIKGTgswt 303
Cdd:smart00219   1 LTLGKKLGEGAFGEVYKGKLKGkggkkkVEVAVKTLkedaSEQQIEEFLREARIMRK--LDHPNVVKLLGVCTEEE---- 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437    304 QLYLITDYHENGSLYDFLKCA--TLDTRALLKLAYSAACGLCHLHTeiygtqgKPAIaHRDLKSKNILIKKNGSCCIADL 381
Cdd:smart00219  75 PLYIVMEYMEGGDLLSYLRKNrpKLSLSDLLSFALQIARGMEYLES-------KNFI-HRDLAARNCLVGENLVVKISDF 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437    382 GLAVKFNSDtnEVDVPLNTRVgTKRYMAPevldESLNKNHFqpYIMADIYSFGLIIWEMarrcITGGiveeyQLPYYNMV 461
Cdd:smart00219 147 GLSRDLYDD--DYYRKRGGKL-PIRWMAP----ESLKEGKF--TSKSDVWSFGVLLWEI----FTLG-----EQPYPGMS 208
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437    462 PsdpsyEDMREVVCVKRLRPIVSNrwnsdeCLRAVLKLMSECWAHNPASRLTALRIKKTL 521
Cdd:smart00219 209 N-----EEVLEYLKNGYRLPQPPN------CPPELYDLMLQCWAEDPEDRPTFSELVEIL 257
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
235-519 1.05e-41

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 149.99  E-value: 1.05e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437    235 QMVRQVGKGRYGEVWMGKWR--GEKVAVKV----FFTTEEASWFRETEIYQTVlmRHENILGFIAADIKGTgswtQLYLI 308
Cdd:smart00220   2 EILEKLGEGSFGKVYLARDKktGKLVAIKVikkkKIKKDRERILREIKILKKL--KHPNIVRLYDVFEDED----KLYLV 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437    309 TDYHENGSLYDFLK-CATLDTRALLKLAYSAACGLCHLHTeiygtQGkpaIAHRDLKSKNILIKKNGSCCIADLGLAVKF 387
Cdd:smart00220  76 MEYCEGGDLFDLLKkRGRLSEDEARFYLRQILSALEYLHS-----KG---IVHRDLKPENILLDEDGHVKLADFGLARQL 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437    388 NSDTNevdvpLNTRVGTKRYMAPEVLDEslnknhfQPYIMA-DIYSFGLIIWEMarrcITGgiveeyQLPYYNmvpsDPS 466
Cdd:smart00220 148 DPGEK-----LTTFVGTPEYMAPEVLLG-------KGYGKAvDIWSLGVILYEL----LTG------KPPFPG----DDQ 201
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 41349437    467 YEDMREVVCVKRLRPIVSNRWNSDECLRavlkLMSECWAHNPASRLTALRIKK 519
Cdd:smart00220 202 LLELFKKIGKPKPPFPPPEWDISPEAKD----LIRKLLVKDPEKRLTAEEALQ 250
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
234-521 2.37e-41

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: 149.18  E-value: 2.37e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437   234 IQMVRQVGKGRYGEVWMGKWRGE------KVAVKVF--FTTEE--ASWFRETEIYQTVlmRHENILGFIAADIKGTgswt 303
Cdd:pfam07714   1 LTLGEKLGEGAFGEVYKGTLKGEgentkiKVAVKTLkeGADEEerEDFLEEASIMKKL--DHPNIVKLLGVCTQGE---- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437   304 QLYLITDYHENGSLYDFLKC--ATLDTRALLKLAYSAACGLCHLHteiygtqGKPAIaHRDLKSKNILIKKNGSCCIADL 381
Cdd:pfam07714  75 PLYIVTEYMPGGDLLDFLRKhkRKLTLKDLLSMALQIAKGMEYLE-------SKNFV-HRDLAARNCLVSENLVVKISDF 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437   382 GLA-VKFNSDTNEVDVPLNTRVgtkRYMAPevldESLNKNHFqpYIMADIYSFGLIIWEMarrcITGGiveeyQLPYYNM 460
Cdd:pfam07714 147 GLSrDIYDDDYYRKRGGGKLPI---KWMAP----ESLKDGKF--TSKSDVWSFGVLLWEI----FTLG-----EQPYPGM 208
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41349437   461 VPSD--PSYEDMRevvcvkRL-RPivsnrwnsDECLRAVLKLMSECWAHNPASRLTALRIKKTL 521
Cdd:pfam07714 209 SNEEvlEFLEDGY------RLpQP--------ENCPDELYDLMKQCWAYDPEDRPTFSELVEDL 258
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
241-440 3.87e-36

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: 133.94  E-value: 3.87e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 241 GKGRYGEVWMGKWR--GEKVAVKVF----FTTEEASWFRETEIYQtvLMRHENILGFIAADIKGTgswtQLYLITDYHEN 314
Cdd:cd00180   2 GKGSFGKVYKARDKetGKKVAVKVIpkekLKKLLEELLREIEILK--KLNHPNIVKLYDVFETEN----FLYLVMEYCEG 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 315 GSLYDFLK--CATLDTRALLKLAYSAACGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNGSCCIADLGLAVKFNSDTN 392
Cdd:cd00180  76 GSLKDLLKenKGPLSEEEALSILRQLLSALEYLHSN--------GIIHRDLKPENILLDSDGTVKLADFGLAKDLDSDDS 147
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 41349437 393 EVDVplNTRVGTKRYMAPEVLDeslnknhfQPYIM--ADIYSFGLIIWEM 440
Cdd:cd00180 148 LLKT--TGGTTPPYYAPPELLG--------GRYYGpkVDIWSLGVILYEL 187
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
238-519 3.69e-35

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: 132.66  E-value: 3.69e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 238 RQVGKGRYGEVWMGKWRGEK-----VAVKV---FFTTEEASWF-RETEIYQTVlmRHENILGFIAADIKGTgswtQLYLI 308
Cdd:cd00192   1 KKLGEGAFGEVYKGKLKGGDgktvdVAVKTlkeDASESERKDFlKEARVMKKL--GHPNVVRLLGVCTEEE----PLYLV 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 309 TDYHENGSLYDFLK----------CATLDTRALLKLAYSAACGLCHLHteiygtqgKPAIAHRDLKSKNILIKKNGSCCI 378
Cdd:cd00192  75 MEYMEGGDLLDFLRksrpvfpspePSTLSLKDLLSFAIQIAKGMEYLA--------SKKFVHRDLAARNCLVGEDLVVKI 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 379 ADLGLAVKFNSDTNEVdvplnTRVGTK---RYMAPevldESLNKNHFQpyIMADIYSFGLIIWEmarrCITGGiveeyQL 455
Cdd:cd00192 147 SDFGLSRDIYDDDYYR-----KKTGGKlpiRWMAP----ESLKDGIFT--SKSDVWSFGVLLWE----IFTLG-----AT 206
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41349437 456 PYYNMvpsdpSYEDMREVVCV-KRL-RPivsnrwnsDECLRAVLKLMSECWAHNPASRLTALRIKK 519
Cdd:cd00192 207 PYPGL-----SNEEVLEYLRKgYRLpKP--------ENCPDELYELMLSCWQLDPEDRPTFSELVE 259
TFP_LU_ECD_BMPR1B cd23613
extracellular domain (ECD) found in bone morphogenetic protein receptor type-1B (BMPR-1B) and ...
59-141 3.17e-34

extracellular domain (ECD) found in bone morphogenetic protein receptor type-1B (BMPR-1B) and similar proteins; BMPR-1B (EC 2.7.11.30, also called BMP type-1B receptor, or CDw293, or activin receptor-like kinase 6 (ALK-6)) on ligand binding forms a receptor complex consisting of two type II and two type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators. BMPR-1B is the receptor for BMP7/OP-1 and GDF5. It positively regulates chondrocyte differentiation through GDF5 interaction. This model corresponds to extracellular domain (ECD) of BMPR-1B, which belongs to Ly-6 antigen/uPA receptor-like (LU) superfamily and exhibits a snake toxin-like fold (also known as three-finger toxin/3FTx fold or three-fingered protein/TFP domain fold).


Pssm-ID: 467133  Cd Length: 86  Bit Score: 124.17  E-value: 3.17e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437  59 LKCYCSGHCPDDAINNTCITNGHCFAIIEEDDQGETTLASGCMKYEGSDFQCKDSPKAQLRRTIECCR-TNLCNQYLQPT 137
Cdd:cd23613   3 LRCHCHHHCPEDSVNNTCRTDGYCFTMIEEDESGVPVVTSGCLGLEGSDFQCRDTPIPHQRRSIECCTdQDYCNKDLHPT 82

                ....
gi 41349437 138 LPPV 141
Cdd:cd23613  83 LPPL 86
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
240-526 1.22e-31

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: 123.15  E-value: 1.22e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 240 VGKGRYGEVWMGKWRGEK-VAVKVFFTTEEASWFRE--TEIYQTVLMRHENI---LGFIAAdiKGTGSwtqlyLITDYHE 313
Cdd:cd14066   1 IGSGGFGTVYKGVLENGTvVAVKRLNEMNCAASKKEflTELEMLGRLRHPNLvrlLGYCLE--SDEKL-----LVYEYMP 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 314 NGSLYDFLKCAT----LDTRALLKLAYSAACGLCHLHTEiygtqGKPAIAHRDLKSKNILIKKNGSCCIADLGLAVKFNS 389
Cdd:cd14066  74 NGSLEDRLHCHKgsppLPWPQRLKIAKGIARGLEYLHEE-----CPPPIIHGDIKSSNILLDEDFEPKLTDFGLARLIPP 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 390 DTNEVDVPLNTrvGTKRYMAPEvldeslnknhfqpYI-------MADIYSFGLIIWEMarrcITGgiveeyQLPYYNmVP 462
Cdd:cd14066 149 SESVSKTSAVK--GTIGYLAPE-------------YIrtgrvstKSDVYSFGVVLLEL----LTG------KPAVDE-NR 202
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41349437 463 SDPSYEDMREVV-------CVKRLRP-IVSNRWNSDECLRAVLKLMSECWAHNPASRLTAlrikKTLAKMVE 526
Cdd:cd14066 203 ENASRKDLVEWVeskgkeeLEDILDKrLVDDDGVEEEEVEALLRLALLCTRSDPSLRPSM----KEVVQMLE 270
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
240-514 1.73e-31

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: 122.49  E-value: 1.73e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 240 VGKGRYGEVWMGKWRGEKVAVKVFFTTEEASWFRET---EIYQTVLmRHENILGFIAAdIKGTGSWTQLYLITDYHENGS 316
Cdd:cd13979  11 LGSGGFGSVYKATYKGETVAVKIVRRRRKNRASRQSfwaELNAARL-RHENIVRVLAA-ETGTDFASLGLIIMEYCGNGT 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 317 LYDFLKCATLDTRALLKLAYSA--ACGLCHLHTeiygtQGkpaIAHRDLKSKNILIKKNGSCCIADLGLAVKFNsDTNEV 394
Cdd:cd13979  89 LQQLIYEGSEPLPLAHRILISLdiARALRFCHS-----HG---IVHLDVKPANILISEQGVCKLCDFGCSVKLG-EGNEV 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 395 DVPLNTRVGTKRYMAPEVLDESLnknhfqPYIMADIYSFGLIIWEMARRcitggiveeyQLPyynmvpsdpsYEDMREV- 473
Cdd:cd13979 160 GTPRSHIGGTYTYRAPELLKGER------VTPKADIYSFGITLWQMLTR----------ELP----------YAGLRQHv 213
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 41349437 474 ---VCVKRLRPIVSNRWNSDECLRAvLKLMSECWAHNPASRLTA 514
Cdd:cd13979 214 lyaVVAKDLRPDLSGLEDSEFGQRL-RSLISRCWSAQPAERPNA 256
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
237-514 3.19e-31

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: 121.54  E-value: 3.19e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 237 VRQVGKGRYGEVWMGKWR--GEKVAVKVFFTTEEASW---FRETEIYQTvlMRHENILGFIAADIKGTgswtQLYLITDY 311
Cdd:cd05122   5 LEKIGKGGFGVVYKARHKktGQIVAIKKINLESKEKKesiLNEIAILKK--CKHPNIVKYYGSYLKKD----ELWIVMEF 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 312 HENGSLYDFLK--CATLD-------TRALLKlaysaacGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNGSCCIADLG 382
Cdd:cd05122  79 CSGGSLKDLLKntNKTLTeqqiayvCKEVLK-------GLEYLHSH--------GIIHRDIKAANILLTSDGEVKLIDFG 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 383 LAVKFNSDTnevdvPLNTRVGTKRYMAPEVLDeslNKNHFQPyimADIYSFGLIIWEMARRcitggiveeyQLPYYNMVP 462
Cdd:cd05122 144 LSAQLSDGK-----TRNTFVGTPYWMAPEVIQ---GKPYGFK---ADIWSLGITAIEMAEG----------KPPYSELPP 202
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 41349437 463 sdpsyedMREVVCVKRLRPIVS-NRWNSDECLRAVLKLmseCWAHNPASRLTA 514
Cdd:cd05122 203 -------MKALFLIATNGPPGLrNPKKWSKEFKDFLKK---CLQKDPEKRPTA 245
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
232-522 3.24e-31

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: 121.30  E-value: 3.24e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 232 KQIQMVRQVGKGRYGEVWMGKWRGEKVAVKVF--FTTEEASWFRETEIYQTvlMRHENILGFIAADIKGTGswtqLYLIT 309
Cdd:cd05039   6 KDLKLGELIGKGEFGDVMLGDYRGQKVAVKCLkdDSTAAQAFLAEASVMTT--LRHPNLVQLLGVVLEGNG----LYIVT 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 310 DYHENGSLYDFLKC---ATLDTRALLKLAYSAACGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNGSCCIADLGLAVK 386
Cdd:cd05039  80 EYMAKGSLVDYLRSrgrAVITRKDQLGFALDVCEGMEYLESK--------KFVHRDLAARNVLVSEDNVAKVSDFGLAKE 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 387 FNSDTNEVDVPLntrvgtkRYMAPEVLDESLNKNhfqpyiMADIYSFGLIIWEmarrcitggIVEEYQLPYynmvPSDPS 466
Cdd:cd05039 152 ASSNQDGGKLPI-------KWTAPEALREKKFST------KSDVWSFGILLWE---------IYSFGRVPY----PRIPL 205
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 41349437 467 YEDMREVVCVKRLRPivsnrwnSDECLRAVLKLMSECWAHNPASRLTALRIKKTLA 522
Cdd:cd05039 206 KDVVPHVEKGYRMEA-------PEGCPPEVYKVMKNCWELDPAKRPTFKQLREKLE 254
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
240-527 5.12e-31

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: 121.00  E-value: 5.12e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 240 VGKGRYGEVWMGKWRGEKVAVKVFFTTEEASWFrETEIYQTVLMRHENILGFIAADIKGtgswTQLYLITDYHENGSLYD 319
Cdd:cd14058   1 VGRGSFGVVCKARWRNQIVAVKIIESESEKKAF-EVEVRQLSRVDHPNIIKLYGACSNQ----KPVCLVMEYAEGGSLYN 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 320 FLKCATldtralLKLAYSAA--------C--GLCHLHteiyGTQGKPAIaHRDLKSKNILIKKNGSCC-IADLGLAVKF- 387
Cdd:cd14058  76 VLHGKE------PKPIYTAAhamswalqCakGVAYLH----SMKPKALI-HRDLKPPNLLLTNGGTVLkICDFGTACDIs 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 388 NSDTNEvdvplntrVGTKRYMAPEVLDESLNKNHfqpyimADIYSFGLIIWEMARRcitggiveeyQLPYYNMvpSDPSY 467
Cdd:cd14058 145 THMTNN--------KGSAAWMAPEVFEGSKYSEK------CDVFSWGIILWEVITR----------RKPFDHI--GGPAF 198
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 468 EDMREVVCVKRLrPIVSNrwnsdeCLRAVLKLMSECWAHNPASRLTALRIKKTLAKMVES 527
Cdd:cd14058 199 RIMWAVHNGERP-PLIKN------CPKPIESLMTRCWSKDPEKRPSMKEIVKIMSHLMQF 251
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
238-513 1.07e-29

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: 117.00  E-value: 1.07e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 238 RQVGKGRYGEVWMGKWRGE-KVAVKVF--FTTEEASWFRETEIYQTVlmRHENILGFIAADIKGTgswtQLYLITDYHEN 314
Cdd:cd05034   1 KKLGAGQFGEVWMGVWNGTtKVAVKTLkpGTMSPEAFLQEAQIMKKL--RHDKLVQLYAVCSDEE----PIYIVTELMSK 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 315 GSLYDFLKCAT---LDTRALLKLAYSAACGLCHLHTEIYgtqgkpaiAHRDLKSKNILIKKNGSCCIADLGLAVKFNSDT 391
Cdd:cd05034  75 GSLLDYLRTGEgraLRLPQLIDMAAQIASGMAYLESRNY--------IHRDLAARNILVGENNVCKVADFGLARLIEDDE 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 392 nevdvpLNTRVGTK---RYMAPevldESLNKNHFQpyIMADIYSFGLIIWEMarrcITGGiveeyQLPYYNMvpsdPSYE 468
Cdd:cd05034 147 ------YTAREGAKfpiKWTAP----EAALYGRFT--IKSDVWSFGILLYEI----VTYG-----RVPYPGM----TNRE 201
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 41349437 469 DMREVVCVKRLrPIVSNrwnsdeCLRAVLKLMSECWAHNPASRLT 513
Cdd:cd05034 202 VLEQVERGYRM-PKPPG------CPDELYDIMLQCWKKEPEERPT 239
TFP_LU_ECD_BMPR1 cd23532
extracellular domain (ECD) found in the family of bone morphogenetic protein receptor type-1 ...
59-140 8.46e-28

extracellular domain (ECD) found in the family of bone morphogenetic protein receptor type-1 (BMPR1); The BMPR1 family includes BMPR-1A (also known as activin receptor-like kinase 3/ALK-3, or serine/threonine-protein kinase receptor R5/SKR5, or CD292) and BMPR-1B (also known as activin receptor-like kinase 6/ALK-6, or CDw293). They form a receptor complex consisting of two type II and two type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators. BMPR-1A is the receptor for BMP2, BMP4, GDF5, and GDF6. It positively regulates chondrocyte differentiation through GDF5 interaction and mediates induction of adipogenesis by GDF6. BMPR-1B is the receptor for BMP7/OP-1 and GDF5. It positively regulates chondrocyte differentiation through GDF5 interaction. Members in this family contain an extracellular domain (ECD), which belongs to Ly-6 antigen/uPA receptor-like (LU) superfamily and exhibits a snake toxin-like fold (also known as three-finger toxin/3FTx fold or three-fingered protein/TFP domain fold).


Pssm-ID: 467062  Cd Length: 90  Bit Score: 106.66  E-value: 8.46e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437  59 LKCYCSGHCPDDAINNTCIT--NGHCFAIIEEDDQG---ETTLASGCMKY-EGSDFQCKDSPKA-QLRRTIECCR-TNLC 130
Cdd:cd23532   1 LRCYCNPHCPDGAVNNTCTTkpGGKCFAAIEEVEDGgekEEEVTYGCLPPeESGILQCKGHLVPhLIPKSIECCNdSDLC 80
                        90
                ....*....|
gi 41349437 131 NQYLQPTLPP 140
Cdd:cd23532  81 NDDLNPTLPE 90
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
232-521 2.90e-27

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: 110.46  E-value: 2.90e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 232 KQIQMVRQVGKGRYGEVWMGKWRGEKVAVKVFFTTEEASWFRETEIYQTVLmRHENILGFIAADIKGTGSwtqLYLITDY 311
Cdd:cd05082   6 KELKLLQTIGKGEFGDVMLGDYRGNKVAVKCIKNDATAQAFLAEASVMTQL-RHSNLVQLLGVIVEEKGG---LYIVTEY 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 312 HENGSLYDFLKC---ATLDTRALLKLAYSAACGLCHLHTEIYgtqgkpaiAHRDLKSKNILIKKNGSCCIADLGLAVKFN 388
Cdd:cd05082  82 MAKGSLVDYLRSrgrSVLGGDCLLKFSLDVCEAMEYLEGNNF--------VHRDLAARNVLVSEDNVAKVSDFGLTKEAS 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 389 SDTNEVDVPLntrvgtkRYMAPEVLDESLNKNHfqpyimADIYSFGLIIWEmarrcitggIVEEYQLPYynmvPSDPsye 468
Cdd:cd05082 154 STQDTGKLPV-------KWTAPEALREKKFSTK------SDVWSFGILLWE---------IYSFGRVPY----PRIP--- 204
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 41349437 469 dMREVVcvkrlrPIVSNRWNSDE---CLRAVLKLMSECWAHNPASRLTALRIKKTL 521
Cdd:cd05082 205 -LKDVV------PRVEKGYKMDApdgCPPAVYDVMKNCWHLDAAMRPSFLQLREQL 253
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
232-513 5.84e-27

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: 109.80  E-value: 5.84e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 232 KQIQMVRQVGKGRYGEVWMGKWRGE-KVAVKVFF--TTEEASWFRETEIYQTvlMRHENILGFIAADIKGTgswtQLYLI 308
Cdd:cd05068   8 KSLKLLRKLGSGQFGEVWEGLWNNTtPVAVKTLKpgTMDPEDFLREAQIMKK--LRHPKLIQLYAVCTLEE----PIYII 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 309 TDYHENGSLYDFL--KCATLDTRALLKLAYSAACGLCHLHTEIYgtqgkpaiAHRDLKSKNILIKKNGSCCIADLGLAVK 386
Cdd:cd05068  82 TELMKHGSLLEYLqgKGRSLQLPQLIDMAAQVASGMAYLESQNY--------IHRDLAARNVLVGENNICKVADFGLARV 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 387 FnsdtnEVDVPLNTRVGTK---RYMAPevldESLNKNHFQpyIMADIYSFGLIIWEMarrcITGGiveeyQLPYYNMvps 463
Cdd:cd05068 154 I-----KVEDEYEAREGAKfpiKWTAP----EAANYNRFS--IKSDVWSFGILLTEI----VTYG-----RIPYPGM--- 210
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 41349437 464 dPSYEDMREVVCVKRLrPIVSNrwnsdeCLRAVLKLMSECWAHNPASRLT 513
Cdd:cd05068 211 -TNAEVLQQVERGYRM-PCPPN------CPPQLYDIMLECWKADPMERPT 252
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
233-514 8.48e-27

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: 109.15  E-value: 8.48e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 233 QIQMVRQVGKGRYGEVWMG--KWRGEKVAVK-VFFT--TEEASWF--RETEIYQTvlMRHENILGFIAADIKGTgswtQL 305
Cdd:cd06606   1 RWKKGELLGKGSFGSVYLAlnLDTGELMAVKeVELSgdSEEELEAleREIRILSS--LKHPNIVRYLGTERTEN----TL 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 306 YLITDYHENGSLYDFL-KCATLD-------TRALLklaysaaCGLCHLHTeiygtQGkpaIAHRDLKSKNILIKKNGSCC 377
Cdd:cd06606  75 NIFLEYVPGGSLASLLkKFGKLPepvvrkyTRQIL-------EGLEYLHS-----NG---IVHRDIKGANILVDSDGVVK 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 378 IADLGLAVKFNSdtNEVDVPLNTRVGTKRYMAPEVLDeslNKNHFQPyimADIYSFGLIIWEMArrciTGgiveeyQLPY 457
Cdd:cd06606 140 LADFGCAKRLAE--IATGEGTKSLRGTPYWMAPEVIR---GEGYGRA---ADIWSLGCTVIEMA----TG------KPPW 201
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 41349437 458 YNMvpsDPSYEDMREVVCVKRLRPIVSnrWNSDECLRAVLKlmseCWAHNPASRLTA 514
Cdd:cd06606 202 SEL---GNPVAALFKIGSSGEPPPIPE--HLSEEAKDFLRK----CLQRDPKKRPTA 249
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
233-514 8.70e-27

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: 108.85  E-value: 8.70e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 233 QIQMVRQVGKGRYGEVWMG-KWR-GEKVAVKVFFTTEEASWFRET---EIYQTVLMRHENILGFIAAdikgTGSWTQLYL 307
Cdd:cd06627   1 NYQLGDLIGRGAFGSVYKGlNLNtGEFVAIKQISLEKIPKSDLKSvmgEIDLLKKLNHPNIVKYIGS----VKTKDSLYI 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 308 ITDYHENGSLYDFLK---------CATLDTRALLKLAYsaacglchLHTeiygtQGkpaIAHRDLKSKNILIKKNGSCCI 378
Cdd:cd06627  77 ILEYVENGSLASIIKkfgkfpeslVAVYIYQVLEGLAY--------LHE-----QG---VIHRDIKGANILTTKDGLVKL 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 379 ADLGLAVKfnsdTNEVDVPLNTRVGTKRYMAPEVLDESlnknhfQPYIMADIYSFGLIIWEMarrcITGgiveeyQLPYY 458
Cdd:cd06627 141 ADFGVATK----LNEVEKDENSVVGTPYWMAPEVIEMS------GVTTASDIWSVGCTVIEL----LTG------NPPYY 200
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 41349437 459 NMVPsdpsyedMREVVCVKRLR--PIVSNrwNSDEClravLKLMSECWAHNPASRLTA 514
Cdd:cd06627 201 DLQP-------MAALFRIVQDDhpPLPEN--ISPEL----RDFLLQCFQKDPTLRPSA 245
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
241-524 1.93e-26

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: 107.74  E-value: 1.93e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 241 GKGRYGEVWMGKW--RGEKVAVKVFFTTEeaswfRETEIYQtvLMRHENILGFIAADIKGTgswtQLYLITDYHENGSLY 318
Cdd:cd14060   2 GGGSFGSVYRAIWvsQDKEVAVKKLLKIE-----KEAEILS--VLSHRNIIQFYGAILEAP----NYGIVTEYASYGSLF 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 319 DFLKCA---TLDTRALLKLAYSAACGLCHLHTEiygtqGKPAIAHRDLKSKNILIKKNGSCCIADLGlAVKFNSDTNEVd 395
Cdd:cd14060  71 DYLNSNeseEMDMDQIMTWATDIAKGMHYLHME-----APVKVIHRDLKSRNVVIAADGVLKICDFG-ASRFHSHTTHM- 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 396 vplnTRVGTKRYMAPEVLdESLNKNHfqpyiMADIYSFGLIIWEMARRCITGGIVEEYQLPYynmvpsdpsyedmreVVC 475
Cdd:cd14060 144 ----SLVGTFPWMAPEVI-QSLPVSE-----TCDTYSYGVVLWEMLTREVPFKGLEGLQVAW---------------LVV 198
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 41349437 476 VKRLRPIVsnrwnSDECLRAVLKLMSECWAHNPASRLTALRIKKTLAKM 524
Cdd:cd14060 199 EKNERPTI-----PSSCPRSFAELMRRCWEADVKERPSFKQIIGILESM 242
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
236-519 2.46e-26

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: 107.60  E-value: 2.46e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 236 MVRQVGKGRYGEVWMGKWR--GEKVAVKV-----FFTTEEASWFRETEIYQtvLMRHENILGFIaaDIKGTGswTQLYLI 308
Cdd:cd14003   4 LGKTLGEGSFGKVKLARHKltGEKVAIKIidkskLKEEIEEKIKREIEIMK--LLNHPNIIKLY--EVIETE--NKIYLV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 309 TDYHENGSLYDFLkcatldtRALLKLAYSAAC--------GLCHLHTeiygtQGkpaIAHRDLKSKNILIKKNGSCCIAD 380
Cdd:cd14003  78 MEYASGGELFDYI-------VNNGRLSEDEARrffqqlisAVDYCHS-----NG---IVHRDLKLENILLDKNGNLKIID 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 381 LGLAVKFNSDTnevdvPLNTRVGTKRYMAPEVLDEslnknhfQPYI--MADIYSFGLIIWEMarrcITGgiveeyQLPYy 458
Cdd:cd14003 143 FGLSNEFRGGS-----LLKTFCGTPAYAAPEVLLG-------RKYDgpKADVWSLGVILYAM----LTG------YLPF- 199
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41349437 459 nmvpSDPSYEDMREVVCVKRLRPivsNRWNSDEClRAVLKLMSEcwaHNPASRLTALRIKK 519
Cdd:cd14003 200 ----DDDNDSKLFRKILKGKYPI---PSHLSPDA-RDLIRRMLV---VDPSKRITIEEILN 249
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
234-521 2.48e-26

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: 108.05  E-value: 2.48e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 234 IQMVRQVGKGRYGEVWMGKWRG-EKVAVKVFF--TTEEASWFRETEIYQTvlMRHENILGFIAADIKgtgswTQLYLITD 310
Cdd:cd05067   9 LKLVERLGAGQFGEVWMGYYNGhTKVAIKSLKqgSMSPDAFLAEANLMKQ--LQHQRLVRLYAVVTQ-----EPIYIITE 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 311 YHENGSLYDFLKCAT---LDTRALLKLAYSAACGLCHLHTEIYgtqgkpaiAHRDLKSKNILIKKNGSCCIADLGLA--V 385
Cdd:cd05067  82 YMENGSLVDFLKTPSgikLTINKLLDMAAQIAEGMAFIEERNY--------IHRDLRAANILVSDTLSCKIADFGLArlI 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 386 KFNSDTnevdvplnTRVGTK---RYMAPevldESLNKNHFQpyIMADIYSFGLIIWEmarrcitggIVEEYQLPYYNMvp 462
Cdd:cd05067 154 EDNEYT--------AREGAKfpiKWTAP----EAINYGTFT--IKSDVWSFGILLTE---------IVTHGRIPYPGM-- 208
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 463 SDPsyEDMREVVCVKRL-RPivsnrwnsDECLRAVLKLMSECWAHNPASRLTALRIKKTL 521
Cdd:cd05067 209 TNP--EVIQNLERGYRMpRP--------DNCPEELYQLMRLCWKERPEDRPTFEYLRSVL 258
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
235-511 7.55e-26

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 110.49  E-value: 7.55e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 235 QMVRQVGKGRYGEVWMGKWR--GEKVAVKVFF-----TTEEASWF-RETEIYQTVlmRHENILGFIAADIKGTgswtQLY 306
Cdd:COG0515  10 RILRLLGRGGMGVVYLARDLrlGRPVALKVLRpelaaDPEARERFrREARALARL--NHPNIVRVYDVGEEDG----RPY 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 307 LITDYHENGSLYDFLK-CATLDTRALLKLAYSAACGLCHLHTeiygtQGkpaIAHRDLKSKNILIKKNGSCCIADLGLAV 385
Cdd:COG0515  84 LVMEYVEGESLADLLRrRGPLPPAEALRILAQLAEALAAAHA-----AG---IVHRDIKPANILLTPDGRVKLIDFGIAR 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 386 KFNSDTNEVDvplNTRVGTKRYMAPEVL-----DESlnknhfqpyimADIYSFGLIIWEMarrcITGgiveeyQLPYynm 460
Cdd:COG0515 156 ALGGATLTQT---GTVVGTPGYMAPEQArgepvDPR-----------SDVYSLGVTLYEL----LTG------RPPF--- 208
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 41349437 461 vPSDPSYEDMREVVCVKRLRPIVSNRWNSDECLRAVLKLMsecwAHNPASR 511
Cdd:COG0515 209 -DGDSPAELLRAHLREPPPPPSELRPDLPPALDAIVLRAL----AKDPEER 254
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
235-520 2.64e-25

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: 104.77  E-value: 2.64e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 235 QMVRQVGKGRYGEVWMGKWR--GEKVAVK---VFFTT--EEASWFRETEIyQTVLMRHENILGFIAadikgtgSWTQ--- 304
Cdd:cd13997   3 HELEQIGSGSFSEVFKVRSKvdGCLYAVKkskKPFRGpkERARALREVEA-HAALGQHPNIVRYYS-------SWEEggh 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 305 LYLITDYHENGSLYDFLKCATLDTRA----LLKLAYSAACGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNGSCCIAD 380
Cdd:cd13997  75 LYIQMELCENGSLQDALEELSPISKLseaeVWDLLLQVALGLAFIHSK--------GIVHLDIKPDNIFISNKGTCKIGD 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 381 LGLAVKfnsdtneVDVPLNTRVGTKRYMAPEVLDEslNKNHFQPyimADIYSFGLIIWEMArrciTGgiveeyqlpyYNM 460
Cdd:cd13997 147 FGLATR-------LETSGDVEEGDSRYLAPELLNE--NYTHLPK---ADIFSLGVTVYEAA----TG----------EPL 200
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 461 VPSDPSYEDMREVVCVKRLRPIVSNRwnsdecLRAVLKLMSEcwaHNPASRLTALRIKKT 520
Cdd:cd13997 201 PRNGQQWQQLRQGKLPLPPGLVLSQE------LTRLLKVMLD---PDPTRRPTADQLLAH 251
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
240-515 1.88e-24

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: 102.53  E-value: 1.88e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 240 VGKGRYGEV---WMGKWRGEkVAVKVF-----FTTEEASWFRETEIYQTvlMRHENILgfiaaDIKGTGSWTQLY-LITD 310
Cdd:cd13978   1 LGSGGFGTVskaRHVSWFGM-VAIKCLhsspnCIEERKALLKEAEKMER--ARHSYVL-----PLLGVCVERRSLgLVME 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 311 YHENGSLYDFLKCATLDTRALLK--LAYSAACGLCHLHTEiygtqgKPAIAHRDLKSKNILIKKNGSCCIADLGLAvKFN 388
Cdd:cd13978  73 YMENGSLKSLLEREIQDVPWSLRfrIIHEIALGMNFLHNM------DPPLLHHDLKPENILLDNHFHVKISDFGLS-KLG 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 389 SDTNEVDVPLNTR--VGTKRYMAPEVLDESLNKnhfqPYIMADIYSFGLIIWEMarrcITGgiveeyQLPYYNmvpSDPS 466
Cdd:cd13978 146 MKSISANRRRGTEnlGGTPIYMAPEAFDDFNKK----PTSKSDVYSFAIVIWAV----LTR------KEPFEN---AINP 208
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 41349437 467 YEDMREVvcVKRLRPIVS--NRWNSDECLRAVLKLMSECWAHNPASRLTAL 515
Cdd:cd13978 209 LLIMQIV--SKGDRPSLDdiGRLKQIENVQELISLMIRCWDGNPDARPTFL 257
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
240-524 2.31e-24

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: 102.09  E-value: 2.31e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 240 VGKGRYGEVWMGKWRGEKVAVKVF-------FTTEEASWFRETEIYQtvLMRHENILGFIAADIKGtgswTQLYLITDYH 312
Cdd:cd14061   2 IGVGGFGKVYRGIWRGEEVAVKAArqdpdedISVTLENVRQEARLFW--MLRHPNIIALRGVCLQP----PNLCLVMEYA 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 313 ENGSLYDFLKCATLDTRALLKLAYSAACGLCHLHTEiygtqGKPAIAHRDLKSKNILIKK--------NGSCCIADLGLA 384
Cdd:cd14061  76 RGGALNRVLAGRKIPPHVLVDWAIQIARGMNYLHNE-----APVPIIHRDLKSSNILILEaienedleNKTLKITDFGLA 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 385 VKFNSdtnevdvplNTRV---GTKRYMAPEVLDESL-NKNhfqpyimADIYSFGLIIWEMarrcITGgiveeyQLPYYNM 460
Cdd:cd14061 151 REWHK---------TTRMsaaGTYAWMAPEVIKSSTfSKA-------SDVWSYGVLLWEL----LTG------EVPYKGI 204
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41349437 461 VPSDPSYEdmrevVCVKRLR-PIVSnrwnsdECLRAVLKLMSECWAHNPASRLTALRIKKTLAKM 524
Cdd:cd14061 205 DGLAVAYG-----VAVNKLTlPIPS------TCPEPFAQLMKDCWQPDPHDRPSFADILKQLENI 258
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
232-518 3.74e-24

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: 101.74  E-value: 3.74e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 232 KQIQMVRQVGKGRYGEVWMGKWRGE-KVAVKVFfTTEEASWFRE--TEIYQTVLMRHENILGFIAADIKGTgswtQLYLI 308
Cdd:cd05148   6 EEFTLERKLGSGYFGEVWEGLWKNRvRVAIKIL-KSDDLLKQQDfqKEVQALKRLRHKHLISLFAVCSVGE----PVYII 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 309 TDYHENGSLYDFLKCA---TLDTRALLKLAYSAACGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNGSCCIADLGLAV 385
Cdd:cd05148  81 TELMEKGSLLAFLRSPegqVLPVASLIDMACQVAEGMAYLEEQ--------NSIHRDLAARNILVGEDLVCKVADFGLAR 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 386 KFNSDtneVDVPLNTRVGTKrYMAPevldESLNKNHFQpyIMADIYSFGLIIWEMARRcitGGIveeyqlPYYNMVpsdp 465
Cdd:cd05148 153 LIKED---VYLSSDKKIPYK-WTAP----EAASHGTFS--TKSDVWSFGILLYEMFTY---GQV------PYPGMN---- 209
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 41349437 466 SYEDMREVVCVKRL-RPIvsnrwnsdECLRAVLKLMSECWAHNPASRLT--ALRIK 518
Cdd:cd05148 210 NHEVYDQITAGYRMpCPA--------KCPQEIYKIMLECWAAEPEDRPSfkALREE 257
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
232-511 4.23e-24

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: 102.07  E-value: 4.23e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 232 KQIQMVRQVGKGRYGEVWMGKW------RGEKVAVKVFFT-TEEAS---WFRETEIYQTvlMRHENILGFIA-ADIKGTG 300
Cdd:cd05038   4 RHLKFIKQLGEGHFGSVELCRYdplgdnTGEQVAVKSLQPsGEEQHmsdFKREIEILRT--LDHEYIVKYKGvCESPGRR 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 301 SwtqLYLITDYHENGSLYDFLK--CATLDTRALLKLAYSAACGLCHLHTEIYgtqgkpaiAHRDLKSKNILIKKNGSCCI 378
Cdd:cd05038  82 S---LRLIMEYLPSGSLRDYLQrhRDQIDLKRLLLFASQICKGMEYLGSQRY--------IHRDLAARNILVESEDLVKI 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 379 ADLGLAVKFNSD------TNEVDVPLntrvgtkRYMAPevldESLNKNHFqpYIMADIYSFGLIIWEMARRCitggivEE 452
Cdd:cd05038 151 SDFGLAKVLPEDkeyyyvKEPGESPI-------FWYAP----ECLRESRF--SSASDVWSFGVTLYELFTYG------DP 211
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41349437 453 YQLPYYN-MVPSDPSYEDMREVVCVKRLRPivSNRWNS-DECLRAVLKLMSECWAHNPASR 511
Cdd:cd05038 212 SQSPPALfLRMIGIAQGQMIVTRLLELLKS--GERLPRpPSCPDEVYDLMKECWEYEPQDR 270
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
240-521 6.62e-24

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: 100.83  E-value: 6.62e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 240 VGKGRYGEVWMGKWRGEKVAVK---------VFFTTEEASwfRETEIYqtVLMRHENILGFIAADIKGtgswTQLYLITD 310
Cdd:cd14148   2 IGVGGFGKVYKGLWRGEEVAVKaarqdpdedIAVTAENVR--QEARLF--WMLQHPNIIALRGVCLNP----PHLCLVME 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 311 YHENGSLYDFLKCATLDTRALLKLAYSAACGLCHLHTEIYgtqgkPAIAHRDLKSKNILI-----KKNGSCC---IADLG 382
Cdd:cd14148  74 YARGGALNRALAGKKVPPHVLVNWAVQIARGMNYLHNEAI-----VPIIHRDLKSSNILIlepieNDDLSGKtlkITDFG 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 383 LAVKFNSDTNEvdvplnTRVGTKRYMAPEVLDESLNKNHfqpyimADIYSFGLIIWEMarrcITGgiveeyQLPYYNMVP 462
Cdd:cd14148 149 LAREWHKTTKM------SAAGTYAWMAPEVIRLSLFSKS------SDVWSFGVLLWEL----LTG------EVPYREIDA 206
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 41349437 463 SDPSYedmrEVVCVKRLRPIVSNrwnsdeCLRAVLKLMSECWAHNPASRLTALRIKKTL 521
Cdd:cd14148 207 LAVAY----GVAMNKLTLPIPST------CPEPFARLLEECWDPDPHGRPDFGSILKRL 255
PK_GC cd13992
Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows ...
251-524 1.03e-23

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: 100.54  E-value: 1.03e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 251 GKWRGEKVAVKVFFTTEEASWFRETEIYQTVLMRHENILGFIAADIKGTgswtQLYLITDYHENGSLYDFL--KCATLDT 328
Cdd:cd13992  21 GVYGGRTVAIKHITFSRTEKRTILQELNQLKELVHDNLNKFIGICINPP----NIAVVTEYCTRGSLQDVLlnREIKMDW 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 329 RALLKLAYSAACGLCHLHteiygtqGKPAIAHRDLKSKNILIKKNGSCCIADLGLAvKFNSDTNEVDVPLNTRVGTKRYM 408
Cdd:cd13992  97 MFKSSFIKDIVKGMNYLH-------SSSIGYHGRLKSSNCLVDSRWVVKLTDFGLR-NLLEEQTNHQLDEDAQHKKLLWT 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 409 APEVLDESLNKNhfQPYIMADIYSFGLIIWEMArrcitggiveEYQLPYYNMVPSDPSYEDMREVVCVKRLRPIVSnrwn 488
Cdd:cd13992 169 APELLRGSLLEV--RGTQKGDVYSFAIILYEIL----------FRSDPFALEREVAIVEKVISGGNKPFRPELAVL---- 232
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 41349437 489 SDECLRAVLKLMSECWAHNPASRLTALRIKKTLAKM 524
Cdd:cd13992 233 LDEFPPRLVLLVKQCWAENPEKRPSFKQIKKTLTEN 268
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
237-514 1.14e-23

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: 100.35  E-value: 1.14e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 237 VRQVGKGRYGEVWMG--KWRGEKVAVKV----FFTTEEA-SWF-RETEIYQTVlmRHENILGFIAADIKGTgswtQLYLI 308
Cdd:cd14014   5 VRLLGRGGMGEVYRArdTLLGRPVAIKVlrpeLAEDEEFrERFlREARALARL--SHPNIVRVYDVGEDDG----RPYIV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 309 TDYHENGSLYDFLK-CATLDTRALLKLAYSAACGLCHLHTeiygtQGkpaIAHRDLKSKNILIKKNGSCCIADLGLAVKF 387
Cdd:cd14014  79 MEYVEGGSLADLLReRGPLPPREALRILAQIADALAAAHR-----AG---IVHRDIKPANILLTEDGRVKLTDFGIARAL 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 388 NSDTNEVDvplNTRVGTKRYMAPEVLDESlnknhfQPYIMADIYSFGLIIWEMarrcITGgiveeyQLPYynmvPSDPSY 467
Cdd:cd14014 151 GDSGLTQT---GSVLGTPAYMAPEQARGG------PVDPRSDIYSLGVVLYEL----LTG------RPPF----DGDSPA 207
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 41349437 468 EDMREVVCVKRLRPIVSNrwnsDECLRAVLKLMSECWAHNPASRLTA 514
Cdd:cd14014 208 AVLAKHLQEAPPPPSPLN----PDVPPALDAIILRALAKDPEERPQS 250
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
233-503 2.24e-23

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: 99.71  E-value: 2.24e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 233 QIQMVRQVGKGRYGEVWMGKWRGEkVAVKVFF----TTEEASWFR-ETEIYQTVlmRHENILGFIaadikGTGSWTQLYL 307
Cdd:cd14150   1 EVSMLKRIGTGSFGTVFRGKWHGD-VAVKILKvtepTPEQLQAFKnEMQVLRKT--RHVNILLFM-----GFMTRPNFAI 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 308 ITDYHENGSLYDFLKCAT--LDTRALLKLAYSAACGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNGSCCIADLGLA- 384
Cdd:cd14150  73 ITQWCEGSSLYRHLHVTEtrFDTMQLIDVARQTAQGMDYLHAK--------NIIHRDLKSNNIFLHEGLTVKIGDFGLAt 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 385 VKFN-SDTNEVDVPlntrVGTKRYMAPEVLD-ESLNKNHFQpyimADIYSFGLIIWEMarrcITGgiveeyQLPYYNMVP 462
Cdd:cd14150 145 VKTRwSGSQQVEQP----SGSILWMAPEVIRmQDTNPYSFQ----SDVYAYGVVLYEL----MSG------TLPYSNINN 206
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 41349437 463 SDpsyedmREVVCVKR--LRPIVSNRWNSdeCLRAVLKLMSEC 503
Cdd:cd14150 207 RD------QIIFMVGRgyLSPDLSKLSSN--CPKAMKRLLIDC 241
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
232-513 2.34e-23

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: 99.73  E-value: 2.34e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 232 KQIQMVRQVGKGRYGEVWMGKWRGE-KVAVKVFF--TTEEASWFRETEIYQTvlMRHENILGFIAADIKGtgswTQLYLI 308
Cdd:cd05072   7 ESIKLVKKLGAGQFGEVWMGYYNNStKVAVKTLKpgTMSVQAFLEEANLMKT--LQHDKLVRLYAVVTKE----EPIYII 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 309 TDYHENGSLYDFLKCATLDTRALLKLA-YSA--ACGLCHLHTEIYgtqgkpaiAHRDLKSKNILIKKNGSCCIADLGLAV 385
Cdd:cd05072  81 TEYMAKGSLLDFLKSDEGGKVLLPKLIdFSAqiAEGMAYIERKNY--------IHRDLRAANVLVSESLMCKIADFGLAR 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 386 KFNSDTnevdvpLNTRVGTK---RYMAPevldESLNKNHFQpyIMADIYSFGLIIWEMarrcITGGiveeyQLPYYNMVP 462
Cdd:cd05072 153 VIEDNE------YTAREGAKfpiKWTAP----EAINFGSFT--IKSDVWSFGILLYEI----VTYG-----KIPYPGMSN 211
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 41349437 463 SDPsyedMREVVCVKRLrPIVSNrwnsdeCLRAVLKLMSECWAHNPASRLT 513
Cdd:cd05072 212 SDV----MSALQRGYRM-PRMEN------CPDELYDIMKTCWKEKAEERPT 251
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
237-514 2.98e-23

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: 99.95  E-value: 2.98e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 237 VRQVGKGRYGEVWMGKWR--GEKVAVKVFFTTEEASWF-----RETEIYQtvLMRHENILGFI-----AADIKGTGSwtq 304
Cdd:cd07840   4 IAQIGEGTYGQVYKARNKktGELVALKKIRMENEKEGFpitaiREIKLLQ--KLDHPNVVRLKeivtsKGSAKYKGS--- 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 305 LYLITDYHE---NGSL----YDF----LKCATldtRALLKlaysaacGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKN 373
Cdd:cd07840  79 IYMVFEYMDhdlTGLLdnpeVKFtesqIKCYM---KQLLE-------GLQYLHSN--------GILHRDIKGSNILINND 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 374 GSCCIADLGLAVKFNSDTNEvdvPLNTRVGTKRYMAPEVLdesLNKNHFQPYImaDIYSFGLIIWEMARR---------- 443
Cdd:cd07840 141 GVLKLADFGLARPYTKENNA---DYTNRVITLWYRPPELL---LGATRYGPEV--DMWSVGCILAELFTGkpifqgktel 212
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 444 ----CIT---GGIVEEY-----QLPYYNMVPSDPSYEDmrevvcvkRLRPIVSNRWNsdeclRAVLKLMSECWAHNPASR 511
Cdd:cd07840 213 eqleKIFelcGSPTEENwpgvsDLPWFENLKPKKPYKR--------RLREVFKNVID-----PSALDLLDKLLTLDPKKR 279

                ...
gi 41349437 512 LTA 514
Cdd:cd07840 280 ISA 282
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
240-522 4.41e-23

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: 98.37  E-value: 4.41e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 240 VGKGRYGEVWMGKWRGEKVAVK-----VFFTTEEASWF-RETEIYQTvlMRHENILGFIAADIKGTgswTQLYLITDYHE 313
Cdd:cd14064   1 IGSGSFGKVYKGRCRNKIVAIKryranTYCSKSDVDMFcREVSILCR--LNHPCVIQFVGACLDDP---SQFAIVTQYVS 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 314 NGSLYDFL--KCATLDTRALLKLAYSAACGLCHLHTeiygtQGKPAIaHRDLKSKNILIKKNGSCCIADLGLA--VKFNS 389
Cdd:cd14064  76 GGSLFSLLheQKRVIDLQSKLIIAVDVAKGMEYLHN-----LTQPII-HRDLNSHNILLYEDGHAVVADFGESrfLQSLD 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 390 DTNEVDVPlntrvGTKRYMAPEVLDESLnknhfQPYIMADIYSFGLIIWEMarrcITGgiveeyQLPYYNMVPSDPSYEd 469
Cdd:cd14064 150 EDNMTKQP-----GNLRWMAPEVFTQCT-----RYSIKADVFSYALCLWEL----LTG------EIPFAHLKPAAAAAD- 208
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 41349437 470 mrevVCVKRLRPIVSNRWNsdeclRAVLKLMSECWAHNPASRLTALRIKKTLA 522
Cdd:cd14064 209 ----MAYHHIRPPIGYSIP-----KPISSLLMRGWNAEPESRPSFVEIVALLE 252
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
240-511 1.23e-22

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: 97.08  E-value: 1.23e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 240 VGKGRYGEVWMGKWRGEkVAVKVFF----TTEEASWFReTEIyqTVL--MRHENILGFIAADIKgtgswTQLYLITDYHE 313
Cdd:cd14062   1 IGSGSFGTVYKGRWHGD-VAVKKLNvtdpTPSQLQAFK-NEV--AVLrkTRHVNILLFMGYMTK-----PQLAIVTQWCE 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 314 NGSLYDFLKcaTLDTR----ALLKLAYSAACGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNGSCCIADLGLA-VKFN 388
Cdd:cd14062  72 GSSLYKHLH--VLETKfemlQLIDIARQTAQGMDYLHAK--------NIIHRDLKSNNIFLHEDLTVKIGDFGLAtVKTR 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 389 SDTNEvdvPLNTRVGTKRYMAPEVLD-ESLNKNHFQpyimADIYSFGLIIWEMarrcITGgiveeyQLPYYNMVPSDpsy 467
Cdd:cd14062 142 WSGSQ---QFEQPTGSILWMAPEVIRmQDENPYSFQ----SDVYAFGIVLYEL----LTG------QLPYSHINNRD--- 201
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 41349437 468 edmREVVCVKR--LRPIVSNRwnSDECLRAVLKLMSECWAHNPASR 511
Cdd:cd14062 202 ---QILFMVGRgyLRPDLSKV--RSDTPKALRRLMEDCIKFQRDER 242
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
239-462 1.64e-22

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: 96.90  E-value: 1.64e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 239 QVGKGRYGEVWMGKWR--GEKVAVKVFFTTEEAswfRETEIYQTVLMR---HENILGFIAADIKGTgswtQLYLITDYHE 313
Cdd:cd06614   7 KIGEGASGEVYKATDRatGKEVAIKKMRLRKQN---KELIINEILIMKeckHPNIVDYYDSYLVGD----ELWVVMEYMD 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 314 NGSLYDFLKCATLD---------TRALLKlaysaacGLCHLHTeiygtQGkpaIAHRDLKSKNILIKKNGSCCIADLGLA 384
Cdd:cd06614  80 GGSLTDIITQNPVRmnesqiayvCREVLQ-------GLEYLHS-----QN---VIHRDIKSDNILLSKDGSVKLADFGFA 144
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41349437 385 VKFNSDTNEvdvpLNTRVGTKRYMAPEVLDEslnknhfQPYIM-ADIYSFGLIIWEMArrcitggiveEYQLPYYNMVP 462
Cdd:cd06614 145 AQLTKEKSK----RNSVVGTPYWMAPEVIKR-------KDYGPkVDIWSLGIMCIEMA----------EGEPPYLEEPP 202
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
235-443 2.99e-22

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: 95.76  E-value: 2.99e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 235 QMVRQVGKGRYGEVWMGKWR--GEKVAVKVFFTTEEASWF--RETEIYQ--TVLMRHENILGFIaaDIKGTGSWTQLYLI 308
Cdd:cd05118   2 EVLRKIGEGAFGTVWLARDKvtGEKVAIKKIKNDFRHPKAalREIKLLKhlNDVEGHPNIVKLL--DVFEHRGGNHLCLV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 309 TDY-HENgsLYDFLKCA--TLDTRALLKLAYSAACGLCHLHteiygtqgKPAIAHRDLKSKNILIK-KNGSCCIADLGLA 384
Cdd:cd05118  80 FELmGMN--LYELIKDYprGLPLDLIKSYLYQLLQALDFLH--------SNGIIHRDLKPENILINlELGQLKLADFGLA 149
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 385 VKFNSDtnevdvPLNTRVGTKRYMAPEVLDESlnknhfQPYIMA-DIYSFGLIIWEMARR 443
Cdd:cd05118 150 RSFTSP------PYTPYVATRWYRAPEVLLGA------KPYGSSiDIWSLGCILAELLTG 197
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
232-524 5.62e-22

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: 95.33  E-value: 5.62e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 232 KQIQMVRQVGKGRYGEVWMGKWRGEKVAVKVFFTTEEASWFREtEIYQTVLMRHENILGFIAADIKgtgswTQLYLITDY 311
Cdd:cd05083   6 QKLTLGEIIGEGEFGAVLQGEYMGQKVAVKNIKCDVTAQAFLE-ETAVMTKLQHKNLVRLLGVILH-----NGLYIVMEL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 312 HENGSLYDFLKC---ATLDTRALLKLAYSAACGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNGSCCIADLGLAvkfN 388
Cdd:cd05083  80 MSKGNLVNFLRSrgrALVPVIQLLQFSLDVAEGMEYLESK--------KLVHRDLAARNILVSEDGVAKISDFGLA---K 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 389 SDTNEVDvplNTRVGTKrYMAPEVLdeslnkNHFQPYIMADIYSFGLIIWEmarrcitggIVEEYQLPYYNMvpsdpsye 468
Cdd:cd05083 149 VGSMGVD---NSRLPVK-WTAPEAL------KNKKFSSKSDVWSYGVLLWE---------VFSYGRAPYPKM-------- 201
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 469 DMREVV-CVK---RLRPivsnrwnSDECLRAVLKLMSECWAHNPASRLTALRIKKTLAKM 524
Cdd:cd05083 202 SVKEVKeAVEkgyRMEP-------PEGCPPDVYSIMTSCWEAEPGKRPSFKKLREKLEKE 254
Pkinase pfam00069
Protein kinase domain;
237-519 6.07e-22

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 94.23  E-value: 6.07e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437   237 VRQVGKGRYGEVWMGK--WRGEKVAVKVFFTTEEASWFRET---EIYQTVLMRHENILGFIaaDIKGTGSWtqLYLITDY 311
Cdd:pfam00069   4 LRKLGSGSFGTVYKAKhrDTGKIVAIKKIKKEKIKKKKDKNilrEIKILKKLNHPNIVRLY--DAFEDKDN--LYLVLEY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437   312 HENGSLYDFLkcatldtrallklaysaacglchlhteiygtQGKPAIAHRDLKS--KNILikkngscciadLGLavkfns 389
Cdd:pfam00069  80 VEGGSLFDLL-------------------------------SEKGAFSEREAKFimKQIL-----------EGL------ 111
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437   390 dtnEVDVPLNTRVGTKRYMAPEVLDEslnknhfQPY-IMADIYSFGLIIWEMarrcITGgiveeyQLPYYNMVPSDPSYE 468
Cdd:pfam00069 112 ---ESGSSLTTFVGTPWYMAPEVLGG-------NPYgPKVDVWSLGCILYEL----LTG------KPPFPGINGNEIYEL 171
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 41349437   469 DMREvvcvkrlrpIVSNRWNSDECLRAVLKLMSECWAHNPASRLTALRIKK 519
Cdd:pfam00069 172 IIDQ---------PYAFPELPSNLSEEAKDLLKKLLKKDPSKRLTATQALQ 213
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
231-525 7.66e-22

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: 95.13  E-value: 7.66e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 231 AKQIQMVRQVGKGRYGEVWMGKWR--GEK---VAVKVFFTT----EEASWFRETEIYQTvlMRHENILGFIAADIKGTgs 301
Cdd:cd05033   3 ASYVTIEKVIGGGEFGEVCSGSLKlpGKKeidVAIKTLKSGysdkQRLDFLTEASIMGQ--FDHPNVIRLEGVVTKSR-- 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 302 wtQLYLITDYHENGSLYDFLKC--ATLDTRALLKLAYSAACGLCHLHTEIYgtqgkpaiAHRDLKSKNILIKKNGSCCIA 379
Cdd:cd05033  79 --PVMIVTEYMENGSLDKFLREndGKFTVTQLVGMLRGIASGMKYLSEMNY--------VHRDLAARNILVNSDLVCKVS 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 380 DLGLAvkfnSDTNEVDVPLNTRVG--TKRYMAPevldESLNKNHFQPyiMADIYSFGLIIWEMarrcITGGiveeyQLPY 457
Cdd:cd05033 149 DFGLS----RRLEDSEATYTTKGGkiPIRWTAP----EAIAYRKFTS--ASDVWSFGIVMWEV----MSYG-----ERPY 209
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41349437 458 YNMvpsdPSYEDMREVVCVKRLRPIVsnrwnsdECLRAVLKLMSECWAHNPASRLTALRIKKTLAKMV 525
Cdd:cd05033 210 WDM----SNQDVIKAVEDGYRLPPPM-------DCPSALYQLMLDCWQKDRNERPTFSQIVSTLDKMI 266
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
238-521 8.22e-22

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: 94.82  E-value: 8.22e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 238 RQVGKGRYGEVWMGKWRGEK--VAVKV----FFTTEEASWFRETEIYQTvlMRHENILGFIaadikGTGSWTQ-LYLITD 310
Cdd:cd05041   1 EKIGRGNFGDVYRGVLKPDNteVAVKTcretLPPDLKRKFLQEARILKQ--YDHPNIVKLI-----GVCVQKQpIMIVME 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 311 YHENGSLYDFL--KCATLDTRALLKLAYSAACGLCHLhteiygtQGKPAIaHRDLKSKNILIKKNGSCCIADLGLAVKfn 388
Cdd:cd05041  74 LVPGGSLLTFLrkKGARLTVKQLLQMCLDAAAGMEYL-------ESKNCI-HRDLAARNCLVGENNVLKISDFGMSRE-- 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 389 SDTNEVDVPLNTRVGTKRYMAPEVLdeslnkNHFQPYIMADIYSFGLIIWEMarrcITGGIVeeyqlPYYNMvpsdpSYE 468
Cdd:cd05041 144 EEDGEYTVSDGLKQIPIKWTAPEAL------NYGRYTSESDVWSFGILLWEI----FSLGAT-----PYPGM-----SNQ 203
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 41349437 469 DMREVVCVK-RLRPivsnrwnSDECLRAVLKLMSECWAHNPASRLTALRIKKTL 521
Cdd:cd05041 204 QTREQIESGyRMPA-------PELCPEAVYRLMLQCWAYDPENRPSFSEIYNEL 250
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
235-437 9.67e-22

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: 94.47  E-value: 9.67e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 235 QMVRQVGKGRYGEVWMGKWR--GEKVAVKV-----FFTTEEASWFRETEIYQTVlmRHENILGFIaaDIKGTGswTQLYL 307
Cdd:cd05117   3 ELGKVLGRGSFGVVRLAVHKktGEEYAVKIidkkkLKSEDEEMLRREIEILKRL--DHPNIVKLY--EVFEDD--KNLYL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 308 ITDYHENGSLYDFL-KCATL---DTRALLKLAYSAacgLCHLHTeiygtQGkpaIAHRDLKSKNILIK---KNGSCCIAD 380
Cdd:cd05117  77 VMELCTGGELFDRIvKKGSFserEAAKIMKQILSA---VAYLHS-----QG---IVHRDLKPENILLAskdPDSPIKIID 145
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 41349437 381 LGLAVKFNSDTnevdvPLNTRVGTKRYMAPEVLDEslnknhfQPYIMA-DIYSFGLII 437
Cdd:cd05117 146 FGLAKIFEEGE-----KLKTVCGTPYYVAPEVLKG-------KGYGKKcDIWSLGVIL 191
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
238-513 9.95e-22

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: 94.60  E-value: 9.95e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 238 RQVGKGRYGEVWMGKWRGE-KVAVKVFF--TTEEASWFRETEIYQtvLMRHENILGFIAadikgTGSWTQLYLITDYHEN 314
Cdd:cd14203   1 VKLGQGCFGEVWMGTWNGTtKVAIKTLKpgTMSPEAFLEEAQIMK--KLRHDKLVQLYA-----VVSEEPIYIVTEFMSK 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 315 GSLYDFLKCAT---LDTRALLKLAYSAACGLCHLHTEIYgtqgkpaiAHRDLKSKNILIKKNGSCCIADLGLAvKFNSDt 391
Cdd:cd14203  74 GSLLDFLKDGEgkyLKLPQLVDMAAQIASGMAYIERMNY--------IHRDLRAANILVGDNLVCKIADFGLA-RLIED- 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 392 NEvdvpLNTRVGTK---RYMAPevldESLNKNHFQpyIMADIYSFGLIIWEMarrcITGGiveeyQLPYYNMVPsdpsye 468
Cdd:cd14203 144 NE----YTARQGAKfpiKWTAP----EAALYGRFT--IKSDVWSFGILLTEL----VTKG-----RVPYPGMNN------ 198
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 41349437 469 dmREVV-CVKRLRPIVSnrwnSDECLRAVLKLMSECWAHNPASRLT 513
Cdd:cd14203 199 --REVLeQVERGYRMPC----PPGCPESLHELMCQCWRKDPEERPT 238
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
232-519 1.63e-21

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: 93.93  E-value: 1.63e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 232 KQIQMVRQVGKGRYGEVWMGKWR--GEKVAVKVFFTTEEASWFRET---EIYQTVLMRHENILGFIAADIKGTGswtqLY 306
Cdd:cd14069   1 EDWDLVQTLGEGAFGEVFLAVNRntEEAVAVKFVDMKRAPGDCPENikkEVCIQKMLSHKNVVRFYGHRREGEF----QY 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 307 LITDYHENGSLYDFL--------KCATLDTRALLklaysaaCGLCHLHTeiygtQGkpaIAHRDLKSKNILIKKNGSCCI 378
Cdd:cd14069  77 LFLEYASGGELFDKIepdvgmpeDVAQFYFQQLM-------AGLKYLHS-----CG---ITHRDIKPENLLLDENDNLKI 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 379 ADLGLAVKFNSDTNEVDvpLNTRVGTKRYMAPEVLDESlnKNHFQPyimADIYSFGLIIWEMarrcITGgiveeyQLPYY 458
Cdd:cd14069 142 SDFGLATVFRYKGKERL--LNKMCGTLPYVAPELLAKK--KYRAEP---VDVWSCGIVLFAM----LAG------ELPWD 204
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41349437 459 NMVPSDPSYEDMREVVCVKrLRPivsnrWNSDEclRAVLKLMSECWAHNPASRLTALRIKK 519
Cdd:cd14069 205 QPSDSCQEYSDWKENKKTY-LTP-----WKKID--TAALSLLRKILTENPNKRITIEDIKK 257
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
305-459 2.26e-21

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: 93.35  E-value: 2.26e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 305 LYLITDYHENGSLYDFL-KCATLD-TRALLklaYSA--ACGLCHLHTeiygtQGkpaIAHRDLKSKNILIKKNGSCCIAD 380
Cdd:cd05123  68 LYLVLDYVPGGELFSHLsKEGRFPeERARF---YAAeiVLALEYLHS-----LG---IIYRDLKPENILLDSDGHIKLTD 136
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 381 LGLAVKFNSDTNEvdvpLNTRVGTKRYMAPEVLDEslnknhfQPYIMA-DIYSFGLIIWEMarrcITGgiveeyQLPYYN 459
Cdd:cd05123 137 FGLAKELSSDGDR----TYTFCGTPEYLAPEVLLG-------KGYGKAvDWWSLGVLLYEM----LTG------KPPFYA 195
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
233-527 2.89e-21

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: 93.59  E-value: 2.89e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 233 QIQMVRQVGKGRYGEVWMGKWRGEkVAVKVFFTT----EEASWFReTEIYQTVLMRHENILGFIAADIKgtgswTQLYLI 308
Cdd:cd14151   9 QITVGQRIGSGSFGTVYKGKWHGD-VAVKMLNVTaptpQQLQAFK-NEVGVLRKTRHVNILLFMGYSTK-----PQLAIV 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 309 TDYHENGSLYDFLKCA--TLDTRALLKLAYSAACGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNGSCCIADLGLA-V 385
Cdd:cd14151  82 TQWCEGSSLYHHLHIIetKFEMIKLIDIARQTAQGMDYLHAK--------SIIHRDLKSNNIFLHEDLTVKIGDFGLAtV 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 386 KFNSDTNEVDVPLNtrvGTKRYMAPEVLD-ESLNKNHFQpyimADIYSFGLIIWEMarrcITGgiveeyQLPYYNMVPSD 464
Cdd:cd14151 154 KSRWSGSHQFEQLS---GSILWMAPEVIRmQDKNPYSFQ----SDVYAFGIVLYEL----MTG------QLPYSNINNRD 216
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41349437 465 psyeDMREVVCVKRLRPIVSN-RWNsdeCLRAVLKLMSECWAHNPASRLTALRIKKTLAKMVES 527
Cdd:cd14151 217 ----QIIFMVGRGYLSPDLSKvRSN---CPKAMKRLMAECLKKKRDERPLFPQILASIELLARS 273
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
238-441 3.56e-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: 93.10  E-value: 3.56e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 238 RQVGKGRYGEVWMG--KWRGEKVAVK---VFFTTEEAS---WFRETEIYQTVlmRHENILGFIAADIKGTgswtQLYLIT 309
Cdd:cd08224   6 KKIGKGQFSVVYRArcLLDGRLVALKkvqIFEMMDAKArqdCLKEIDLLQQL--NHPNIIKYLASFIENN----ELNIVL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 310 DYHENGSLYDFLKCAT-----LDTRALLKLAYSAACGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNGSCCIADLGLA 384
Cdd:cd08224  80 ELADAGDLSRLIKHFKkqkrlIPERTIWKYFVQLCSALEHMHSK--------RIMHRDIKPANVFITANGVVKLGDLGLG 151
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 41349437 385 VKFNSDTNEVdvplNTRVGTKRYMAPEVLDEslnknhfQPYIMA-DIYSFGLIIWEMA 441
Cdd:cd08224 152 RFFSSKTTAA----HSLVGTPYYMSPERIRE-------QGYDFKsDIWSLGCLLYEMA 198
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
235-440 4.66e-21

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: 92.54  E-value: 4.66e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 235 QMVRQVGKGRYGEVWMGKWR--GEKVAVKVFF------TTEEASWFRETEIyQTVLmRHENILGFIAADIKGTGswtqLY 306
Cdd:cd14007   3 EIGKPLGKGKFGNVYLAREKksGFIVALKVISksqlqkSGLEHQLRREIEI-QSHL-RHPNILRLYGYFEDKKR----IY 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 307 LITDYHENGSLYDFLKCATLDTRallKLA----YSAACGLCHLHteiygtqgKPAIAHRDLKSKNILIKKNGSCCIADLG 382
Cdd:cd14007  77 LILEYAPNGELYKELKKQKRFDE---KEAakyiYQLALALDYLH--------SKNIIHRDIKPENILLGSNGELKLADFG 145
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 41349437 383 LAVKFNSDtnevdvPLNTRVGTKRYMAPEVLdesLNKNHFQpyiMADIYSFGLIIWEM 440
Cdd:cd14007 146 WSVHAPSN------RRKTFCGTLDYLPPEMV---EGKEYDY---KVDIWSLGVLCYEL 191
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
240-511 6.65e-21

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: 92.41  E-value: 6.65e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 240 VGKGRYGEVWMGKWRGEKVAVKVF-------FTTEEASWFRETEIYQtvLMRHENILGFIAADIKGtgswTQLYLITDYH 312
Cdd:cd14146   2 IGVGGFGKVYRATWKGQEVAVKAArqdpdedIKATAESVRQEAKLFS--MLRHPNIIKLEGVCLEE----PNLCLVMEFA 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 313 ENGSLYDFLKCATLDTRA----------LLKLAYSAACGLCHLHTEIYgtqgkPAIAHRDLKSKNILIKK--------NG 374
Cdd:cd14146  76 RGGTLNRALAAANAAPGPrrarripphiLVNWAVQIARGMLYLHEEAV-----VPILHRDLKSSNILLLEkiehddicNK 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 375 SCCIADLGLAVKFNSDTNEvdvplnTRVGTKRYMAPEVLDESLNKNHfqpyimADIYSFGLIIWEMarrcITGgiveeyQ 454
Cdd:cd14146 151 TLKITDFGLAREWHRTTKM------SAAGTYAWMAPEVIKSSLFSKG------SDIWSYGVLLWEL----LTG------E 208
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 41349437 455 LPYYNMVPSDPSYEdmrevVCVKRLR-PIVSNrwnsdeCLRAVLKLMSECWAHNPASR 511
Cdd:cd14146 209 VPYRGIDGLAVAYG-----VAVNKLTlPIPST------CPEPFAKLMKECWEQDPHIR 255
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
232-511 9.34e-21

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: 92.01  E-value: 9.34e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 232 KQIQMVRQVGKGRYGEVWMGKWRGEKVAVK---------VFFTTEEASwfRETEIYQtvLMRHENILGFIAADIKGtgsw 302
Cdd:cd14147   3 QELRLEEVIGIGGFGKVYRGSWRGELVAVKaarqdpdedISVTAESVR--QEARLFA--MLAHPNIIALKAVCLEE---- 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 303 TQLYLITDYHENGSLYDFLKCATLDTRALLKLAYSAACGLCHLHTEIYgtqgKPAIaHRDLKSKNILIKKNG-------- 374
Cdd:cd14147  75 PNLCLVMEYAAGGPLSRALAGRRVPPHVLVNWAVQIARGMHYLHCEAL----VPVI-HRDLKSNNILLLQPIenddmehk 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 375 SCCIADLGLAVKFNSDTNEvdvplnTRVGTKRYMAPEVLDESLnknhFQPYimADIYSFGLIIWEMarrcITGgiveeyQ 454
Cdd:cd14147 150 TLKITDFGLAREWHKTTQM------SAAGTYAWMAPEVIKAST----FSKG--SDVWSFGVLLWEL----LTG------E 207
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 41349437 455 LPYYNMVPSDPSYEdmrevVCVKRLR-PIVSNrwnsdeCLRAVLKLMSECWAHNPASR 511
Cdd:cd14147 208 VPYRGIDCLAVAYG-----VAVNKLTlPIPST------CPEPFAQLMADCWAQDPHRR 254
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
237-441 1.58e-20

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: 90.98  E-value: 1.58e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 237 VRQVGKGRYGEVWMGKWR--GEKVAVKVFFTT-----EEASWFRETEIYQTvlMRHENILGFIAADIKGTgswtQLYLIT 309
Cdd:cd08215   5 IRVIGKGSFGSAYLVRRKsdGKLYVLKEIDLSnmsekEREEALNEVKLLSK--LKHPNIVKYYESFEENG----KLCIVM 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 310 DYHENGSLYDFLKcATLDTRALLK----LAYSA--ACGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNGSCCIADLGL 383
Cdd:cd08215  79 EYADGGDLAQKIK-KQKKKGQPFPeeqiLDWFVqiCLALKYLHSR--------KILHRDLKTQNIFLTKDGVVKLGDFGI 149
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 41349437 384 AvKFNSDTNEVdvpLNTRVGTKRYMAPEVLDEslnknhfQPY-IMADIYSFGLIIWEMA 441
Cdd:cd08215 150 S-KVLESTTDL---AKTVVGTPYYLSPELCEN-------KPYnYKSDIWALGCVLYELC 197
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
240-511 2.23e-20

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: 90.25  E-value: 2.23e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 240 VGKGRYGEVWMGKWRGEKVAVKVffTTEEaswfRETEIYQTVLMRHENILGFiaadiKGTGSWTQLY-LITDYHENGSLY 318
Cdd:cd14059   1 LGSGAQGAVFLGKFRGEEVAVKK--VRDE----KETDIKHLRKLNHPNIIKF-----KGVCTQAPCYcILMEYCPYGQLY 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 319 DFLKCATLDTRALL-KLAYSAACGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNGSCCIADLGLAVKFNSDTNEVdvp 397
Cdd:cd14059  70 EVLRAGREITPSLLvDWSKQIASGMNYLHLH--------KIIHRDLKSPNVLVTYNDVLKISDFGTSKELSEKSTKM--- 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 398 lnTRVGTKRYMAPEVL-DESLNKNhfqpyimADIYSFGLIIWEMarrcITGgiveeyQLPYYNMVPSDPSYEdmrevVCV 476
Cdd:cd14059 139 --SFAGTVAWMAPEVIrNEPCSEK-------VDIWSFGVVLWEL----LTG------EIPYKDVDSSAIIWG-----VGS 194
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 41349437 477 KRLR-PIVSNrwnsdeCLRAVLKLMSECWAHNPASR 511
Cdd:cd14059 195 NSLQlPVPST------CPDGFKLLMKQCWNSKPRNR 224
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
240-514 2.55e-20

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: 91.00  E-value: 2.55e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 240 VGKGRYGEVWMGKW--RGEKVAVKVF-FTTEEaswFRETEIYQTVLMRHENILGFIAADIKGTGSW---TQLYLITDYHE 313
Cdd:cd06917   9 VGRGSYGAVYRGYHvkTGRVVALKVLnLDTDD---DDVSDIQKEVALLSQLKLGQPKNIIKYYGSYlkgPSLWIIMDYCE 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 314 NGSLYDFLKCATLDTRALLKLAYSAACGLCHLHteiygtqgKPAIAHRDLKSKNILIKKNGSCCIADLGLAVKFNSDTNE 393
Cdd:cd06917  86 GGSIRTLMRAGPIAERYIAVIMREVLVALKFIH--------KDGIIHRDIKAANILVTNTGNVKLCDFGVAASLNQNSSK 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 394 vdvpLNTRVGTKRYMAPEVLDESLNKNhfqpyIMADIYSFGLIIWEMArrciTGGiveeyqlPYYNMVPSdpsyedMREV 473
Cdd:cd06917 158 ----RSTFVGTPYWMAPEVITEGKYYD-----TKADIWSLGITTYEMA----TGN-------PPYSDVDA------LRAV 211
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 41349437 474 VCVKRLRPivsNRWNSDECLRAVLKLMSECWAHNPASRLTA 514
Cdd:cd06917 212 MLIPKSKP---PRLEGNGYSPLLKEFVAACLDEEPKDRLSA 249
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
234-513 2.58e-20

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: 90.86  E-value: 2.58e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 234 IQMVRQVGKGRYGEVWMGKW-RGEKVAVKVFF--TTEEASWFRETEIYQTvlMRHENILGFIAADIKgtgswTQLYLITD 310
Cdd:cd05073  13 LKLEKKLGAGQFGEVWMATYnKHTKVAVKTMKpgSMSVEAFLAEANVMKT--LQHDKLVKLHAVVTK-----EPIYIITE 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 311 YHENGSLYDFLKCATLDTRALLKLA-YSA--ACGLCHLHTEIYgtqgkpaiAHRDLKSKNILIKKNGSCCIADLGLAvKF 387
Cdd:cd05073  86 FMAKGSLLDFLKSDEGSKQPLPKLIdFSAqiAEGMAFIEQRNY--------IHRDLRAANILVSASLVCKIADFGLA-RV 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 388 NSDTNEVdvplnTRVGTK---RYMAPevldESLNKNHFQpyIMADIYSFGLIIWEmarrcitggIVEEYQLPYynmvPSD 464
Cdd:cd05073 157 IEDNEYT-----AREGAKfpiKWTAP----EAINFGSFT--IKSDVWSFGILLME---------IVTYGRIPY----PGM 212
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 41349437 465 PSYEDMREVVCVKRLRpivsnrwNSDECLRAVLKLMSECWAHNPASRLT 513
Cdd:cd05073 213 SNPEVIRALERGYRMP-------RPENCPEELYNIMMRCWKNRPEERPT 254
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
234-513 4.17e-20

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: 90.51  E-value: 4.17e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 234 IQMVRQVGKGRYGEVWMGKWRGE-KVAVKVFF--TTEEASWFRETEIYQTvlMRHENILGFIAadikgTGSWTQLYLITD 310
Cdd:cd05070  11 LQLIKRLGNGQFGEVWMGTWNGNtKVAIKTLKpgTMSPESFLEEAQIMKK--LKHDKLVQLYA-----VVSEEPIYIVTE 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 311 YHENGSLYDFLKCA---TLDTRALLKLAYSAACGLCHLHTEIYgtqgkpaiAHRDLKSKNILIKKNGSCCIADLGLAVKF 387
Cdd:cd05070  84 YMSKGSLLDFLKDGegrALKLPNLVDMAAQVAAGMAYIERMNY--------IHRDLRSANILVGNGLICKIADFGLARLI 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 388 NsdtnevDVPLNTRVGTK---RYMAPEVldeslnKNHFQPYIMADIYSFGLIIWEMarrcITGGiveeyQLPYynmvPSD 464
Cdd:cd05070 156 E------DNEYTARQGAKfpiKWTAPEA------ALYGRFTIKSDVWSFGILLTEL----VTKG-----RVPY----PGM 210
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 41349437 465 PSYEDMREVVCVKRLrPIvsnrwnSDECLRAVLKLMSECWAHNPASRLT 513
Cdd:cd05070 211 NNREVLEQVERGYRM-PC------PQDCPISLHELMIHCWKKDPEERPT 252
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
238-447 7.16e-20

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: 89.87  E-value: 7.16e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 238 RQVGKGRYGEVWMGKWRGEKVAVKVFFTTEEASWFRETEIYQTVL-----MRHENI---LGFiaadikgTGSWTQLYLIT 309
Cdd:cd14158  21 NKLGEGGFGVVFKGYINDKNVAVKKLAAMVDISTEDLTKQFEQEIqvmakCQHENLvelLGY-------SCDGPQLCLVY 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 310 DYHENGSLYDFLKCATlDTRAL-----LKLAYSAACGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNGSCCIADLGLA 384
Cdd:cd14158  94 TYMPNGSLLDRLACLN-DTPPLswhmrCKIAQGTANGINYLHEN--------NHIHRDIKSANILLDETFVPKISDFGLA 164
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41349437 385 VKFNSDTNEVdvplNTR--VGTKRYMAPEVLDESLNknhfqpyIMADIYSFGLIIWEMarrcITG 447
Cdd:cd14158 165 RASEKFSQTI----MTEriVGTTAYMAPEALRGEIT-------PKSDIFSFGVVLLEI----ITG 214
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
233-524 9.40e-20

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: 89.33  E-value: 9.40e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 233 QIQMVRQVGKGRYGEVWMGKWRGEkVAVKVF---FTTEEASWFRETEIYQTVLMRHENILGFIAADIKGtgswTQLYLIT 309
Cdd:cd14063   1 ELEIKEVIGKGRFGRVHRGRWHGD-VAIKLLnidYLNEEQLEAFKEEVAAYKNTRHDNLVLFMGACMDP----PHLAIVT 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 310 DYHENGSLYDFLKCA--TLDTRALLKLAYSAACGLCHLHTEiygtqgkpAIAHRDLKSKNILIkKNGSCCIADLGL-AVK 386
Cdd:cd14063  76 SLCKGRTLYSLIHERkeKFDFNKTVQIAQQICQGMGYLHAK--------GIIHKDLKSKNIFL-ENGRVVITDFGLfSLS 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 387 FNSDTNEVDVPLNTRVGTKRYMAPEV---LDESLNKNHFQPYIMA-DIYSFGLIIWEMarrcITGGiveeyqLPYYNmvp 462
Cdd:cd14063 147 GLLQPGRREDTLVIPNGWLCYLAPEIiraLSPDLDFEESLPFTKAsDVYAFGTVWYEL----LAGR------WPFKE--- 213
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41349437 463 sDPSYEDMREVVCVKRLRPivsNRWNSDeclRAVLKLMSECWAHNPASRLTALRIKKTLAKM 524
Cdd:cd14063 214 -QPAESIIWQVGCGKKQSL---SQLDIG---REVKDILMQCWAYDPEKRPTFSDLLRMLERL 268
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
234-514 1.45e-19

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: 88.42  E-value: 1.45e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 234 IQMVRQVGKGRYGEVWMG--KWRGEKVAVKVFFTTEEASwFRET---EIYQTVLMRHENILGFIAADIKGTgswtQLYLI 308
Cdd:cd06623   3 LERVKVLGQGSSGVVYKVrhKPTGKIYALKKIHVDGDEE-FRKQllrELKTLRSCESPYVVKCYGAFYKEG----EISIV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 309 TDYHENGSLYDFLK-CATLDTRALLKLAYSAACGLCHLHTeiygtqgKPAIAHRDLKSKNILIKKNGSCCIADLGLAvKF 387
Cdd:cd06623  78 LEYMDGGSLADLLKkVGKIPEPVLAYIARQILKGLDYLHT-------KRHIIHRDIKPSNLLINSKGEVKIADFGIS-KV 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 388 NSDTnevDVPLNTRVGTKRYMAPEVLDEslnknhfQPYIM-ADIYSFGLIIWEmarrCITGgiveeyQLPYYNmvPSDPS 466
Cdd:cd06623 150 LENT---LDQCNTFVGTVTYMSPERIQG-------ESYSYaADIWSLGLTLLE----CALG------KFPFLP--PGQPS 207
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 41349437 467 YEDMREVVCVKRLRPIVSNRWnSDEcLRAVLKLmseCWAHNPASRLTA 514
Cdd:cd06623 208 FFELMQAICDGPPPSLPAEEF-SPE-FRDFISA---CLQKDPKKRPSA 250
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
239-513 1.55e-19

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: 88.59  E-value: 1.55e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 239 QVGKGRYGEVWMGKWRGE-KVAVKVFF--TTEEASWFRETEIYQTvlMRHENILGFIAadikgTGSWTQLYLITDYHENG 315
Cdd:cd05071  16 KLGQGCFGEVWMGTWNGTtRVAIKTLKpgTMSPEAFLQEAQVMKK--LRHEKLVQLYA-----VVSEEPIYIVTEYMSKG 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 316 SLYDFLKCAT---LDTRALLKLAYSAACGLCHLHTEIYgtqgkpaiAHRDLKSKNILIKKNGSCCIADLGLAVKFNsdtn 392
Cdd:cd05071  89 SLLDFLKGEMgkyLRLPQLVDMAAQIASGMAYVERMNY--------VHRDLRAANILVGENLVCKVADFGLARLIE---- 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 393 evDVPLNTRVGTK---RYMAPEVldeslnKNHFQPYIMADIYSFGLIIWEMArrciTGGiveeyQLPYYNMVpsdpSYED 469
Cdd:cd05071 157 --DNEYTARQGAKfpiKWTAPEA------ALYGRFTIKSDVWSFGILLTELT----TKG-----RVPYPGMV----NREV 215
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 41349437 470 MREVVCVKRLrPIVSnrwnsdECLRAVLKLMSECWAHNPASRLT 513
Cdd:cd05071 216 LDQVERGYRM-PCPP------ECPESLHDLMCQCWRKEPEERPT 252
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
232-463 1.76e-19

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: 88.09  E-value: 1.76e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 232 KQIQMVRQVGKGRYGEVWMGKWR--GEKVAVKVFFTTEE-ASWFRETEIYQTVlmRHENILGFIAADIKGTgswtQLYLI 308
Cdd:cd06612   3 EVFDILEKLGEGSYGSVYKAIHKetGQVVAIKVVPVEEDlQEIIKEISILKQC--DSPYIVKYYGSYFKNT----DLWIV 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 309 TDYHENGSLYDFLK--CATLDTRALLKLAYSAACGLCHLHteiygtqgKPAIAHRDLKSKNILIKKNGSCCIADLGLAVK 386
Cdd:cd06612  77 MEYCGAGSVSDIMKitNKTLTEEEIAAILYQTLKGLEYLH--------SNKKIHRDIKAGNILLNEEGQAKLADFGVSGQ 148
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41349437 387 FNSDTNEVdvplNTRVGTKRYMAPEVLDESlNKNHfqpyiMADIYSFGLIIWEMArrcitggiveEYQLPYYNMVPS 463
Cdd:cd06612 149 LTDTMAKR----NTVIGTPFWMAPEVIQEI-GYNN-----KADIWSLGITAIEMA----------EGKPPYSDIHPM 205
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
235-442 1.90e-19

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: 88.36  E-value: 1.90e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 235 QMVRQVGKGRYGEVWMGKWR--GEKVAVKV----FFTTEEASWFRETEIYQTvLMRHENILG----FIAADikgtgswtQ 304
Cdd:cd07830   2 KVIKQLGDGTFGSVYLARNKetGELVAIKKmkkkFYSWEECMNLREVKSLRK-LNEHPNIVKlkevFREND--------E 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 305 LYLITDYHEnGSLYDFLKcatldTRALLKLAYSA--------ACGLCHLHTEIYgtqgkpaiAHRDLKSKNILIKKNGSC 376
Cdd:cd07830  73 LYFVFEYME-GNLYQLMK-----DRKGKPFSESVirsiiyqiLQGLAHIHKHGF--------FHRDLKPENLLVSGPEVV 138
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41349437 377 CIADLGLAVKFNSDTnevdvPLNTRVGTKRYMAPEVLDESLNKNHfqPyimADIYSFGLIIWEMAR 442
Cdd:cd07830 139 KIADFGLAREIRSRP-----PYTDYVSTRWYRAPEILLRSTSYSS--P---VDIWALGCIMAELYT 194
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
230-503 2.98e-19

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: 88.16  E-value: 2.98e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 230 IAKQIQMVRQVGKGRYGEVWMGKWRGEkVAVKVFFTT----EEASWFReTEIYQTVLMRHENILGFIAADIKGtgswtQL 305
Cdd:cd14149  10 EASEVMLSTRIGSGSFGTVYKGKWHGD-VAVKILKVVdptpEQFQAFR-NEVAVLRKTRHVNILLFMGYMTKD-----NL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 306 YLITDYHENGSLYDFLKcaTLDTR----ALLKLAYSAACGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNGSCCIADL 381
Cdd:cd14149  83 AIVTQWCEGSSLYKHLH--VQETKfqmfQLIDIARQTAQGMDYLHAK--------NIIHRDMKSNNIFLHEGLTVKIGDF 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 382 GLA-VKFN-SDTNEVDVPlntrVGTKRYMAPEVLDESLNknhfQPY-IMADIYSFGLIIWEMarrcITGgiveeyQLPYY 458
Cdd:cd14149 153 GLAtVKSRwSGSQQVEQP----TGSILWMAPEVIRMQDN----NPFsFQSDVYSYGIVLYEL----MTG------ELPYS 214
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 41349437 459 NMVPSDpsyedmREVVCVKR--LRPIVSNRWNSdeCLRAVLKLMSEC 503
Cdd:cd14149 215 HINNRD------QIIFMVGRgyASPDLSKLYKN--CPKAMKRLVADC 253
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
234-436 4.79e-19

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: 87.02  E-value: 4.79e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 234 IQMVRQVGKGRYGEVWMGK--WRGEKVAVKVFFT----TEEASWFRETEIYQTV-----LMRHENILGFIaaDIKGTGSW 302
Cdd:cd13993   2 YQLISPIGEGAYGVVYLAVdlRTGRKYAIKCLYKsgpnSKDGNDFQKLPQLREIdlhrrVSRHPNIITLH--DVFETEVA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 303 TqlYLITDYHENGSLYD-------FLKCATLDTRALLKLAysAACGLCHLHteiygtqgkpAIAHRDLKSKNILIKKN-G 374
Cdd:cd13993  80 I--YIVLEYCPNGDLFEaitenriYVGKTELIKNVFLQLI--DAVKHCHSL----------GIYHRDIKPENILLSQDeG 145
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41349437 375 SCCIADLGLAVkfNSDTNevdvpLNTRVGTKRYMAPEVLDESLNKNHFQPYIMADIYSFGLI 436
Cdd:cd13993 146 TVKLCDFGLAT--TEKIS-----MDFGVGSEFYMAPECFDEVGRSLKGYPCAAGDIWSLGII 200
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
228-511 6.98e-19

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: 86.98  E-value: 6.98e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 228 RTIAKQIQMVRQVGKGRYGEVWMGKW--RGEKVAVKVFFTTEEaswfRETEIYQTVLM-----RHENILGFIAADIKGT- 299
Cdd:cd06636  12 RDPAGIFELVEVVGNGTYGQVYKGRHvkTGQLAAIKVMDVTED----EEEEIKLEINMlkkysHHRNIATYYGAFIKKSp 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 300 -GSWTQLYLITDYHENGSLYDFLKCATLDTRALLKLAY---SAACGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNGS 375
Cdd:cd06636  88 pGHDDQLWLVMEFCGAGSVTDLVKNTKGNALKEDWIAYicrEILRGLAHLHAH--------KVIHRDIKGQNVLLTENAE 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 376 CCIADLGLAVKFNSDTNEvdvpLNTRVGTKRYMAPEVLDESLNKNHFQPYiMADIYSFGLIIWEMArrcitggiveEYQL 455
Cdd:cd06636 160 VKLVDFGVSAQLDRTVGR----RNTFIGTPYWMAPEVIACDENPDATYDY-RSDIWSLGITAIEMA----------EGAP 224
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 41349437 456 PYYNMVPsdpsyedMREVVCVKRLRP--IVSNRWNsdeclRAVLKLMSECWAHNPASR 511
Cdd:cd06636 225 PLCDMHP-------MRALFLIPRNPPpkLKSKKWS-----KKFIDFIEGCLVKNYLSR 270
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
239-521 7.61e-19

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: 86.66  E-value: 7.61e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 239 QVGKGRYGEVWMGKWRGE-KVAVKVFF--TTEEASWFRETEIYQTvlMRHENILGFIAadikgTGSWTQLYLITDYHENG 315
Cdd:cd05069  19 KLGQGCFGEVWMGTWNGTtKVAIKTLKpgTMMPEAFLQEAQIMKK--LRHDKLVPLYA-----VVSEEPIYIVTEFMGKG 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 316 SLYDFLKCAT---LDTRALLKLAYSAACGLCHLHTEIYgtqgkpaiAHRDLKSKNILIKKNGSCCIADLGLAVKFNsdtn 392
Cdd:cd05069  92 SLLDFLKEGDgkyLKLPQLVDMAAQIADGMAYIERMNY--------IHRDLRAANILVGDNLVCKIADFGLARLIE---- 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 393 evDVPLNTRVGTK---RYMAPEVldeslnKNHFQPYIMADIYSFGLIIWEMarrcITGGiveeyQLPYYNMVpsdpSYED 469
Cdd:cd05069 160 --DNEYTARQGAKfpiKWTAPEA------ALYGRFTIKSDVWSFGILLTEL----VTKG-----RVPYPGMV----NREV 218
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 41349437 470 MREVVCVKRLrPIVSNrwnsdeCLRAVLKLMSECWAHNPASRLTALRIKKTL 521
Cdd:cd05069 219 LEQVERGYRM-PCPQG------CPESLHELMKLCWKKDPDERPTFEYIQSFL 263
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
231-511 1.66e-18

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: 85.84  E-value: 1.66e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 231 AKQIQMVRQVGKGRYGEVWMGKW------RGEKVAVKVF-FTTEE--ASWFRETEIYQTvlMRHENILGFiaadiKG--- 298
Cdd:cd14205   3 ERHLKFLQQLGKGNFGSVEMCRYdplqdnTGEVVAVKKLqHSTEEhlRDFEREIEILKS--LQHDNIVKY-----KGvcy 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 299 TGSWTQLYLITDYHENGSLYDFLKC--ATLDTRALLKLAYSAACGLCHLHTEIYgtqgkpaiAHRDLKSKNILIKKNGSC 376
Cdd:cd14205  76 SAGRRNLRLIMEYLPYGSLRDYLQKhkERIDHIKLLQYTSQICKGMEYLGTKRY--------IHRDLATRNILVENENRV 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 377 CIADLGLAVKFNSDTN--EVDVPLNTRVgtkRYMAPEVLDESlnknHFQpyIMADIYSFGLIIwemarrcitggiveeYQ 454
Cdd:cd14205 148 KIGDFGLTKVLPQDKEyyKVKEPGESPI---FWYAPESLTES----KFS--VASDVWSFGVVL---------------YE 203
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41349437 455 LPYYNMVPSDPSYEDMREV-------VCVKRLRPIVSNRWN---SDECLRAVLKLMSECWAHNPASR 511
Cdd:cd14205 204 LFTYIEKSKSPPAEFMRMIgndkqgqMIVFHLIELLKNNGRlprPDGCPDEIYMIMTECWNNNVNQR 270
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
232-442 1.66e-18

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: 85.76  E-value: 1.66e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 232 KQIQMVRQVGKGRYGEVWMG--KWRGEKVAVKVFfTTEEAS---WFRETEIYQTVLMRHENILGFIAADIKGTgswtQLY 306
Cdd:cd06609   1 ELFTLLERIGKGSFGEVYKGidKRTNQVVAIKVI-DLEEAEdeiEDIQQEIQFLSQCDSPYITKYYGSFLKGS----KLW 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 307 LITDYHENGSLYDFLKCATLD-------TRALLKlaysaacGLCHLHTeiygtQGKpaiAHRDLKSKNILIKKNGSCCIA 379
Cdd:cd06609  76 IIMEYCGGGSVLDLLKPGPLDetyiafiLREVLL-------GLEYLHS-----EGK---IHRDIKAANILLSEEGDVKLA 140
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41349437 380 DLGLAVKFNSDTNEvdvpLNTRVGTKRYMAPEVLDESlNKNHfqpyiMADIYSFGLIIWEMAR 442
Cdd:cd06609 141 DFGVSGQLTSTMSK----RNTFVGTPFWMAPEVIKQS-GYDE-----KADIWSLGITAIELAK 193
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
235-441 2.34e-18

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: 85.05  E-value: 2.34e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 235 QMVRQVGKGRYGEVWMGKWR--GEKVAVKVFFTTEEaswfRETEIYQTVLM-----RHENILGFIAADIKG--TGSWTQL 305
Cdd:cd06608   9 ELVEVIGEGTYGKVYKARHKktGQLAAIKIMDIIED----EEEEIKLEINIlrkfsNHPNIATFYGAFIKKdpPGGDDQL 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 306 YLITDYHENGSLYDFLKcATLDTRALLK---LAY---SAACGLCHLHteiygtqgKPAIAHRDLKSKNILIKKNGSCCIA 379
Cdd:cd06608  85 WLVMEYCGGGSVTDLVK-GLRKKGKRLKeewIAYilrETLRGLAYLH--------ENKVIHRDIKGQNILLTEEAEVKLV 155
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41349437 380 DLGLAVKFNSdTNEVDvplNTRVGTKRYMAPEVLdeSLNKNHFQPYIM-ADIYSFGLIIWEMA 441
Cdd:cd06608 156 DFGVSAQLDS-TLGRR---NTFIGTPYWMAPEVI--ACDQQPDASYDArCDVWSLGITAIELA 212
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
232-514 2.39e-18

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: 85.10  E-value: 2.39e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 232 KQIQMVRQVGKGRYGEVWMGKW--RGEKVAVKVF----FTTEEASWFRETEIYQTVlmRHENILGFIAADIKGTgswtQL 305
Cdd:cd06610   1 DDYELIEVIGSGATAVVYAAYClpKKEKVAIKRIdlekCQTSMDELRKEIQAMSQC--NHPNVVSYYTSFVVGD----EL 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 306 YLITDYHENGSLYDFLK-----------CATLDTRALLKlaysaacGLCHLHteiygtqgKPAIAHRDLKSKNILIKKNG 374
Cdd:cd06610  75 WLVMPLLSGGSLLDIMKssyprggldeaIIATVLKEVLK-------GLEYLH--------SNGQIHRDVKAGNILLGEDG 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 375 SCCIADLGLAVKFNSDTNEVDVPLNTRVGTKRYMAPEVLDESLNKNHfqpyiMADIYSFGLIIWEMArrciTGgiveeyQ 454
Cdd:cd06610 140 SVKIADFGVSASLATGGDRTRKVRKTFVGTPCWMAPEVMEQVRGYDF-----KADIWSFGITAIELA----TG------A 204
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41349437 455 LPYYNMVPSD----------PSYEDMREV-VCVKRLRpivsnrwnsdeclravlKLMSECWAHNPASRLTA 514
Cdd:cd06610 205 APYSKYPPMKvlmltlqndpPSLETGADYkKYSKSFR-----------------KMISLCLQKDPSKRPTA 258
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
235-514 2.43e-18

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: 85.23  E-value: 2.43e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 235 QMVRQVGKGRYGEVWMGKWR--GEKVAVKVF-FTTEE----ASWFRETEIYQTvlMRHENILGFIaaDIKGTGSwtQLYL 307
Cdd:cd07829   2 EKLEKLGEGTYGVVYKAKDKktGEIVALKKIrLDNEEegipSTALREISLLKE--LKHPNIVKLL--DVIHTEN--KLYL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 308 ITDYHENgSLYDFLKCAT--LDTRALLKLAYSAACGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNGSCCIADLGLAV 385
Cdd:cd07829  76 VFEYCDQ-DLKKYLDKRPgpLPPNLIKSIMYQLLRGLAYCHSH--------RILHRDLKPQNLLINRDGVLKLADFGLAR 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 386 KFNsdtnevdVPLNT---RVGTKRYMAPEVLdesLNKNHFQPYImaDIYSFGLIIWEMARRC-----------------I 445
Cdd:cd07829 147 AFG-------IPLRTythEVVTLWYRAPEIL---LGSKHYSTAV--DIWSVGCIFAELITGKplfpgdseidqlfkifqI 214
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41349437 446 TGGIVEE-----YQLPYYNMVPsdPSYEdmrevvcVKRLRPIVSNrwNSDEClravLKLMSECWAHNPASRLTA 514
Cdd:cd07829 215 LGTPTEEswpgvTKLPDYKPTF--PKWP-------KNDLEKVLPR--LDPEG----IDLLSKMLQYNPAKRISA 273
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
240-467 4.01e-18

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: 84.08  E-value: 4.01e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 240 VGKGRYGEVW--MGKWRGEKVAVKVF-FTTEEASWFRETEIYQTvlMRHENILGFIAADIKGTgswtQLYLITDYHENGS 316
Cdd:cd14065   1 LGKGFFGEVYkvTHRETGKVMVMKELkRFDEQRSFLKEVKLMRR--LSHPNILRFIGVCVKDN----KLNFITEYVNGGT 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 317 LYDFLKCA--TLDTRALLKLAYSAACGLCHLHTEiygtqgkpAIAHRDLKSKNILIK---KNGSCCIADLGLAVKF-NSD 390
Cdd:cd14065  75 LEELLKSMdeQLPWSQRVSLAKDIASGMAYLHSK--------NIIHRDLNSKNCLVReanRGRNAVVADFGLAREMpDEK 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 391 TNEVD--VPLNTrVGTKRYMAPEVLD-ESLNKNhfqpyimADIYSFGLIIWEMARRcitggiveeyqlpyynmVPSDPSY 467
Cdd:cd14065 147 TKKPDrkKRLTV-VGSPYWMAPEMLRgESYDEK-------VDVFSFGIVLCEIIGR-----------------VPADPDY 201
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
235-440 4.99e-18

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: 83.84  E-value: 4.99e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 235 QMVRQVGKGRYGEVWMGKWR--GEKVAVKVF----FTTEEASWFRETEIYQTVLMRHENILGFIaaDIkgtgsWT---QL 305
Cdd:cd14081   4 RLGKTLGKGQTGLVKLAKHCvtGQKVAIKIVnkekLSKESVLMKVEREIAIMKLIEHPNVLKLY--DV-----YEnkkYL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 306 YLITDYHENGSLYDFL-KCATLDTRALLKLAYSAACGL--CHLHTeiygtqgkpaIAHRDLKSKNILIKKNGSCCIADLG 382
Cdd:cd14081  77 YLVLEYVSGGELFDYLvKKGRLTEKEARKFFRQIISALdyCHSHS----------ICHRDLKPENLLLDEKNNIKIADFG 146
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41349437 383 LA-VKFNSDTnevdvpLNTRVGTKRYMAPEVLDEslnknhfQPY--IMADIYSFGLIIWEM 440
Cdd:cd14081 147 MAsLQPEGSL------LETSCGSPHYACPEVIKG-------EKYdgRKADIWSCGVILYAL 194
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
240-514 6.39e-18

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: 84.29  E-value: 6.39e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 240 VGKGRYGEVW--MGKWRGEKVAVKVFFTTEEASWFRET---EIYQTVLMRHENILGFIAAdIKGTGswtQLYLITDYHEN 314
Cdd:cd07833   9 VGEGAYGVVLkcRNKATGEIVAIKKFKESEDDEDVKKTalrEVKVLRQLRHENIVNLKEA-FRRKG---RLYLVFEYVER 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 315 gSLYDFLKC--ATLDTRALLKLAYSAACGLCHLHteiygtqgKPAIAHRDLKSKNILIKKNGSCCIADLGLAVKFNSDTN 392
Cdd:cd07833  85 -TLLELLEAspGGLPPDAVRSYIWQLLQAIAYCH--------SHNIIHRDIKPENILVSESGVLKLCDFGFARALTARPA 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 393 evdVPLNTRVGTKRYMAPEVL--DESLNKNhfqpyimADIYSFGLIIWEMA------------------RRCItGGIVEE 452
Cdd:cd07833 156 ---SPLTDYVATRWYRAPELLvgDTNYGKP-------VDVWAIGCIMAELLdgeplfpgdsdidqlyliQKCL-GPLPPS 224
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41349437 453 YQL-----PYYN--MVPsDPSYEDMREvvcvKRLRPIVSNRWnsdeclravLKLMSECWAHNPASRLTA 514
Cdd:cd07833 225 HQElfssnPRFAgvAFP-EPSQPESLE----RRYPGKVSSPA---------LDFLKACLRMDPKERLTC 279
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
233-524 6.58e-18

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: 83.62  E-value: 6.58e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 233 QIQMVRQVGKGRYGEVWMGKWR--GEKVAVKVFF--TTEEASWFRETEIYQTvlMRHENILGFIaadikgtGSWTQ---L 305
Cdd:cd05052   7 DITMKHKLGGGQYGEVYEGVWKkyNLTVAVKTLKedTMEVEEFLKEAAVMKE--IKHPNLVQLL-------GVCTReppF 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 306 YLITDYHENGSLYDFLKCA---TLDTRALLKLAYSAACGLCHLHTEIYgtqgkpaiAHRDLKSKNILIKKNGSCCIADLG 382
Cdd:cd05052  78 YIITEFMPYGNLLDYLRECnreELNAVVLLYMATQIASAMEYLEKKNF--------IHRDLAARNCLVGENHLVKVADFG 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 383 LAVKFNSDTnevdvpLNTRVGTK---RYMAPevldESLNKNHFQpyIMADIYSFGLIIWEMArrcitggiveEYQLPYYN 459
Cdd:cd05052 150 LSRLMTGDT------YTAHAGAKfpiKWTAP----ESLAYNKFS--IKSDVWAFGVLLWEIA----------TYGMSPYP 207
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41349437 460 MVPSDPSYEDMREvvcvkrlrpivSNRWNSDE-CLRAVLKLMSECWAHNPASRLTALRIKKTLAKM 524
Cdd:cd05052 208 GIDLSQVYELLEK-----------GYRMERPEgCPPKVYELMRACWQWNPSDRPSFAEIHQALETM 262
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
241-519 6.94e-18

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: 83.76  E-value: 6.94e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 241 GKGRYGEVWMGKWR--GEKVAVKVF-------------FTTEEASWF----RETEIYQTvlMRHENILGFIAA--DIKGT 299
Cdd:cd14008   2 GRGSFGKVKLALDTetGQLYAIKIFnksrlrkrregknDRGKIKNALddvrREIAIMKK--LDHPNIVRLYEVidDPESD 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 300 gswtQLYLITDYHENGSLYDFL---KCATLDTRALLKLAYSAACGLCHLHTeiygtQGkpaIAHRDLKSKNILIKKNGSC 376
Cdd:cd14008  80 ----KLYLVLEYCEGGPVMELDsgdRVPPLPEETARKYFRDLVLGLEYLHE-----NG---IVHRDIKPENLLLTADGTV 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 377 CIADLGLAVKFNSDTNEvdvpLNTRVGTKRYMAPEVLDESLNKNHFQPyimADIYSFGLIIWEMarrcITGgiveeyQLP 456
Cdd:cd14008 148 KISDFGVSEMFEDGNDT----LQKTAGTPAFLAPELCDGDSKTYSGKA---ADIWALGVTLYCL----VFG------RLP 210
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41349437 457 YYnmvpsDPSYEDMREVVCVKRLRPIVSNrwNSDECLRAVLKLMSEcwaHNPASRLTALRIKK 519
Cdd:cd14008 211 FN-----GDNILELYEAIQNQNDEFPIPP--ELSPELKDLLRRMLE---KDPEKRITLKEIKE 263
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
233-522 7.60e-18

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: 83.46  E-value: 7.60e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 233 QIQMVRQVGKGRYGEVWMGKWRGE-KVAVKvffTTEEASWFRETEIYQT-VLMR--HENILGFIAADIKGtgswTQLYLI 308
Cdd:cd05112   5 ELTFVQEIGSGQFGLVHLGYWLNKdKVAIK---TIREGAMSEEDFIEEAeVMMKlsHPKLVQLYGVCLEQ----APICLV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 309 TDYHENGSLYDFLKC--ATLDTRALLKLAYSAACGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNGSCCIADLGLAvK 386
Cdd:cd05112  78 FEFMEHGCLSDYLRTqrGLFSAETLLGMCLDVCEGMAYLEEA--------SVIHRDLAARNCLVGENQVVKVSDFGMT-R 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 387 FnsdtnEVDVPLNTRVGTK---RYMAPEVLDeslnknhFQPY-IMADIYSFGLIIWEmarrcitggIVEEYQLPYYNMVP 462
Cdd:cd05112 149 F-----VLDDQYTSSTGTKfpvKWSSPEVFS-------FSRYsSKSDVWSFGVLMWE---------VFSEGKIPYENRSN 207
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41349437 463 SdpsyEDMREVVCVKRL-RPIVsnrwnsdeCLRAVLKLMSECWAHNPASRLTALRIKKTLA 522
Cdd:cd05112 208 S----EVVEDINAGFRLyKPRL--------ASTHVYEIMNHCWKERPEDRPSFSLLLRQLA 256
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
235-462 9.11e-18

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: 83.12  E-value: 9.11e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 235 QMVRQVGKGRYGEVWMGKWR--GEKVAVKVFFTTEEASWfreTEIYQTVLM----RHENILGFIAADIKGTgswtQLYLI 308
Cdd:cd06613   3 ELIQRIGSGTYGDVYKARNIatGELAAVKVIKLEPGDDF---EIIQQEISMlkecRHPNIVAYFGSYLRRD----KLWIV 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 309 TDYHENGSLYDFLKCatldTRALLKLAYSAAC-----GLCHLHTeiygtQGKpaiAHRDLKSKNILIKKNGSCCIADLGL 383
Cdd:cd06613  76 MEYCGGGSLQDIYQV----TGPLSELQIAYVCretlkGLAYLHS-----TGK---IHRDIKGANILLTEDGDVKLADFGV 143
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41349437 384 AVKFNSDTNEvdvpLNTRVGTKRYMAPEVLDESLNKNHFQpyiMADIYSFGLIIWEMArrcitggiveEYQLPYYNMVP 462
Cdd:cd06613 144 SAQLTATIAK----RKSFIGTPYWMAPEVAAVERKGGYDG---KCDIWALGITAIELA----------ELQPPMFDLHP 205
PKc_TOPK cd14001
Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer ...
266-470 1.31e-17

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: 83.22  E-value: 1.31e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 266 TEEASWFREteiyqtvlMRHENILGFIAADIKGTGSwtqLYLITDYHENgSLYDFLKcATLDTR-------ALLKLAYSA 338
Cdd:cd14001  53 KEEAKILKS--------LNHPNIVGFRAFTKSEDGS---LCLAMEYGGK-SLNDLIE-ERYEAGlgpfpaaTILKVALSI 119
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 339 ACGLCHLHTEIYgtqgkpaIAHRDLKSKNILIKKN-GSCCIADLGLAVKFNSDTNEVDVPLNTRVGTKRYMAPEVLDESL 417
Cdd:cd14001 120 ARALEYLHNEKK-------ILHGDIKSGNVLIKGDfESVKLCDFGVSLPLTENLEVDSDPKAQYVGTEPWKAKEALEEGG 192
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 41349437 418 ---NKnhfqpyimADIYSFGLIIWEMarrcITGGIveeyqlPYYNMVPSDPSYEDM 470
Cdd:cd14001 193 vitDK--------ADIFAYGLVLWEM----MTLSV------PHLNLLDIEDDDEDE 230
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
240-455 1.34e-17

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: 83.57  E-value: 1.34e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 240 VGKGRYGEVWMGKWR--GEKVAVKVFFTTEEASWF-----RETEIYQtvLMRHENILGFI----AADIKGTGSWTQLYLI 308
Cdd:cd07865  20 IGQGTFGEVFKARHRktGQIVALKKVLMENEKEGFpitalREIKILQ--LLKHENVVNLIeicrTKATPYNRYKGSIYLV 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 309 TDYHENgSLYDFLKCATLD-----TRALLKLAYSaacGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNGSCCIADLGL 383
Cdd:cd07865  98 FEFCEH-DLAGLLSNKNVKftlseIKKVMKMLLN---GLYYIHRN--------KILHRDMKAANILITKDGVLKLADFGL 165
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41349437 384 AVKFNSDTNEVDVPLNTRVGTKRYMAPEVLdesLNKNHFQPYImaDIYSFGLIIWEM-ARRCITGGIVEEYQL 455
Cdd:cd07865 166 ARAFSLAKNSQPNRYTNRVVTLWYRPPELL---LGERDYGPPI--DMWGAGCIMAEMwTRSPIMQGNTEQHQL 233
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
234-474 1.38e-17

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: 82.78  E-value: 1.38e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 234 IQMVRQVGKGRYGEVWM--GKWRGEKVAVKVFFTTEEASWFRETEIYQTVLMRHE--NILGFIAADIkgtgSWTQLYLIT 309
Cdd:cd06605   3 LEYLGELGEGNGGVVSKvrHRPSGQIMAVKVIRLEIDEALQKQILRELDVLHKCNspYIVGFYGAFY----SEGDISICM 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 310 DYHENGSLYDFLKCA-TLDTRALLKLAYSAACGLCHLHTeiygtqgKPAIAHRDLKSKNILIKKNGSCCIADLGLAvkfn 388
Cdd:cd06605  79 EYMDGGSLDKILKEVgRIPERILGKIAVAVVKGLIYLHE-------KHKIIHRDVKPSNILVNSRGQVKLCDFGVS---- 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 389 sdTNEVDVPLNTRVGTKRYMAPevldESLNKNHFQpyIMADIYSFGLIIWEMArrcitggiVEEYQLPYYNMVPSDPSYE 468
Cdd:cd06605 148 --GQLVDSLAKTFVGTRSYMAP----ERISGGKYT--VKSDIWSLGLSLVELA--------TGRFPYPPPNAKPSMMIFE 211

                ....*.
gi 41349437 469 DMREVV 474
Cdd:cd06605 212 LLSYIV 217
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
235-441 1.68e-17

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: 81.97  E-value: 1.68e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 235 QMVRQVGKGRYGEVWMGKWR--GEKVAVKVF---FTTEEASWFRETEIYQ-TVLMRHENILGFIAAdikgtgsWTQ---L 305
Cdd:cd14050   4 TILSKLGEGSFGEVFKVRSRedGKLYAVKRSrsrFRGEKDRKRKLEEVERhEKLGEHPNCVRFIKA-------WEEkgiL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 306 YLITDYHEnGSLYDFL-KCATLDTRALLKLAYSAACGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNGSCCIADLGLA 384
Cdd:cd14050  77 YIQTELCD-TSLQQYCeETHSLPESEVWNILLDLLKGLKHLHDH--------GLIHLDIKPANIFLSKDGVCKLGDFGLV 147
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 41349437 385 VKFnsDTNEVDvplNTRVGTKRYMAPEVLDESLNKNhfqpyimADIYSFGLIIWEMA 441
Cdd:cd14050 148 VEL--DKEDIH---DAQEGDPRYMAPELLQGSFTKA-------ADIFSLGITILELA 192
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
235-514 1.76e-17

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: 82.35  E-value: 1.76e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 235 QMVRQVGKGRYGEVWMG--KWRGEKVAVKVF-FTTEEASWFRET--EIYQTVLMRHENILGFIAADIKGTgswtQLYLIT 309
Cdd:cd06626   3 QRGNKIGEGTFGKVYTAvnLDTGELMAMKEIrFQDNDPKTIKEIadEMKVLEGLDHPNLVRYYGVEVHRE----EVYIFM 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 310 DYHENGSLYDFLKCATLDTRALLKL-AYSAACGLCHLHTeiygtQGkpaIAHRDLKSKNILIKKNGSCCIADLGLAVKF- 387
Cdd:cd06626  79 EYCQEGTLEELLRHGRILDEAVIRVyTLQLLEGLAYLHE-----NG---IVHRDIKPANIFLDSNGLIKLGDFGSAVKLk 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 388 NSDTNEVDVPLNTRVGTKRYMAPEVLDESLNKNHFQPyimADIYSFGLIIWEMArrciTGgiveeyQLPYYNMvpsDPSY 467
Cdd:cd06626 151 NNTTTMAPGEVNSLVGTPAYMAPEVITGNKGEGHGRA---ADIWSLGCVVLEMA----TG------KRPWSEL---DNEW 214
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 41349437 468 EDMREVVCvKRLRPIVSNRWNSDEClravLKLMSECWAHNPASRLTA 514
Cdd:cd06626 215 AIMYHVGM-GHKPPIPDSLQLSPEG----KDFLSRCLESDPKKRPTA 256
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
233-525 2.02e-17

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: 82.85  E-value: 2.02e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 233 QIQMVRQVGKGRYGEVWMGKWRG------EKVAVKVFFTTEEAS------WFRETEIYQTVlMRHENILGFIaadikgtG 300
Cdd:cd05053  13 RLTLGKPLGEGAFGQVVKAEAVGldnkpnEVVTVAVKMLKDDATekdlsdLVSEMEMMKMI-GKHKNIINLL-------G 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 301 SWTQ---LYLITDYHENGSLYDFLKC-----------------ATLDTRALLKLAYSAACGLCHLHTeiygtqgKPAIaH 360
Cdd:cd05053  85 ACTQdgpLYVVVEYASKGNLREFLRArrppgeeaspddprvpeEQLTQKDLVSFAYQVARGMEYLAS-------KKCI-H 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 361 RDLKSKNILIKKNGSCCIADLGLAvkfnSDTNEVDV---PLNTRVGTKrYMAPEVLDESLNKNHfqpyimADIYSFGLII 437
Cdd:cd05053 157 RDLAARNVLVTEDNVMKIADFGLA----RDIHHIDYyrkTTNGRLPVK-WMAPEALFDRVYTHQ------SDVWSFGVLL 225
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 438 WEmarrcitggIVEEYQLPYYNmVPSDPSYEDMREvvcVKRLRPIVSnrwnsdeCLRAVLKLMSECWAHNPASRLTALRI 517
Cdd:cd05053 226 WE---------IFTLGGSPYPG-IPVEELFKLLKE---GHRMEKPQN-------CTQELYMLMRDCWHEVPSQRPTFKQL 285

                ....*...
gi 41349437 518 KKTLAKMV 525
Cdd:cd05053 286 VEDLDRIL 293
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
235-445 2.05e-17

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: 83.34  E-value: 2.05e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 235 QMVRQVGKGRYGEVWMG--KWRGEKVAVK----VFFTTEEAS-WFRETEIYQtvLMRHENILGFIaaDI---KGTGSWTQ 304
Cdd:cd07834   3 ELLKPIGSGAYGVVCSAydKRTGRKVAIKkisnVFDDLIDAKrILREIKILR--HLKHENIIGLL--DIlrpPSPEEFND 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 305 LYLITDYHENgSLYDFLKC-ATLDTRALLKLAYSAACGLCHLHTeiygtqgkpA-IAHRDLKSKNILIKKNGSCCIADLG 382
Cdd:cd07834  79 VYIVTELMET-DLHKVIKSpQPLTDDHIQYFLYQILRGLKYLHS---------AgVIHRDLKPSNILVNSNCDLKICDFG 148
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41349437 383 LAVKFNSDtnEVDVPLNTRVGTKRYMAPEVLdesLNKNHFQPYImaDIYSFGLIIWEMARRCI 445
Cdd:cd07834 149 LARGVDPD--EDKGFLTEYVVTRWYRAPELL---LSSKKYTKAI--DIWSVGCIFAELLTRKP 204
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
231-522 2.33e-17

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: 81.73  E-value: 2.33e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 231 AKQIQMVRQVGKGRYGEVWMGKWRGE-KVAVKVFF--TTEEASWFRETEiyqtVLMR--HENILGFIAADIKgtgsWTQL 305
Cdd:cd05059   3 PSELTFLKELGSGQFGVVHLGKWRGKiDVAIKMIKegSMSEDDFIEEAK----VMMKlsHPKLVQLYGVCTK----QRPI 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 306 YLITDYHENGSLYDFLKC--ATLDTRALLKLAYSAACGLCHLHTEIYgtqgkpaiAHRDLKSKNILIKKNGSCCIADLGL 383
Cdd:cd05059  75 FIVTEYMANGCLLNYLRErrGKFQTEQLLEMCKDVCEAMEYLESNGF--------IHRDLAARNCLVGEQNVVKVSDFGL 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 384 AvKFnsdtnEVDVPLNTRVGTK---RYMAPEVldesLNKNHFQPyiMADIYSFGLIIWEMarrcITGGiveeyQLPYYNM 460
Cdd:cd05059 147 A-RY-----VLDDEYTSSVGTKfpvKWSPPEV----FMYSKFSS--KSDVWSFGVLMWEV----FSEG-----KMPYERF 205
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41349437 461 VPSdpsyEDMREVVCVKRL-RPivsnrwnsDECLRAVLKLMSECWAHNPASRLTALRIKKTLA 522
Cdd:cd05059 206 SNS----EVVEHISQGYRLyRP--------HLAPTEVYTIMYSCWHEKPEERPTFKILLSQLT 256
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
239-521 2.46e-17

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: 81.90  E-value: 2.46e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 239 QVGKGRYGEVWMGKWRGEK--VAVKVFFTT----EEASWFRETEIYQTvlMRHENILGFIaadikgtGSWTQ---LYLIT 309
Cdd:cd05084   3 RIGRGNFGEVFSGRLRADNtpVAVKSCRETlppdLKAKFLQEARILKQ--YSHPNIVRLI-------GVCTQkqpIYIVM 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 310 DYHENGSLYDFLKC--ATLDTRALLKLAYSAACGLCHLhteiygtQGKPAIaHRDLKSKNILIKKNGSCCIADLGLAvkf 387
Cdd:cd05084  74 ELVQGGDFLTFLRTegPRLKVKELIRMVENAAAGMEYL-------ESKHCI-HRDLAARNCLVTEKNVLKISDFGMS--- 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 388 nsdTNEVDVPLNTRVGTK----RYMAPEVLdeslnkNHFQPYIMADIYSFGLIIWEMARRCITggiveeyqlPYYNmvps 463
Cdd:cd05084 143 ---REEEDGVYAATGGMKqipvKWTAPEAL------NYGRYSSESDVWSFGILLWETFSLGAV---------PYAN---- 200
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 464 dPSYEDMREVV--CVKRLRPivsnrwnsDECLRAVLKLMSECWAHNPASRLTALRIKKTL 521
Cdd:cd05084 201 -LSNQQTREAVeqGVRLPCP--------ENCPDEVYRLMEQCWEYDPRKRPSFSTVHQDL 251
STKc_KSR1 cd14152
Catalytic domain of the Serine/Threonine Kinase, Kinase Suppressor of Ras 1; STKs catalyze the ...
233-524 3.16e-17

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: 81.94  E-value: 3.16e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 233 QIQMVRQVGKGRYGEVWMGKWRGEkVAVKVF----FTTEEASWFREtEIYQTVLMRHENILGFIAADIKGtgswTQLYLI 308
Cdd:cd14152   1 QIELGELIGQGRWGKVHRGRWHGE-VAIRLLeidgNNQDHLKLFKK-EVMNYRQTRHENVVLFMGACMHP----PHLAII 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 309 TDYHENGSLYDFLK--CATLDTRALLKLAYSAACGLCHLHTEiygtqgkpAIAHRDLKSKNILIkKNGSCCIADLGL--- 383
Cdd:cd14152  75 TSFCKGRTLYSFVRdpKTSLDINKTRQIAQEIIKGMGYLHAK--------GIVHKDLKSKNVFY-DNGKVVITDFGLfgi 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 384 --AVKFNSDTNEVDVPLNTRVgtkrYMAPEVLDESL--NKNHFQPYI-MADIYSFGLIIWEMARRcitggiveeyQLPYY 458
Cdd:cd14152 146 sgVVQEGRRENELKLPHDWLC----YLAPEIVREMTpgKDEDCLPFSkAADVYAFGTIWYELQAR----------DWPLK 211
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41349437 459 NMvPSDPSYEDMREVVCVKRLRPIVSnrwnsdeCLRAVLKLMSECWAHNPASRLTALRIKKTLAKM 524
Cdd:cd14152 212 NQ-PAEALIWQIGSGEGMKQVLTTIS-------LGKEVTEILSACWAFDLEERPSFTLLMDMLEKL 269
PTK_CCK4 cd05046
Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also ...
234-523 4.19e-17

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: 81.36  E-value: 4.19e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 234 IQMVRQVGKGRYGEVWMGKWRG------EK-VAVKVFFTTEE---ASWF-RETEIYQTVlmRHENI---LGFI-AADikg 298
Cdd:cd05046   7 LQEITTLGRGEFGEVFLAKAKGieeeggETlVLVKALQKTKDenlQSEFrRELDMFRKL--SHKNVvrlLGLCrEAE--- 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 299 tgswtQLYLITDYHENGSLYDFL----------KCATLDTRALLKLAYSAACGLCHLHTEIYgtqgkpaiAHRDLKSKNI 368
Cdd:cd05046  82 -----PHYMILEYTDLGDLKQFLratkskdeklKPPPLSTKQKVALCTQIALGMDHLSNARF--------VHRDLAARNC 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 369 LIKKNGSCCIADLGLA-VKFNSD---TNEVDVPLntrvgtkRYMAPEVLDEslnkNHFQpyIMADIYSFGLIIWEmarrc 444
Cdd:cd05046 149 LVSSQREVKVSLLSLSkDVYNSEyykLRNALIPL-------RWLAPEAVQE----DDFS--TKSDVWSFGVLMWE----- 210
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 445 itggIVEEYQLPYYNMvpsdpSYEDMREVVCVKRLR-PIVSNrwnsdeCLRAVLKLMSECWAHNPASRLTALRIKKTLAK 523
Cdd:cd05046 211 ----VFTQGELPFYGL-----SDEEVLNRLQAGKLElPVPEG------CPSRLYKLMTRCWAVNPKDRPSFSELVSALGE 275
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
234-525 4.31e-17

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: 82.15  E-value: 4.31e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 234 IQMVRQVGKGRYGEVWMGKWRG-------EKVAVKVFFTTEEASwfrETEIYQ------TVLMRHENILGFIAADIKGTg 300
Cdd:cd05055  37 LSFGKTLGAGAFGKVVEATAYGlsksdavMKVAVKMLKPTAHSS---EREALMselkimSHLGNHENIVNLLGACTIGG- 112
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 301 swtQLYLITDYHENGSLYDFL---KCATLDTRALLKLAYSAACGLCHLHTeiygtqgKPAIaHRDLKSKNILIKKNGSCC 377
Cdd:cd05055 113 ---PILVITEYCCYGDLLNFLrrkRESFLTLEDLLSFSYQVAKGMAFLAS-------KNCI-HRDLAARNVLLTHGKIVK 181
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 378 IADLGLAVKFNSDTNEVdVPLNTRVGTKrYMAPEVLDESLNKnhfqpyIMADIYSFGLIIWEMARRCITggiveeyqlPY 457
Cdd:cd05055 182 ICDFGLARDIMNDSNYV-VKGNARLPVK-WMAPESIFNCVYT------FESDVWSYGILLWEIFSLGSN---------PY 244
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41349437 458 YNMvPSDPSYEDMrevvcVKRLRPIVSNRWNSDEclraVLKLMSECWAHNPASRLTALRIKKTLAKMV 525
Cdd:cd05055 245 PGM-PVDSKFYKL-----IKEGYRMAQPEHAPAE----IYDIMKTCWDADPLKRPTFKQIVQLIGKQL 302
Activin_recp pfam01064
Activin types I and II receptor domain; This Pfam entry consists of both TGF-beta receptor ...
59-131 4.67e-17

Activin types I and II receptor domain; This Pfam entry consists of both TGF-beta receptor types. This is an alignment of the hydrophilic cysteine-rich ligand-binding domains, Both receptor types, (type I and II) posses a 9 amino acid cysteine box, with the the consensus CCX{4-5}CN. The type I receptors also possess 7 extracellular residues preceding the cysteine box.


Pssm-ID: 460048  Cd Length: 78  Bit Score: 76.00  E-value: 4.67e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41349437    59 LKCYCSGH-CPDDAINNTCITNGHCFAIIEEDDQGETTL-ASGCMKYEGSDFQCKDSPKAQLRRTIECCRTNLCN 131
Cdd:pfam01064   1 LKCYCNPLkCNDDNVNFTCETDGQCFSSWELDTDGFIECvKKGCLSPEDDPFECKTSNKPHSLYRIECCKTDFCN 75
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
235-440 5.72e-17

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: 80.95  E-value: 5.72e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 235 QMVRQVGKGRYGEVWMGKWR--GEKVAVKVF------FTTEEASWFRETEIYQTVLMRHENILG------FIAADIKGTG 300
Cdd:cd14077   4 EFVKTIGAGSMGKVKLAKHIrtGEKCAIKIIprasnaGLKKEREKRLEKEISRDIRTIREAALSsllnhpHICRLRDFLR 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 301 SWTQLYLITDYHENGSLYDF-LKCATLDTRALLKLAYSAACGLCHLHteiygtqgKPAIAHRDLKSKNILIKKNGSCCIA 379
Cdd:cd14077  84 TPNHYYMLFEYVDGGQLLDYiISHGKLKEKQARKFARQIASALDYLH--------RNSIVHRDLKIENILISKSGNIKII 155
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41349437 380 DLGLAVKFNSDTNevdvpLNTRVGTKRYMAPEVLDEslnknhfQPYI--MADIYSFGLIIWEM 440
Cdd:cd14077 156 DFGLSNLYDPRRL-----LRTFCGSLYFAAPELLQA-------QPYTgpEVDVWSFGVVLYVL 206
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
240-511 6.10e-17

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: 80.86  E-value: 6.10e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 240 VGKGRYGEVWMGKWRGEKVAVKVfftteeASWFRETEIYQTV-----------LMRHENILGFIAADIKGtgswTQLYLI 308
Cdd:cd14145  14 IGIGGFGKVYRAIWIGDEVAVKA------ARHDPDEDISQTIenvrqeaklfaMLKHPNIIALRGVCLKE----PNLCLV 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 309 TDYHENGSLYDFLKCATLDTRALLKLAYSAACGLCHLHTEIYgtqgKPAIaHRDLKSKNILIKK--------NGSCCIAD 380
Cdd:cd14145  84 MEFARGGPLNRVLSGKRIPPDILVNWAVQIARGMNYLHCEAI----VPVI-HRDLKSSNILILEkvengdlsNKILKITD 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 381 LGLAVKFNSDTNEvdvplnTRVGTKRYMAPEVLDESLNKNHfqpyimADIYSFGLIIWEMarrcITGgiveeyQLPYYNM 460
Cdd:cd14145 159 FGLAREWHRTTKM------SAAGTYAWMAPEVIRSSMFSKG------SDVWSYGVLLWEL----LTG------EVPFRGI 216
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 41349437 461 VPSDPSYedmrEVVCVKRLRPIVSNrwnsdeCLRAVLKLMSECWAHNPASR 511
Cdd:cd14145 217 DGLAVAY----GVAMNKLSLPIPST------CPEPFARLMEDCWNPDPHSR 257
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
240-447 9.02e-17

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: 80.62  E-value: 9.02e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 240 VGKGRYGEVWMGKW-RGEKVAVKVFFTTEEASWFR--ETEIYQTVLMRHENI---LGFIAAdikgtgSWTQLyLITDYHE 313
Cdd:cd14664   1 IGRGGAGTVYKGVMpNGTLVAVKRLKGEGTQGGDHgfQAEIQTLGMIRHRNIvrlRGYCSN------PTTNL-LVYEYMP 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 314 NGSLYDFL-----KCATLDTRALLKLAYSAACGLCHLHTEIygtqgKPAIAHRDLKSKNILIKKNGSCCIADLGLAVKFN 388
Cdd:cd14664  74 NGSLGELLhsrpeSQPPLDWETRQRIALGSARGLAYLHHDC-----SPLIIHRDVKSNNILLDEEFEAHVADFGLAKLMD 148
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 41349437 389 SDTNEVdvpLNTRVGTKRYMAPEVLdESLNKNHfqpyiMADIYSFGLIIWEMarrcITG 447
Cdd:cd14664 149 DKDSHV---MSSVAGSYGYIAPEYA-YTGKVSE-----KSDVYSYGVVLLEL----ITG 194
PTKc_Axl cd05075
Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the ...
233-527 1.23e-16

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: 80.05  E-value: 1.23e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 233 QIQMVRQVGKGRYGEVWMGKWRGEKVAVKVFFTTEEASWFRETE----IYQTVLMR---HENILGFIAADIKGTGS--WT 303
Cdd:cd05075   1 KLALGKTLGEGEFGSVMEGQLNQDDSVLKVAVKTMKIAICTRSEmedfLSEAVCMKefdHPNVMRLIGVCLQNTESegYP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 304 QLYLITDYHENGSLYDFLKCATLD-------TRALLKLAYSAACGLCHLHTEIYgtqgkpaiAHRDLKSKNILIKKNGSC 376
Cdd:cd05075  81 SPVVILPFMKHGDLHSFLLYSRLGdcpvylpTQMLVKFMTDIASGMEYLSSKNF--------IHRDLAARNCMLNENMNV 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 377 CIADLGLAVK-FNSDTnevdvplnTRVGTKRYMAPE-VLDESLNKNHFQpyIMADIYSFGLIIWEMARRCitggiveeyQ 454
Cdd:cd05075 153 CVADFGLSKKiYNGDY--------YRQGRISKMPVKwIAIESLADRVYT--TKSDVWSFGVTMWEIATRG---------Q 213
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41349437 455 LPYYNmVPSDPSYEDMREvvcvkrlrpivSNRWNSD-ECLRAVLKLMSECWAHNPASRLTALRIKKTLAKMVES 527
Cdd:cd05075 214 TPYPG-VENSEIYDYLRQ-----------GNRLKQPpDCLDGLYELMSSCWLLNPKDRPSFETLRCELEKILKD 275
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
228-441 1.27e-16

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: 80.53  E-value: 1.27e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 228 RTIAKQIQMVRQVGKGRYGEVWMGKW--RGEKVAVKVFFTTEEaswfRETEIYQTVLM-----RHENILGFIAADIKGT- 299
Cdd:cd06637   2 RDPAGIFELVELVGNGTYGQVYKGRHvkTGQLAAIKVMDVTGD----EEEEIKQEINMlkkysHHRNIATYYGAFIKKNp 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 300 -GSWTQLYLITDYHENGSLYDFLKCATLDTRALLKLAY---SAACGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNGS 375
Cdd:cd06637  78 pGMDDQLWLVMEFCGAGSVTDLIKNTKGNTLKEEWIAYicrEILRGLSHLHQH--------KVIHRDIKGQNVLLTENAE 149
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41349437 376 CCIADLGLAVKFNSDTNEvdvpLNTRVGTKRYMAPEVLdeSLNKNHFQPY-IMADIYSFGLIIWEMA 441
Cdd:cd06637 150 VKLVDFGVSAQLDRTVGR----RNTFIGTPYWMAPEVI--ACDENPDATYdFKSDLWSLGITAIEMA 210
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
236-514 1.35e-16

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: 80.31  E-value: 1.35e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 236 MVRQVGKGRYGEVWMG--KWRGEKVAVKVFFTTEEA--------SWFRETEIYQTvlMRHENILGFIaaDIKGTGSWTQL 305
Cdd:cd07841   4 KGKKLGEGTYAVVYKArdKETGRIVAIKKIKLGERKeakdginfTALREIKLLQE--LKHPNIIGLL--DVFGHKSNINL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 306 ---YLITDYH---ENGSLydFLKCAtlDTRALLKLAYSaacGLCHLHteiygtqgKPAIAHRDLKSKNILIKKNGSCCIA 379
Cdd:cd07841  80 vfeFMETDLEkviKDKSI--VLTPA--DIKSYMLMTLR---GLEYLH--------SNWILHRDLKPNNLLIASDGVLKLA 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 380 DLGLAVKFNSDtnevDVPLNTRVGTKRYMAPEVLdesLNKNHFQPYImaDIYSFGLIIWE----------------MARR 443
Cdd:cd07841 145 DFGLARSFGSP----NRKMTHQVVTRWYRAPELL---FGARHYGVGV--DMWSVGCIFAElllrvpflpgdsdidqLGKI 215
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41349437 444 CITGGIVEE------YQLPYYN-MVPSDPsyedmrevvcvKRLRPIVSNRwnSDEClravLKLMSECWAHNPASRLTA 514
Cdd:cd07841 216 FEALGTPTEenwpgvTSLPDYVeFKPFPP-----------TPLKQIFPAA--SDDA----LDLLQRLLTLNPNKRITA 276
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
237-441 1.39e-16

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: 79.60  E-value: 1.39e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 237 VRQVGKGRYGEVWMGKWR--GEKVAVKVFF-----TTEEASWFRETEIYQTvlMRHENILGFIAAdikgTGSWTQLYLIT 309
Cdd:cd14002   6 LELIGEGSFGKVYKGRRKytGQVVALKFIPkrgksEKELRNLRQEIEILRK--LNHPNIIEMLDS----FETKKEFVVVT 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 310 DYHEnGSLYDFLKC-ATLDTRALLKLAYSAACGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNGSCCIADLGLAVKFN 388
Cdd:cd14002  80 EYAQ-GELFQILEDdGTLPEEEVRSIAKQLVSALHYLHSN--------RIIHRDMKPQNILIGKGGVVKLCDFGFARAMS 150
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 41349437 389 SDTnevdVPLNTRVGTKRYMAPEVLDEslnknhfQPY-IMADIYSFGLIIWEMA 441
Cdd:cd14002 151 CNT----LVLTSIKGTPLYMAPELVQE-------QPYdHTADLWSLGCILYELF 193
PK_GC-A_B cd14042
Pseudokinase domain of the membrane Guanylate Cyclase receptors, GC-A and GC-B; The ...
250-524 1.55e-16

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: 79.95  E-value: 1.55e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 250 MGKWRGEKVAVK-VFFTTEEASWFRETEIYQTVLMRHENILGFIAADIKGTgswtQLYLITDYHENGSLYDFLK--CATL 326
Cdd:cd14042  25 TGYYKGNLVAIKkVNKKRIDLTREVLKELKHMRDLQHDNLTRFIGACVDPP----NICILTEYCPKGSLQDILEneDIKL 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 327 DTRALLKLAYSAACGLCHLH-TEIygtqgkpaIAHRDLKSKNILIKKNGSCCIADLGLAVKFNSDTNEVDVPLNTRvgTK 405
Cdd:cd14042 101 DWMFRYSLIHDIVKGMHYLHdSEI--------KSHGNLKSSNCVVDSRFVLKITDFGLHSFRSGQEPPDDSHAYYA--KL 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 406 RYMAPEVLdeSLNKNHFQPYIMADIYSFGLIIWEMARRcitggiveeyQLPYYNMVPSDPSyedmREVVCVKR------- 478
Cdd:cd14042 171 LWTAPELL--RDPNPPPPGTQKGDVYSFGIILQEIATR----------QGPFYEEGPDLSP----KEIIKKKVrngekpp 234
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 41349437 479 LRPIVSNRWNSDEclraVLKLMSECWAHNPASRLTALRIKKTLAKM 524
Cdd:cd14042 235 FRPSLDELECPDE----VLSLMQRCWAEDPEERPDFSTLRNKLKKL 276
TFP_LU_ECD_Tkv cd23596
extracellular domain (ECD) found in Drosophila melanogaster receptor protein serine/threonine ...
59-136 1.56e-16

extracellular domain (ECD) found in Drosophila melanogaster receptor protein serine/threonine kinase Thickveins and similar proteins; Thickveins (Tkv) is a decapentaplegic (dpp) type I receptor encoded by the thick veins (tkv) gene that is expressed in a highly localized and dynamic pattern during development. Thickveins is the ortholog of the human activin receptor-like kinase (ALK)-3/6. It contains an extracellular domain (ECD), which belongs to Ly-6 antigen/uPA receptor-like (LU) superfamily and exhibits a snake toxin-like fold (also known as three-finger toxin/3FTx fold or three-fingered protein/TFP domain fold).


Pssm-ID: 467125  Cd Length: 88  Bit Score: 74.68  E-value: 1.56e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437  59 LKCYCSGHCPDDAINNTCITN--GHCFAIIEEDDQGET-----TLASGCM-KYEGSDFQCKD--SPKAQlRRTIECCR-T 127
Cdd:cd23596   1 LTCYCEGHCPEGVSNGTCEVKpgGKCFTAVEEVYNEETgeyepERTYGCLpPEEGGLMQCKGylVPHAI-PKSIECCNdT 79

                ....*....
gi 41349437 128 NLCNQYLQP 136
Cdd:cd23596  80 DFCNKDLFP 88
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
240-526 1.64e-16

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: 79.44  E-value: 1.64e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 240 VGKGRYGEVWMGKWR--GEKVAVKV-FFTTEEASWFRETEIYQTvlMRHENILGFIAADIKGTgswtQLYLITDYHENGS 316
Cdd:cd14155   1 IGSGFFSEVYKVRHRtsGQVMALKMnTLSSNRANMLREVQLMNR--LSHPNILRFMGVCVHQG----QLHALTEYINGGN 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 317 LYDFLKCAT-LDTRALLKLAYSAACGLCHLHTEiygtqgkpAIAHRDLKSKNILIKK--NG-SCCIADLGLAVKFNSDTN 392
Cdd:cd14155  75 LEQLLDSNEpLSWTVRVKLALDIARGLSYLHSK--------GIFHRDLTSKNCLIKRdeNGyTAVVGDFGLAEKIPDYSD 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 393 EVDvPLNTrVGTKRYMAPEVLdeslnknHFQPY-IMADIYSFGLIIWEMARRcitggiveeyqlpyynmVPSDPSYEDMR 471
Cdd:cd14155 147 GKE-KLAV-VGSPYWMAPEVL-------RGEPYnEKADVFSYGIILCEIIAR-----------------IQADPDYLPRT 200
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 41349437 472 EV--VCVKRLRPIVSnrwnsdECLRAVLKLMSECWAHNPASRLTALRIKKTLAKMVE 526
Cdd:cd14155 201 EDfgLDYDAFQHMVG------DCPPDFLQLAFNCCNMDPKSRPSFHDIVKTLEEILE 251
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
233-440 1.65e-16

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: 80.07  E-value: 1.65e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 233 QIQMVRQVGKGRYGEVWMGKWR--GEKVAVK-VFFTTEEA----SWFRETEIYQTvLMRHENILGFIAADIKGTGswtqL 305
Cdd:cd07832   1 RYKILGRIGEGAHGIVFKAKDRetGETVALKkVALRKLEGgipnQALREIKALQA-CQGHPYVVKLRDVFPHGTG----F 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 306 YLITDYHEnGSLYDFLKC---------ATLDTRALLKlaysaacGLCHLHteiygtqgKPAIAHRDLKSKNILIKKNGSC 376
Cdd:cd07832  76 VLVFEYML-SSLSEVLRDeerplteaqVKRYMRMLLK-------GVAYMH--------ANRIMHRDLKPANLLISSTGVL 139
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41349437 377 CIADLGLAVKFNSDTnevDVPLNTRVGTKRYMAPEVLdesLNKNHFQPYImaDIYSFGLIIWEM 440
Cdd:cd07832 140 KIADFGLARLFSEED---PRLYSHQVATRWYRAPELL---YGSRKYDEGV--DLWAVGCIFAEL 195
PK_GC_unk cd14045
Pseudokinase domain of the unknown subfamily of membrane Guanylate Cyclase receptors; The ...
251-524 1.88e-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: 79.52  E-value: 1.88e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 251 GKWRGEKVAVKVF----FTTEEAswFREtEIYQTVLMRHENILGFIAADIKgtgsWTQLYLITDYHENGSLYDFLKCATL 326
Cdd:cd14045  26 GIYDGRTVAIKKIakksFTLSKR--IRK-EVKQVRELDHPNLCKFIGGCIE----VPNVAIITEYCPKGSLNDVLLNEDI 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 327 DTRALLKLAYSA--ACGLCHLHteiygtQGKpaIAHRDLKSKNILIKKNGSCCIADLGLAVKFNSDTNEVDVPLNTRVgT 404
Cdd:cd14045  99 PLNWGFRFSFATdiARGMAYLH------QHK--IYHGRLKSSNCVIDDRWVCKIADYGLTTYRKEDGSENASGYQQRL-M 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 405 KRYMAPEVLdeslNKNHFQPYIMADIYSFGLIIWEMARRcitggiveeyqlpyynmvpSDPSYED---MREVVCVKRLRP 481
Cdd:cd14045 170 QVYLPPENH----SNTDTEPTQATDVYSYAIILLEIATR-------------------NDPVPEDdysLDEAWCPPLPEL 226
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 41349437 482 IVSNRWNSDECLRAVLKLMSECWAHNPASRLTALRIKKTLAKM 524
Cdd:cd14045 227 ISGKTENSCPCPADYVELIRRCRKNNPAQRPTFEQIKKTLHKI 269
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
283-441 2.92e-16

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: 78.74  E-value: 2.92e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 283 MRHENILGFIAADIKGTGswTQLYLITDYHENGSLYDFLK-CATLDTR----ALLKLAYSAACGLCHLHteiYGTQGKPA 357
Cdd:cd08217  56 LKHPNIVRYYDRIVDRAN--TTLYIVMEYCEGGDLAQLIKkCKKENQYipeeFIWKIFTQLLLALYECH---NRSVGGGK 130
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 358 IAHRDLKSKNILIKKNGSCCIADLGLAVKFNSDTNEVdvplNTRVGTKRYMAPEVLDEslnknhfQPY-IMADIYSFGLI 436
Cdd:cd08217 131 ILHRDLKPANIFLDSDNNVKLGDFGLARVLSHDSSFA----KTYVGTPYYMSPELLNE-------QSYdEKSDIWSLGCL 199

                ....*
gi 41349437 437 IWEMA 441
Cdd:cd08217 200 IYELC 204
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
240-440 2.95e-16

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: 78.42  E-value: 2.95e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 240 VGKGRYGEVWMGKWR--GEKVAVKVFFTTEEASWFRE---TEIyqTVL--MRHENILGFIaaDIKGTGswTQLYLITDYH 312
Cdd:cd14009   1 IGRGSFATVWKGRHKqtGEVVAIKEISRKKLNKKLQEnleSEI--AILksIKHPNIVRLY--DVQKTE--DFIYLVLEYC 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 313 ENGSLYDFLKcatldTRALLKLAySA-------ACGLCHLHteiygtqgKPAIAHRDLKSKNILIKKNGSCC---IADLG 382
Cdd:cd14009  75 AGGDLSQYIR-----KRGRLPEA-VArhfmqqlASGLKFLR--------SKNIIHRDLKPQNLLLSTSGDDPvlkIADFG 140
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 41349437 383 LAvKFNSDTNEVDvplnTRVGTKRYMAPEVLdeslnknHFQPY-IMADIYSFGLIIWEM 440
Cdd:cd14009 141 FA-RSLQPASMAE----TLCGSPLYMAPEIL-------QFQKYdAKADLWSVGAILFEM 187
STKc_RIP4_like cd14025
Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar ...
238-518 3.84e-16

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: 78.69  E-value: 3.84e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 238 RQVGKGRYGEVWMGK---WRGEkVAVKVFFTTE-EASWFRE--TEIYQTVLMRHENILGFIAADIKGTGswtqlyLITDY 311
Cdd:cd14025   2 EKVGSGGFGQVYKVRhkhWKTW-LAIKCPPSLHvDDSERMEllEEAKKMEMAKFRHILPVYGICSEPVG------LVMEY 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 312 HENGSLYDFLKCATLDTRALLKLAYSAACGLCHLHTEiygtqgKPAIAHRDLKSKNILIKKNGSCCIADLGLAvKFNSDT 391
Cdd:cd14025  75 METGSLEKLLASEPLPWELRFRIIHETAVGMNFLHCM------KPPLLHLDLKPANILLDAHYHVKISDFGLA-KWNGLS 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 392 NEVDVPLNTRVGTKRYMAPEVLDESlNKNHFQPYimaDIYSFGLIIWEMARRcitggiveeyQLPYynmvpSDPSYEDMR 471
Cdd:cd14025 148 HSHDLSRDGLRGTIAYLPPERFKEK-NRCPDTKH---DVYSFAIVIWGILTQ----------KKPF-----AGENNILHI 208
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 41349437 472 EVVCVKRLRP---IVSNRWNSdEClRAVLKLMSECWAHNPASRLTALRIK 518
Cdd:cd14025 209 MVKVVKGHRPslsPIPRQRPS-EC-QQMICLMKRCWDQDPRKRPTFQDIT 256
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
237-442 5.13e-16

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: 78.58  E-value: 5.13e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 237 VRQVGKGRYGEVWMG-KWRGEKV-AVKVFFTTEEASWFRETEIYQTVLMRHEN--ILGFIAADIKGTgswtQLYLITDYH 312
Cdd:cd06641   9 LEKIGKGSFGEVFKGiDNRTQKVvAIKIIDLEEAEDEIEDIQQEITVLSQCDSpyVTKYYGSYLKDT----KLWIIMEYL 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 313 ENGSLYDFLKCATLDTRALLKLAYSAACGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNGSCCIADLGLAVKFnSDTN 392
Cdd:cd06641  85 GGGSALDLLEPGPLDETQIATILREILKGLDYLHSE--------KKIHRDIKAANVLLSEHGEVKLADFGVAGQL-TDTQ 155
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 41349437 393 evdVPLNTRVGTKRYMAPEVLDESLNKNHfqpyimADIYSFGLIIWEMAR 442
Cdd:cd06641 156 ---IKRN*FVGTPFWMAPEVIKQSAYDSK------ADIWSLGITAIELAR 196
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
239-442 5.39e-16

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: 78.18  E-value: 5.39e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 239 QVGKGRYGEVWMG--KWRGEKVAVKVFFTTEEASWFRETEIYQTVLMRHEN--ILGFIAADIKGTgswtQLYLITDYHEN 314
Cdd:cd06642  11 RIGKGSFGEVYKGidNRTKEVVAIKIIDLEEAEDEIEDIQQEITVLSQCDSpyITRYYGSYLKGT----KLWIIMEYLGG 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 315 GSLYDFLKCATLDTRALLKLAYSAACGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNGSCCIADLGLAVKFnSDTNev 394
Cdd:cd06642  87 GSALDLLKPGPLEETYIATILREILKGLDYLHSE--------RKIHRDIKAANVLLSEQGDVKLADFGVAGQL-TDTQ-- 155
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 41349437 395 dVPLNTRVGTKRYMAPEVLDESLNKnhfqpyIMADIYSFGLIIWEMAR 442
Cdd:cd06642 156 -IKRNTFVGTPFWMAPEVIKQSAYD------FKADIWSLGITAIELAK 196
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
235-441 5.73e-16

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: 77.83  E-value: 5.73e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 235 QMVRQVGKGRYGEVWMG--KWRGEKVAVKVFFTTEEASWFRET--EIYQTVLM----RHENILGFIAADIKGTgswtQLY 306
Cdd:cd06632   3 QKGQLLGSGSFGSVYEGfnGDTGDFFAVKEVSLVDDDKKSRESvkQLEQEIALlsklRHPNIVQYYGTEREED----NLY 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 307 LITDYHENGSLYDFLK--------CATLDTRALLKlaysaacGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNGSCCI 378
Cdd:cd06632  79 IFLEYVPGGSIHKLLQrygafeepVIRLYTRQILS-------GLAYLHSR--------NTVHRDIKGANILVDTNGVVKL 143
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41349437 379 ADLGLA--VKFNSDTNEVdvplntrVGTKRYMAPEVLDESLNKNHFQpyimADIYSFGLIIWEMA 441
Cdd:cd06632 144 ADFGMAkhVEAFSFAKSF-------KGSPYWMAPEVIMQKNSGYGLA----VDIWSLGCTVLEMA 197
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
234-513 8.60e-16

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: 77.66  E-value: 8.60e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 234 IQMVRQVGKGRYGEVWM------GKWRGEKVAVKVFFT----TEEASWFRETEIYQTvlMRHENILGF--IAADIKGTGs 301
Cdd:cd05079   6 LKRIRDLGEGHFGKVELcrydpeGDNTGEQVAVKSLKPesggNHIADLKKEIEILRN--LYHENIVKYkgICTEDGGNG- 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 302 wtqLYLITDYHENGSLYDFL--KCATLDTRALLKLAYSAACGLCHLHTEIYgtqgkpaiAHRDLKSKNILIKKNGSCCIA 379
Cdd:cd05079  83 ---IKLIMEFLPSGSLKEYLprNKNKINLKQQLKYAVQICKGMDYLGSRQY--------VHRDLAARNVLVESEHQVKIG 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 380 DLGL--AVKFNSDTNEVDVPLNTRVgtkRYMAPEVLdeslnkNHFQPYIMADIYSFGLIIWEMARRCITggiveEYQ--L 455
Cdd:cd05079 152 DFGLtkAIETDKEYYTVKDDLDSPV---FWYAPECL------IQSKFYIASDVWSFGVTLYELLTYCDS-----ESSpmT 217
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41349437 456 PYYNMVpsDPSYEDMREVVCVKRLR-----PIVSNrwnsdeCLRAVLKLMSECWAHNPASRLT 513
Cdd:cd05079 218 LFLKMI--GPTHGQMTVTRLVRVLEegkrlPRPPN------CPEEVYQLMRKCWEFQPSKRTT 272
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
240-440 9.97e-16

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: 76.95  E-value: 9.97e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 240 VGKGRYGEVWMGKWR--GEKVAVKVFFTTEEASWF------RETEIYQTvlMRHENILGFIAAdIKGTgswTQLYLITDY 311
Cdd:cd14162   8 LGHGSYAVVKKAYSTkhKCKVAIKIVSKKKAPEDYlqkflpREIEVIKG--LKHPNLICFYEA-IETT---SRVYIIMEL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 312 HENGSLYDFLKCATLDTRALLKLAYSAAC-GLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNGSCCIADLGLAVKFNSD 390
Cdd:cd14162  82 AENGDLLDYIRKNGALPEPQARRWFRQLVaGVEYCHSK--------GVVHRDLKCENLLLDKNNNLKITDFGFARGVMKT 153
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 41349437 391 TNEVDVPLNTRVGTKRYMAPEVLdeslnknHFQPY--IMADIYSFGLIIWEM 440
Cdd:cd14162 154 KDGKPKLSETYCGSYAYASPEIL-------RGIPYdpFLSDIWSMGVVLYTM 198
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
274-457 1.02e-15

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: 77.27  E-value: 1.02e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 274 ETEIYQTVlmRHENILGFIAADIkgTGSWTQLYLITDYHENGSLYDFLKCAT-LDTRALLKLAYSAACGLCHLHTEiygt 352
Cdd:cd13983  50 EIEILKSL--KHPNIIKFYDSWE--SKSKKEVIFITELMTSGTLKQYLKRFKrLKLKVIKSWCRQILEGLNYLHTR---- 121
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 353 qgKPAIAHRDLKSKNILIKKN-GSCCIADLGLAVKFNSDTNEvdvplnTRVGTKRYMAPEVLDESLNKNhfqpyimADIY 431
Cdd:cd13983 122 --DPPIIHRDLKCDNIFINGNtGEVKIGDLGLATLLRQSFAK------SVIGTPEFMAPEMYEEHYDEK-------VDIY 186
                       170       180
                ....*....|....*....|....*.
gi 41349437 432 SFGLIIWEMArrciTGgiveEYqlPY 457
Cdd:cd13983 187 AFGMCLLEMA----TG----EY--PY 202
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
233-524 1.07e-15

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: 77.45  E-value: 1.07e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 233 QIQMVRQVGKGRYGEVWMGKWRGEK------VAVKVFFTTEEASWFRET--EIYQTVLMRHENILGFIaadikGTGSWTQ 304
Cdd:cd05057   8 ELEKGKVLGSGAFGTVYKGVWIPEGekvkipVAIKVLREETGPKANEEIldEAYVMASVDHPHLVRLL-----GICLSSQ 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 305 LYLITDYHENGSLYDFLK--CATLDTRALLKLAYSAACGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNGSCCIADLG 382
Cdd:cd05057  83 VQLITQLMPLGCLLDYVRnhRDNIGSQLLLNWCVQIAKGMSYLEEK--------RLVHRDLAARNVLVKTPNHVKITDFG 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 383 LAVKFNSDTNEV-----DVPLntrvgtkRYMAPEVLdeslnknHFQPYI-MADIYSFGLIIWEMarrcITGGiveeyQLP 456
Cdd:cd05057 155 LAKLLDVDEKEYhaeggKVPI-------KWMALESI-------QYRIYThKSDVWSYGVTVWEL----MTFG-----AKP 211
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41349437 457 YYNMVPSDPSyeDMREVvcVKRL-RPivsnrwnsDECLRAVLKLMSECWAHNPASRLTALRIKKTLAKM 524
Cdd:cd05057 212 YEGIPAVEIP--DLLEK--GERLpQP--------PICTIDVYMVLVKCWMIDAESRPTFKELANEFSKM 268
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
239-440 1.17e-15

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: 77.07  E-value: 1.17e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 239 QVGKGRYGEVWMGKWR--GEKVAVKVFFTTEEASWFRETEIYQT-VL--MRHENILGFIAADIKGTgswtQLYLITDYHE 313
Cdd:cd08529   7 KLGKGSFGVVYKVVRKvdGRVYALKQIDISRMSRKMREEAIDEArVLskLNSPYVIKYYDSFVDKG----KLNIVMEYAE 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 314 NGSLYDFLKCAT---LDTRALLKLAYSAACGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNGSCCIADLGLAVKFNSD 390
Cdd:cd08529  83 NGDLHSLIKSQRgrpLPEDQIWKFFIQTLLGLSHLHSK--------KILHRDIKSMNIFLDKGDNVKIGDLGVAKILSDT 154
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 41349437 391 TNEVdvplNTRVGTKRYMAPEVLDEslnknhfQPY-IMADIYSFGLIIWEM 440
Cdd:cd08529 155 TNFA----QTIVGTPYYLSPELCED-------KPYnEKSDVWALGCVLYEL 194
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
235-520 1.35e-15

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: 76.67  E-value: 1.35e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 235 QMVRQVGKGRYGEVWMGK--WRGEKVAVKVFfTTEEASWFRET-----EIYQTVLMRHENILGFIAAdikgTGSWTQLYL 307
Cdd:cd14663   3 ELGRTLGEGTFAKVKFARntKTGESVAIKII-DKEQVAREGMVeqikrEIAIMKLLRHPNIVELHEV----MATKTKIFF 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 308 ITDYHENGSLYDFL-KCATLDTRALLKLAYS--AACGLCHLHteiygtqgkpAIAHRDLKSKNILIKKNGSCCIADLGLA 384
Cdd:cd14663  78 VMELVTGGELFSKIaKNGRLKEDKARKYFQQliDAVDYCHSR----------GVFHRDLKPENLLLDEDGNLKISDFGLS 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 385 VKfnSDTNEVDVPLNTRVGTKRYMAPEVLDEslnknhfQPYI--MADIYSFGLIIWEMARRCitggiveeyqLPYynmvp 462
Cdd:cd14663 148 AL--SEQFRQDGLLHTTCGTPNYVAPEVLAR-------RGYDgaKADIWSCGVILFVLLAGY----------LPF----- 203
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 41349437 463 SDPSYEDMREVVCVKRLR-PivsnRWNSDECLRavlkLMSECWAHNPASRLTALRIKKT 520
Cdd:cd14663 204 DDENLMALYRKIMKGEFEyP----RWFSPGAKS----LIKRILDPNPSTRITVEQIMAS 254
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
238-439 1.40e-15

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: 76.53  E-value: 1.40e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 238 RQVGKGRYGEVWMGKWRGEK--VAVKVFFTTE------EASWFRETEIyQTVLmRHENIL---GFIAadikgtgSWTQLY 306
Cdd:cd14116  11 RPLGKGKFGNVYLAREKQSKfiLALKVLFKAQlekagvEHQLRREVEI-QSHL-RHPNILrlyGYFH-------DATRVY 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 307 LITDYHENGSLYDFL-KCATLDTR--ALLKLAYSAACGLCHlhteiygtqgKPAIAHRDLKSKNILIKKNGSCCIADLGL 383
Cdd:cd14116  82 LILEYAPLGTVYRELqKLSKFDEQrtATYITELANALSYCH----------SKRVIHRDIKPENLLLGSAGELKIADFGW 151
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 41349437 384 AVKFNSDTNevdvplNTRVGTKRYMAPEVLDeslNKNHFQPyimADIYSFGLIIWE 439
Cdd:cd14116 152 SVHAPSSRR------TTLCGTLDYLPPEMIE---GRMHDEK---VDLWSLGVLCYE 195
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
241-517 1.41e-15

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: 76.88  E-value: 1.41e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 241 GKGRYGEVWMGKWRGEKVAVKVF--------------------FTTEEASWFRETEIYQTVL--MRHENILGFIAADIKg 298
Cdd:cd14000   3 GDGGFGSVYRASYKGEPVAVKIFnkhtssnfanvpadtmlrhlRATDAMKNFRLLRQELTVLshLHHPSIVYLLGIGIH- 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 299 tgswtQLYLITDYHENGSLYDFLK-----CATLDTRALLKLAYSAACGLCHLHteiygtqgKPAIAHRDLKSKNILI--- 370
Cdd:cd14000  82 -----PLMLVLELAPLGSLDHLLQqdsrsFASLGRTLQQRIALQVADGLRYLH--------SAMIIYRDLKSHNVLVwtl 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 371 --KKNGSCCIADLGLAVK-FNSDTNEVDvplntrvGTKRYMAPEVLDESLNKNHfqpyiMADIYSFGLIIWEMarrcITG 447
Cdd:cd14000 149 ypNSAIIIKIADYGISRQcCRMGAKGSE-------GTPGFRAPEIARGNVIYNE-----KVDVFSFGMLLYEI----LSG 212
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41349437 448 G--IVEEYQLPyynmvpsdpsyedmREVVCVKRLRPIVSNRwnsdECL--RAVLKLMSECWAHNPASRLTALRI 517
Cdd:cd14000 213 GapMVGHLKFP--------------NEFDIHGGLRPPLKQY----ECApwPEVEVLMKKCWKENPQQRPTAVTV 268
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
235-441 1.46e-15

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: 77.08  E-value: 1.46e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 235 QMVRQVGKGRYGEVWMGKWR---GEKVAVKVF-----FTTEEASWFRETEIYQTV-LMRHENILGFIaadikgtGSWT-- 303
Cdd:cd14052   3 ANVELIGSGEFSQVYKVSERvptGKVYAVKKLkpnyaGAKDRLRRLEEVSILRELtLDGHDNIVQLI-------DSWEyh 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 304 -QLYLITDYHENGSLYDFLK----CATLDTRALLKLAYSAACGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNGSCCI 378
Cdd:cd14052  76 gHLYIQTELCENGSLDVFLSelglLGRLDEFRVWKILVELSLGLRFIHDH--------HFVHLDLKPANVLITFEGTLKI 147
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41349437 379 ADLGLAVKFnsdtnevdvPLNT---RVGTKRYMAPEVLdesLNKNHFQPyimADIYSFGLIIWEMA 441
Cdd:cd14052 148 GDFGMATVW---------PLIRgieREGDREYIAPEIL---SEHMYDKP---ADIFSLGLILLEAA 198
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
234-517 1.80e-15

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: 76.61  E-value: 1.80e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 234 IQMVRQVGKGRYGEVWMGKWRG-------EKVAVKvffTTEEASWFRE-TEIYQTV-LMRHEN------ILGFIAadikg 298
Cdd:cd05032   8 ITLIRELGQGSFGMVYEGLAKGvvkgepeTRVAIK---TVNENASMRErIEFLNEAsVMKEFNchhvvrLLGVVS----- 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 299 TGSWTqlYLITDYHENGSLYDFLKC-----------ATLDTRALLKLAYSAACGLCHLHTEIYgtqgkpaiAHRDLKSKN 367
Cdd:cd05032  80 TGQPT--LVVMELMAKGDLKSYLRSrrpeaennpglGPPTLQKFIQMAAEIADGMAYLAAKKF--------VHRDLAARN 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 368 ILIKKNGSCCIADLGLAvkfnSDTNEVDVplnTRVGTK-----RYMAPEvldeSLNKNHFQPYimADIYSFGLIIWEMAr 442
Cdd:cd05032 150 CMVAEDLTVKIGDFGMT----RDIYETDY---YRKGGKgllpvRWMAPE----SLKDGVFTTK--SDVWSFGVVLWEMA- 215
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41349437 443 rciTGGiveeyQLPYYNMvpsdpSYEDMREVVCVKRL--RPivsnrwnsDECLRAVLKLMSECWAHNPASRLTALRI 517
Cdd:cd05032 216 ---TLA-----EQPYQGL-----SNEEVLKFVIDGGHldLP--------ENCPDKLLELMRMCWQYNPKMRPTFLEI 271
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
235-517 1.92e-15

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: 76.36  E-value: 1.92e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 235 QMVRQVGKGRYGEVWM------GKWRGEKVAVK--VFFTTEEASWF-RETEIYQTvlMRHENILGFIaadikgtgSWTQ- 304
Cdd:cd14098   3 QIIDRLGSGTFAEVKKavevetGKMRAIKQIVKrkVAGNDKNLQLFqREINILKS--LEHPGIVRLI--------DWYEd 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 305 ---LYLITDYHENGSLYDFL----KCATLDTRALLKLAYSAacgLCHLHteiygtqgKPAIAHRDLKSKNILIKKNGSCC 377
Cdd:cd14098  73 dqhIYLVMEYVEGGDLMDFImawgAIPEQHARELTKQILEA---MAYTH--------SMGITHRDLKPENILITQDDPVI 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 378 --IADLGLAVKFNSDTNevdvpLNTRVGTKRYMAPEVLdESLNKNHFQPYI-MADIYSFGLIIWEMArrciTGGIveeyq 454
Cdd:cd14098 142 vkISDFGLAKVIHTGTF-----LVTFCGTMAYLAPEIL-MSKEQNLQGGYSnLVDMWSVGCLVYVML----TGAL----- 206
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 455 lpyynmvPSDPSYEDMrevvCVKRLR-------PIVSNRWnSDECLRAVLKLMSEcwahNPASRLTALRI 517
Cdd:cd14098 207 -------PFDGSSQLP----VEKRIRkgrytqpPLVDFNI-SEEAIDFILRLLDV----DPEKRMTAAQA 260
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
336-440 1.96e-15

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: 76.63  E-value: 1.96e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 336 YSA--ACGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNGSCCIADLGLAVKF-NSDTnevdvpLNTRVGTKRYMAPEV 412
Cdd:cd05605 107 YAAeiTCGLEHLHSE--------RIVYRDLKPENILLDDHGHVRISDLGLAVEIpEGET------IRGRVGTVGYMAPEV 172
                        90       100
                ....*....|....*....|....*...
gi 41349437 413 LDESlnKNHFQPyimaDIYSFGLIIWEM 440
Cdd:cd05605 173 VKNE--RYTFSP----DWWGLGCLIYEM 194
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
239-442 2.00e-15

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: 76.63  E-value: 2.00e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 239 QVGKGRYGEVWMG--KWRGEKVAVKVFFTTEEASWFRETEIYQTVLMRHEN--ILGFIAADIKGTgswtQLYLITDYHEN 314
Cdd:cd06640  11 RIGKGSFGEVFKGidNRTQQVVAIKIIDLEEAEDEIEDIQQEITVLSQCDSpyVTKYYGSYLKGT----KLWIIMEYLGG 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 315 GSLYDFLKCATLDTRALLKLAYSAACGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNGSCCIADLGLAVKFnSDTNev 394
Cdd:cd06640  87 GSALDLLRAGPFDEFQIATMLKEILKGLDYLHSE--------KKIHRDIKAANVLLSEQGDVKLADFGVAGQL-TDTQ-- 155
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 41349437 395 dVPLNTRVGTKRYMAPEVLDESLNKNHfqpyimADIYSFGLIIWEMAR 442
Cdd:cd06640 156 -IKRNTFVGTPFWMAPEVIQQSAYDSK------ADIWSLGITAIELAK 196
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
239-517 2.01e-15

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: 77.00  E-value: 2.01e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 239 QVGKGRYGEVWMG--KWRGEKVAVKVFFTTEEASwfRETEIYQTVLMR---HENILGFIAADIKGTgswtQLYLITDYHE 313
Cdd:cd06658  29 KIGEGSTGIVCIAteKHTGKQVAVKKMDLRKQQR--RELLFNEVVIMRdyhHENVVDMYNSYLVGD----ELWVVMEFLE 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 314 NGSLYDFLKCATLDTRALLKLAYSAACGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNGSCCIADLGLAVKFNSdtne 393
Cdd:cd06658 103 GGALTDIVTHTRMNEEQIATVCLSVLRALSYLHNQ--------GVIHRDIKSDSILLTSDGRIKLSDFGFCAQVSK---- 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 394 vDVP-LNTRVGTKRYMAPEVLDEslnknhfQPY-IMADIYSFGLIIWEMarrcITGgiveeyQLPYYNmvpsDPSYEDMR 471
Cdd:cd06658 171 -EVPkRKSLVGTPYWMAPEVISR-------LPYgTEVDIWSLGIMVIEM----IDG------EPPYFN----EPPLQAMR 228
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 41349437 472 EVvcVKRLRPIVSNRWNSDECLRAVLKLMsecWAHNPASRLTALRI 517
Cdd:cd06658 229 RI--RDNLPPRVKDSHKVSSVLRGFLDLM---LVREPSQRATAQEL 269
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
239-514 2.21e-15

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: 76.33  E-value: 2.21e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 239 QVGKGRYGEVWMG--KWRGEKVAVKVFFTTEEASwfRETEIYQTVLMR---HENILGFIAADIKGTgswtQLYLITDYHE 313
Cdd:cd06648  14 KIGEGSTGIVCIAtdKSTGRQVAVKKMDLRKQQR--RELLFNEVVIMRdyqHPNIVEMYSSYLVGD----ELWVVMEFLE 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 314 NGSLYDFLKCATLDTRALLKLAYSAACGLCHLHTeiygtQGkpaIAHRDLKSKNILIKKNGSCCIADLGlavkFNSDTNE 393
Cdd:cd06648  88 GGALTDIVTHTRMNEEQIATVCRAVLKALSFLHS-----QG---VIHRDIKSDSILLTSDGRVKLSDFG----FCAQVSK 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 394 vDVP-LNTRVGTKRYMAPEVLDESlnknhfqPY-IMADIYSFGLIIWEMArrcitggiveEYQLPYYNmvpsDPSYEDMR 471
Cdd:cd06648 156 -EVPrRKSLVGTPYWMAPEVISRL-------PYgTEVDIWSLGIMVIEMV----------DGEPPYFN----EPPLQAMK 213
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 41349437 472 evvcvkRLRPIVSNRWNSDECLRAVLK-LMSECWAHNPASRLTA 514
Cdd:cd06648 214 ------RIRDNEPPKLKNLHKVSPRLRsFLDRMLVRDPAQRATA 251
PTKc_ALK_LTK cd05036
Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte ...
232-511 2.25e-15

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: 76.27  E-value: 2.25e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 232 KQIQMVRQVGKGRYGEVWMGKWRGE-------KVAVKVF--FTTEEASWFRETEIYQTVLMRHENILGFIAADIKGTGSw 302
Cdd:cd05036   6 KNLTLIRALGQGAFGEVYEGTVSGMpgdpsplQVAVKTLpeLCSEQDEMDFLMEALIMSKFNHPNIVRCIGVCFQRLPR- 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 303 tqlYLITDYHENGSLYDFL--------KCATLDTRALLKLAYSAACGlCHLHTEiygtqgKPAIaHRDLKSKNILIKKNG 374
Cdd:cd05036  85 ---FILLELMAGGDLKSFLrenrprpeQPSSLTMLDLLQLAQDVAKG-CRYLEE------NHFI-HRDIAARNCLLTCKG 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 375 S---CCIADLGLAvkfnSDTNEVDVplnTRVGTK-----RYMAPEVLDESLNKNHfqpyimADIYSFGLIIWEmarrcit 446
Cdd:cd05036 154 PgrvAKIGDFGMA----RDIYRADY---YRKGGKamlpvKWMPPEAFLDGIFTSK------TDVWSFGVLLWE------- 213
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41349437 447 ggIVEEYQLPYynmvPSDPSYEDMREVVCVKRLRPivsnrwnSDECLRAVLKLMSECWAHNPASR 511
Cdd:cd05036 214 --IFSLGYMPY----PGKSNQEVMEFVTSGGRMDP-------PKNCPGPVYRIMTQCWQHIPEDR 265
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
235-441 2.76e-15

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: 76.57  E-value: 2.76e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 235 QMVRQVGKGRYGEVW--MGKWRGEKVAVKVFFTTEEASWFRETE--IYQTvLMRHENILGFIAADIKGTG-SWTQLYLIT 309
Cdd:cd06639  25 DIIETIGKGTYGKVYkvTNKKDGSLAAVKILDPISDVDEEIEAEynILRS-LPNHPNVVKFYGMFYKADQyVGGQLWLVL 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 310 DYHENGSLYDF----LKCAT-LDTRALLKLAYSAACGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNGSCCIADLGLA 384
Cdd:cd06639 104 ELCNGGSVTELvkglLKCGQrLDEAMISYILYGALLGLQHLHNN--------RIIHRDVKGNNILLTTEGGVKLVDFGVS 175
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 41349437 385 VKFNSdtneVDVPLNTRVGTKRYMAPEVLdeSLNKNHFQPY-IMADIYSFGLIIWEMA 441
Cdd:cd06639 176 AQLTS----ARLRRNTSVGTPFWMAPEVI--ACEQQYDYSYdARCDVWSLGITAIELA 227
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
234-513 3.78e-15

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: 76.09  E-value: 3.78e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 234 IQMVRQVGKGRYGEVWMGKW------RGEKVAVKVFFT----TEEASWFRETEIYQTvlMRHENILGFIAADIKGTGSWT 303
Cdd:cd05080   6 LKKIRDLGEGHFGKVSLYCYdptndgTGEMVAVKALKAdcgpQHRSGWKQEIDILKT--LYHENIVKYKGCCSEQGGKSL 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 304 QLylITDYHENGSLYDFLKCATLDTRALLKLAYSAACGLCHLHTEIYgtqgkpaiAHRDLKSKNILIKKNGSCCIADLGL 383
Cdd:cd05080  84 QL--IMEYVPLGSLRDYLPKHSIGLAQLLLFAQQICEGMAYLHSQHY--------IHRDLAARNVLLDNDRLVKIGDFGL 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 384 AVKFNSDTNEVDVPLNTRVGTKRYmAPEVLDEslnkNHFqpYIMADIYSFGLIIWEMARRCitggivEEYQLPyynmvps 463
Cdd:cd05080 154 AKAVPEGHEYYRVREDGDSPVFWY-APECLKE----YKF--YYASDVWSFGVTLYELLTHC------DSSQSP------- 213
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 41349437 464 DPSYEDMREV----VCVKRLRPIVSNRWN---SDECLRAVLKLMSECWAHNPASRLT 513
Cdd:cd05080 214 PTKFLEMIGIaqgqMTVVRLIELLERGERlpcPDKCPQEVYHLMKNCWETEASFRPT 270
PK_ILK cd14057
Pseudokinase domain of Integrin Linked Kinase; The pseudokinase domain shows similarity to ...
246-524 4.74e-15

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: 74.83  E-value: 4.74e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 246 GEVWMGKWRGEKVAVKVF----FTTEEASWFREtEIYQTVLMRHENILGFIAAdikgTGSWTQLYLITDYHENGSLYDFL 321
Cdd:cd14057   9 GELWKGRWQGNDIVAKILkvrdVTTRISRDFNE-EYPRLRIFSHPNVLPVLGA----CNSPPNLVVISQYMPYGSLYNVL 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 322 KCAT---LDTRALLKLAYSAACGLCHLHTEiygtqgKPAIAHRDLKSKNILIKKNGSCCI--ADlglaVKFN-SDTNEVD 395
Cdd:cd14057  84 HEGTgvvVDQSQAVKFALDIARGMAFLHTL------EPLIPRHHLNSKHVMIDEDMTARInmAD----VKFSfQEPGKMY 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 396 VPlntrvgtkRYMAPEVLD---ESLNKNHfqpyimADIYSFGLIIWEMARRcitggiveeyQLPYYNMVPSDPSyedMRe 472
Cdd:cd14057 154 NP--------AWMAPEALQkkpEDINRRS------ADMWSFAILLWELVTR----------EVPFADLSNMEIG---MK- 205
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 41349437 473 vVCVKRLRPIVSNRWNSDEClravlKLMSECWAHNPASRLTALRIKKTLAKM 524
Cdd:cd14057 206 -IALEGLRVTIPPGISPHMC-----KLMKICMNEDPGKRPKFDMIVPILEKM 251
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
238-519 4.93e-15

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: 75.12  E-value: 4.93e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 238 RQVGKGRYGEVWMGKWRGEK--VAVKVFFTTEE-----ASWFRETEIYQtvLMRHENILGFIaaDIKGTGSWtqLYLITD 310
Cdd:cd14071   6 RTIGKGNFAVVKLARHRITKteVAIKIIDKSQLdeenlKKIYREVQIMK--MLNHPHIIKLY--QVMETKDM--LYLVTE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 311 YHENGSLYDFL----KCATLDTRALLKLAYSAAcGLCHLHTeiygtqgkpaIAHRDLKSKNILIKKNGSCCIADLGLAVK 386
Cdd:cd14071  80 YASNGEIFDYLaqhgRMSEKEARKKFWQILSAV-EYCHKRH----------IVHRDLKAENLLLDANMNIKIADFGFSNF 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 387 FNSDTnevdvPLNTRVGTKRYMAPEVLDeslNKNHFQPYImaDIYSFGLIIWEMarrcITGGiveeyqLPYynmvpSDPS 466
Cdd:cd14071 149 FKPGE-----LLKTWCGSPPYAAPEVFE---GKEYEGPQL--DIWSLGVVLYVL----VCGA------LPF-----DGST 203
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 41349437 467 YEDMREVVCVKRLR-PIvsnrWNSDEC---LRAVLKLmsecwahNPASRLTALRIKK 519
Cdd:cd14071 204 LQTLRDRVLSGRFRiPF----FMSTDCehlIRRMLVL-------DPSKRLTIEQIKK 249
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
232-440 4.96e-15

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: 74.92  E-value: 4.96e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 232 KQIQMVRQVGKGRYGEVWMGKWRGE-KVAVKVFF--TTEEASWFRETEIYQTvlMRHENILGFIAADIKGtgswTQLYLI 308
Cdd:cd05113   4 KDLTFLKELGTGQFGVVKYGKWRGQyDVAIKMIKegSMSEDEFIEEAKVMMN--LSHEKLVQLYGVCTKQ----RPIFII 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 309 TDYHENGSLYDFLKCAT--LDTRALLKLAYSAACGLCHLHTEIYgtqgkpaiAHRDLKSKNILIKKNGSCCIADLGLAVK 386
Cdd:cd05113  78 TEYMANGCLLNYLREMRkrFQTQQLLEMCKDVCEAMEYLESKQF--------LHRDLAARNCLVNDQGVVKVSDFGLSRY 149
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 41349437 387 FnsdtneVDVPLNTRVGTK---RYMAPEVLdeslnkNHFQPYIMADIYSFGLIIWEM 440
Cdd:cd05113 150 V------LDDEYTSSVGSKfpvRWSPPEVL------MYSKFSSKSDVWAFGVLMWEV 194
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
235-441 5.59e-15

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: 74.78  E-value: 5.59e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 235 QMVRQVGKGRYGEVWMGKWRGEK---VAVKVFFTTEEASWFRETEIYQTVL--MRHENILGFIAADIKGTGswtQLYLIT 309
Cdd:cd08223   3 QFLRVIGKGSYGEVWLVRHKRDRkqyVIKKLNLKNASKRERKAAEQEAKLLskLKHPNIVSYKESFEGEDG---FLYIVM 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 310 DYHENGSLYDFLKCAT---LDTRALLKLAYSAACGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNGSCCIADLGLAVK 386
Cdd:cd08223  80 GFCEGGDLYTRLKEQKgvlLEERQVVEWFVQIAMALQYMHER--------NILHRDLKTQNIFLTKSNIIKVGDLGIARV 151
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 41349437 387 FNSDTNEVdvplNTRVGTKRYMAPEVLDeslNKnhfqPY-IMADIYSFGLIIWEMA 441
Cdd:cd08223 152 LESSSDMA----TTLIGTPYYMSPELFS---NK----PYnHKSDVWALGCCVYEMA 196
PTKc_Mer cd14204
Catalytic Domain of the Protein Tyrosine Kinase, Mer; PTKs catalyze the transfer of the ...
240-527 6.01e-15

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: 75.36  E-value: 6.01e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 240 VGKGRYGEVWMGKWR-----GEKVAVKVF----FTTEEASWFreteIYQTVLMR---HENILGFIAADIK-GTGSWTQLY 306
Cdd:cd14204  15 LGEGEFGSVMEGELQqpdgtNHKVAVKTMkldnFSQREIEEF----LSEAACMKdfnHPNVIRLLGVCLEvGSQRIPKPM 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 307 LITDYHENGSLYDFLKCATLDT-------RALLKLAYSAACGLCHLHTEIYgtqgkpaiAHRDLKSKNILIKKNGSCCIA 379
Cdd:cd14204  91 VILPFMKYGDLHSFLLRSRLGSgpqhvplQTLLKFMIDIALGMEYLSSRNF--------LHRDLAARNCMLRDDMTVCVA 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 380 DLGLAVKFNSDtnevDVPLNTRVGTK--RYMAPEVLDESLNKnhfqpyIMADIYSFGLIIWEMARRCITggiveeyqlPY 457
Cdd:cd14204 163 DFGLSKKIYSG----DYYRQGRIAKMpvKWIAVESLADRVYT------VKSDVWAFGVTMWEIATRGMT---------PY 223
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 458 ynmvPSDPSYEDMREVVCVKRLRpivsnrwNSDECLRAVLKLMSECWAHNPASRLTALRIKKTLAKMVES 527
Cdd:cd14204 224 ----PGVQNHEIYDYLLHGHRLK-------QPEDCLDELYDIMYSCWRSDPTDRPTFTQLRENLEKLLES 282
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
225-462 6.27e-15

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: 75.07  E-value: 6.27e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 225 LVQRTIAKQIQMVRQVGKGRYGEVWMGK--WRGEKVAVKVFfTTEEASWFR--ETEIYQTVLMRHENILGFIAADIkgtg 300
Cdd:cd06646   2 ILRRNPQHDYELIQRVGSGTYGDVYKARnlHTGELAAVKII-KLEPGDDFSliQQEIFMVKECKHCNIVAYFGSYL---- 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 301 SWTQLYLITDYHENGSLYDFLKCatldTRALLKLAYSAAC-----GLCHLHTeiygtQGKpaiAHRDLKSKNILIKKNGS 375
Cdd:cd06646  77 SREKLWICMEYCGGGSLQDIYHV----TGPLSELQIAYVCretlqGLAYLHS-----KGK---MHRDIKGANILLTDNGD 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 376 CCIADLGLAVKFNSDTNEvdvpLNTRVGTKRYMAPEVLDESLNKNHFQpyiMADIYSFGLIIWEMArrcitggiveEYQL 455
Cdd:cd06646 145 VKLADFGVAAKITATIAK----RKSFIGTPYWMAPEVAAVEKNGGYNQ---LCDIWAVGITAIELA----------ELQP 207

                ....*..
gi 41349437 456 PYYNMVP 462
Cdd:cd06646 208 PMFDLHP 214
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
230-525 6.77e-15

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: 75.01  E-value: 6.77e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 230 IAKQiqmvRQVGKGRYGEVWMG--KWRGEK---VAVKVF---FTTEEaswfRETEIYQTVLM---RHENILGFIAADIKg 298
Cdd:cd05063   7 ITKQ----KVIGAGEFGEVFRGilKMPGRKevaVAIKTLkpgYTEKQ----RQDFLSEASIMgqfSHHNIIRLEGVVTK- 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 299 tgsWTQLYLITDYHENGSLYDFLK--CATLDTRALLKLAYSAACGLCHLHTEIYgtqgkpaiAHRDLKSKNILIKKNGSC 376
Cdd:cd05063  78 ---FKPAMIITEYMENGALDKYLRdhDGEFSSYQLVGMLRGIAAGMKYLSDMNY--------VHRDLAARNILVNSNLEC 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 377 CIADLGLAVKFNSDTNEVdvplNTRVGTK---RYMAPEVLDeslnknhFQPYIMA-DIYSFGLIIWEMarrcITGGivee 452
Cdd:cd05063 147 KVSDFGLSRVLEDDPEGT----YTTSGGKipiRWTAPEAIA-------YRKFTSAsDVWSFGIVMWEV----MSFG---- 207
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41349437 453 yQLPYYNMvpsdPSYEDMREVVCVKRL-RPIvsnrwnsdECLRAVLKLMSECWAHNPASRLTALRIKKTLAKMV 525
Cdd:cd05063 208 -ERPYWDM----SNHEVMKAINDGFRLpAPM--------DCPSAVYQLMLQCWQQDRARRPRFVDIVNLLDKLL 268
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
234-440 7.76e-15

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: 74.68  E-value: 7.76e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 234 IQMVRQVGKGRYGEVWMGK--WRGEKVAVKVFFTTEEAS---WFRETEIYQTvLMRHENILGFIAADIKGTGSWTQLYLI 308
Cdd:cd13985   2 YQVTKQLGEGGFSYVYLAHdvNTGRRYALKRMYFNDEEQlrvAIKEIEIMKR-LCGHPNIVQYYDSAILSSEGRKEVLLL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 309 TDYHEnGSLYDFLKcATLDTR----ALLKLAYSAACGLCHLHTEiygtqgKPAIAHRDLKSKNILIKKNGSCCIADlgla 384
Cdd:cd13985  81 MEYCP-GSLVDILE-KSPPSPlseeEVLRIFYQICQAVGHLHSQ------SPPIIHRDIKIENILFSNTGRFKLCD---- 148
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 385 vkFNSDTNEvDVPLNTRVG------------TKRYMAPEVLDESLNKNhfqpyI--MADIYSFGLIIWEM 440
Cdd:cd13985 149 --FGSATTE-HYPLERAEEvniieeeiqkntTPMYRAPEMIDLYSKKP-----IgeKADIWALGCLLYKL 210
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
233-439 7.79e-15

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 76.02  E-value: 7.79e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437  233 QIQMVRQVGKGRYGEVWMGKWR--GEKVAVKVFFTTEEAS----WFRETEIYQTVlmRHENILGfiAADIKGTGSWTQLY 306
Cdd:PLN00034  75 ELERVNRIGSGAGGTVYKVIHRptGRLYALKVIYGNHEDTvrrqICREIEILRDV--NHPNVVK--CHDMFDHNGEIQVL 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437  307 LitDYHENGSLyDFLKCAtlDTRALLKLAYSAACGLCHLHteiygtqgKPAIAHRDLKSKNILIKKNGSCCIADLGLAVK 386
Cdd:PLN00034 151 L--EFMDGGSL-EGTHIA--DEQFLADVARQILSGIAYLH--------RRHIVHRDIKPSNLLINSAKNVKIADFGVSRI 217
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 41349437  387 FNSDTNevdvPLNTRVGTKRYMAPEVLDESLNKNHFQPYiMADIYSFGLIIWE 439
Cdd:PLN00034 218 LAQTMD----PCNSSVGTIAYMSPERINTDLNHGAYDGY-AGDIWSLGVSILE 265
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
243-513 8.95e-15

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: 74.46  E-value: 8.95e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 243 GRYGEVWMGKWRGEK-VAVKVFFTTEEASWFRETEIYQTVLMRHEN------ILGFIAADikgtGSWTqlyLITDYHENG 315
Cdd:cd14027   4 GGFGKVSLCFHRTQGlVVLKTVYTGPNCIEHNEALLEEGKMMNRLRhsrvvkLLGVILEE----GKYS---LVMEYMEKG 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 316 SLYDFLKCATLDTRALLKLAYSAACGLCHLHteiygtqgKPAIAHRDLKSKNILIKKNGSCCIADLGLAV-----KFNSD 390
Cdd:cd14027  77 NLMHVLKKVSVPLSVKGRIILEIIEGMAYLH--------GKGVIHKDLKPENILVDNDFHIKIADLGLASfkmwsKLTKE 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 391 TN----EVDVPLNTRVGTKRYMAPevldESLNKNHFQPYIMADIYSFGLIIWemarrcitggIVEEYQLPYYNMVPSDPS 466
Cdd:cd14027 149 EHneqrEVDGTAKKNAGTLYYMAP----EHLNDVNAKPTEKSDVYSFAIVLW----------AIFANKEPYENAINEDQI 214
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 41349437 467 YedmrevVCVKR-LRPIVSNRwnSDECLRAVLKLMSECWAHNPASRLT 513
Cdd:cd14027 215 I------MCIKSgNRPDVDDI--TEYCPREIIDLMKLCWEANPEARPT 254
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
237-440 8.98e-15

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: 74.64  E-value: 8.98e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 237 VRQVGKGRYGEVWMGKWRGEKV--AVKVFFTTEEASwFRETEIYQTVLMR---HENILGFIAAdikgtgsW---TQLYLI 308
Cdd:cd13996  11 IELLGSGGFGSVYKVRNKVDGVtyAIKKIRLTEKSS-ASEKVLREVKALAklnHPNIVRYYTA-------WveePPLYIQ 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 309 TDYHENGSLYDFLKCAT----LDTRALLKLAYSAACGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKN-GSCCIADLGL 383
Cdd:cd13996  83 MELCEGGTLRDWIDRRNssskNDRKLALELFKQILKGVSYIHSK--------GIVHRDLKPSNIFLDNDdLQVKIGDFGL 154
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41349437 384 AVKFNSDTNEVDVP----------LNTRVGTKRYMAPEVLDESLNKNHfqpyimADIYSFGLIIWEM 440
Cdd:cd13996 155 ATSIGNQKRELNNLnnnnngntsnNSVGIGTPLYASPEQLDGENYNEK------ADIYSLGIILFEM 215
PTKc_Tie1 cd05089
Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; ...
240-528 1.11e-14

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: 74.65  E-value: 1.11e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 240 VGKGRYGEV--WMGKWRGEKVAVKVFFTTEEAS------WFRETEIYqTVLMRHENILGFIAA-DIKGtgswtQLYLITD 310
Cdd:cd05089  10 IGEGNFGQVikAMIKKDGLKMNAAIKMLKEFASendhrdFAGELEVL-CKLGHHPNIINLLGAcENRG-----YLYIAIE 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 311 YHENGSLYDFLK-----------------CATLDTRALLKLAYSAACGLCHLHTEIYgtqgkpaiAHRDLKSKNILIKKN 373
Cdd:cd05089  84 YAPYGNLLDFLRksrvletdpafakehgtASTLTSQQLLQFASDVAKGMQYLSEKQF--------IHRDLAARNVLVGEN 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 374 GSCCIADLGLavkfnSDTNEVDVPLNTRVGTKRYMAPEVLDESLNKNHfqpyimADIYSFGLIIWEMARrciTGGIveey 453
Cdd:cd05089 156 LVSKIADFGL-----SRGEEVYVKKTMGRLPVRWMAIESLNYSVYTTK------SDVWSFGVLLWEIVS---LGGT---- 217
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41349437 454 qlPYYNMVPSDpSYEDMREVVCVKRLRpivsnrwnsdECLRAVLKLMSECWAHNPASRLTALRIKKTLAKMVESQ 528
Cdd:cd05089 218 --PYCGMTCAE-LYEKLPQGYRMEKPR----------NCDDEVYELMRQCWRDRPYERPPFSQISVQLSRMLEAR 279
PK_KSR2 cd14153
Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to ...
233-524 1.16e-14

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: 74.27  E-value: 1.16e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 233 QIQMVRQVGKGRYGEVWMGKWRGEkVAVKVFFTTEE-----ASWFRETEIYQTVlmRHENILGFIAADIkgtgSWTQLYL 307
Cdd:cd14153   1 QLEIGELIGKGRFGQVYHGRWHGE-VAIRLIDIERDneeqlKAFKREVMAYRQT--RHENVVLFMGACM----SPPHLAI 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 308 ITDYHENGSLYDFLKCA--TLDTRALLKLAYSAACGLCHLHTEiygtqgkpAIAHRDLKSKNILIkKNGSCCIADLGL-- 383
Cdd:cd14153  74 ITSLCKGRTLYSVVRDAkvVLDVNKTRQIAQEIVKGMGYLHAK--------GILHKDLKSKNVFY-DNGKVVITDFGLft 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 384 ---AVKFNSDTNEVDVPlntrVGTKRYMAPEVL-----DESLNKNHFQPYimADIYSFGLIIWEMARRcitggiveeyQL 455
Cdd:cd14153 145 isgVLQAGRREDKLRIQ----SGWLCHLAPEIIrqlspETEEDKLPFSKH--SDVFAFGTIWYELHAR----------EW 208
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41349437 456 PYYNMvPSDPSYEDMRevvcvKRLRPIVSNRWNSDEclraVLKLMSECWAHNPASRLTALRIKKTLAKM 524
Cdd:cd14153 209 PFKTQ-PAEAIIWQVG-----SGMKPNLSQIGMGKE----ISDILLFCWAYEQEERPTFSKLMEMLEKL 267
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
240-494 1.63e-14

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: 73.50  E-value: 1.63e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 240 VGKGRYGEV--WMGKWRGEKV--AVKVFFTTEEASWFRETEIYQT------VLMRHENILGFIAADIKGTGSWTQlylIT 309
Cdd:cd13994   1 IGKGATSVVriVTKKNPRSGVlyAVKEYRRRDDESKRKDYVKRLTseyiisSKLHHPNIVKVLDLCQDLHGKWCL---VM 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 310 DYHENGSLYDFLKcatlDTRALLKLAysAAC-------GLCHLHTeiygtQGkpaIAHRDLKSKNILIKKNGSCCIADLG 382
Cdd:cd13994  78 EYCPGGDLFTLIE----KADSLSLEE--KDCffkqilrGVAYLHS-----HG---IAHRDLKPENILLDEDGVLKLTDFG 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 383 LAVKFNsDTNEVDVPLNTR-VGTKRYMAPEVldesLNKNHFQPYiMADIYSFGLII---------WEMArrCITGGIVEE 452
Cdd:cd13994 144 TAEVFG-MPAEKESPMSAGlCGSEPYMAPEV----FTSGSYDGR-AVDVWSCGIVLfalftgrfpWRSA--KKSDSAYKA 215
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 41349437 453 Y--QLPYYNMVPSDPSYEDMREV--VCVKRLRPIVSNRWNSDECLR 494
Cdd:cd13994 216 YekSGDFTNGPYEPIENLLPSECrrLIYRMLHPDPEKRITIDEALN 261
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
235-443 1.64e-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: 73.86  E-value: 1.64e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 235 QMVRQVGKGRYGEVWMGKWR--GEKVAVK-VFFTTEE----ASWFRETEIYQTvlMRHENILGFIaaDIKGTGSwtQLYL 307
Cdd:cd07835   2 QKLEKIGEGTYGVVYKARDKltGEIVALKkIRLETEDegvpSTAIREISLLKE--LNHPNIVRLL--DVVHSEN--KLYL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 308 ITDY--HENGSLYDFLKCATLDTRALLKLAYSAACGL--CHLHTeiygtqgkpaIAHRDLKSKNILIKKNGSCCIADLGL 383
Cdd:cd07835  76 VFEFldLDLKKYMDSSPLTGLDPPLIKSYLYQLLQGIafCHSHR----------VLHRDLKPQNLLIDTEGALKLADFGL 145
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41349437 384 AVKFNsdtnevdVPLNT---RVGTKRYMAPEVLdesLNKNHFQPYImaDIYSFGLIIWEMARR 443
Cdd:cd07835 146 ARAFG-------VPVRTythEVVTLWYRAPEIL---LGSKHYSTPV--DIWSVGCIFAEMVTR 196
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
241-440 2.01e-14

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: 73.99  E-value: 2.01e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 241 GKGRYGEVW--MGKWRGEKVAVKVF---FTTEEASWFRETEI-YQTvlMRHENILGFIaadikgtgSW----TQLYLITD 310
Cdd:cd14090  11 GEGAYASVQtcINLYTGKEYAVKIIekhPGHSRSRVFREVETlHQC--QGHPNILQLI--------EYfeddERFYLVFE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 311 YHENGSLYDFL-KCATLDTRALLKLAYSAACGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNGSCC---IADLGLA-- 384
Cdd:cd14090  81 KMRGGPLLSHIeKRVHFTEQEASLVVRDIASALDFLHDK--------GIAHRDLKPENILCESMDKVSpvkICDFDLGsg 152
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 41349437 385 VKFNSDTNE-VDVP-LNTRVGTKRYMAPEVLDESLNKNHFqpY-IMADIYSFGLIIWEM 440
Cdd:cd14090 153 IKLSSTSMTpVTTPeLLTPVGSAEYMAPEVVDAFVGEALS--YdKRCDLWSLGVILYIM 209
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
240-443 2.02e-14

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: 73.70  E-value: 2.02e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 240 VGKGRYGEVW--MGKWRGEKVAVKVFFTTEEASwfRETEIYQTVLMR---HENILGFIAADIKGTgswtQLYLITDYHEN 314
Cdd:cd14154   1 LGKGFFGQAIkvTHRETGEVMVMKELIRFDEEA--QRNFLKEVKVMRsldHPNVLKFIGVLYKDK----KLNLITEYIPG 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 315 GSLYDFLK--CATLDTRALLKLAYSAACGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNGSCCIADLGLAVKFNSDTN 392
Cdd:cd14154  75 GTLKDVLKdmARPLPWAQRVRFAKDIASGMAYLHSM--------NIIHRDLNSHNCLVREDKTVVVADFGLARLIVEERL 146
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41349437 393 EVDVPLN----------------TRVGTKRYMAPEVL-----DESLnknhfqpyimaDIYSFGLIIWEMARR 443
Cdd:cd14154 147 PSGNMSPsetlrhlkspdrkkryTVVGNPYWMAPEMLngrsyDEKV-----------DIFSFGIVLCEIIGR 207
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
240-522 2.24e-14

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: 73.12  E-value: 2.24e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 240 VGKGRYGEVWMGKWRgEKVAVKVFFTTEE------ASWFRETEIYQTvlMRHENILGFIaadikgtGSWTQ---LYLITD 310
Cdd:cd05085   4 LGKGNFGEVYKGTLK-DKTPVAVKTCKEDlpqelkIKFLSEARILKQ--YDHPNIVKLI-------GVCTQrqpIYIVME 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 311 YHENGSLYDFL--KCATLDTRALLKLAYSAACGLCHLhteiygtQGKPAIaHRDLKSKNILIKKNGSCCIADLGLAVKFN 388
Cdd:cd05085  74 LVPGGDFLSFLrkKKDELKTKQLVKFSLDAAAGMAYL-------ESKNCI-HRDLAARNCLVGENNALKISDFGMSRQED 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 389 ----SDTNEVDVPLntrvgtkRYMAPEVLdeslnkNHFQPYIMADIYSFGLIIWEMarrcITGGIVeeyqlPYYNMvpsd 464
Cdd:cd05085 146 dgvySSSGLKQIPI-------KWTAPEAL------NYGRYSSESDVWSFGILLWET----FSLGVC-----PYPGM---- 199
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 41349437 465 pSYEDMREVVcVKRLRPIVSNRwnsdeCLRAVLKLMSECWAHNPASRLTALRIKKTLA 522
Cdd:cd05085 200 -TNQQAREQV-EKGYRMSAPQR-----CPEDIYKIMQRCWDYNPENRPKFSELQKELA 250
PTKc_c-ros cd05044
Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the ...
240-521 2.34e-14

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: 73.22  E-value: 2.34e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 240 VGKGRYGEVWMGKWRGE--------KVAVKVF---FTTEEASWFreteIYQTVLM---RHENILGFIAADIKGTgswtQL 305
Cdd:cd05044   3 LGSGAFGEVFEGTAKDIlgdgsgetKVAVKTLrkgATDQEKAEF----LKEAHLMsnfKHPNILKLLGVCLDND----PQ 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 306 YLITDYHENGSLYDFLK--------CATLDTRALLKLAYSAACGLCHLHteiygtqgKPAIAHRDLKSKNILIKKNGSCC 377
Cdd:cd05044  75 YIILELMEGGDLLSYLRaarptaftPPLLTLKDLLSICVDVAKGCVYLE--------DMHFVHRDLAARNCLVSSKDYRE 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 378 ----IADLGLAVK-FNSDTNEVD----VPLntrvgtkRYMAPEVLDESLNKNHfqpyimADIYSFGLIIWEMarrcITGG 448
Cdd:cd05044 147 rvvkIGDFGLARDiYKNDYYRKEgeglLPV-------RWMAPESLVDGVFTTQ------SDVWAFGVLMWEI----LTLG 209
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41349437 449 iveeyQLPYynmvPSDPSYEDMREVVCVKRLRPivsnrwnSDECLRAVLKLMSECWAHNPASRLTALRIKKTL 521
Cdd:cd05044 210 -----QQPY----PARNNLEVLHFVRAGGRLDQ-------PDNCPDDLYELMLRCWSTDPEERPSFARILEQL 266
PTKc_Tie cd05047
Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
240-526 2.37e-14

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: 73.15  E-value: 2.37e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 240 VGKGRYGEVW--MGKWRGEKVAVKVFFTTEEAS------WFRETEIYqTVLMRHENILGFIAA-DIKGtgswtQLYLITD 310
Cdd:cd05047   3 IGEGNFGQVLkaRIKKDGLRMDAAIKRMKEYASkddhrdFAGELEVL-CKLGHHPNIINLLGAcEHRG-----YLYLAIE 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 311 YHENGSLYDFLK-----------------CATLDTRALLKLAYSAACGLCHLHTEIYgtqgkpaiAHRDLKSKNILIKKN 373
Cdd:cd05047  77 YAPHGNLLDFLRksrvletdpafaianstASTLSSQQLLHFAADVARGMDYLSQKQF--------IHRDLAARNILVGEN 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 374 GSCCIADLGLavkfnSDTNEVDVPLNTRVGTKRYMAPEVLDESLNKNHfqpyimADIYSFGLIIWEMARrciTGGIveey 453
Cdd:cd05047 149 YVAKIADFGL-----SRGQEVYVKKTMGRLPVRWMAIESLNYSVYTTN------SDVWSYGVLLWEIVS---LGGT---- 210
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41349437 454 qlPYYNMVPSDpSYEDMREVVCVKRLRpivsnrwnsdECLRAVLKLMSECWAHNPASRLTALRIKKTLAKMVE 526
Cdd:cd05047 211 --PYCGMTCAE-LYEKLPQGYRLEKPL----------NCDDEVYDLMRQCWREKPYERPSFAQILVSLNRMLE 270
PTKc_Ror cd05048
Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan ...
228-511 2.42e-14

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: 73.56  E-value: 2.42e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 228 RTIAKQIQMVRQVGKGRYGEVWMGKWRG-------EKVAVKVFftTEEAS------WFRETEIYQTvlMRHENILGFIAA 294
Cdd:cd05048   1 EIPLSAVRFLEELGEGAFGKVYKGELLGpsseesaISVAIKTL--KENASpktqqdFRREAELMSD--LQHPNIVCLLGV 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 295 DIKGtgswtQLY-LITDYHENGSLYDFL-----------------KCATLDTRALLKLAYSAACGLCHLHTEIYgtqgkp 356
Cdd:cd05048  77 CTKE-----QPQcMLFEYMAHGDLHEFLvrhsphsdvgvssdddgTASSLDQSDFLHIAIQIAAGMEYLSSHHY------ 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 357 aiAHRDLKSKNILIKKNGSCCIADLGLAVK-FNSDTNEVdvpLNTRVGTKRYMAPevldESLNKNHFQPyiMADIYSFGL 435
Cdd:cd05048 146 --VHRDLAARNCLVGDGLTVKISDFGLSRDiYSSDYYRV---QSKSLLPVRWMPP----EAILYGKFTT--ESDVWSFGV 214
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41349437 436 IIWEmarrcitggiVEEYQL-PYYNMvpsdpSYEDMREVVcvkRLRPIVSnrwNSDECLRAVLKLMSECWAHNPASR 511
Cdd:cd05048 215 VLWE----------IFSYGLqPYYGY-----SNQEVIEMI---RSRQLLP---CPEDCPARVYSLMVECWHEIPSRR 270
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
235-514 2.97e-14

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: 73.24  E-value: 2.97e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 235 QMVRQVGKGRYGEVWMGKWRGEKV--AVKVFFTTEEAS---WFRETEIYQTVlmRHENILGFIAADIKGTgswtQLYLIT 309
Cdd:cd06611   8 EIIGELGDGAFGKVYKAQHKETGLfaAAKIIQIESEEEledFMVEIDILSEC--KHPNIVGLYEAYFYEN----KLWILI 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 310 DYHENGSLYDFLkcatLDTRALLKLAYSAAC------GLCHLHTEIygtqgkpaIAHRDLKSKNILIKKNGSCCIADLGL 383
Cdd:cd06611  82 EFCDGGALDSIM----LELERGLTEPQIRYVcrqmleALNFLHSHK--------VIHRDLKAGNILLTLDGDVKLADFGV 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 384 AVKFNSDTNEVDvplnTRVGTKRYMAPEVLDESLNKNhfQPY-IMADIYSFGLIIWEMARRcitggiveeyQLPYYNMVP 462
Cdd:cd06611 150 SAKNKSTLQKRD----TFIGTPYWMAPEVVACETFKD--NPYdYKADIWSLGITLIELAQM----------EPPHHELNP 213
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 41349437 463 sdpsyedMREVVCVKRLRP---IVSNRWNSDecLRAVLKlmsECWAHNPASRLTA 514
Cdd:cd06611 214 -------MRVLLKILKSEPptlDQPSKWSSS--FNDFLK---SCLVKDPDDRPTA 256
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
240-440 3.23e-14

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: 73.05  E-value: 3.23e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 240 VGKGRYGEVW--MGKWRGEKVAVKVFFTTEEASwfRETEIYQTVLMR---HENILGFIAADIKGTgswtQLYLITDYHEN 314
Cdd:cd14222   1 LGKGFFGQAIkvTHKATGKVMVMKELIRCDEET--QKTFLTEVKVMRsldHPNVLKFIGVLYKDK----RLNLLTEFIEG 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 315 GSLYDFLKCATLDT-RALLKLAYSAACGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNGSCCIADLGLAVKFNSDTNE 393
Cdd:cd14222  75 GTLKDFLRADDPFPwQQKVSFAKGIASGMAYLHSM--------SIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEEKKK 146
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41349437 394 --VDVPLN--------------TRVGTKRYMAPEVldesLNKNHFQPYImaDIYSFGLIIWEM 440
Cdd:cd14222 147 ppPDKPTTkkrtlrkndrkkryTVVGNPYWMAPEM----LNGKSYDEKV--DIFSFGIVLCEI 203
PTKc_TAM cd05035
Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer ...
238-525 3.35e-14

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: 72.95  E-value: 3.35e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 238 RQVGKGRYGEVWMGKWRGE-----KVAVKVFFTTEEASWFRETEIYQTVLMR---HENILGFIAADIKGT--GSWTQLYL 307
Cdd:cd05035   5 KILGEGEFGSVMEAQLKQDdgsqlKVAVKTMKVDIHTYSEIEEFLSEAACMKdfdHPNVMRLIGVCFTASdlNKPPSPMV 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 308 ITDYHENGSLYDFLKCATLD-------TRALLKLAYSAACGLCHLHTEIYgtqgkpaiAHRDLKSKNILIKKNGSCCIAD 380
Cdd:cd05035  85 ILPFMKHGDLHSYLLYSRLGglpeklpLQTLLKFMVDIAKGMEYLSNRNF--------IHRDLAARNCMLDENMTVCVAD 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 381 LGLAVKFNSDtnevDVPLNTRVGTK--RYMAPevldESLNKNHFQPyiMADIYSFGLIIWEMARRCitggiveeyQLPYY 458
Cdd:cd05035 157 FGLSRKIYSG----DYYRQGRISKMpvKWIAL----ESLADNVYTS--KSDVWSFGVTMWEIATRG---------QTPYP 217
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41349437 459 NmVPSDPSYEDMREvvcvkrlrpivSNRWNS-DECLRAVLKLMSECWAHNPASRLTALRIKKTLAKMV 525
Cdd:cd05035 218 G-VENHEIYDYLRN-----------GNRLKQpEDCLDEVYFLMYFCWTVDPKDRPTFTKLREVLENIL 273
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
241-440 3.49e-14

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: 72.79  E-value: 3.49e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 241 GKGRYGEVWM--GKWRGEKVAVKVFFTTEEASWFRETEIYQTVLMR--HENILGFIAAdikgtgsWTQ---LYLITDYHE 313
Cdd:cd14046  15 GKGAFGQVVKvrNKLDGRYYAIKKIKLRSESKNNSRILREVMLLSRlnHQHVVRYYQA-------WIEranLYIQMEYCE 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 314 NGSLYDFLKCATL-DTRALLKLAYSAACGLCHLHTeiygtQGkpaIAHRDLKSKNILIKKNGSCCIADLGLA--VKFNSD 390
Cdd:cd14046  88 KSTLRDLIDSGLFqDTDRLWRLFRQILEGLAYIHS-----QG---IIHRDLKPVNIFLDSNGNVKIGDFGLAtsNKLNVE 159
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41349437 391 T------------NEVDVPLNTRVGTKRYMAPEVLDeSLNKNHFQPyimADIYSFGLIIWEM 440
Cdd:cd14046 160 LatqdinkstsaaLGSSGDLTGNVGTALYVAPEVQS-GTKSTYNEK---VDMYSLGIIFFEM 217
PTKc_Trk cd05049
Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze ...
231-523 4.19e-14

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: 72.88  E-value: 4.19e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 231 AKQIQMVRQVGKGRYGEVWMGKWR-----GEK--VAVKVFFTTEEAS----WFRETEIYQTvlMRHENILGFIAADIKGT 299
Cdd:cd05049   4 RDTIVLKRELGEGAFGKVFLGECYnlepeQDKmlVAVKTLKDASSPDarkdFEREAELLTN--LQHENIVKFYGVCTEGD 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 300 gswtQLYLITDYHENGSLYDFLKCATLDTRA---------------LLKLAYSAACGLCHLHTEIYgtqgkpaiAHRDLK 364
Cdd:cd05049  82 ----PLLMVFEYMEHGDLNKFLRSHGPDAAFlasedsapgeltlsqLLHIAVQIASGMVYLASQHF--------VHRDLA 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 365 SKNILIKKNGSCCIADLGLAvkfnSDTNEVDVplnTRVGTK-----RYMAPEvldeSLNKNHFQpyIMADIYSFGLIIWE 439
Cdd:cd05049 150 TRNCLVGTNLVVKIGDFGMS----RDIYSTDY---YRVGGHtmlpiRWMPPE----SILYRKFT--TESDVWSFGVVLWE 216
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 440 MarrcITGGiveeyQLPYYNMvpsdpSYEDMREVVCVKRL--RPivsnrwnsDECLRAVLKLMSECWAHNPASRLTALRI 517
Cdd:cd05049 217 I----FTYG-----KQPWFQL-----SNTEVIECITQGRLlqRP--------RTCPSEVYAVMLGCWKREPQQRLNIKDI 274

                ....*.
gi 41349437 518 KKTLAK 523
Cdd:cd05049 275 HKRLQE 280
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
235-519 4.47e-14

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: 72.22  E-value: 4.47e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 235 QMVRQVGKGRYGEV----WMGKWRGEKVAVKVFFTTEEASWF------RETEIYQTVlmRHENILGFIaaDIKGTGSwtQ 304
Cdd:cd14080   3 RLGKTIGEGSYSKVklaeYTKSGLKEKVACKIIDKKKAPKDFlekflpRELEILRKL--RHPNIIQVY--SIFERGS--K 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 305 LYLITDYHENGSLYDF-LKCATLDTRALLKLAYSAACGLCHLHTeiygtQGkpaIAHRDLKSKNILIKKNGSCCIADLGL 383
Cdd:cd14080  77 VFIFMEYAEHGDLLEYiQKRGALSESQARIWFRQLALAVQYLHS-----LD---IAHRDLKCENILLDSNNNVKLSDFGF 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 384 AvKFNSDtNEVDVPLNTRVGTKRYMAPEVLDEslnknhfQPYI--MADIYSFGLIIWEMarrcITGgiveeyqlpyynMV 461
Cdd:cd14080 149 A-RLCPD-DDGDVLSKTFCGSAAYAAPEILQG-------IPYDpkKYDIWSLGVILYIM----LCG------------SM 203
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41349437 462 PSDPS-----YED--MREVVCVKRLRPIvsnrwnSDECLRAVLKLMSecwaHNPASRLTALRIKK 519
Cdd:cd14080 204 PFDDSnikkmLKDqqNRKVRFPSSVKKL------SPECKDLIDQLLE----PDPTKRATIEEILN 258
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
235-447 4.56e-14

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: 73.48  E-value: 4.56e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 235 QMVRQVGKGRYGEVWMGKWR--GEKVAVKV----FFTTEEAS-WFRETEIYQtvLMRHENILGFIaaDIKGTGS----WT 303
Cdd:cd07851  18 QNLSPVGSGAYGQVCSAFDTktGRKVAIKKlsrpFQSAIHAKrTYRELRLLK--HMKHENVIGLL--DVFTPASsledFQ 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 304 QLYLITdyHENGS-LYDFLKCATLDTRALLKLAYSAACGLCHLHTeiygtqgkPAIAHRDLKSKNILIKKNGSCCIADLG 382
Cdd:cd07851  94 DVYLVT--HLMGAdLNNIVKCQKLSDDHIQFLVYQILRGLKYIHS--------AGIIHRDLKPSNLAVNEDCELKILDFG 163
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41349437 383 LAVKFNSDtnevdvpLNTRVGTKRYMAPEVLdesLNKNHFQPYImaDIYSFGLIIWEMarrcITG 447
Cdd:cd07851 164 LARHTDDE-------MTGYVATRWYRAPEIM---LNWMHYNQTV--DIWSVGCIMAEL----LTG 212
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
336-442 4.71e-14

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: 72.56  E-value: 4.71e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 336 YSA--ACGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNGSCCIADLGLAVKFNSDTnevdvPLNTRVGTKRYMAPEVL 413
Cdd:cd05577 100 YAAeiICGLEHLHNR--------FIVYRDLKPENILLDDHGHVRISDLGLAVEFKGGK-----KIKGRVGTHGYMAPEVL 166
                        90       100
                ....*....|....*....|....*....
gi 41349437 414 DESLNKNHfqpyiMADIYSFGLIIWEMAR 442
Cdd:cd05577 167 QKEVAYDF-----SVDWFALGCMLYEMIA 190
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
239-514 7.05e-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: 72.33  E-value: 7.05e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 239 QVGKGRYGEVWMG--KWRGEKVAVKVFFTTEEASwfRETEIYQTVLMR---HENILGFIAADIKGTgswtQLYLITDYHE 313
Cdd:cd06659  28 KIGEGSTGVVCIAreKHSGRQVAVKMMDLRKQQR--RELLFNEVVIMRdyqHPNVVEMYKSYLVGE----ELWVLMEYLQ 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 314 NGSLYDFLKCATLDTRALLKLAYSAACGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNGSCCIADLGLAVKFNSdtne 393
Cdd:cd06659 102 GGALTDIVSQTRLNEEQIATVCEAVLQALAYLHSQ--------GVIHRDIKSDSILLTLDGRVKLSDFGFCAQISK---- 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 394 vDVP-LNTRVGTKRYMAPEVLDESlnknhfqPY-IMADIYSFGLIIWEmarrcitggiveeyqlpyynMVPSDPSYEDMR 471
Cdd:cd06659 170 -DVPkRKSLVGTPYWMAPEVISRC-------PYgTEVDIWSLGIMVIE--------------------MVDGEPPYFSDS 221
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 41349437 472 EVVCVKRLR----PIVSNRWNSDECLRAVLKLMsecWAHNPASRLTA 514
Cdd:cd06659 222 PVQAMKRLRdsppPKLKNSHKASPVLRDFLERM---LVRDPQERATA 265
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
238-440 8.49e-14

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: 71.86  E-value: 8.49e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 238 RQVGKGRYGEVWMGKWR--GEKVAVKV----FFTTE--EASWFRETEIYQtvLMRHENI--LGFIAADIkgtgswTQLYL 307
Cdd:cd05581   7 KPLGEGSYSTVVLAKEKetGKEYAIKVldkrHIIKEkkVKYVTIEKEVLS--RLAHPGIvkLYYTFQDE------SKLYF 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 308 ITDYHENGSLYDFL-KCATLDTRALlKLaYSA--ACGLCHLHTeiygtQGkpaIAHRDLKSKNILIKKNGSCCIADLGLA 384
Cdd:cd05581  79 VLEYAPNGDLLEYIrKYGSLDEKCT-RF-YTAeiVLALEYLHS-----KG---IIHRDLKPENILLDEDMHIKITDFGTA 148
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41349437 385 VKFNS---------DTNEVDVPLNTR----VGTKRYMAPEVLDEslNKNHFQpyimADIYSFGLIIWEM 440
Cdd:cd05581 149 KVLGPdsspestkgDADSQIAYNQARaasfVGTAEYVSPELLNE--KPAGKS----SDLWALGCIIYQM 211
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
230-442 1.20e-13

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: 72.39  E-value: 1.20e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 230 IAKQIQMVRQVGKGRYGEV---WMGKWRgEKVAVKVF---FTT--EEASWFRETEIYQTvlMRHENILGFIAADIKGTG- 300
Cdd:cd07878  13 VPERYQNLTPVGSGAYGSVcsaYDTRLR-QKVAVKKLsrpFQSliHARRTYRELRLLKH--MKHENVIGLLDVFTPATSi 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 301 -SWTQLYLITDYHeNGSLYDFLKCATLDTRALLKLAYSAACGLCHLHTeiygtqgkPAIAHRDLKSKNILIKKNGSCCIA 379
Cdd:cd07878  90 eNFNEVYLVTNLM-GADLNNIVKCQKLSDEHVQFLIYQLLRGLKYIHS--------AGIIHRDLKPSNVAVNEDCELRIL 160
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41349437 380 DLGLAvkfnsdtNEVDVPLNTRVGTKRYMAPEVLdesLNKNHFQPYImaDIYSFGLIIWEMAR 442
Cdd:cd07878 161 DFGLA-------RQADDEMTGYVATRWYRAPEIM---LNWMHYNQTV--DIWSVGCIMAELLK 211
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
235-511 1.24e-13

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: 70.98  E-value: 1.24e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 235 QMVRQVGKGRYGEVWM--GKWRGEKVAVKVFFTTEEASW------FReteiYQTVLMRHENILGFIAADIK---GTGSWT 303
Cdd:cd13975   3 KLGRELGRGQYGVVYAcdSWGGHFPCALKSVVPPDDKHWndlaleFH----YTRSLPKHERIVSLHGSVIDysyGGGSSI 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 304 QLYLITD-YHENgsLYDFLKcATLDTRALLKLAYSAACGLCHLHTeiygtQGkpaIAHRDLKSKNILIKKNGSCCIADLG 382
Cdd:cd13975  79 AVLLIMErLHRD--LYTGIK-AGLSLEERLQIALDVVEGIRFLHS-----QG---LVHRDIKLKNVLLDKKNRAKITDLG 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 383 LAVKfnsdtnEVdVPLNTRVGTKRYMAPEVLDeslnkNHFQPYImaDIYSFGLIIWEmarrcITGGIVeeyQLP--YYNM 460
Cdd:cd13975 148 FCKP------EA-MMSGSIVGTPIHMAPELFS-----GKYDNSV--DVYAFGILFWY-----LCAGHV---KLPeaFEQC 205
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 41349437 461 VPSDPSYEDMREVVCVKRLrPIVsnrwnSDECLRavlkLMSECWAHNPASR 511
Cdd:cd13975 206 ASKDHLWNNVRKGVRPERL-PVF-----DEECWN----LMEACWSGDPSQR 246
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
235-516 1.25e-13

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: 71.54  E-value: 1.25e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 235 QMVRQVGKGRYGEVWMGKWR--GEKVAVK--VFFTTEE---ASWFRETEiyqtvLMR------HENILGFIaaDI---KG 298
Cdd:cd07838   2 EEVAEIGEGAYGTVYKARDLqdGRFVALKkvRVPLSEEgipLSTIREIA-----LLKqlesfeHPNVVRLL--DVchgPR 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 299 TGSWTQLYLITDYHENgSLYDFL-KCAT--LDTRALLKLAYSAACGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNGS 375
Cdd:cd07838  75 TDRELKLTLVFEHVDQ-DLATYLdKCPKpgLPPETIKDLMRQLLRGLDFLHSH--------RIVHRDLKPQNILVTSDGQ 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 376 CCIADLGLAVKFnsdtnEVDVPLNTRVGTKRYMAPEVLdesLNKNHFQPyimADIYSFGLIIWEMA-RRCITGGIVEEYQ 454
Cdd:cd07838 146 VKLADFGLARIY-----SFEMALTSVVVTLWYRAPEVL---LQSSYATP---VDMWSVGCIFAELFnRRPLFRGSSEADQ 214
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41349437 455 LPYYNMVPSDPSYEDMREVVCVKRL----RPIVSNRWNSDECLRAVLKLMSECWAHNPASRLTALR 516
Cdd:cd07838 215 LGKIFDVIGLPSEEEWPRNSALPRSsfpsYTPRPFKSFVPEIDEEGLDLLKKMLTFNPHKRISAFE 280
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
235-442 1.35e-13

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: 70.75  E-value: 1.35e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 235 QMVRQVGKGRYGEVWMGKWRGEK--------VAVKVFFTTEEASWFRETEIYQTvlMRHENILGFIAA--DIkgtgswTQ 304
Cdd:cd05578   3 QILRVIGKGSFGKVCIVQKKDTKkmfamkymNKQKCIEKDSVRNVLNELEILQE--LEHPFLVNLWYSfqDE------ED 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 305 LYLITDYHENGSL-YDFLKCATLDTRALLKLAYSAACGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNGSCCIADLGL 383
Cdd:cd05578  75 MYMVVDLLLGGDLrYHLQQKVKFSEETVKFYICEIVLALDYLHSK--------NIIHRDIKPDNILLDEQGHVHITDFNI 146
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 41349437 384 AVKFNSDTNevdvpLNTRVGTKRYMAPEVLDeslNKNHfqpYIMADIYSFGLIIWEMAR 442
Cdd:cd05578 147 ATKLTDGTL-----ATSTSGTKPYMAPEVFM---RAGY---SFAVDWWSLGVTAYEMLR 194
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
232-440 1.47e-13

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: 71.07  E-value: 1.47e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 232 KQIQMVRQVGKGRYGEVWMGKWR--GEKVAVKVFftteeaswfretEIYQTVLMRHE-------NILG-----FIaadIK 297
Cdd:cd05580   1 DDFEFLKTLGTGSFGRVRLVKHKdsGKYYALKIL------------KKAKIIKLKQVehvlnekRILSevrhpFI---VN 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 298 GTGSWT---QLYLITDYHENGSLYDFL-KCATLDTRALLKLAYSAACGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKN 373
Cdd:cd05580  66 LLGSFQddrNLYMVMEYVPGGELFSLLrRSGRFPNDVAKFYAAEVVLALEYLHSL--------DIVYRDLKPENLLLDSD 137
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41349437 374 GSCCIADLGLAVKFNSDTnevdvplNTRVGTKRYMAPEVLdesLNKNHFQPyimADIYSFGLIIWEM 440
Cdd:cd05580 138 GHIKITDFGFAKRVKDRT-------YTLCGTPEYLAPEII---LSKGHGKA---VDWWALGILIYEM 191
PTKc_Tyro3 cd05074
Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the ...
232-511 2.18e-13

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: 70.72  E-value: 2.18e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 232 KQIQMVRQVGKGRYGEVWMGKWR-----GEKVAVKVFFTTEEASWFRETEIYQTVLMR---HENILGFIAADI--KGTGS 301
Cdd:cd05074   9 QQFTLGRMLGKGEFGSVREAQLKsedgsFQKVAVKMLKADIFSSSDIEEFLREAACMKefdHPNVIKLIGVSLrsRAKGR 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 302 WTQLYLITDYHENGSLYDFLKCA-------TLDTRALLKLAYSAACGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNG 374
Cdd:cd05074  89 LPIPMVILPFMKHGDLHTFLLMSrigeepfTLPLQTLVRFMIDIASGMEYLSSK--------NFIHRDLAARNCMLNENM 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 375 SCCIADLGLAVKFNSDTnevdvplNTRVGTK-----RYMAPEVLDESLNKNHfqpyimADIYSFGLIIWEMARRCitggi 449
Cdd:cd05074 161 TVCVADFGLSKKIYSGD-------YYRQGCAsklpvKWLALESLADNVYTTH------SDVWAFGVTMWEIMTRG----- 222
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41349437 450 veeyQLPYynmvPSDPSYEDMREVVCVKRLRpivsnrwNSDECLRAVLKLMSECWAHNPASR 511
Cdd:cd05074 223 ----QTPY----AGVENSEIYNYLIKGNRLK-------QPPDCLEDVYELMCQCWSPEPKCR 269
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
235-440 2.61e-13

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: 69.72  E-value: 2.61e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 235 QMVRQVGKGRYGEVWMGKWR--GEKVAVKVF----FTTEEASWFRETEIYQTVLMRHENILG----FIAADikgtgswtQ 304
Cdd:cd14073   4 ELLETLGKGTYGKVKLAIERatGREVAIKSIkkdkIEDEQDMVRIRREIEIMSSLNHPHIIRiyevFENKD--------K 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 305 LYLITDYHENGSLYDFL-KCATL---DTRALLKLAYSAAcGLCHLHteiygtqgkpAIAHRDLKSKNILIKKNGSCCIAD 380
Cdd:cd14073  76 IVIVMEYASGGELYDYIsERRRLperEARRIFRQIVSAV-HYCHKN----------GVVHRDLKLENILLDQNGNAKIAD 144
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41349437 381 LGLAVKFNSDTnevdvPLNTRVGTKRYMAPEVLDEslnknhfQPYI--MADIYSFGLIIWEM 440
Cdd:cd14073 145 FGLSNLYSKDK-----LLQTFCGSPLYASPEIVNG-------TPYQgpEVDCWSLGVLLYTL 194
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
238-525 2.73e-13

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: 70.81  E-value: 2.73e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 238 RQVGKGRYGEVWMGKWRG---------EKVAVKVFFT--TEE--ASWFRETEIYQtVLMRHENILGFIaadikgtGSWTQ 304
Cdd:cd05098  19 KPLGEGCFGQVVLAEAIGldkdkpnrvTKVAVKMLKSdaTEKdlSDLISEMEMMK-MIGKHKNIINLL-------GACTQ 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 305 ---LYLITDYHENGSLYDFLKC-----------------ATLDTRALLKLAYSAACGLCHLHTeiygtqgKPAIaHRDLK 364
Cdd:cd05098  91 dgpLYVIVEYASKGNLREYLQArrppgmeycynpshnpeEQLSSKDLVSCAYQVARGMEYLAS-------KKCI-HRDLA 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 365 SKNILIKKNGSCCIADLGLAvkfnSDTNEVDVPLNTRVG--TKRYMAPEVLDESLNKNHfqpyimADIYSFGLIIWEMAr 442
Cdd:cd05098 163 ARNVLVTEDNVMKIADFGLA----RDIHHIDYYKKTTNGrlPVKWMAPEALFDRIYTHQ------SDVWSFGVLLWEIF- 231
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 443 rcITGGIveeyqlPYYNmVPSDPSYEDMREvvcvkrlrpivSNRWNS-DECLRAVLKLMSECWAHNPASRLTALRIKKTL 521
Cdd:cd05098 232 --TLGGS------PYPG-VPVEELFKLLKE-----------GHRMDKpSNCTNELYMMMRDCWHAVPSQRPTFKQLVEDL 291

                ....
gi 41349437 522 AKMV 525
Cdd:cd05098 292 DRIV 295
PTKc_EphR_A cd05066
Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze ...
231-525 3.16e-13

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: 69.90  E-value: 3.16e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 231 AKQIQMVRQVGKGRYGEVWMGKWR--GEK---VAVKV----FFTTEEASWFRETEIYQTvlMRHENILGFIAADIKGTgs 301
Cdd:cd05066   3 ASCIKIEKVIGAGEFGEVCSGRLKlpGKReipVAIKTlkagYTEKQRRDFLSEASIMGQ--FDHPNIIHLEGVVTRSK-- 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 302 wtQLYLITDYHENGSLYDFLKC--ATLDTRALLKLAYSAACGLCHLHTEIYgtqgkpaiAHRDLKSKNILIKKNGSCCIA 379
Cdd:cd05066  79 --PVMIVTEYMENGSLDAFLRKhdGQFTVIQLVGMLRGIASGMKYLSDMGY--------VHRDLAARNILVNSNLVCKVS 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 380 DLGLAVKFNSDTnevDVPLNTRVGT--KRYMAPEVLdeslnknHFQPYIMA-DIYSFGLIIWEmarrcitggiVEEY-QL 455
Cdd:cd05066 149 DFGLSRVLEDDP---EAAYTTRGGKipIRWTAPEAI-------AYRKFTSAsDVWSYGIVMWE----------VMSYgER 208
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 456 PYYNMVPSDPsyedMREVVCVKRLRPIVsnrwnsdECLRAVLKLMSECWAHNPASRLTALRIKKTLAKMV 525
Cdd:cd05066 209 PYWEMSNQDV----IKAIEEGYRLPAPM-------DCPAALHQLMLDCWQKDRNERPKFEQIVSILDKLI 267
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
336-440 3.85e-13

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: 69.93  E-value: 3.85e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 336 YSA--ACGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNGSCCIADLGLAVKFNSDTnevdvPLNTRVGTKRYMAPEVL 413
Cdd:cd05607 109 YSAqiTCGILHLHSL--------KIVYRDMKPENVLLDDNGNCRLSDLGLAVEVKEGK-----PITQRAGTNGYMAPEIL 175
                        90       100
                ....*....|....*....|....*...
gi 41349437 414 DEslnknhfQPY-IMADIYSFGLIIWEM 440
Cdd:cd05607 176 KE-------ESYsYPVDWFAMGCSIYEM 196
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
240-443 4.35e-13

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: 69.60  E-value: 4.35e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 240 VGKGRYGEVWMGKWR--GEKVAVKVFFTTEEASwfRETEIYQTVLMR---HENILGFIAADIKGTgswtQLYLITDYHEN 314
Cdd:cd14221   1 LGKGCFGQAIKVTHRetGEVMVMKELIRFDEET--QRTFLKEVKVMRcleHPNVLKFIGVLYKDK----RLNFITEYIKG 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 315 GSLYDFLKcaTLDTR----ALLKLAYSAACGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNGSCCIADLGLAVKFNSD 390
Cdd:cd14221  75 GTLRGIIK--SMDSHypwsQRVSFAKDIASGMAYLHSM--------NIIHRDLNSHNCLVRENKSVVVADFGLARLMVDE 144
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41349437 391 TNEVDVPLN----------TRVGTKRYMAPEVL-----DESLnknhfqpyimaDIYSFGLIIWEMARR 443
Cdd:cd14221 145 KTQPEGLRSlkkpdrkkryTVVGNPYWMAPEMIngrsyDEKV-----------DVFSFGIVLCEIIGR 201
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
232-444 4.35e-13

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: 69.76  E-value: 4.35e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 232 KQIQMVRQVGKGRYGEVWMGKWRGEK--VAVKVFFTTE----EASWFRETEIYQTVlmRHENILGFIAADIKGTGSwtQL 305
Cdd:cd06621   1 DKIVELSSLGEGAGGSVTKCRLRNTKtiFALKTITTDPnpdvQKQILRELEINKSC--ASPYIVKYYGAFLDEQDS--SI 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 306 YLITDYHENGSL---YDFLKCATLDT--RALLKLAYSAACGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNGSCCIAD 380
Cdd:cd06621  77 GIAMEYCEGGSLdsiYKKVKKKGGRIgeKVLGKIAESVLKGLSYLHSR--------KIIHRDIKPSNILLTRKGQVKLCD 148
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41349437 381 LGLAVKFnsdTNEVDvplNTRVGTKRYMAPEVLDEslnknhfQPY-IMADIYSFGLIIWEMARRC 444
Cdd:cd06621 149 FGVSGEL---VNSLA---GTFTGTSYYMAPERIQG-------GPYsITSDVWSLGLTLLEVAQNR 200
PTKc_FGFR4 cd05099
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs ...
238-527 4.56e-13

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: 69.99  E-value: 4.56e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 238 RQVGKGRYGEV------WMGKWRGEK---VAVKVF----FTTEEASWFRETEIYQtVLMRHENILGFIaadikgtGSWTQ 304
Cdd:cd05099  18 KPLGEGCFGQVvraeayGIDKSRPDQtvtVAVKMLkdnaTDKDLADLISEMELMK-LIGKHKNIINLL-------GVCTQ 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 305 ---LYLITDYHENGSLYDFLKC-----------------ATLDTRALLKLAYSAACGLCHLhteiygtQGKPAIaHRDLK 364
Cdd:cd05099  90 egpLYVIVEYAAKGNLREFLRArrppgpdytfditkvpeEQLSFKDLVSCAYQVARGMEYL-------ESRRCI-HRDLA 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 365 SKNILIKKNGSCCIADLGLAvkfnSDTNEVDVPLNTRVGTK--RYMAPEVLDESLNKNHfqpyimADIYSFGLIIWEMAr 442
Cdd:cd05099 162 ARNVLVTEDNVMKIADFGLA----RGVHDIDYYKKTSNGRLpvKWMAPEALFDRVYTHQ------SDVWSFGILMWEIF- 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 443 rcITGGiveeyqlPYYNMVPSDPSYEDMREvvcVKRL-RPivSNrwnsdeCLRAVLKLMSECWAHNPASRLTALRIKKTL 521
Cdd:cd05099 231 --TLGG-------SPYPGIPVEELFKLLRE---GHRMdKP--SN------CTHELYMLMRECWHAVPTQRPTFKQLVEAL 290

                ....*.
gi 41349437 522 AKMVES 527
Cdd:cd05099 291 DKVLAA 296
STKc_IRAK1 cd14159
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; ...
240-439 4.89e-13

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: 69.85  E-value: 4.89e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 240 VGKGRYGEVWMGKWRGEKVAVKVFFTTEEASW------FReTEIYQTVLMRHENILGFIAADIKGtgswtQLY-LITDYH 312
Cdd:cd14159   1 IGEGGFGCVYQAVMRNTEYAVKRLKEDSELDWsvvknsFL-TEVEKLSRFRHPNIVDLAGYSAQQ-----GNYcLIYVYL 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 313 ENGSLYDFLKCAT----LDTRALLKLAYSAACGLCHLHteiygtQGKPAIAHRDLKSKNILIKKNGSCCIADLGLAvKFN 388
Cdd:cd14159  75 PNGSLEDRLHCQVscpcLSWSQRLHVLLGTARAIQYLH------SDSPSLIHGDVKSSNILLDAALNPKLGDFGLA-RFS 147
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 41349437 389 SDTNEvdvPLNTRV--------GTKRYMAPEVLDESlnknhfQPYIMADIYSFGLIIWE 439
Cdd:cd14159 148 RRPKQ---PGMSSTlartqtvrGTLAYLPEEYVKTG------TLSVEIDVYSFGVVLLE 197
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
235-440 5.03e-13

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: 70.13  E-value: 5.03e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 235 QMVRQVGKGRYGEV----WMGKWRGEKVAVKVFFTTEEASWFRETEIYQTVLMR----HENILGFIAADIKGTGSWTQLY 306
Cdd:cd07857   3 ELIKELGQGAYGIVcsarNAETSEEETVAIKKITNVFSKKILAKRALRELKLLRhfrgHKNITCLYDMDIVFPGNFNELY 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 307 LitdYHE--NGSLYDFLKCATLDTRALLK-LAYSAACGLCHLHTeiygtqgkPAIAHRDLKSKNILIKKNGSCCIADLGL 383
Cdd:cd07857  83 L---YEElmEADLHQIIRSGQPLTDAHFQsFIYQILCGLKYIHS--------ANVLHRDLKPGNLLVNADCELKICDFGL 151
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 41349437 384 AVKFNSDTNEVDVPLNTRVGTKRYMAPEVLdesLNknhFQPYIMA-DIYSFGLIIWEM 440
Cdd:cd07857 152 ARGFSENPGENAGFMTEYVATRWYRAPEIM---LS---FQSYTKAiDVWSVGCILAEL 203
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
241-517 6.12e-13

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: 68.83  E-value: 6.12e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 241 GKGRYGEVWMGKWRGEKVAVKVFFTTEEASWFREtEIYQTVLMRHENILGFIAADIKGTgswtqlYLITDYHENGSLYDF 320
Cdd:cd14068   3 GDGGFGSVYRAVYRGEDVAVKIFNKHTSFRLLRQ-ELVVLSHLHHPSLVALLAAGTAPR------MLVMELAPKGSLDAL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 321 LK--CATLDTRALLKLAYSAACGLCHLHTEIygtqgkpaIAHRDLKSKNIL---IKKNGSCC--IADLGLAVKFNSdtne 393
Cdd:cd14068  76 LQqdNASLTRTLQHRIALHVADGLRYLHSAM--------IIYRDLKPHNVLlftLYPNCAIIakIADYGIAQYCCR---- 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 394 vdVPLNTRVGTKRYMAPEVLDESLNKNHfqpyiMADIYSFGLIIWEMarrcITGG--IVEEYQLPyynmvpsdpsyEDMR 471
Cdd:cd14068 144 --MGIKTSEGTPGFRAPEVARGNVIYNQ-----QADVYSFGLLLYDI----LTCGerIVEGLKFP-----------NEFD 201
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 41349437 472 EVVCVKRLRPIVSNR----WNSDEclravlKLMSECWAHNPASRLTALRI 517
Cdd:cd14068 202 ELAIQGKLPDPVKEYgcapWPGVE------ALIKDCLKENPQCRPTSAQV 245
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
235-440 6.84e-13

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: 68.83  E-value: 6.84e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 235 QMVRQVGKGRYGEVWMGKWRGEK---VAVKVFFTT-----EEASwfrETEIYQTVLMRHENILGFIAAdIKGTGswtQLY 306
Cdd:cd08225   3 EIIKKIGEGSFGKIYLAKAKSDSehcVIKEIDLTKmpvkeKEAS---KKEVILLAKMKHPNIVTFFAS-FQENG---RLF 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 307 LITDYHENGSLYDFL---KCATLDTRALLKLAYSAACGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNGSCC-IADLG 382
Cdd:cd08225  76 IVMEYCDGGDLMKRInrqRGVLFSEDQILSWFVQISLGLKHIHDR--------KILHRDIKSQNIFLSKNGMVAkLGDFG 147
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 41349437 383 LAVKFNsDTNEVdvpLNTRVGTKRYMAPEVLDEslnknhfQPY-IMADIYSFGLIIWEM 440
Cdd:cd08225 148 IARQLN-DSMEL---AYTCVGTPYYLSPEICQN-------RPYnNKTDIWSLGCVLYEL 195
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
233-513 9.38e-13

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: 68.19  E-value: 9.38e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 233 QIQMVRQVGKGRYGEVWMGKwR---GEKVAVKVFFTTEEASWFRETEIYQTVLM---RHENILGFIAADIKGTgswtQLY 306
Cdd:cd08530   1 DFKVLKKLGKGSYGSVYKVK-RlsdNQVYALKEVNLGSLSQKEREDSVNEIRLLasvNHPNIIRYKEAFLDGN----RLC 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 307 LITDYHENGSLYDFL-----KCATLDTRALLKLAYSAACGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNGSCCIADL 381
Cdd:cd08530  76 IVMEYAPFGDLSKLIskrkkKRRLFPEDDIWRIFIQMLRGLKALHDQ--------KILHRDLKSANILLSAGDLVKIGDL 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 382 GLAVKFNSDTnevdvpLNTRVGTKRYMAPEVLDEslnknhfQPY-IMADIYSFGLIIWEMARrcitggiveeYQLPYynm 460
Cdd:cd08530 148 GISKVLKKNL------AKTQIGTPLYAAPEVWKG-------RPYdYKSDIWSLGCLLYEMAT----------FRPPF--- 201
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 41349437 461 vpSDPSYEDMREVVCVKRLrPIVSNRWNSDeclraVLKLMSECWAHNPASRLT 513
Cdd:cd08530 202 --EARTMQELRYKVCRGKF-PPIPPVYSQD-----LQQIIRSLLQVNPKKRPS 246
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
239-440 9.95e-13

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: 69.24  E-value: 9.95e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 239 QVGKGRYGEVWMGKW----RGEKVAVKVFftteEASWFRETEIYQTVL--------MRHENILGFIAADI-KGTGSwtqL 305
Cdd:cd07842   7 CIGRGTYGRVYKAKRkngkDGKEYAIKKF----KGDKEQYTGISQSACreiallreLKHENVVSLVEVFLeHADKS---V 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 306 YLITDYHEngslYDFL---------KCATLDTRALLKLAYSAACGLCHLHTEIygtqgkpaIAHRDLKSKNILIKKNGSC 376
Cdd:cd07842  80 YLLFDYAE----HDLWqiikfhrqaKRVSIPPSMVKSLLWQILNGIHYLHSNW--------VLHRDLKPANILVMGEGPE 147
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41349437 377 C----IADLGLAVKFNSdtnevdvPL------NTRVGTKRYMAPEVLdesLNKNHFQPYImaDIYSFGLIIWEM 440
Cdd:cd07842 148 RgvvkIGDLGLARLFNA-------PLkpladlDPVVVTIWYRAPELL---LGARHYTKAI--DIWAIGCIFAEL 209
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
235-455 1.01e-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: 68.69  E-value: 1.01e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 235 QMVRQVGKGRYGEVWMGKWR--GEKVAVKVFFTTEEASWFRETEIYQTVLMR---HENILGFIaaDIkgTGSWTQLYLIT 309
Cdd:cd07860   3 QKVEKIGEGTYGVVYKARNKltGEVVALKKIRLDTETEGVPSTAIREISLLKelnHPNIVKLL--DV--IHTENKLYLVF 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 310 DYHeNGSLYDFLKCATLD--TRALLK-LAYSAACGL--CHLHTeiygtqgkpaIAHRDLKSKNILIKKNGSCCIADLGLA 384
Cdd:cd07860  79 EFL-HQDLKKFMDASALTgiPLPLIKsYLFQLLQGLafCHSHR----------VLHRDLKPQNLLINTEGAIKLADFGLA 147
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41349437 385 VKFNsdtnevdVPLNT---RVGTKRYMAPEVLdesLNKNHFQPYImaDIYSFGLIIWEM-ARRCITGGIVEEYQL 455
Cdd:cd07860 148 RAFG-------VPVRTythEVVTLWYRAPEIL---LGCKYYSTAV--DIWSLGCIFAEMvTRRALFPGDSEIDQL 210
PTKc_InsR cd05061
Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer ...
232-521 1.08e-12

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: 68.84  E-value: 1.08e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 232 KQIQMVRQVGKGRYGEVWMGKWR----GE---KVAVKVffTTEEAS------WFRETEIYQTVLMRHE-NILGFIAadiK 297
Cdd:cd05061   6 EKITLLRELGQGSFGMVYEGNARdiikGEaetRVAVKT--VNESASlrerieFLNEASVMKGFTCHHVvRLLGVVS---K 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 298 GTGSWTQLYLITdyheNGSLYDFLKCATLDT-----------RALLKLAYSAACGLCHLHTEIYgtqgkpaiAHRDLKSK 366
Cdd:cd05061  81 GQPTLVVMELMA----HGDLKSYLRSLRPEAennpgrppptlQEMIQMAAEIADGMAYLNAKKF--------VHRDLAAR 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 367 NILIKKNGSCCIADLGLAvkfnSDTNEVDVplnTRVGTK-----RYMAPEvldeSLNKNHFQPYimADIYSFGLIIWE-- 439
Cdd:cd05061 149 NCMVAHDFTVKIGDFGMT----RDIYETDY---YRKGGKgllpvRWMAPE----SLKDGVFTTS--SDMWSFGVVLWEit 215
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 440 -MARRCITGgiVEEYQLPYYNMvpsDPSYEDmrevvcvkrlRPivsnrwnsDECLRAVLKLMSECWAHNPASRLTALRIK 518
Cdd:cd05061 216 sLAEQPYQG--LSNEQVLKFVM---DGGYLD----------QP--------DNCPERVTDLMRMCWQFNPKMRPTFLEIV 272

                ...
gi 41349437 519 KTL 521
Cdd:cd05061 273 NLL 275
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
235-441 1.16e-12

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: 68.50  E-value: 1.16e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 235 QMVRQVGKGRYGEVW--MGKWRGEKVAVKVFFTTEEASWFRETEiYQTV--LMRHENILGFIA----ADIKgTGSwtQLY 306
Cdd:cd06638  21 EIIETIGKGTYGKVFkvLNKKNGSKAAVKILDPIHDIDEEIEAE-YNILkaLSDHPNVVKFYGmyykKDVK-NGD--QLW 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 307 LITDYHENGSLYD----FLKCATLDTRALLK-LAYSAACGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNGSCCIADL 381
Cdd:cd06638  97 LVLELCNGGSVTDlvkgFLKRGERMEEPIIAyILHEALMGLQHLHVN--------KTIHRDVKGNNILLTTEGGVKLVDF 168
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41349437 382 GLAVKFNSDTNEvdvpLNTRVGTKRYMAPEVL--DESLNKNHFQpyiMADIYSFGLIIWEMA 441
Cdd:cd06638 169 GVSAQLTSTRLR----RNTSVGTPFWMAPEVIacEQQLDSTYDA---RCDVWSLGITAIELG 223
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
256-440 1.20e-12

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: 68.40  E-value: 1.20e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 256 EKVAVKVF-------FTTEEASWFRETEIYQTVLMR----HENILgfiaaDIKGT-GSWTQLYLITDYHENGSLYDFL-K 322
Cdd:cd14182  29 QEYAVKIIditgggsFSPEEVQELREATLKEIDILRkvsgHPNII-----QLKDTyETNTFFFLVFDLMKKGELFDYLtE 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 323 CATLDTRALLKLAYSAACGLCHLHteiygtqgKPAIAHRDLKSKNILIKKNGSCCIADLGLAVKFnsDTNEvdvPLNTRV 402
Cdd:cd14182 104 KVTLSEKETRKIMRALLEVICALH--------KLNIVHRDLKPENILLDDDMNIKLTDFGFSCQL--DPGE---KLREVC 170
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 41349437 403 GTKRYMAPEVLDESLNKNHFQPYIMADIYSFGLIIWEM 440
Cdd:cd14182 171 GTPGYLAPEIIECSMDDNHPGYGKEVDMWSTGVIMYTL 208
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
238-522 1.40e-12

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: 67.76  E-value: 1.40e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 238 RQVGKGRYGEVWMGKWRGEK-----VAVKVFFTTEEAS----WFRETEIYQTvlMRHENILGFIaadikGTGSWTQLYLI 308
Cdd:cd05060   1 KELGHGNFGSVRKGVYLMKSgkeveVAVKTLKQEHEKAgkkeFLREASVMAQ--LDHPCIVRLI-----GVCKGEPLMLV 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 309 TDYHENGSLYDFL-KCATLDTRALLKLAYSAACGLCHLHTEIYgtqgkpaiAHRDLKSKNILIKKNGSCCIADLGLAVKF 387
Cdd:cd05060  74 MELAPLGPLLKYLkKRREIPVSDLKELAHQVAMGMAYLESKHF--------VHRDLAARNVLLVNRHQAKISDFGMSRAL 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 388 NSDTNEVDVPLNTRVGTKRYmAPEvldeSLNKNHFQPyiMADIYSFGLIIWEMARRcitggiveeyqlpyynmvpSDPSY 467
Cdd:cd05060 146 GAGSDYYRATTAGRWPLKWY-APE----CINYGKFSS--KSDVWSYGVTLWEAFSY-------------------GAKPY 199
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41349437 468 EDMREVVCVKRL-------RPivsnrwnsDECLRAVLKLMSECWAHNPASRLTALRIKKTLA 522
Cdd:cd05060 200 GEMKGPEVIAMLesgerlpRP--------EECPQEIYSIMLSCWKYRPEDRPTFSELESTFR 253
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
233-529 1.52e-12

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: 68.50  E-value: 1.52e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 233 QIQMVRQVGKGRYGEVWMGKWRG-------EKVAVKVFFTTEEAS------WFRETEIYQtVLMRHENILGFIAADIKGT 299
Cdd:cd05101  25 KLTLGKPLGEGCFGQVVMAEAVGidkdkpkEAVTVAVKMLKDDATekdlsdLVSEMEMMK-MIGKHKNIINLLGACTQDG 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 300 gswtQLYLITDYHENGSLYDFLKC-----------------ATLDTRALLKLAYSAACGLCHLHTEiygtqgkpAIAHRD 362
Cdd:cd05101 104 ----PLYVIVEYASKGNLREYLRArrppgmeysydinrvpeEQMTFKDLVSCTYQLARGMEYLASQ--------KCIHRD 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 363 LKSKNILIKKNGSCCIADLGLAvkfnSDTNEVDVPLNTRVG--TKRYMAPEVLDESLNKNHfqpyimADIYSFGLIIWEM 440
Cdd:cd05101 172 LAARNVLVTENNVMKIADFGLA----RDINNIDYYKKTTNGrlPVKWMAPEALFDRVYTHQ------SDVWSFGVLMWEI 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 441 ArrcITGGIveeyqlPYYNmVPSDPSYEDMREvvcvkrlrpivSNRWNSD-ECLRAVLKLMSECWAHNPASRltalrikK 519
Cdd:cd05101 242 F---TLGGS------PYPG-IPVEELFKLLKE-----------GHRMDKPaNCTNELYMMMRDCWHAVPSQR-------P 293
                       330
                ....*....|
gi 41349437 520 TLAKMVESQD 529
Cdd:cd05101 294 TFKQLVEDLD 303
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
226-440 1.63e-12

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: 68.74  E-value: 1.63e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 226 VQRTIAKQIQMVRQVGKGRYGEVW--MGKWRGEKVAVKVFF-----TTEEASWFRETeIYQTVLMRHENI---LGFIAAD 295
Cdd:cd07852   1 IDKHILRRYEILKKLGKGAYGIVWkaIDKKTGEVVALKKIFdafrnATDAQRTFREI-MFLQELNDHPNIiklLNVIRAE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 296 ikgtgSWTQLYLITDY-----------------HENGSLYDFLKCatldtrallkLAYsaacglchLHTEiygtqgkpAI 358
Cdd:cd07852  80 -----NDKDIYLVFEYmetdlhaviranilediHKQYIMYQLLKA----------LKY--------LHSG--------GV 128
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 359 AHRDLKSKNILIKKNGSCCIADLGLAVKFNSDTNEVDVPLNTR-VGTKRYMAPEVLdesLNKNHfqpYIMA-DIYSFGLI 436
Cdd:cd07852 129 IHRDLKPSNILLNSDCRVKLADFGLARSLSQLEEDDENPVLTDyVATRWYRAPEIL---LGSTR---YTKGvDMWSVGCI 202

                ....
gi 41349437 437 IWEM 440
Cdd:cd07852 203 LGEM 206
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
237-441 1.66e-12

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: 67.45  E-value: 1.66e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 237 VRQVGKGRYGEVWMGKWRGEK-------VAVKVFFTTEEASWFRETEIYQtvLMRHENILGFIAADIKGTGswtqLYLIT 309
Cdd:cd08220   5 IRVVGRGAYGTVYLCRRKDDNklviikqIPVEQMTKEERQAALNEVKVLS--MLHHPNIIEYYESFLEDKA----LMIVM 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 310 DYHENGSLYDFL---KCATLDTRALLKLAYSAACGLCHLHTEIygtqgkpaIAHRDLKSKNILI-KKNGSCCIADLGLAV 385
Cdd:cd08220  79 EYAPGGTLFEYIqqrKGSLLSEEEILHFFVQILLALHHVHSKQ--------ILHRDLKTQNILLnKKRTVVKIGDFGISK 150
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 41349437 386 KFNSDTNEvdvplNTRVGTKRYMAPEVLDESlnknhfqPYIM-ADIYSFGLIIWEMA 441
Cdd:cd08220 151 ILSSKSKA-----YTVVGTPCYISPELCEGK-------PYNQkSDIWALGCVLYELA 195
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
235-458 1.84e-12

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: 67.54  E-value: 1.84e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 235 QMVRQVGKGRYGEVWMGK--WRGEKVAVKVFFTTEEAS-----WFRETEIYQtvLMRHENILG-FIAADIKGTgswtqLY 306
Cdd:cd14072   3 RLLKTIGKGNFAKVKLARhvLTGREVAIKIIDKTQLNPsslqkLFREVRIMK--ILNHPNIVKlFEVIETEKT-----LY 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 307 LITDYHENGSLYDFL----KCATLDTRALLKLAYSAAcGLCHlhteiygtqgKPAIAHRDLKSKNILIKKNGSCCIADLG 382
Cdd:cd14072  76 LVMEYASGGEVFDYLvahgRMKEKEARAKFRQIVSAV-QYCH----------QKRIVHRDLKAENLLLDADMNIKIADFG 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 383 LAVKFNSDTNevdvpLNTRVGTKRYMAPEVLDeslNKNHFQPYImaDIYSFGLIIW---------------EMARRCITG 447
Cdd:cd14072 145 FSNEFTPGNK-----LDTFCGSPPYAAPELFQ---GKKYDGPEV--DVWSLGVILYtlvsgslpfdgqnlkELRERVLRG 214
                       250
                ....*....|.
gi 41349437 448 giveEYQLPYY 458
Cdd:cd14072 215 ----KYRIPFY 221
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
241-514 2.05e-12

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: 67.68  E-value: 2.05e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 241 GKGRYGE-VWMGKWRGEKVAVK------VFFTTEEASWFRETEiyqtvlmRHENILGFIAADIKGTGSWTQLYLIT---- 309
Cdd:cd13982  10 GYGSEGTiVFRGTFDGRPVAVKrllpefFDFADREVQLLRESD-------EHPNVIRYFCTEKDRQFLYIALELCAaslq 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 310 DYHENGSLYDFLKCATLDtraLLKLAYSAACGLCHLHTEiygtqgkpAIAHRDLKSKNILI-----KKNGSCCIADLGLA 384
Cdd:cd13982  83 DLVESPRESKLFLRPGLE---PVRLLRQIASGLAHLHSL--------NIVHRDLKPQNILIstpnaHGNVRAMISDFGLC 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 385 VKFNSDTNEVdVPLNTRVGTKRYMAPEVLDESLNKNhfqPYIMADIYSFGLIIWEMarrcITGGiveeyqlpyynMVPSD 464
Cdd:cd13982 152 KKLDVGRSSF-SRRSGVAGTSGWIAPEMLSGSTKRR---QTRAVDIFSLGCVFYYV----LSGG-----------SHPFG 212
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 41349437 465 PSYEdmrevvcvkRLRPIVSNRWNSDECLRAVLK------LMSECWAHNPASRLTA 514
Cdd:cd13982 213 DKLE---------REANILKGKYSLDKLLSLGEHgpeaqdLIERMIDFDPEKRPSA 259
PTKc_EphR_B cd05065
Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze ...
240-525 2.11e-12

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: 67.59  E-value: 2.11e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 240 VGKGRYGEVWMGKWR--GEK---VAVKVF---FTTEEaswfRETEIYQTVLM---RHENILGFIAADIKGTgswtQLYLI 308
Cdd:cd05065  12 IGAGEFGEVCRGRLKlpGKReifVAIKTLksgYTEKQ----RRDFLSEASIMgqfDHPNIIHLEGVVTKSR----PVMII 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 309 TDYHENGSLYDFLKC--ATLDTRALLKLAYSAACGLCHLHTEIYgtqgkpaiAHRDLKSKNILIKKNGSCCIADLGLAVK 386
Cdd:cd05065  84 TEFMENGALDSFLRQndGQFTVIQLVGMLRGIAAGMKYLSEMNY--------VHRDLAARNILVNSNLVCKVSDFGLSRF 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 387 FNSDTNevDVPLNTRVGTK---RYMAPEVLdeslnknHFQPYIMA-DIYSFGLIIWEmarrcitggiVEEY-QLPYYNMV 461
Cdd:cd05065 156 LEDDTS--DPTYTSSLGGKipiRWTAPEAI-------AYRKFTSAsDVWSYGIVMWE----------VMSYgERPYWDMS 216
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41349437 462 PSDPsyedMREVVCVKRLRPIVsnrwnsdECLRAVLKLMSECWAHNPASRLTALRIKKTLAKMV 525
Cdd:cd05065 217 NQDV----INAIEQDYRLPPPM-------DCPTALHQLMLDCWQKDRNLRPKFGQIVNTLDKMI 269
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
239-522 2.18e-12

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: 67.37  E-value: 2.18e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 239 QVGKGRYGEVWMGKWRGE-----KVAVKVF----FTTEEA--SWFRETEIYQTvlMRHENIL---GFIAADikgtgswtQ 304
Cdd:cd05040   2 KLGDGSFGVVRRGEWTTPsgkviQVAVKCLksdvLSQPNAmdDFLKEVNAMHS--LDHPNLIrlyGVVLSS--------P 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 305 LYLITDYHENGSLYDFLK--CATLDTRALLKLAYSAACGLCHLhteiygtQGKPAIaHRDLKSKNILIKKNGSCCIADLG 382
Cdd:cd05040  72 LMMVTELAPLGSLLDRLRkdQGHFLISTLCDYAVQIANGMAYL-------ESKRFI-HRDLAARNILLASKDKVKIGDFG 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 383 L--AVKFNSD---TNE-VDVPLntrvgtkRYMAPevldESLNKNHFQPyiMADIYSFGLIIWEMarrcITGGiveeyQLP 456
Cdd:cd05040 144 LmrALPQNEDhyvMQEhRKVPF-------AWCAP----ESLKTRKFSH--ASDVWMFGVTLWEM----FTYG-----EEP 201
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41349437 457 YYNMVPS------DPSYEdmrevvcvkRL-RPivsnrwnsDECLRAVLKLMSECWAHNPASRLTALRIKKTLA 522
Cdd:cd05040 202 WLGLNGSqilekiDKEGE---------RLeRP--------DDCPQDIYNVMLQCWAHKPADRPTFVALRDFLP 257
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
233-526 2.18e-12

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: 67.19  E-value: 2.18e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 233 QIQMVRQVGKGRYGEVWMGKWRGE-KVAVKVFfttEEASWFRETEIYQTVLM---RHENIlgfiaadIKGTGSWTQ---L 305
Cdd:cd05114   5 ELTFMKELGSGLFGVVRLGKWRAQyKVAIKAI---REGAMSEEDFIEEAKVMmklTHPKL-------VQLYGVCTQqkpI 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 306 YLITDYHENGSLYDFL--KCATLDTRALLKLAYSAACGLCHLHTEIYgtqgkpaiAHRDLKSKNILIKKNGSCCIADLGL 383
Cdd:cd05114  75 YIVTEFMENGCLLNYLrqRRGKLSRDMLLSMCQDVCEGMEYLERNNF--------IHRDLAARNCLVNDTGVVKVSDFGM 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 384 AVKFnsdtneVDVPLNTRVGTK---RYMAPEVLdeslnknHFQPY-IMADIYSFGLIIWEmarrcitggIVEEYQLPYyn 459
Cdd:cd05114 147 TRYV------LDDQYTSSSGAKfpvKWSPPEVF-------NYSKFsSKSDVWSFGVLMWE---------VFTEGKMPF-- 202
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41349437 460 mvPSDPSYEDMREVVCVKRL-RPIVSNrwnsdeclRAVLKLMSECWAHNPASRLTALRIKKTLAKMVE 526
Cdd:cd05114 203 --ESKSNYEVVEMVSRGHRLyRPKLAS--------KSVYEVMYSCWHEKPEGRPTFADLLRTITEIAE 260
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
232-462 2.26e-12

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: 67.26  E-value: 2.26e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 232 KQIQMVRQVGKGRYGEVW--MGKWRGEKVAVKVFFTTEEASwfRETEIYQTVLMR---HENILGFIAADIKGTgswtQLY 306
Cdd:cd06647   7 KKYTRFEKIGQGASGTVYtaIDVATGQEVAIKQMNLQQQPK--KELIINEILVMRenkNPNIVNYLDSYLVGD----ELW 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 307 LITDYHENGSLYDFLKCATLDTRALlklaySAACGLCHLHTEIYGTQGkpaIAHRDLKSKNILIKKNGSCCIADLGLAVK 386
Cdd:cd06647  81 VVMEYLAGGSLTDVVTETCMDEGQI-----AAVCRECLQALEFLHSNQ---VIHRDIKSDNILLGMDGSVKLTDFGFCAQ 152
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41349437 387 FNSDTNEvdvpLNTRVGTKRYMAPEVldesLNKNHFQPYImaDIYSFGLIIWEMArrcitggiveEYQLPYYNMVP 462
Cdd:cd06647 153 ITPEQSK----RSTMVGTPYWMAPEV----VTRKAYGPKV--DIWSLGIMAIEMV----------EGEPPYLNENP 208
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
239-441 2.85e-12

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: 66.95  E-value: 2.85e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 239 QVGKGRYGEVWMGKWRGEKVAV-------KVFFTTEEASWFRETEIYQTvlMRHENILGFI---AADIKGTGSwtqLYLI 308
Cdd:cd14033   8 EIGRGSFKTVYRGLDTETTVEVawcelqtRKLSKGERQRFSEEVEMLKG--LQHPNIVRFYdswKSTVRGHKC---IILV 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 309 TDYHENGSLYDFLK-CATLDTRALLKLAYSAACGLCHLHTEIygtqgkPAIAHRDLKSKNILIK-KNGSCCIADLGLA-V 385
Cdd:cd14033  83 TELMTSGTLKTYLKrFREMKLKLLQRWSRQILKGLHFLHSRC------PPILHRDLKCDNIFITgPTGSVKIGDLGLAtL 156
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 41349437 386 KFNSDTNEVdvplntrVGTKRYMAPEVLDESLNKnhfqpyiMADIYSFGLIIWEMA 441
Cdd:cd14033 157 KRASFAKSV-------IGTPEFMAPEMYEEKYDE-------AVDVYAFGMCILEMA 198
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
233-447 3.00e-12

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: 67.12  E-value: 3.00e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 233 QIQMVRQVGKGRYGEVWMGKWR--GEKVAVK-VFFTTEEASwfRETEIYQTVLM---RHENILGFiaADIKGTGSwtQLY 306
Cdd:cd07836   1 NFKQLEKLGEGTYATVYKGRNRttGEIVALKeIHLDAEEGT--PSTAIREISLMkelKHENIVRL--HDVIHTEN--KLM 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 307 LITDYHENgSLYDFL-----KCAtLDTRALLKLAYSAACGL--CHLHteiygtqgkpAIAHRDLKSKNILIKKNGSCCIA 379
Cdd:cd07836  75 LVFEYMDK-DLKKYMdthgvRGA-LDPNTVKSFTYQLLKGIafCHEN----------RVLHRDLKPQNLLINKRGELKLA 142
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41349437 380 DLGLAVKFNsdtnevdVPLNT---RVGTKRYMAPEVLdesLNKNHFQPYImaDIYSFGLIIWEMarrcITG 447
Cdd:cd07836 143 DFGLARAFG-------IPVNTfsnEVVTLWYRAPDVL---LGSRTYSTSI--DIWSVGCIMAEM----ITG 197
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
310-441 3.29e-12

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: 67.46  E-value: 3.29e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 310 DYHENGSLYDFLKCA-TLDTRALLKLAYSAACGLCHLHTEIygtqgkpAIAHRDLKSKNILIKKNGSCCIADLGLAVKFn 388
Cdd:cd06615  79 EHMDGGSLDQVLKKAgRIPENILGKISIAVLRGLTYLREKH-------KIMHRDVKPSNILVNSRGEIKLCDFGVSGQL- 150
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 41349437 389 sdtneVDVPLNTRVGTKRYMAPevldESLNKNHFQpyIMADIYSFGLIIWEMA 441
Cdd:cd06615 151 -----IDSMANSFVGTRSYMSP----ERLQGTHYT--VQSDIWSLGLSLVEMA 192
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
240-441 3.94e-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: 66.55  E-value: 3.94e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 240 VGKGRYGEVWMGKWRG--EKVAVKvffTTEEAswfRETEIYQTVLM----RHENILGFIAadikgtgsW--TQ--LYLIT 309
Cdd:cd14010   8 IGRGKHSVVYKGRRKGtiEFVAIK---CVDKS---KRPEVLNEVRLthelKHPNVLKFYE--------WyeTSnhLWLVV 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 310 DYHENGSLYDFLKCAT-LDTRALLKLAYSAACGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNGSCCIADLGLA---- 384
Cdd:cd14010  74 EYCTGGDLETLLRQDGnLPESSVRKFGRDLVRGLHYIHSK--------GIIYCDLKPSNILLDGNGTLKLSDFGLArreg 145
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41349437 385 -------VKFNSDTNEVDVPLNTRV-GTKRYMAPEVLdeslnknHFQPYIMA-DIYSFGLIIWEMA 441
Cdd:cd14010 146 eilkelfGQFSDEGNVNKVSKKQAKrGTPYYMAPELF-------QGGVHSFAsDLWALGCVLYEMF 204
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
237-493 4.34e-12

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: 66.26  E-value: 4.34e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 237 VRQVGKGRYGEVWMGKWRGEKVAVKVFFTTEEA----SWFR---------ETEIYQTV-LMRHENI---LGFIAADIkgt 299
Cdd:cd14004   5 LKEMGEGAYGQVNLAIYKSKGKEVVIKFIFKERilvdTWVRdrklgtvplEIHILDTLnKRSHPNIvklLDFFEDDE--- 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 300 gswtQLYLITDYHENG-SLYDFLKCATLDTRALLKLAY-SAACGLCHLHTeiygtQGkpaIAHRDLKSKNILIKKNGSCC 377
Cdd:cd14004  82 ----FYYLVMEKHGSGmDLFDFIERKPNMDEKEAKYIFrQVADAVKHLHD-----QG---IVHRDIKDENVILDGNGTIK 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 378 IADLGLAVKFNSDtnevdvPLNTRVGTKRYMAPEVLDESLNKNHFQpyimaDIYSFGLIIWEMarrcitggIVEEYqlPY 457
Cdd:cd14004 150 LIDFGSAAYIKSG------PFDTFVGTIDYAAPEVLRGNPYGGKEQ-----DIWALGVLLYTL--------VFKEN--PF 208
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 41349437 458 YNM-----VPSDPSYEDMREVV-CVKR-LRPIVSNRWNSDECL 493
Cdd:cd14004 209 YNIeeileADLRIPYAVSEDLIdLISRmLNRDVGDRPTIEELL 251
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
230-440 4.48e-12

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: 67.37  E-value: 4.48e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 230 IAKQIQMVRQVGKGRYGEVWMG--KWRGEKVAVKVF---FTT--EEASWFRETEIYQTvlMRHENILGF--IAADIKGTG 300
Cdd:cd07877  15 VPERYQNLSPVGSGAYGSVCAAfdTKTGLRVAVKKLsrpFQSiiHAKRTYRELRLLKH--MKHENVIGLldVFTPARSLE 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 301 SWTQLYLITdyHENGS-LYDFLKCATLDTRALLKLAYSAACGLCHLHTeiygtqgkPAIAHRDLKSKNILIKKNGSCCIA 379
Cdd:cd07877  93 EFNDVYLVT--HLMGAdLNNIVKCQKLTDDHVQFLIYQILRGLKYIHS--------ADIIHRDLKPSNLAVNEDCELKIL 162
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41349437 380 DLGLAvkfnsdtNEVDVPLNTRVGTKRYMAPEVLdesLNKNHFQpyIMADIYSFGLIIWEM 440
Cdd:cd07877 163 DFGLA-------RHTDDEMTGYVATRWYRAPEIM---LNWMHYN--QTVDIWSVGCIMAEL 211
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
232-511 4.59e-12

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: 66.84  E-value: 4.59e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 232 KQIQMVRQVGKGRYGEVWM------GKWRGEKVAVKVF--FTTEEASWF-RETEIYQTvlMRHENILGFiaADIKGTGSW 302
Cdd:cd05081   4 RHLKYISQLGKGNFGSVELcrydplGDNTGALVAVKQLqhSGPDQQRDFqREIQILKA--LHSDFIVKY--RGVSYGPGR 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 303 TQLYLITDYHENGSLYDFLK--CATLDTRALLKLAYSAACGLCHLHTEIYgtqgkpaiAHRDLKSKNILIKKNGSCCIAD 380
Cdd:cd05081  80 RSLRLVMEYLPSGCLRDFLQrhRARLDASRLLLYSSQICKGMEYLGSRRC--------VHRDLAARNILVESEAHVKIAD 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 381 LGLA--VKFNSDTNEVDVPLNTRVgtkRYMAPEVLDESLNKNHfqpyimADIYSFGLIIwemarrcitggiveeYQLPYY 458
Cdd:cd05081 152 FGLAklLPLDKDYYVVREPGQSPI---FWYAPESLSDNIFSRQ------SDVWSFGVVL---------------YELFTY 207
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41349437 459 NMVPSDPSYEDMREVVCvKRLRPIV---------SNRWNSD-ECLRAVLKLMSECWAHNPASR 511
Cdd:cd05081 208 CDKSCSPSAEFLRMMGC-ERDVPALcrllelleeGQRLPAPpACPAEVHELMKLCWAPSPQDR 269
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
230-514 4.63e-12

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: 67.33  E-value: 4.63e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 230 IAKQIQMVRQVGKGRYGEVWMG--KWRGEKVAVKVFFTTEEASWFRET--EIYQTVLMRHENILGFIaaDIKGTGSWTQL 305
Cdd:cd07849   3 VGPRYQNLSYIGEGAYGMVCSAvhKPTGQKVAIKKISPFEHQTYCLRTlrEIKILLRFKHENIIGIL--DIQRPPTFESF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 306 ---YLITDYHENgSLYDFLKCATLDTRALLKLAYSAACGLCHLHTeiygtqgkPAIAHRDLKSKNILIKKNGSCCIADLG 382
Cdd:cd07849  81 kdvYIVQELMET-DLYKLIKTQHLSNDHIQYFLYQILRGLKYIHS--------ANVLHRDLKPSNLLLNTNCDLKICDFG 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 383 LAvkfNSDTNEVDVP--LNTRVGTKRYMAPEVLdesLNknhFQPYIMA-DIYSFGLIIWEM-ARRCITGGIVEEYQLPYY 458
Cdd:cd07849 152 LA---RIADPEHDHTgfLTEYVATRWYRAPEIM---LN---SKGYTKAiDIWSVGCILAEMlSNRPLFPGKDYLHQLNLI 222
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41349437 459 NMVPSDPSYEDMREVVCVKRLRPIVSNRWNSDECLRAV--------LKLMSECWAHNPASRLTA 514
Cdd:cd07849 223 LGILGTPSQEDLNCIISLKARNYIKSLPFKPKVPWNKLfpnadpkaLDLLDKMLTFNPHKRITV 286
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
232-462 4.73e-12

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: 66.67  E-value: 4.73e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 232 KQIQMVRQVGKGRYGEVW--MGKWRGEKVAVKVFFTTEEASwfRETEIYQTVLMRHE---NILGFIAADIKGTgswtQLY 306
Cdd:cd06654  20 KKYTRFEKIGQGASGTVYtaMDVATGQEVAIRQMNLQQQPK--KELIINEILVMRENknpNIVNYLDSYLVGD----ELW 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 307 LITDYHENGSLYDFLKCATLDTRALLKLAYSAACGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNGSCCIADLGLAVK 386
Cdd:cd06654  94 VVMEYLAGGSLTDVVTETCMDEGQIAAVCRECLQALEFLHSN--------QVIHRDIKSDNILLGMDGSVKLTDFGFCAQ 165
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41349437 387 FNSDTNEvdvpLNTRVGTKRYMAPEVldesLNKNHFQPYImaDIYSFGLIIWEMArrcitggiveEYQLPYYNMVP 462
Cdd:cd06654 166 ITPEQSK----RSTMVGTPYWMAPEV----VTRKAYGPKV--DIWSLGIMAIEMI----------EGEPPYLNENP 221
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
316-441 5.04e-12

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: 66.68  E-value: 5.04e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 316 SLYDFLKCA-----TLDTRALLKLAYSAACGLCHLHTEIygtqgkpAIAHRDLKSKNILIKKNGSCCIADLGLAVKF-NS 389
Cdd:cd06617  85 SLDKFYKKVydkglTIPEDILGKIAVSIVKALEYLHSKL-------SVIHRDVKPSNVLINRNGQVKLCDFGISGYLvDS 157
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 41349437 390 DTNEVDvplntrVGTKRYMAPEVLDESLNKNHFQpyIMADIYSFGLIIWEMA 441
Cdd:cd06617 158 VAKTID------AGCKPYMAPERINPELNQKGYD--VKSDVWSLGITMIELA 201
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
235-440 5.49e-12

Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK2 is a tetrameric protein with two catalytic (alpha) and two regulatory (beta) subunits. It is constitutively active and ubiquitously expressed, and is found in the cytoplasm, nucleus, as well as in the plasma membrane. It phosphorylates a wide variety of substrates including gylcogen synthase, cell cycle proteins, nuclear proteins (e.g. DNA topoisomerase II), and ion channels (e.g. ENaC), among others. It may be considered a master kinase controlling the activity or lifespan of many other kinases and exerting its effect over cell fate, gene expression, protein synthesis and degradation, and viral infection. CK2 is implicated in every stage of the cell cycle and is required for cell cycle progression. It plays crucial roles in cell differentiation, proliferation, and survival, and is thus implicated in cancer. CK2 is not an oncogene by itself but elevated CK2 levels create an environment that enhances the survival of tumor cells. The CK2 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: 271034 [Multi-domain]  Cd Length: 306  Bit Score: 66.80  E-value: 5.49e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 235 QMVRQVGKGRYGEVWMGK--WRGEKVAVKVFFTTEEASWFRETEIYQTvLMRHENILGFIAA---DIKGTGSwtqlyLIT 309
Cdd:cd14132  21 EIIRKIGRGKYSEVFEGIniGNNEKVVIKVLKPVKKKKIKREIKILQN-LRGGPNIVKLLDVvkdPQSKTPS-----LIF 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 310 DYHENGSLYD-FLKCATLDTR----ALLK-LAYsaacglCHlhteiygTQGkpaIAHRDLKSKNILI-KKNGSCCIADLG 382
Cdd:cd14132  95 EYVNNTDFKTlYPTLTDYDIRyymyELLKaLDY------CH-------SKG---IMHRDVKPHNIMIdHEKRKLRLIDWG 158
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41349437 383 LAVKFNSDTNevdvpLNTRVGTKRYMAPEVL------DESLnknhfqpyimaDIYSFGLIIWEM 440
Cdd:cd14132 159 LAEFYHPGQE-----YNVRVASRYYKGPELLvdyqyyDYSL-----------DMWSLGCMLASM 206
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
233-525 5.77e-12

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: 66.52  E-value: 5.77e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 233 QIQMVRQVGKGRYGEVWMG---KWRG----EKVAVKVFFTTEEASWFR----ETEIYQTVlmRHENIlgfiaadIKGTGS 301
Cdd:cd05045   1 NLVLGKTLGEGEFGKVVKAtafRLKGragyTTVAVKMLKENASSSELRdllsEFNLLKQV--NHPHV-------IKLYGA 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 302 WTQ---LYLITDYHENGSLYDFLK------CATL--------------DTRA-----LLKLAYSAACGLCHLhteiygtq 353
Cdd:cd05045  72 CSQdgpLLLIVEYAKYGSLRSFLResrkvgPSYLgsdgnrnssyldnpDERAltmgdLISFAWQISRGMQYL-------- 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 354 GKPAIAHRDLKSKNILIKKNGSCCIADLGLAvkfnSDTNEVDVPLNT---RVGTKrYMAPEVLDESLNKNHfqpyimADI 430
Cdd:cd05045 144 AEMKLVHRDLAARNVLVAEGRKMKISDFGLS----RDVYEEDSYVKRskgRIPVK-WMAIESLFDHIYTTQ------SDV 212
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 431 YSFGLIIWEMarrcITGGiveeyQLPYYNMVPsdpsyedmrevvcvKRLRPIVSNRW---NSDECLRAVLKLMSECWAHN 507
Cdd:cd05045 213 WSFGVLLWEI----VTLG-----GNPYPGIAP--------------ERLFNLLKTGYrmeRPENCSEEMYNLMLTCWKQE 269
                       330
                ....*....|....*...
gi 41349437 508 PASRLTALRIKKTLAKMV 525
Cdd:cd05045 270 PDKRPTFADISKELEKMM 287
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
232-462 5.86e-12

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: 66.67  E-value: 5.86e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 232 KQIQMVRQVGKGRYGEVW--MGKWRGEKVAVKVFFTTEEASwfRETEIYQTVLMRHE---NILGFIAADIKGTgswtQLY 306
Cdd:cd06656  19 KKYTRFEKIGQGASGTVYtaIDIATGQEVAIKQMNLQQQPK--KELIINEILVMRENknpNIVNYLDSYLVGD----ELW 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 307 LITDYHENGSLYDFLKCATLDTRALLKLAYSAACGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNGSCCIADLGLAVK 386
Cdd:cd06656  93 VVMEYLAGGSLTDVVTETCMDEGQIAAVCRECLQALDFLHSN--------QVIHRDIKSDNILLGMDGSVKLTDFGFCAQ 164
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41349437 387 FNSDTNEvdvpLNTRVGTKRYMAPEVldesLNKNHFQPYImaDIYSFGLIIWEMArrcitggiveEYQLPYYNMVP 462
Cdd:cd06656 165 ITPEQSK----RSTMVGTPYWMAPEV----VTRKAYGPKV--DIWSLGIMAIEMV----------EGEPPYLNENP 220
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
239-440 6.22e-12

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: 66.85  E-value: 6.22e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 239 QVGKGRYGEVW--MGKWRGEKVAVKVF---FTTE--EASWFRETEIYQTvlMRHENILGFIAADIKGTG--SWTQLYLIT 309
Cdd:cd07879  22 QVGSGAYGSVCsaIDKRTGEKVAIKKLsrpFQSEifAKRAYRELTLLKH--MQHENVIGLLDVFTSAVSgdEFQDFYLVM 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 310 DYHENgslyDFLKC--ATLDTRALLKLAYSAACGLCHLHteiygtqgKPAIAHRDLKSKNILIKKNGSCCIADLGLAvkf 387
Cdd:cd07879 100 PYMQT----DLQKImgHPLSEDKVQYLVYQMLCGLKYIH--------SAGIIHRDLKPGNLAVNEDCELKILDFGLA--- 164
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 41349437 388 nsdtNEVDVPLNTRVGTKRYMAPEVLdesLNKNHFQPYImaDIYSFGLIIWEM 440
Cdd:cd07879 165 ----RHADAEMTGYVVTRWYRAPEVI---LNWMHYNQTV--DIWSVGCIMAEM 208
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
239-514 6.81e-12

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: 66.40  E-value: 6.81e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 239 QVGKGRYGEVW--MGKWRGEKVAVK-VFFTTEE----ASWFRETEIYQtVLMRHENILGFIAADIKGTGSWTQLYLITDY 311
Cdd:cd07837   8 KIGEGTYGKVYkaRDKNTGKLVALKkTRLEMEEegvpSTALREVSLLQ-MLSQSIYIVRLLDVEHVEENGKPLLYLVFEY 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 312 HENgSLYDFL------KCATLDTRALLKLAYSAACGLCHLHteiygtqgKPAIAHRDLKSKNILIKKNGSCC-IADLGLA 384
Cdd:cd07837  87 LDT-DLKKFIdsygrgPHNPLPAKTIQSFMYQLCKGVAHCH--------SHGVMHRDLKPQNLLVDKQKGLLkIADLGLG 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 385 VKFNsdtnevdVPLNT---RVGTKRYMAPEVLdesLNKNHFQPYImaDIYSFGLIIWEMARR-CITGGIVEEYQLPYYNM 460
Cdd:cd07837 158 RAFT-------IPIKSythEIVTLWYRAPEVL---LGSTHYSTPV--DMWSVGCIFAEMSRKqPLFPGDSELQQLLHIFR 225
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41349437 461 VPSDPSYEDMREvvcVKRLRPI-VSNRWNSDECLRAV-------LKLMSECWAHNPASRLTA 514
Cdd:cd07837 226 LLGTPNEEVWPG---VSKLRDWhEYPQWKPQDLSRAVpdlepegVDLLTKMLAYDPAKRISA 284
PTK_Ryk cd05043
Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase ...
243-511 7.24e-12

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: 65.94  E-value: 7.24e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 243 GRYGEVWMGKWRGEKVAVKVFFT---TEEASWFRETEIYQTVLM----RHENILGFIAADIKGTGSWTQLYLITDYhenG 315
Cdd:cd05043  17 GTFGRIFHGILRDEKGKEEEVLVktvKDHASEIQVTMLLQESSLlyglSHQNLLPILHVCIEDGEKPMVLYPYMNW---G 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 316 SLYDFL-KCA--------TLDTRALLKLAYSAACGLCHLHteiygtqgKPAIAHRDLKSKNILIKKNGSCCIADLGLAVK 386
Cdd:cd05043  94 NLKLFLqQCRlseannpqALSTQQLVHMALQIACGMSYLH--------RRGVIHKDIAARNCVIDDELQVKITDNALSRD 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 387 -FNSD-----TNEvDVPLntrvgtkRYMAPEvldeSLNKNHFQPyiMADIYSFGLIIWEMArrciTGGiveeyQLPYynm 460
Cdd:cd05043 166 lFPMDyhclgDNE-NRPI-------KWMSLE----SLVNKEYSS--ASDVWSFGVLLWELM----TLG-----QTPY--- 219
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 41349437 461 VPSDPsYEDMREVVCVKRL-RPIvsnrwNSDECLRAVlklMSECWAHNPASR 511
Cdd:cd05043 220 VEIDP-FEMAAYLKDGYRLaQPI-----NCPDELFAV---MACCWALDPEER 262
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
235-440 1.14e-11

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: 66.19  E-value: 1.14e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 235 QMVRQVGKGRYGEVWMGKWRGEKV--AVKVFfttEEASWFRETEiyQTVLMRHENIL------GFIAADIKGTGSWTQLY 306
Cdd:cd05602  10 HFLKVIGKGSFGKVLLARHKSDEKfyAVKVL---QKKAILKKKE--EKHIMSERNVLlknvkhPFLVGLHFSFQTTDKLY 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 307 LITDYHENGSLYDFL---KCaTLDTRALLkLAYSAACGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNGSCCIADLGL 383
Cdd:cd05602  85 FVLDYINGGELFYHLqreRC-FLEPRARF-YAAEIASALGYLHSL--------NIVYRDLKPENILLDSQGHIVLTDFGL 154
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 41349437 384 AvKFNSDTNEVDvplNTRVGTKRYMAPEVLdeslnknHFQPY-IMADIYSFGLIIWEM 440
Cdd:cd05602 155 C-KENIEPNGTT---STFCGTPEYLAPEVL-------HKQPYdRTVDWWCLGAVLYEM 201
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
237-443 1.18e-11

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: 65.83  E-value: 1.18e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 237 VRQVGKGRYGEVWMGK--WRGEKVAVKVFftteEASWFRETEIYQTVL--------MRHENILGFIAADIKGTGSWtqly 306
Cdd:cd06633  26 LHEIGHGSFGAVYFATnsHTNEVVAIKKM----SYSGKQTNEKWQDIIkevkflqqLKHPNTIEYKGCYLKDHTAW---- 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 307 LITDYHEnGSLYDFLKC--ATLDTRALLKLAYSAACGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNGSCCIADLGLA 384
Cdd:cd06633  98 LVMEYCL-GSASDLLEVhkKPLQEVEIAAITHGALQGLAYLHSH--------NMIHRDIKAGNILLTEPGQVKLADFGSA 168
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 41349437 385 vkfnsdtnEVDVPLNTRVGTKRYMAPEVLdESLNKNHFQPYImaDIYSFGLIIWEMARR 443
Cdd:cd06633 169 --------SIASPANSFVGTPYWMAPEVI-LAMDEGQYDGKV--DIWSLGITCIELAER 216
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
240-440 1.19e-11

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: 65.44  E-value: 1.19e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 240 VGKGRYGEVW--MGKWRGEKVAVKVFFTT---EEASWFRETE-IYQTvlMRHENIL---GFIAADikgtgswTQLYLITD 310
Cdd:cd14174  10 LGEGAYAKVQgcVSLQNGKEYAVKIIEKNaghSRSRVFREVEtLYQC--QGNKNILeliEFFEDD-------TRFYLVFE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 311 YHENGSLYDFL-KCATLDTRALLKLAYSAACGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNGSC-----CIADLGLA 384
Cdd:cd14174  81 KLRGGSILAHIqKRKHFNEREASRVVRDIASALDFLHTK--------GIAHRDLKPENILCESPDKVspvkiCDFDLGSG 152
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 41349437 385 VKFNSDTNEVDVP-LNTRVGTKRYMAPEVLDESLNKNHFQPYiMADIYSFGLIIWEM 440
Cdd:cd14174 153 VKLNSACTPITTPeLTTPCGSAEYMAPEVVEVFTDEATFYDK-RCDLWSLGVILYIM 208
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
230-437 1.20e-11

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: 65.49  E-value: 1.20e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 230 IAKQIQMVRQVGKGRYGEVWMG--KWRGEKVAVKV----FFTTEEASWFR-----ETEIYQTVLMRHENILG----FIAA 294
Cdd:cd14084   4 LRKKYIMSRTLGSGACGEVKLAydKSTCKKVAIKIinkrKFTIGSRREINkprniETEIEILKKLSHPCIIKiedfFDAE 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 295 DikgtgswtQLYLITDYHENGSLYDFLKCATLDTRALLKL-AYSAACGLCHLHTeiygtQGkpaIAHRDLKSKNILIKKN 373
Cdd:cd14084  84 D--------DYYIVLELMEGGELFDRVVSNKRLKEAICKLyFYQMLLAVKYLHS-----NG---IIHRDLKPENVLLSSQ 147
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41349437 374 GSCC---IADLGLAvKFNSDTNevdvPLNTRVGTKRYMAPEVldesLNKNHFQPYIMA-DIYSFGLII 437
Cdd:cd14084 148 EEEClikITDFGLS-KILGETS----LMKTLCGTPTYLAPEV----LRSFGTEGYTRAvDCWSLGVIL 206
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
255-438 1.28e-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: 65.07  E-value: 1.28e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 255 GEKVAVKVFFTTEE-----------ASWFRETEIYQTVlMRHENILGFIaaDIKGTGSWtqLYLITDYHENGSLYDFL-K 322
Cdd:cd14093  28 GQEFAVKIIDITGEksseneaeelrEATRREIEILRQV-SGHPNIIELH--DVFESPTF--IFLVFELCRKGELFDYLtE 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 323 CATL---DTRALLKLAYSAacgLCHLHteiygtqgKPAIAHRDLKSKNILIKKNGSCCIADLGLAVKFNSdtnevDVPLN 399
Cdd:cd14093 103 VVTLsekKTRRIMRQLFEA---VEFLH--------SLNIVHRDLKPENILLDDNLNVKISDFGFATRLDE-----GEKLR 166
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 41349437 400 TRVGTKRYMAPEVLDESLNKNHFQPYIMADIYSFGLIIW 438
Cdd:cd14093 167 ELCGTPGYLAPEVLKCSMYDNAPGYGKEVDMWACGVIMY 205
PTKc_FGFR3 cd05100
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs ...
233-529 1.43e-11

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: 65.81  E-value: 1.43e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 233 QIQMVRQVGKGRYGEVWMGKWRG-EK--------VAVKVF---FTTEEAS-WFRETEIYQtVLMRHENILGFIAADIKGT 299
Cdd:cd05100  13 RLTLGKPLGEGCFGQVVMAEAIGiDKdkpnkpvtVAVKMLkddATDKDLSdLVSEMEMMK-MIGKHKNIINLLGACTQDG 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 300 gswtQLYLITDYHENGSLYDFLKC-----------------ATLDTRALLKLAYSAACGLCHLHTEiygtqgkpAIAHRD 362
Cdd:cd05100  92 ----PLYVLVEYASKGNLREYLRArrppgmdysfdtcklpeEQLTFKDLVSCAYQVARGMEYLASQ--------KCIHRD 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 363 LKSKNILIKKNGSCCIADLGLAvkfnSDTNEVDVPLNTRVG--TKRYMAPEVLDESLNKNHfqpyimADIYSFGLIIWEM 440
Cdd:cd05100 160 LAARNVLVTEDNVMKIADFGLA----RDVHNIDYYKKTTNGrlPVKWMAPEALFDRVYTHQ------SDVWSFGVLLWEI 229
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 441 ArrcITGGIveeyqlPYYNmVPSDPSYEDMREvvcvkrlrpivSNRWNSD-ECLRAVLKLMSECWAHNPASRltalrikK 519
Cdd:cd05100 230 F---TLGGS------PYPG-IPVEELFKLLKE-----------GHRMDKPaNCTHELYMIMRECWHAVPSQR-------P 281
                       330
                ....*....|
gi 41349437 520 TLAKMVESQD 529
Cdd:cd05100 282 TFKQLVEDLD 291
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
238-440 1.66e-11

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: 65.04  E-value: 1.66e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 238 RQVGKGRYGEVWMGKWR--GEKVAVKVFFTTE------EASWFRETEIYQTVLMRhenilgFIAADIKGTGSWTQLYLIT 309
Cdd:cd05630   6 RVLGKGGFGEVCACQVRatGKMYACKKLEKKRikkrkgEAMALNEKQILEKVNSR------FVVSLAYAYETKDALCLVL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 310 DYHENGSL----YDFLKCATLDTRALLkLAYSAACGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNGSCCIADLGLAV 385
Cdd:cd05630  80 TLMNGGDLkfhiYHMGQAGFPEARAVF-YAAEICCGLEDLHRE--------RIVYRDLKPENILLDDHGHIRISDLGLAV 150
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 41349437 386 KFNSDTNevdvpLNTRVGTKRYMAPEVLDESlnKNHFQPyimaDIYSFGLIIWEM 440
Cdd:cd05630 151 HVPEGQT-----IKGRVGTVGYMAPEVVKNE--RYTFSP----DWWALGCLLYEM 194
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
274-440 1.76e-11

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: 64.50  E-value: 1.76e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 274 ETEIYQTvlMRHENILGFIAA--DIKGTgswtqlYLITDYHENGSLYDFLK---CATL-DTRALLklaYSAACGLCHLHt 347
Cdd:cd14099  51 EIKIHRS--LKHPNIVKFHDCfeDEENV------YILLELCSNGSLMELLKrrkALTEpEVRYFM---RQILSGVKYLH- 118
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 348 eiygtqgKPAIAHRDLKSKNILIKKNGSCCIADLGLAVKFNSDtNEVDVplnTRVGTKRYMAPEVLDESlnKNHFQpyiM 427
Cdd:cd14099 119 -------SNRIIHRDLKLGNLFLDENMNVKIGDFGLAARLEYD-GERKK---TLCGTPNYIAPEVLEKK--KGHSF---E 182
                       170
                ....*....|...
gi 41349437 428 ADIYSFGLIIWEM 440
Cdd:cd14099 183 VDIWSLGVILYTL 195
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
240-440 1.82e-11

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: 65.41  E-value: 1.82e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 240 VGKGRYGEVWMGKWR--GEKVAVKVF-----FTTEEASWFREteiyqtvlmrHENILGfiaadiKGTGSW-TQL------ 305
Cdd:cd05601   9 IGRGHFGEVQVVKEKatGDIYAMKVLkksetLAQEEVSFFEE----------ERDIMA------KANSPWiTKLqyafqd 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 306 ----YLITDYHENGSLYDFL-KCATLDTRALLKLaYSAACGLC-H-LHTEIYgtqgkpaiAHRDLKSKNILIKKNGSCCI 378
Cdd:cd05601  73 senlYLVMEYHPGGDLLSLLsRYDDIFEESMARF-YLAELVLAiHsLHSMGY--------VHRDIKPENILIDRTGHIKL 143
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41349437 379 ADLGLAVKFNSDTnevDVPLNTRVGTKRYMAPEVLdESLNKNHFQPY-IMADIYSFGLIIWEM 440
Cdd:cd05601 144 ADFGSAAKLSSDK---TVTSKMPVGTPDYIAPEVL-TSMNGGSKGTYgVECDWWSLGIVAYEM 202
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
230-440 1.85e-11

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: 64.36  E-value: 1.85e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 230 IAKQIQMVRQVGKGRYGEVWMGK--WRGEKVAVKVFFTT--EEASwfrETEIYQTV----LMRHENILG-FIAADIKgtg 300
Cdd:cd14074   1 IAGLYDLEETLGRGHFAVVKLARhvFTGEKVAVKVIDKTklDDVS---KAHLFQEVrcmkLVQHPNVVRlYEVIDTQ--- 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 301 swTQLYLITDYHENGSLYDFLkcatldtrallklaYSAACGLCHLHTEIYGTQGKPAIA--------HRDLKSKNILI-K 371
Cdd:cd14074  75 --TKLYLILELGDGGDMYDYI--------------MKHENGLNEDLARKYFRQIVSAISychklhvvHRDLKPENVVFfE 138
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41349437 372 KNGSCCIADLGLAVKFNSDTNevdvpLNTRVGTKRYMAPEVLdesLNKNHFQPYImaDIYSFGLIIWEM 440
Cdd:cd14074 139 KQGLVKLTDFGFSNKFQPGEK-----LETSCGSLAYSAPEIL---LGDEYDAPAV--DIWSLGVILYML 197
PTKc_DDR cd05051
Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze ...
232-513 1.91e-11

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: 65.05  E-value: 1.91e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 232 KQIQMVRQVGKGRYGEV---------------WMGKWRGEK---VAVKVF-----FTTEEAswFrETEIYQTVLMRHENI 288
Cdd:cd05051   5 EKLEFVEKLGEGQFGEVhlceanglsdltsddFIGNDNKDEpvlVAVKMLrpdasKNARED--F-LKEVKIMSQLKDPNI 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 289 LGFIAADIKGTgswtQLYLITDYHENGSLYDFLKCATLDTRALLKLAY---SAACgLCHLHTEIygTQGKPAIA-----H 360
Cdd:cd05051  82 VRLLGVCTRDE----PLCMIVEYMENGDLNQFLQKHEAETQGASATNSktlSYGT-LLYMATQI--ASGMKYLEslnfvH 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 361 RDLKSKNILIKKNGSCCIADLGLAVK-FNSDTNEVD----VPLntrvgtkRYMAPE-VLDESLNKNhfqpyimADIYSFG 434
Cdd:cd05051 155 RDLATRNCLVGPNYTIKIADFGMSRNlYSGDYYRIEgravLPI-------RWMAWEsILLGKFTTK-------SDVWAFG 220
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 435 LIIWEM---ARRcitggiveeyQlPYYNMvpSDPS--------YEDMREVVCVKRLRpivsnrwnsdECLRAVLKLMSEC 503
Cdd:cd05051 221 VTLWEIltlCKE----------Q-PYEHL--TDEQvienagefFRDDGMEVYLSRPP----------NCPKEIYELMLEC 277
                       330
                ....*....|
gi 41349437 504 WAHNPASRLT 513
Cdd:cd05051 278 WRRDEEDRPT 287
PTKc_Aatyk1 cd05087
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 1; PTKs ...
237-471 1.98e-11

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: 64.62  E-value: 1.98e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 237 VRQVGKGRYGEVWMGK----WRGEKVAVKVFFTT----EEASWFRETEIYQTvlMRHENILGFIAAdikgTGSWTQLYLI 308
Cdd:cd05087   2 LKEIGHGWFGKVFLGEvnsgLSSTQVVVKELKASasvqDQMQFLEEAQPYRA--LQHTNLLQCLAQ----CAEVTPYLLV 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 309 TDYHENGSLYDFLKCA------TLDTRALLKLAYSAACGLCHLHTEIYgtqgkpaiAHRDLKSKNILIKKNGSCCIADLG 382
Cdd:cd05087  76 MEFCPLGDLKGYLRSCraaesmAPDPLTLQRMACEVACGLLHLHRNNF--------VHSDLALRNCLLTADLTVKIGDYG 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 383 LA-VKFNSD----TNEVDVPLntrvgtkRYMAPEVLDESlnknHFQPYIM-----ADIYSFGLIIWEM-----------A 441
Cdd:cd05087 148 LShCKYKEDyfvtADQLWVPL-------RWIAPELVDEV----HGNLLVVdqtkqSNVWSLGVTIWELfelgnqpyrhyS 216
                       250       260       270
                ....*....|....*....|....*....|....
gi 41349437 442 RRCITGGIVEEYQL----PYYNMVPSDPSYEDMR 471
Cdd:cd05087 217 DRQVLTYTVREQQLklpkPQLKLSLAERWYEVMQ 250
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
236-440 2.61e-11

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: 64.82  E-value: 2.61e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 236 MVRQVGKGRYGEVWMGKWR--GEKVAVKVFFTTEEASWFRETEIYQTVLMR---HENILGF--IAAD-------IKGTGS 301
Cdd:cd07864  11 IIGIIGEGTYGQVYKAKDKdtGELVALKKVRLDNEKEGFPITAIREIKILRqlnHRSVVNLkeIVTDkqdaldfKKDKGA 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 302 WtqlYLITDYHENgSLYDFLKCATLD-----TRALLKLAYSaacGLCHLHteiygtqgKPAIAHRDLKSKNILIKKNGSC 376
Cdd:cd07864  91 F---YLVFEYMDH-DLMGLLESGLVHfsedhIKSFMKQLLE---GLNYCH--------KKNFLHRDIKCSNILLNNKGQI 155
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41349437 377 CIADLGLAVKFNSDTNEvdvPLNTRVGTKRYMAPEVLdesLNKNHFQPYImaDIYSFGLIIWEM 440
Cdd:cd07864 156 KLADFGLARLYNSEESR---PYTNKVITLWYRPPELL---LGEERYGPAI--DVWSCGCILGEL 211
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
233-444 2.73e-11

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: 64.48  E-value: 2.73e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 233 QIQMVRQVGKGRYGEVW--MGKWRGEKVAVKVFFTTEEASWFREteIYQTVLMRHENILGFIaadIKGTGSWTQ---LYL 307
Cdd:cd06622   2 EIEVLDELGKGNYGSVYkvLHRPTGVTMAMKEIRLELDESKFNQ--IIMELDILHKAVSPYI---VDFYGAFFIegaVYM 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 308 ITDYHENGS---LYD-FLKCATLDTRALLKLAYSAACGLCHLHTEIygtqgkpAIAHRDLKSKNILIKKNGSCCIADLGL 383
Cdd:cd06622  77 CMEYMDAGSldkLYAgGVATEGIPEDVLRRITYAVVKGLKFLKEEH-------NIIHRDVKPTNVLVNGNGQVKLCDFGV 149
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41349437 384 AvkfnsdTNEVDVPLNTRVGTKRYMAPEVLdESLNKNHFQPY-IMADIYSFGLIIWEMARRC 444
Cdd:cd06622 150 S------GNLVASLAKTNIGCQSYMAPERI-KSGGPNQNPTYtVQSDVWSLGLSILEMALGR 204
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
240-514 2.87e-11

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: 64.70  E-value: 2.87e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 240 VGKGRYGEVWMGKWR--GEKVAVK-VFFTTEE----ASWFRETEIYQTVlmRHENILGFIaaDIKGTGSWTQLYLITDY- 311
Cdd:cd07845  15 IGEGTYGIVYRARDTtsGEIVALKkVRMDNERdgipISSLREITLLLNL--RHPNIVELK--EVVVGKHLDSIFLVMEYc 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 312 -HENGSLYD-----F----LKCATLDtraLLKlaysaacGLCHLHTEIygtqgkpaIAHRDLKSKNILIKKNGSCCIADL 381
Cdd:cd07845  91 eQDLASLLDnmptpFsesqVKCLMLQ---LLR-------GLQYLHENF--------IIHRDLKVSNLLLTDKGCLKIADF 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 382 GLAVKFNSdtneVDVPLNTRVGTKRYMAPEVLDESLNknhfqpYIMA-DIYSFGLIIWE-MARRCITGGIVEEYQLpyyN 459
Cdd:cd07845 153 GLARTYGL----PAKPMTPKVVTLWYRAPELLLGCTT------YTTAiDMWAVGCILAElLAHKPLLPGKSEIEQL---D 219
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41349437 460 MV------PSDPSYEDMREVVCVKR----------LRPIVSnrWNSDeclrAVLKLMSECWAHNPASRLTA 514
Cdd:cd07845 220 LIiqllgtPNESIWPGFSDLPLVGKftlpkqpynnLKHKFP--WLSE----AGLRLLNFLLMYDPKKRATA 284
PTKc_Ror1 cd05090
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
234-511 2.90e-11

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: 64.26  E-value: 2.90e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 234 IQMVRQVGKGRYGEVWMGKW------RGEKVAVKVFFTTEEASWFRETEIYQTVL--MRHENILGFIaadikgtGSWTQ- 304
Cdd:cd05090   7 VRFMEELGECAFGKIYKGHLylpgmdHAQLVAIKTLKDYNNPQQWNEFQQEASLMteLHHPNIVCLL-------GVVTQe 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 305 --LYLITDYHENGSLYDFL---------KCA---------TLDTRALLKLAYSAACGLCHLHTEIYgtqgkpaiAHRDLK 364
Cdd:cd05090  80 qpVCMLFEFMNQGDLHEFLimrsphsdvGCSsdedgtvksSLDHGDFLHIAIQIAAGMEYLSSHFF--------VHKDLA 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 365 SKNILIKKNGSCCIADLGLAVK-FNSDTNEVD----VPLntrvgtkRYMAPevldESLNKNHFQPyiMADIYSFGLIIWE 439
Cdd:cd05090 152 ARNILVGEQLHVKISDLGLSREiYSSDYYRVQnkslLPI-------RWMPP----EAIMYGKFSS--DSDIWSFGVVLWE 218
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41349437 440 MArrcitggiveEYQL-PYYNMvpsdpSYEDMREVVCVKRLRPIvsnrwnSDECLRAVLKLMSECWAHNPASR 511
Cdd:cd05090 219 IF----------SFGLqPYYGF-----SNQEVIEMVRKRQLLPC------SEDCPPRMYSLMTECWQEIPSRR 270
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
240-440 2.96e-11

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: 64.61  E-value: 2.96e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 240 VGKGRYGEVWMGKWR--GEKVAVKVFfttEEASWFRETEiyQTVLMRHENIL------GFIAADIKGTGSWTQLYLITDY 311
Cdd:cd05603   3 IGKGSFGKVLLAKRKcdGKFYAVKVL---QKKTILKKKE--QNHIMAERNVLlknlkhPFLVGLHYSFQTSEKLYFVLDY 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 312 HENGSLYDFL---KCaTLDTRALLKLAySAACGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNGSCCIADLGLAvkfn 388
Cdd:cd05603  78 VNGGELFFHLqreRC-FLEPRARFYAA-EVASAIGYLHSL--------NIIYRDLKPENILLDCQGHVVLTDFGLC---- 143
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 41349437 389 SDTNEVDVPLNTRVGTKRYMAPEVLDEslnknhfQPYIMA-DIYSFGLIIWEM 440
Cdd:cd05603 144 KEGMEPEETTSTFCGTPEYLAPEVLRK-------EPYDRTvDWWCLGAVLYEM 189
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
274-415 2.99e-11

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: 63.88  E-value: 2.99e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 274 ETEIYQTVlmRHENILGFIAaDIKGTgswTQLYLITDYHENGSLYDFLKCATLDT-RALLKLAYSAACGLCHLHteiygt 352
Cdd:cd14095  48 EVAILRRV--KHPNIVQLIE-EYDTD---TELYLVMELVKGGDLFDAITSSTKFTeRDASRMVTDLAQALKYLH------ 115
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41349437 353 qgKPAIAHRDLKSKNILIKKN--GSCCI--ADLGLAVkfnsdtnEVDVPLNTRVGTKRYMAPEVLDE 415
Cdd:cd14095 116 --SLSIVHRDIKPENLLVVEHedGSKSLklADFGLAT-------EVKEPLFTVCGTPTYVAPEILAE 173
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
237-440 3.05e-11

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: 64.97  E-value: 3.05e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 237 VRQVGKGRYGEVW--MGKWRGEKVAVKVFFTTEEASWF-----RETEIYQTvlMRHENILGFI---AADIKgTGSWTQLY 306
Cdd:cd07880  20 LKQVGSGAYGTVCsaLDRRTGAKVAIKKLYRPFQSELFakrayRELRLLKH--MKHENVIGLLdvfTPDLS-LDRFHDFY 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 307 LITDYHeNGSLYDFLKCATLDTRALLKLAYSAACGLCHLHTeiygtqgkPAIAHRDLKSKNILIKKNGSCCIADLGLAvk 386
Cdd:cd07880  97 LVMPFM-GTDLGKLMKHEKLSEDRIQFLVYQMLKGLKYIHA--------AGIIHRDLKPGNLAVNEDCELKILDFGLA-- 165
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 41349437 387 fnsdtNEVDVPLNTRVGTKRYMAPEVLdesLNKNHFQPYImaDIYSFGLIIWEM 440
Cdd:cd07880 166 -----RQTDSEMTGYVVTRWYRAPEVI---LNWMHYTQTV--DIWSVGCIMAEM 209
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
235-440 3.51e-11

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: 63.53  E-value: 3.51e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 235 QMVRQVGKGRYGEVWM--GKWRGEKVAVKVFFTTEEASWFR------ETEIYQTVLMRHENILGFI-AADIKGTgswtqL 305
Cdd:cd06625   3 KQGKLLGQGAFGQVYLcyDADTGRELAVKQVEIDPINTEASkevkalECEIQLLKNLQHERIVQYYgCLQDEKS-----L 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 306 YLITDYHENGSLYDFLKC-ATLDTRALLKLAYSAACGLCHLHTEIygtqgkpaIAHRDLKSKNILIKKNGSCCIADLGLA 384
Cdd:cd06625  78 SIFMEYMPGGSVKDEIKAyGALTENVTRKYTRQILEGLAYLHSNM--------IVHRDIKGANILRDSNGNVKLGDFGAS 149
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 41349437 385 VKFNsdTNEVDVPLNTRVGTKRYMAPEVLD-ESLNKNhfqpyimADIYSFGLIIWEM 440
Cdd:cd06625 150 KRLQ--TICSSTGMKSVTGTPYWMSPEVINgEGYGRK-------ADIWSVGCTVVEM 197
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
240-523 3.51e-11

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: 63.50  E-value: 3.51e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 240 VGKGRYGEVWMG--KWRGEKVAVKVFF--TTEEASWFRETEIYQTvLMRHENILGFIAADIKGTGSwtqlYLIT-DYHEN 314
Cdd:cd13987   1 LGEGTYGKVLLAvhKGSGTKMALKFVPkpSTKLKDFLREYNISLE-LSVHPHIIKTYDVAFETEDY----YVFAqEYAPY 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 315 GSLYDFLK-CATLDTRALLKLAYSAACGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNgSCC---IADLGLavkfnsd 390
Cdd:cd13987  76 GDLFSIIPpQVGLPEERVKRCAAQLASALDFMHSK--------NLVHRDIKPENVLLFDK-DCRrvkLCDFGL------- 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 391 TNEVDVPLNTRVGTKRYMAPEVLDESLNKNhFQPYIMADIYSFGLIIWemarRCITGgiveeyQLPYYNMVPSDPSYEdm 470
Cdd:cd13987 140 TRRVGSTVKRVSGTIPYTAPEVCEAKKNEG-FVVDPSIDVWAFGVLLF----CCLTG------NFPWEKADSDDQFYE-- 206
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 41349437 471 REVVCVKRLRPIVSNRWN--SDECLRAVLKLMSecwaHNPASRLTALRIKKTLAK 523
Cdd:cd13987 207 EFVRWQKRKNTAVPSQWRrfTPKALRMFKKLLA----PEPERRCSIKEVFKYLGD 257
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
240-447 3.57e-11

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: 63.54  E-value: 3.57e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 240 VGKGRYGEVWMGKWR---GEKVAVKVFFTTE--EASWFRETEIYQTVLMRHENILGFIaaDIKGTGSwtQLYLITDYHEN 314
Cdd:cd14120   1 IGHGAFAVVFKGRHRkkpDLPVAIKCITKKNlsKSQNLLGKEIKILKELSHENVVALL--DCQETSS--SVYLVMEYCNG 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 315 GSLYDFL-KCATL--DT-RALLKlaySAACGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNGSCC---------IADL 381
Cdd:cd14120  77 GDLADYLqAKGTLseDTiRVFLQ---QIAAAMKALHSK--------GIVHRDLKPQNILLSHNSGRKpspndirlkIADF 145
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41349437 382 GLAVKFNSDTNEVdvplnTRVGTKRYMAPEVLdESLNKNhfqpyIMADIYSFGLIIWEmarrCITG 447
Cdd:cd14120 146 GFARFLQDGMMAA-----TLCGSPMYMAPEVI-MSLQYD-----AKADLWSIGTIVYQ----CLTG 196
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
240-440 3.59e-11

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: 64.51  E-value: 3.59e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 240 VGKGRYGEVWMGKWR--GEKVAVKVFFTTEEAswfRETEIYQTVLMRheNILGFIAAD----IKGTG----SWTQLYLIT 309
Cdd:cd05586   1 IGKGTFGQVYQVRKKdtRRIYAMKVLSKKVIV---AKKEVAHTIGER--NILVRTALDespfIVGLKfsfqTPTDLYLVT 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 310 DYHENGSLYDFLKCATL--DTRALLKLAySAACGLCHLHteiygtqgKPAIAHRDLKSKNILIKKNGSCCIADLGLAvKF 387
Cdd:cd05586  76 DYMSGGELFWHLQKEGRfsEDRAKFYIA-ELVLALEHLH--------KNDIVYRDLKPENILLDANGHIALCDFGLS-KA 145
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 41349437 388 NSDTNEVDvplNTRVGTKRYMAPEVL--DESLNKnhfqpyiMADIYSFGLIIWEM 440
Cdd:cd05586 146 DLTDNKTT---NTFCGTTEYLAPEVLldEKGYTK-------MVDFWSLGVLVFEM 190
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
238-440 3.93e-11

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: 63.65  E-value: 3.93e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 238 RQVGKGRYGEVWMGKWR--GEKVAVKVFFTTEEASWF------RETEIYQTVlmRHENILG----FIAADIKgtgswtqL 305
Cdd:cd14165   7 INLGEGSYAKVKSAYSErlKCNVAIKIIDKKKAPDDFvekflpRELEILARL--NHKSIIKtyeiFETSDGK-------V 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 306 YLITDYHENGSLYDFLKC-ATLDTRALLKLAY--SAACGLCHlhteiygtqgKPAIAHRDLKSKNILIKKNGSCCIADLG 382
Cdd:cd14165  78 YIVMELGVQGDLLEFIKLrGALPEDVARKMFHqlSSAIKYCH----------ELDIVHRDLKCENLLLDKDFNIKLTDFG 147
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 41349437 383 LAVKFNSDTNEVDVPLNTRVGTKRYMAPEVLDeslnKNHFQPYiMADIYSFGLIIWEM 440
Cdd:cd14165 148 FSKRCLRDENGRIVLSKTFCGSAAYAAPEVLQ----GIPYDPR-IYDIWSLGVILYIM 200
PTKc_TrkA cd05092
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze ...
239-521 4.16e-11

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: 63.83  E-value: 4.16e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 239 QVGKGRYGEVWMGKW-----RGEK--VAVKVFFTTEEAS---WFRETEIYqTVLmRHENILGFIAADIKGTgswtQLYLI 308
Cdd:cd05092  12 ELGEGAFGKVFLAEChnllpEQDKmlVAVKALKEATESArqdFQREAELL-TVL-QHQHIVRFYGVCTEGE----PLIMV 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 309 TDYHENGSLYDFLK----------------CATLDTRALLKLAYSAACGLCHLHTEIYgtqgkpaiAHRDLKSKNILIKK 372
Cdd:cd05092  86 FEYMRHGDLNRFLRshgpdakildggegqaPGQLTLGQMLQIASQIASGMVYLASLHF--------VHRDLATRNCLVGQ 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 373 NGSCCIADLGLAvkfnSDTNEVDVplnTRVGTK-----RYMAPEvldeSLNKNHFQpyIMADIYSFGLIIWEMarrcITG 447
Cdd:cd05092 158 GLVVKIGDFGMS----RDIYSTDY---YRVGGRtmlpiRWMPPE----SILYRKFT--TESDIWSFGVVLWEI----FTY 220
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41349437 448 GIVEEYQLpyynmvpsdpsyEDMREVVCVKRLRPIVSNRwnsdECLRAVLKLMSECWAHNPASRLTALRIKKTL 521
Cdd:cd05092 221 GKQPWYQL------------SNTEAIECITQGRELERPR----TCPPEVYAIMQGCWQREPQQRHSIKDIHSRL 278
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
233-440 4.26e-11

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: 63.99  E-value: 4.26e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 233 QIQMVRQVGKGRYGEVWMGKWR--GEKVAVKVFFTTEEASWFRETEIY--QTVLMR--HENILGFIAAdikgtgSWTQ-- 304
Cdd:cd05612   2 DFERIKTIGTGTFGRVHLVRDRisEHYYALKVMAIPEVIRLKQEQHVHneKRVLKEvsHPFIIRLFWT------EHDQrf 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 305 LYLITDYHENGSLYDFLKCA-TLDTRALLKLAYSAACGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNGSCCIADLGL 383
Cdd:cd05612  76 LYMLMEYVPGGELFSYLRNSgRFSNSTGLFYASEIVCALEYLHSK--------EIVYRDLKPENILLDKEGHIKLTDFGF 147
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 41349437 384 AVKFNSDTnevdvplNTRVGTKRYMAPEVLDeslNKNHFQPyimADIYSFGLIIWEM 440
Cdd:cd05612 148 AKKLRDRT-------WTLCGTPEYLAPEVIQ---SKGHNKA---VDWWALGILIYEM 191
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
232-443 4.30e-11

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: 63.90  E-value: 4.30e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 232 KQIQMVRQVGKGRYGEVWMG---KWRGEKVAVK-VFFTTEEA----SWFRETEIYQTV-LMRHENILG-FIAADIKGTGS 301
Cdd:cd07862   1 QQYECVAEIGEGAYGKVFKArdlKNGGRFVALKrVRVQTGEEgmplSTIREVAVLRHLeTFEHPNVVRlFDVCTVSRTDR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 302 WTQLYLITDyHENGSLYDFLKCAT---LDTRALLKLAYSAACGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNGSCCI 378
Cdd:cd07862  81 ETKLTLVFE-HVDQDLTTYLDKVPepgVPTETIKDMMFQLLRGLDFLHSH--------RVVHRDLKPQNILVTSSGQIKL 151
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41349437 379 ADLGLAVKFNsdtneVDVPLNTRVGTKRYMAPEVLdesLNKNHFQPyimADIYSFGLIIWEMARR 443
Cdd:cd07862 152 ADFGLARIYS-----FQMALTSVVVTLWYRAPEVL---LQSSYATP---VDLWSVGCIFAEMFRR 205
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
232-462 4.48e-11

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: 63.97  E-value: 4.48e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 232 KQIQMVRQVGKGRYGEVWMGK--WRGEKVAVKVFFTTEEASwfRETEIYQTVLMR---HENILGFIAADIKGTgswtQLY 306
Cdd:cd06655  19 KKYTRYEKIGQGASGTVFTAIdvATGQEVAIKQINLQKQPK--KELIINEILVMKelkNPNIVNFLDSFLVGD----ELF 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 307 LITDYHENGSLYDFLKCATLDTRALLKLAYSAACGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNGSCCIADLGLAVK 386
Cdd:cd06655  93 VVMEYLAGGSLTDVVTETCMDEAQIAAVCRECLQALEFLHAN--------QVIHRDIKSDNVLLGMDGSVKLTDFGFCAQ 164
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41349437 387 FNSDTNEvdvpLNTRVGTKRYMAPEVldesLNKNHFQPYImaDIYSFGLIIWEMArrcitggiveEYQLPYYNMVP 462
Cdd:cd06655 165 ITPEQSK----RSTMVGTPYWMAPEV----VTRKAYGPKV--DIWSLGIMAIEMV----------EGEPPYLNENP 220
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
238-438 4.97e-11

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: 63.68  E-value: 4.97e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 238 RQVGKGRYGEVWMGK--WRGEKVAVKVFFTTEEAswfRETEIYQTV-----LMRHENILGFIAADIKGTGSWTQL---YL 307
Cdd:cd14036   6 RVIAEGGFAFVYEAQdvGTGKEYALKRLLSNEEE---KNKAIIQEInfmkkLSGHPNIVQFCSAASIGKEESDQGqaeYL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 308 ITDYHENGSLYDFLK------CATLDTraLLKLAYSAACGLCHLHTEiygtqgKPAIAHRDLKSKNILIKKNGSCCIADl 381
Cdd:cd14036  83 LLTELCKGQLVDFVKkveapgPFSPDT--VLKIFYQTCRAVQHMHKQ------SPPIIHRDLKIENLLIGNQGQIKLCD- 153
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41349437 382 glavkFNSDTNEVDVPLN--------------TRVGTKRYMAPEVLDESLNknhFQPYIMADIYSFGLIIW 438
Cdd:cd14036 154 -----FGSATTEAHYPDYswsaqkrslvedeiTRNTTPMYRTPEMIDLYSN---YPIGEKQDIWALGCILY 216
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
240-464 5.67e-11

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: 63.11  E-value: 5.67e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 240 VGKGRYGEVWMGKWRGE---KVAVKVF----FTTEEASWFRETEIYQTvlMRHENILGFIA-ADIKGTgswtqLYLITDY 311
Cdd:cd14202  10 IGHGAFAVVFKGRHKEKhdlEVAVKCInkknLAKSQTLLGKEIKILKE--LKHENIVALYDfQEIANS-----VYLVMEY 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 312 HENGSLYDFL---KCATLDTRALLKLAYSAACGLCHlhteiygtqgKPAIAHRDLKSKNILIKKNG-------SCCI--A 379
Cdd:cd14202  83 CNGGDLADYLhtmRTLSEDTIRLFLQQIAGAMKMLH----------SKGIIHRDLKPQNILLSYSGgrksnpnNIRIkiA 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 380 DLGLAVKFNSDTNEVdvplnTRVGTKRYMAPEVldesLNKNHFQPyiMADIYSFGLIIWEmarrCITGgiveeyQLPYYN 459
Cdd:cd14202 153 DFGFARYLQNNMMAA-----TLCGSPMYMAPEV----IMSQHYDA--KADLWSIGTIIYQ----CLTG------KAPFQA 211

                ....*
gi 41349437 460 MVPSD 464
Cdd:cd14202 212 SSPQD 216
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
239-519 7.04e-11

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: 7.04e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 239 QVGKGRYGEVWMG--KWRGEKVAVKVFFTTEEASwfRETEIYQTVLMR---HENILGFIAADIKGTgswtQLYLITDYHE 313
Cdd:cd06657  27 KIGEGSTGIVCIAtvKSSGKLVAVKKMDLRKQQR--RELLFNEVVIMRdyqHENVVEMYNSYLVGD----ELWVVMEFLE 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 314 NGSLYDFLKCATLDTRALLKLAYSAACGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNGSCCIADLGLAVKFNSDTNE 393
Cdd:cd06657 101 GGALTDIVTHTRMNEEQIAAVCLAVLKALSVLHAQ--------GVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPR 172
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 394 vdvpLNTRVGTKRYMAPEVldesLNKNHFQPYImaDIYSFGLIIWEMArrcitggiveEYQLPYYNmvpsDPSYEDMREV 473
Cdd:cd06657 173 ----RKSLVGTPYWMAPEL----ISRLPYGPEV--DIWSLGIMVIEMV----------DGEPPYFN----EPPLKAMKMI 228
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 41349437 474 vcVKRLRPIVSNRWNSDECLRAVLKLMsecWAHNPASRLTALRIKK 519
Cdd:cd06657 229 --RDNLPPKLKNLHKVSPSLKGFLDRL---LVRDPAQRATAAELLK 269
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
304-471 7.73e-11

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: 63.54  E-value: 7.73e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 304 QLYLITDYHENGSLYDFLKCA-TLDTRALLKLAYSAACGLCHLhteiygtQGKPAIAHRDLKSKNILIKKNGSCCIADLG 382
Cdd:cd06650  77 EISICMEHMDGGSLDQVLKKAgRIPEQILGKVSIAVIKGLTYL-------REKHKIMHRDVKPSNILVNSRGEIKLCDFG 149
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 383 LAVKFnsdtneVDVPLNTRVGTKRYMAPevldESLNKNHFQpyIMADIYSFGLIIWEMA--RRCITGGIVEEYQLPYYNM 460
Cdd:cd06650 150 VSGQL------IDSMANSFVGTRSYMSP----ERLQGTHYS--VQSDIWSMGLSLVEMAvgRYPIPPPDAKELELMFGCQ 217
                       170
                ....*....|.
gi 41349437 461 VPSDPSYEDMR 471
Cdd:cd06650 218 VEGDAAETPPR 228
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
240-519 7.73e-11

Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase 8; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP3K8 is also called Tumor progression locus 2 (Tpl2) or Cancer Osaka thyroid (Cot), and was first identified as a proto-oncogene in T-cell lymphoma induced by MoMuL virus and in breast carcinoma induced by MMTV. Activated MAP3K8 induces various MAPK pathways including Extracellular Regulated Kinase (ERK) 1/2, c-Jun N-terminal kinase (JNK), and p38. It plays a pivotal role in innate immunity, linking Toll-like receptors to the production of TNF and the activation of ERK in macrophages. It is also required in interleukin-1beta production and is critical in host defense against Gram-positive bacteria. 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 MAP3K8 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: 270897 [Multi-domain]  Cd Length: 256  Bit Score: 62.72  E-value: 7.73e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 240 VGKGRYGEVWMGKWRGEK--VAVKVFFTTEeaswFRETEIYQTVLMRHENIlgfiaADIKGTGSWTQ-LYLITDYHENGS 316
Cdd:cd13995  12 IPRGAFGKVYLAQDTKTKkrMACKLIPVEQ----FKPSDVEIQACFRHENI-----AELYGALLWEEtVHLFMEAGEGGS 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 317 LYDFLK-CATLDTRALLKLAYSAACGLCHLHTEiygtqgkpAIAHRDLKSKNILIKkNGSCCIADLGLAVKFnsdTNEVD 395
Cdd:cd13995  83 VLEKLEsCGPMREFEIIWVTKHVLKGLDFLHSK--------NIIHHDIKPSNIVFM-STKAVLVDFGLSVQM---TEDVY 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 396 VPLNTRvGTKRYMAPEVLdesLNKNHfqpYIMADIYSFGLIIWEMarrcITGgiveeyQLPYYNMVPSD--PSYedmreV 473
Cdd:cd13995 151 VPKDLR-GTEIYMSPEVI---LCRGH---NTKADIYSLGATIIHM----QTG------SPPWVRRYPRSayPSY-----L 208
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 41349437 474 VCVKRLRPIVSNRwnSDECLRAVLKLMSECWAHNPASRLTALRIKK 519
Cdd:cd13995 209 YIIHKQAPPLEDI--AQDCSPAMRELLEAALERNPNHRSSAAELLK 252
PTKc_Ror2 cd05091
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
234-511 8.16e-11

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: 63.11  E-value: 8.16e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 234 IQMVRQVGKGRYGEVWMGKWRG-------EKVAVKVFFTTEEASwFREtEIYQTVLMR----HENILGFIAADIKGTgsw 302
Cdd:cd05091   8 VRFMEELGEDRFGKVYKGHLFGtapgeqtQAVAIKTLKDKAEGP-LRE-EFRHEAMLRsrlqHPNIVCLLGVVTKEQ--- 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 303 tQLYLITDYHENGSLYDFLKC-----------------ATLDTRALLKLAYSAACGLCHLHTEiygtqgkpAIAHRDLKS 365
Cdd:cd05091  83 -PMSMIFSYCSHGDLHEFLVMrsphsdvgstdddktvkSTLEPADFLHIVTQIAAGMEYLSSH--------HVVHKDLAT 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 366 KNILIKKNGSCCIADLGLAVK-FNSDTNEVdvpLNTRVGTKRYMAPEVLdeslnkNHFQPYIMADIYSFGLIIWEmarrc 444
Cdd:cd05091 154 RNVLVFDKLNVKISDLGLFREvYAADYYKL---MGNSLLPIRWMSPEAI------MYGKFSIDSDIWSYGVVLWE----- 219
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41349437 445 itggiVEEYQL-PYYNMvpsdpSYEDMREVVCVKRLRPIvsnrwnSDECLRAVLKLMSECWAHNPASR 511
Cdd:cd05091 220 -----VFSYGLqPYCGY-----SNQDVIEMIRNRQVLPC------PDDCPAWVYTLMLECWNEFPSRR 271
STKc_RIP2 cd14026
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze ...
237-529 8.29e-11

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: 63.01  E-value: 8.29e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 237 VRQVGKGRYGEVWMGK---WRgEKVAVKVF------FTTEEASWFRETEIYQTVlmRHENILgfiaaDIKGTGSWTQLY- 306
Cdd:cd14026   2 LRYLSRGAFGTVSRARhadWR-VTVAIKCLkldspvGDSERNCLLKEAEILHKA--RFSYIL-----PILGICNEPEFLg 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 307 LITDYHENGSLYDFLKCATLDTRAL----LKLAYSAACGLCHLHTEiygtqgKPAIAHRDLKSKNILIKKNGSCCIADLG 382
Cdd:cd14026  74 IVTEYMTNGSLNELLHEKDIYPDVAwplrLRILYEIALGVNYLHNM------SPPLLHHDLKTQNILLDGEFHVKIADFG 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 383 LA----VKFNSDTNEVDVPLNtrvGTKRYMAPEVLDESLNKnhfQPYIMADIYSFGLIIWE-MARRcitggiveeyqlpy 457
Cdd:cd14026 148 LSkwrqLSISQSRSSKSAPEG---GTIIYMPPEEYEPSQKR---RASVKHDIYSYAIIMWEvLSRK-------------- 207
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41349437 458 ynmVPSDPSYEDMREVVCVKR-LRPIVS-NRWNSDECLRA-VLKLMSECWAHNPASRLTALRIKKTLAKMVESQD 529
Cdd:cd14026 208 ---IPFEEVTNPLQIMYSVSQgHRPDTGeDSLPVDIPHRAtLINLIESGWAQNPDERPSFLKCLIELEPVLRTFD 279
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
241-441 9.19e-11

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: 62.43  E-value: 9.19e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 241 GKGRYGEVWMGKWRGEKV--AVK-VFFTTEEASWFRETEIYQTVLMRHENILGFIAADIKGT-----------GSWTQLy 306
Cdd:cd06624  17 GKGTFGVVYAARDLSTQVriAIKeIPERDSREVQPLHEEIALHSRLSHKNIVQYLGSVSEDGffkifmeqvpgGSLSAL- 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 307 LITDYhenGSLYDFLKCATLDTRALLKlaysaacGLCHLHTEiygtqgkpAIAHRDLKSKNILIKK-NGSCCIADLGlav 385
Cdd:cd06624  96 LRSKW---GPLKDNENTIGYYTKQILE-------GLKYLHDN--------KIVHRDIKGDNVLVNTySGVVKISDFG--- 154
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 386 kfnsdTNEVDVPLN----TRVGTKRYMAPEVLDESLnKNHFQPyimADIYSFGLIIWEMA 441
Cdd:cd06624 155 -----TSKRLAGINpcteTFTGTLQYMAPEVIDKGQ-RGYGPP---ADIWSLGCTIIEMA 205
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
255-514 9.48e-11

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: 62.68  E-value: 9.48e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 255 GEKVAVKVF------FTTEEASWFRETEIYQTVLMRHENILGFIAADIKGTGSWTQLYLITDYHENGSLYDFL-KCATL- 326
Cdd:cd14181  35 GQEFAVKIIevtaerLSPEQLEEVRSSTLKEIHILRQVSGHPSIITLIDSYESSTFIFLVFDLMRRGELFDYLtEKVTLs 114
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 327 --DTRALLKLAYSAacgLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNGSCCIADLGLAVKFnsdtnEVDVPLNTRVGT 404
Cdd:cd14181 115 ekETRSIMRSLLEA---VSYLHAN--------NIVHRDLKPENILLDDQLHIKLSDFGFSCHL-----EPGEKLRELCGT 178
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 405 KRYMAPEVLDESLNKNHFQPYIMADIYSFGLIIwemarrcitggiveeyqlpyYNMVPSDPSYEDMREVVcvkRLRPIVS 484
Cdd:cd14181 179 PGYLAPEILKCSMDETHPGYGKEVDLWACGVIL--------------------FTLLAGSPPFWHRRQML---MLRMIME 235
                       250       260       270
                ....*....|....*....|....*....|....*
gi 41349437 485 NRWNS-----DECLRAVLKLMSECWAHNPASRLTA 514
Cdd:cd14181 236 GRYQFsspewDDRSSTVKDLISRLLVVDPEIRLTA 270
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
235-445 1.12e-10

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: 62.28  E-value: 1.12e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 235 QMVRQVGKGRYGEVWMGKWR-GEKVAVKVFFT---TEEASWF---RETEIYQTvlMRHENILGFIAAdikgTGSWTQLYL 307
Cdd:cd14161   6 EFLETLGKGTYGRVKKARDSsGRLVAIKSIRKdriKDEQDLLhirREIEIMSS--LNHPHIISVYEV----FENSSKIVI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 308 ITDYHENGSLYDFL----KCATLDTRALLKLAYSAAcGLCHlhteiygtqgKPAIAHRDLKSKNILIKKNGSCCIADLGL 383
Cdd:cd14161  80 VMEYASRGDLYDYIserqRLSELEARHFFRQIVSAV-HYCH----------ANGIVHRDLKLENILLDANGNIKIADFGL 148
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41349437 384 AVKFNSDTNevdvpLNTRVGTKRYMAPEVLDEslnknhfQPYI--MADIYSFGLIIWEMARRCI 445
Cdd:cd14161 149 SNLYNQDKF-----LQTYCGSPLYASPEIVNG-------RPYIgpEVDSWSLGVLLYILVHGTM 200
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
235-517 1.17e-10

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: 62.35  E-value: 1.17e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 235 QMVRQVGKGRYGEVWMGKWRGEKV--AVKVFFTTEE---ASWFRETEIYQTVlmRHENILGFIAADikgtgswtqlylit 309
Cdd:cd06643   8 EIVGELGDGAFGKVYKAQNKETGIlaAAKVIDTKSEeelEDYMVEIDILASC--DHPNIVKLLDAF-------------- 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 310 dYHENG--SLYDFLKCATLDT------RALLKLAYSAAC-----GLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNGSC 376
Cdd:cd06643  72 -YYENNlwILIEFCAGGAVDAvmleleRPLTEPQIRVVCkqtleALVYLHEN--------KIIHRDLKAGNILFTLDGDI 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 377 CIADLGLAVKFNSDTNEVDvplnTRVGTKRYMAPEVLDESLNKNhfQPY-IMADIYSFGLIIWEMArrcitggiveEYQL 455
Cdd:cd06643 143 KLADFGVSAKNTRTLQRRD----SFIGTPYWMAPEVVMCETSKD--RPYdYKADVWSLGVTLIEMA----------QIEP 206
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41349437 456 PYYNMVPsdpsyedMREVVCVKRLRPIV---SNRWNSDeclraVLKLMSECWAHNPASRLTALRI 517
Cdd:cd06643 207 PHHELNP-------MRVLLKIAKSEPPTlaqPSRWSPE-----FKDFLRKCLEKNVDARWTTSQL 259
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
235-441 1.19e-10

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: 62.44  E-value: 1.19e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 235 QMVRQVGKGRYGEVWMGKWR--GEKVAVKVFFTTEEASWFRET---EIYQTVLMRHENILGFIAADIKGTgswtQLYLIT 309
Cdd:cd07846   4 ENLGLVGEGSYGMVMKCRHKetGQIVAIKKFLESEDDKMVKKIamrEIKMLKQLRHENLVNLIEVFRRKK----RWYLVF 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 310 DYHENGSLYDFLK-CATLDTRALLKLAYSA--ACGLCHLHTeiygtqgkpaIAHRDLKSKNILIKKNGSCCIADLGLAVK 386
Cdd:cd07846  80 EFVDHTVLDDLEKyPNGLDESRVRKYLFQIlrGIDFCHSHN----------IIHRDIKPENILVSQSGVVKLCDFGFART 149
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 41349437 387 FNSdTNEVdvpLNTRVGTKRYMAPEVL--DESLNKnhfqpyiMADIYSFGLIIWEMA 441
Cdd:cd07846 150 LAA-PGEV---YTDYVATRWYRAPELLvgDTKYGK-------AVDVWAVGCLVTEML 195
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
232-460 1.69e-10

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: 61.70  E-value: 1.69e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 232 KQIQMVRQVGKGRYGEVWMG--KWRGEKVAVK-VFFTTEEAswfreTEIYQTVL--------MRHENILGFIAADIKGTG 300
Cdd:cd06607   1 KIFEDLREIGHGSFGAVYYArnKRTSEVVAIKkMSYSGKQS-----TEKWQDIIkevkflrqLRHPNTIEYKGCYLREHT 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 301 SWtqlyLITDYHEnGSLYDFLKcatLDTRALLKLAYSAAC-----GLCHLHTeiygtQGKpaiAHRDLKSKNILIKKNGS 375
Cdd:cd06607  76 AW----LVMEYCL-GSASDIVE---VHKKPLQEVEIAAIChgalqGLAYLHS-----HNR---IHRDVKAGNILLTEPGT 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 376 CCIADLGLAvkfnsdtnEVDVPLNTRVGTKRYMAPEV---LDESlnknhfqPYI-MADIYSFGLIIWEMARRcitggive 451
Cdd:cd06607 140 VKLADFGSA--------SLVCPANSFVGTPYWMAPEVilaMDEG-------QYDgKVDVWSLGITCIELAER-------- 196

                ....*....
gi 41349437 452 eyQLPYYNM 460
Cdd:cd06607 197 --KPPLFNM 203
PTKc_IGF-1R cd05062
Catalytic domain of the Protein Tyrosine Kinase, Insulin-like Growth Factor-1 Receptor; PTKs ...
232-517 2.00e-10

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: 61.59  E-value: 2.00e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 232 KQIQMVRQVGKGRYGEVWMGKWRG-------EKVAVKvffTTEEASWFRETEIY--QTVLMRHEN------ILGFIAadi 296
Cdd:cd05062   6 EKITMSRELGQGSFGMVYEGIAKGvvkdepeTRVAIK---TVNEAASMRERIEFlnEASVMKEFNchhvvrLLGVVS--- 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 297 KGTGSWTQLYLITdyheNGSLYDFLKCATLDT-----------RALLKLAYSAACGLCHLHTEIYgtqgkpaiAHRDLKS 365
Cdd:cd05062  80 QGQPTLVIMELMT----RGDLKSYLRSLRPEMennpvqappslKKMIQMAGEIADGMAYLNANKF--------VHRDLAA 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 366 KNILIKKNGSCCIADLGLAvkfnSDTNEVDVplnTRVGTK-----RYMAPEVLDESLNKNHfqpyimADIYSFGLIIWEM 440
Cdd:cd05062 148 RNCMVAEDFTVKIGDFGMT----RDIYETDY---YRKGGKgllpvRWMSPESLKDGVFTTY------SDVWSFGVVLWEI 214
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41349437 441 ARrcitggIVEEyqlPYYNMvpsdpSYEDMREVVCVKRL--RPivsnrwnsDECLRAVLKLMSECWAHNPASRLTALRI 517
Cdd:cd05062 215 AT------LAEQ---PYQGM-----SNEQVLRFVMEGGLldKP--------DNCPDMLFELMRMCWQYNPKMRPSFLEI 271
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
239-494 2.05e-10

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: 61.20  E-value: 2.05e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 239 QVGKGRYGEVWMGKWR--GEKVAVKVFFTT---EEASWFRETEIYQTVLMRHENILGFIAAdikgTGSWTQLYLITDYHE 313
Cdd:cd14075   9 ELGSGNFSQVKLGIHQltKEKVAIKILDKTkldQKTQRLLSREISSMEKLHHPNIIRLYEV----VETLSKLHLVMEYAS 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 314 NGSLYDFL----KCATLDTRALLKLAYSAacgLCHLHteiygtqgKPAIAHRDLKSKNILIKKNGSCCIADLGLAVKFNS 389
Cdd:cd14075  85 GGELYTKIstegKLSESEAKPLFAQIVSA---VKHMH--------ENNIIHRDLKAENVFYASNNCVKVGDFGFSTHAKR 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 390 DTNevdvpLNTRVGTKRYMAPEVL-DEslnkNHFQPYImaDIYSFGLIIWEMA--------------RRCITGGiveEYQ 454
Cdd:cd14075 154 GET-----LNTFCGSPPYAAPELFkDE----HYIGIYV--DIWALGVLLYFMVtgvmpfraetvaklKKCILEG---TYT 219
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 41349437 455 LPYYnmvPSDPSYEDMREVvcvkrLRPIVSNRWNSDECLR 494
Cdd:cd14075 220 IPSY---VSEPCQELIRGI-----LQPVPSDRYSIDEIKN 251
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
230-485 2.15e-10

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: 62.00  E-value: 2.15e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 230 IAKQIQMVRQVGKGRYGEVW--MGKWRGEKVAVK----VFFTTEEAS-WFRETEIYQTVlmRHENILGFiaADI----KG 298
Cdd:cd07855   3 VGDRYEPIETIGSGAYGVVCsaIDTKSGQKVAIKkipnAFDVVTTAKrTLRELKILRHF--KHDNIIAI--RDIlrpkVP 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 299 TGSWTQLYLITDYHENgSLYDFLKCA---TLD-TRALLklaYSAACGLCHLHTeiygtqgkPAIAHRDLKSKNILIKKNG 374
Cdd:cd07855  79 YADFKDVYVVLDLMES-DLHHIIHSDqplTLEhIRYFL---YQLLRGLKYIHS--------ANVIHRDLKPSNLLVNENC 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 375 SCCIADLGLAVKFNSDTNEVDVPLNTRVGTKRYMAPEVLDEslnknhFQPYIMA-DIYSFGLIIWEM-ARRCITGGIVEE 452
Cdd:cd07855 147 ELKIGDFGMARGLCTSPEEHKYFMTEYVATRWYRAPELMLS------LPEYTQAiDMWSVGCIFAEMlGRRQLFPGKNYV 220
                       250       260       270
                ....*....|....*....|....*....|...
gi 41349437 453 YQLPYYNMVPSDPSYEDMREVVCvKRLRPIVSN 485
Cdd:cd07855 221 HQLQLILTVLGTPSQAVINAIGA-DRVRRYIQN 252
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
235-441 2.26e-10

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: 61.58  E-value: 2.26e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 235 QMVRQVGKGRYGEVW--MGKWRGEKVAVK--VFFTTEEASWFRE--TEIYQTVLMRHENILGFIAADIKGTgswtQLYLI 308
Cdd:cd08228   5 QIEKKIGRGQFSEVYraTCLLDRKPVALKkvQIFEMMDAKARQDcvKEIDLLKQLNHPNVIKYLDSFIEDN----ELNIV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 309 TDYHENGSLYDFLKC-----ATLDTRALLKLAYSAACGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNGSCCIADLGL 383
Cdd:cd08228  81 LELADAGDLSQMIKYfkkqkRLIPERTVWKYFVQLCSAVEHMHSR--------RVMHRDIKPANVFITATGVVKLGDLGL 152
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 41349437 384 AVKFNSDTNEVdvplNTRVGTKRYMAPEVLDEslNKNHFQpyimADIYSFGLIIWEMA 441
Cdd:cd08228 153 GRFFSSKTTAA----HSLVGTPYYMSPERIHE--NGYNFK----SDIWSLGCLLYEMA 200
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
235-440 2.32e-10

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: 62.30  E-value: 2.32e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 235 QMVRQVGKGRYGEVWMGKWR--GEKVAVKVfftteeaswfreteIYQTVLMRHENILGFIAA-DIKGTGS--W-TQL--- 305
Cdd:cd05573   4 EVIKVIGRGAFGEVWLVRDKdtGQVYAMKI--------------LRKSDMLKREQIAHVRAErDILADADspWiVRLhya 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 306 -------YLITDYHENGSLYDFL-KCATLD---TR---ALLKLAysaacgLCHLHteiygtqgKPAIAHRDLKSKNILIK 371
Cdd:cd05573  70 fqdedhlYLVMEYMPGGDLMNLLiKYDVFPeetARfyiAELVLA------LDSLH--------KLGFIHRDIKPDNILLD 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 372 KNGSCCIADLGLAVKFNSDTNEVDVPL-------------------------NTRVGTKRYMAPEVLDEslnknhfQPY- 425
Cdd:cd05573 136 ADGHIKLADFGLCTKMNKSGDRESYLNdsvntlfqdnvlarrrphkqrrvraYSAVGTPDYIAPEVLRG-------TGYg 208
                       250
                ....*....|....*
gi 41349437 426 IMADIYSFGLIIWEM 440
Cdd:cd05573 209 PECDWWSLGVILYEM 223
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
340-440 2.41e-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: 61.91  E-value: 2.41e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 340 CGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNGSCCIADLGLAVKFNSDTNevdvpLNTRVGTKRYMAPEVLDESlnK 419
Cdd:cd05632 115 CGLEDLHRE--------NTVYRDLKPENILLDDYGHIRISDLGLAVKIPEGES-----IRGRVGTVGYMAPEVLNNQ--R 179
                        90       100
                ....*....|....*....|.
gi 41349437 420 NHFQPyimaDIYSFGLIIWEM 440
Cdd:cd05632 180 YTLSP----DYWGLGCLIYEM 196
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
239-474 3.03e-10

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: 60.98  E-value: 3.03e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 239 QVGKGRYGEVWMGKWR---GEKVAVKVFFTTEEASWFRETEIYQTV------------LMRHENILGFIAADIKGTgswt 303
Cdd:cd08528   7 LLGSGAFGCVYKVRKKsngQTLLALKEINMTNPAFGRTEQERDKSVgdiisevniikeQLRHPNIVRYYKTFLEND---- 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 304 QLYLITDYHENGSLYDFL-----KCATLDTRALLKLAYSAACGLCHLHTEiygtqgkPAIAHRDLKSKNILIKKNGSCCI 378
Cdd:cd08528  83 RLYIVMELIEGAPLGEHFsslkeKNEHFTEDRIWNIFVQMVLALRYLHKE-------KQIVHRDLKPNNIMLGEDDKVTI 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 379 ADLGLAVKFNSDTNEvdvpLNTRVGTKRYMAPEVLdeslnKNhfQPYI-MADIYSFGLIIWEMArrcitggiveEYQLPY 457
Cdd:cd08528 156 TDFGLAKQKGPESSK----MTSVVGTILYSCPEIV-----QN--EPYGeKADIWALGCILYQMC----------TLQPPF 214
                       250       260       270
                ....*....|....*....|....*....|...
gi 41349437 458 Y--NM--------------VPSDPSYEDMREVV 474
Cdd:cd08528 215 YstNMltlatkiveaeyepLPEGMYSDDITFVI 247
PK_IRAK3 cd14160
Pseudokinase domain of Interleukin-1 Receptor Associated Kinase 3; The pseudokinase domain ...
240-524 3.14e-10

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: 61.05  E-value: 3.14e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 240 VGKGRYGEVWMGKWRGEKVAVKVFFTTEEASW-------FRETEIYQtvLMRHENILGfIAADIKGTgswTQLYLITDYH 312
Cdd:cd14160   1 IGEGEIFEVYRVRIGNRSYAVKLFKQEKKMQWkkhwkrfLSELEVLL--LFQHPNILE-LAAYFTET---EKFCLVYPYM 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 313 ENGSLYDFLKCATLDT----RALLKLAYSAACGLCHLHTeiygTQGKPAIAHrDLKSKNILIKKNGSCCIADLGLA-VKF 387
Cdd:cd14160  75 QNGTLFDRLQCHGVTKplswHERINILIGIAKAIHYLHN----SQPCTVICG-NISSANILLDDQMQPKLTDFALAhFRP 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 388 NSDTNEVDVPLNTRVGTKRYMAPEvldESLNKNHFQpyIMADIYSFGLIIWEMARRCitggiveeyqlpyyNMVPSDPSY 467
Cdd:cd14160 150 HLEDQSCTINMTTALHKHLWYMPE---EYIRQGKLS--VKTDVYSFGIVIMEVLTGC--------------KVVLDDPKH 210
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 41349437 468 EDMREVvcvkrLRPIVSNRwNSDECLRaVLKLMSECWAHNPASRLTALRIKKTLAKM 524
Cdd:cd14160 211 LQLRDL-----LHELMEKR-GLDSCLS-FLDLKFPPCPRNFSAKLFRLAGRCTATKA 260
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
238-440 3.24e-10

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: 60.96  E-value: 3.24e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 238 RQVGKGRYGEVWMGkWRGEK--------VAVKVFFTTEEASWFRETEIYQTVL----MRHENILGFIaaDIKGTGSWTQL 305
Cdd:cd14076   7 RTLGEGEFGKVKLG-WPLPKanhrsgvqVAIKLIRRDTQQENCQTSKIMREINilkgLTHPNIVRLL--DVLKTKKYIGI 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 306 YLitDYHENGSLYDFLkcatLDTRallKLAYSAAC--------GLCHLHteiygtqgKPAIAHRDLKSKNILIKKNGSCC 377
Cdd:cd14076  84 VL--EFVSGGELFDYI----LARR---RLKDSVACrlfaqlisGVAYLH--------KKGVVHRDLKLENLLLDKNRNLV 146
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41349437 378 IADLGLAVKFNSDTNEVdvpLNTRVGTKRYMAPEVLdeslnkNHFQPYI--MADIYSFGLIIWEM 440
Cdd:cd14076 147 ITDFGFANTFDHFNGDL---MSTSCGSPCYAAPELV------VSDSMYAgrKADIWSCGVILYAM 202
PTKc_Tie2 cd05088
Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the ...
234-528 3.30e-10

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: 61.17  E-value: 3.30e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 234 IQMVRQVGKGRYGEVWMGKWRGEKV----AVKVFFTTEEASWFRETEIYQTVLMR---HENILGFIAA-DIKGtgswtQL 305
Cdd:cd05088   9 IKFQDVIGEGNFGQVLKARIKKDGLrmdaAIKRMKEYASKDDHRDFAGELEVLCKlghHPNIINLLGAcEHRG-----YL 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 306 YLITDYHENGSLYDFLK-----------------CATLDTRALLKLAYSAACGLCHLHTEIYgtqgkpaiAHRDLKSKNI 368
Cdd:cd05088  84 YLAIEYAPHGNLLDFLRksrvletdpafaianstASTLSSQQLLHFAADVARGMDYLSQKQF--------IHRDLAARNI 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 369 LIKKNGSCCIADLGLavkfnSDTNEVDVPLNTRVGTKRYMAPEVLDESLNKNHfqpyimADIYSFGLIIWEMARrciTGG 448
Cdd:cd05088 156 LVGENYVAKIADFGL-----SRGQEVYVKKTMGRLPVRWMAIESLNYSVYTTN------SDVWSYGVLLWEIVS---LGG 221
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 449 IveeyqlPYYNMVPSDpSYEDMREVVCVKrlRPIvsnrwnsdECLRAVLKLMSECWAHNPASRLTALRIKKTLAKMVESQ 528
Cdd:cd05088 222 T------PYCGMTCAE-LYEKLPQGYRLE--KPL--------NCDDEVYDLMRQCWREKPYERPSFAQILVSLNRMLEER 284
PTKc_Kit cd05104
Catalytic domain of the Protein Tyrosine Kinase, Kit; PTKs catalyze the transfer of the ...
325-528 3.49e-10

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: 61.84  E-value: 3.49e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 325 TLDTRALLKLAYSAACGLCHLHTeiygtqgKPAIaHRDLKSKNILIKKNGSCCIADLGLAVKFNSDTNEVdVPLNTRVGT 404
Cdd:cd05104 210 ALDTEDLLSFSYQVAKGMEFLAS-------KNCI-HRDLAARNILLTHGRITKICDFGLARDIRNDSNYV-VKGNARLPV 280
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 405 KrYMAPEVLDESLNKnhFQpyimADIYSFGLIIWEmarrcitggIVEEYQLPYYNMvPSDPSYEDMrevvcVKRlrpivS 484
Cdd:cd05104 281 K-WMAPESIFECVYT--FE----SDVWSYGILLWE---------IFSLGSSPYPGM-PVDSKFYKM-----IKE-----G 333
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 41349437 485 NRWNSDECLRA-VLKLMSECWAHNPASRLTAlrikKTLAKMVESQ 528
Cdd:cd05104 334 YRMDSPEFAPSeMYDIMRSCWDADPLKRPTF----KQIVQLIEQQ 374
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
231-441 3.76e-10

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: 60.92  E-value: 3.76e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 231 AKQIQMVRQVGKGRYGEVWMGKWR--GEKVAVKVFFTTEEASW----FRETEIYQTVlmRHENILGFIAADIKGTGswtQ 304
Cdd:cd06620   4 NQDLETLKDLGAGNGGSVSKVLHIptGTIMAKKVIHIDAKSSVrkqiLRELQILHEC--HSPYIVSFYGAFLNENN---N 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 305 LYLITDYHENGSLYDFLKCAT-LDTRALLKLAYSAACGLCHLHTEIYgtqgkpaIAHRDLKSKNILIKKNGSCCIADLGL 383
Cdd:cd06620  79 IIICMEYMDCGSLDKILKKKGpFPEEVLGKIAVAVLEGLTYLYNVHR-------IIHRDIKPSNILVNSKGQIKLCDFGV 151
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 41349437 384 AVKFnsdTNEVdvpLNTRVGTKRYMAPEVLdESLNKNhfqpyIMADIYSFGLIIWEMA 441
Cdd:cd06620 152 SGEL---INSI---ADTFVGTSTYMSPERI-QGGKYS-----VKSDVWSLGLSIIELA 197
PTK_HER3 cd05111
Pseudokinase domain of the Protein Tyrosine Kinase, HER3; HER3 (ErbB3) is a member of the EGFR ...
233-440 3.91e-10

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: 60.74  E-value: 3.91e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 233 QIQMVRQVGKGRYGEVWMGKW--RGEKVAVKVFFTTEEASWFRET--EIYQTVL----MRHENILGFIaadikGTGSWTQ 304
Cdd:cd05111   8 ELRKLKVLGSGVFGTVHKGIWipEGDSIKIPVAIKVIQDRSGRQSfqAVTDHMLaigsLDHAYIVRLL-----GICPGAS 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 305 LYLITDYHENGSLYDFLKC--ATLDTRALLKLAYSAACGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNGSCCIADLG 382
Cdd:cd05111  83 LQLVTQLLPLGSLLDHVRQhrGSLGPQLLLNWCVQIAKGMYYLEEH--------RMVHRNLAARNVLLKSPSQVQVADFG 154
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41349437 383 LAVKFNSDT-----NEVDVPLntrvgtkRYMAPEVLdeslnknHFQPYI-MADIYSFGLIIWEM 440
Cdd:cd05111 155 VADLLYPDDkkyfySEAKTPI-------KWMALESI-------HFGKYThQSDVWSYGVTVWEM 204
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
225-462 3.97e-10

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: 60.83  E-value: 3.97e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 225 LVQRTIAKQIQMVRQVGKGRYGEVWMGK--WRGEKVAVKVF-FTTEEASWFRETEIYQTVLMRHENILGFIAADIKGTGS 301
Cdd:cd06645   4 LSRRNPQEDFELIQRIGSGTYGDVYKARnvNTGELAAIKVIkLEPGEDFAVVQQEIIMMKDCKHSNIVAYFGSYLRRDKL 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 302 WTQLylitDYHENGSLYDFLKC-ATLDTRALLKLAYSAACGLCHLHTeiygtQGKpaiAHRDLKSKNILIKKNGSCCIAD 380
Cdd:cd06645  84 WICM----EFCGGGSLQDIYHVtGPLSESQIAYVSRETLQGLYYLHS-----KGK---MHRDIKGANILLTDNGHVKLAD 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 381 LGLAVKFNSDTNEvdvpLNTRVGTKRYMAPEVLDESLNKNHFQpyiMADIYSFGLIIWEMArrcitggiveEYQLPYYNM 460
Cdd:cd06645 152 FGVSAQITATIAK----RKSFIGTPYWMAPEVAAVERKGGYNQ---LCDIWAVGITAIELA----------ELQPPMFDL 214

                ..
gi 41349437 461 VP 462
Cdd:cd06645 215 HP 216
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
238-440 4.06e-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: 60.78  E-value: 4.06e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 238 RQVGKGRYGEVWMGKWR--GEKVAVKVFFTTE------EASWFRETEIYQTVLMRHENILGFiAADIKGTgswtqLYLIT 309
Cdd:cd05631   6 RVLGKGGFGEVCACQVRatGKMYACKKLEKKRikkrkgEAMALNEKRILEKVNSRFVVSLAY-AYETKDA-----LCLVL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 310 DYHENGSL----YDFLKCATLDTRALLkLAYSAACGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNGSCCIADLGLAV 385
Cdd:cd05631  80 TIMNGGDLkfhiYNMGNPGFDEQRAIF-YAAELCCGLEDLQRE--------RIVYRDLKPENILLDDRGHIRISDLGLAV 150
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 41349437 386 KFNSDTNevdvpLNTRVGTKRYMAPEVLDESlnKNHFQPyimaDIYSFGLIIWEM 440
Cdd:cd05631 151 QIPEGET-----VRGRVGTVGYMAPEVINNE--KYTFSP----DWWGLGCLIYEM 194
TFP_LU_ECD_Babo cd23598
extracellular domain (ECD) found in Drosophila melanogaster Baboon and similar proteins; ...
59-132 4.23e-10

extracellular domain (ECD) found in Drosophila melanogaster Baboon and similar proteins; Baboon (Babo) is the Drosophila transforming growth factor-beta (TGF-beta)/activin-specific type I receptor that transmits signals through dSmad2. Baboon/dSmad2-mediated TGF-beta signaling is required during late larval stage for development of adult-specific neurons. In addition to dSmad2, it can Mad and bone morphogenetic protein (BMP)-specific R-Smad. Baboon is the ortholog of the human activin receptor-like kinase (ALK)-4/5/7. It contains an extracellular domain (ECD), which belongs to Ly-6 antigen/uPA receptor-like (LU) superfamily and exhibits a snake toxin-like fold (also known as three-finger toxin/3FTx fold or three-fingered protein/TFP domain fold).


Pssm-ID: 467127  Cd Length: 78  Bit Score: 56.20  E-value: 4.23e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437  59 LKCYCSGhCPDDaiNNTCITNGHCFAIIEEDDQGETTLASGCMKYE-----GSDFQCKDSPKAQLRRTIECCR-TNLCNQ 132
Cdd:cd23598   1 LKCYCDI-CKKT--NYTCETDGVCFTSTSLVKNGVIEYSYRCLDKKrlfppENPLICHSSKPRNDTFVIKCCKdYDFCNR 77
PTKc_Aatyk cd05042
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinases; PTKs ...
238-514 5.00e-10

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: 60.29  E-value: 5.00e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 238 RQVGKGRYGEVWMGK----WRGEKVAVKVFFTT----EEASWFRETEIYQTvlMRHENILGFIAADIKGTgswtQLYLIT 309
Cdd:cd05042   1 QEIGNGWFGKVLLGEiysgTSVAQVVVKELKASanpkEQDTFLKEGQPYRI--LQHPNILQCLGQCVEAI----PYLLVM 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 310 DYHENGSLYDFLKCATL------DTRALLKLAYSAACGLCHLHTEIYgtqgkpaiAHRDLKSKNILIKKNGSCCIADLGL 383
Cdd:cd05042  75 EFCDLGDLKAYLRSEREhergdsDTRTLQRMACEVAAGLAHLHKLNF--------VHSDLALRNCLLTSDLTVKIGDYGL 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 384 A-VKFNSDTNEVD----VPLntrvgtkRYMAPEVLDEslnknhFQPYIM-------ADIYSFGLIIWEMarrcitggiVE 451
Cdd:cd05042 147 AhSRYKEDYIETDdklwFPL-------RWTAPELVTE------FHDRLLvvdqtkySNIWSLGVTLWEL---------FE 204
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41349437 452 EYQLPYYNMVPSDPSYEDMRE---VVCVKRLRPIVSNRWnsdeclravLKLMSECWAhNPASRLTA 514
Cdd:cd05042 205 NGAQPYSNLSDLDVLAQVVREqdtKLPKPQLELPYSDRW---------YEVLQFCWL-SPEQRPAA 260
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
264-441 5.46e-10

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: 60.50  E-value: 5.46e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 264 FTTEEASWFREtEIYQTVLMRHENILGFI---AADIKGTGSwtqLYLITDYHENGSLYDFLK-CATLDTRALLKLAYSAA 339
Cdd:cd14031  48 LTKAEQQRFKE-EAEMLKGLQHPNIVRFYdswESVLKGKKC---IVLVTELMTSGTLKTYLKrFKVMKPKVLRSWCRQIL 123
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 340 CGLCHLHTEiygtqgKPAIAHRDLKSKNILIK-KNGSCCIADLGLAVKFNSDTNEvdvplnTRVGTKRYMAPEVLDESLN 418
Cdd:cd14031 124 KGLQFLHTR------TPPIIHRDLKCDNIFITgPTGSVKIGDLGLATLMRTSFAK------SVIGTPEFMAPEMYEEHYD 191
                       170       180
                ....*....|....*....|...
gi 41349437 419 KNhfqpyimADIYSFGLIIWEMA 441
Cdd:cd14031 192 ES-------VDVYAFGMCMLEMA 207
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
233-443 6.03e-10

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: 60.36  E-value: 6.03e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 233 QIQMVRQVGKGRYGEVWMGKWR--GEKVAVKV-----------FFTTEEASWFRETEIYQtvlmrHENILGF--IAADIK 297
Cdd:cd07863   1 QYEPVAEIGVGAYGTVYKARDPhsGHFVALKSvrvqtnedglpLSTVREVALLKRLEAFD-----HPNIVRLmdVCATSR 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 298 gTGSWTQLYLITDyHENGSLYDFLKCAT---LDTRALLKLAYSAACGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNG 374
Cdd:cd07863  76 -TDRETKVTLVFE-HVDQDLRTYLDKVPppgLPAETIKDLMRQFLRGLDFLHAN--------CIVHRDLKPENILVTSGG 145
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41349437 375 SCCIADLGLAVKFNsdtneVDVPLNTRVGTKRYMAPEVLdesLNKNHFQPyimADIYSFGLIIWEMARR 443
Cdd:cd07863 146 QVKLADFGLARIYS-----CQMALTPVVVTLWYRAPEVL---LQSTYATP---VDMWSVGCIFAEMFRR 203
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
235-442 6.67e-10

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: 60.51  E-value: 6.67e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 235 QMVRQVGKGRYGEVWMG--KWRGEKVAVKVF---F--TTEEASWFRETeiyqtVLMR---HENILGFIAADI--KGTGSW 302
Cdd:cd07850   3 QNLKPIGSGAQGIVCAAydTVTGQNVAIKKLsrpFqnVTHAKRAYREL-----VLMKlvnHKNIIGLLNVFTpqKSLEEF 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 303 TQLYLITDyhengsLYDFLKCAT----LDTRALLKLAYSAACGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNGSCCI 378
Cdd:cd07850  78 QDVYLVME------LMDANLCQViqmdLDHERMSYLLYQMLCGIKHLHSA--------GIIHRDLKPSNIVVKSDCTLKI 143
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41349437 379 ADLGLAVKFNSDTNevdvpLNTRVGTKRYMAPEV-LDESLNKNhfqpyimADIYSFGLIIWEMAR 442
Cdd:cd07850 144 LDFGLARTAGTSFM-----MTPYVVTRYYRAPEViLGMGYKEN-------VDIWSVGCIMGEMIR 196
PTKc_EphR_A10 cd05064
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A10; PTKs catalyze the ...
231-525 7.26e-10

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: 59.94  E-value: 7.26e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 231 AKQIQMVRQVGKGRYGEVWMG--KWRGEK---VAVKVFFTTEEASWFRE--TEIYQTVLMRHENILGFIAADIKGTgswt 303
Cdd:cd05064   4 NKSIKIERILGTGRFGELCRGclKLPSKRelpVAIHTLRAGCSDKQRRGflAEALTLGQFDHSNIVRLEGVITRGN---- 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 304 QLYLITDYHENGSLYDFLKC--ATLDTRALLKLAYSAACGLCHLhTEIygtqgkpAIAHRDLKSKNILIKKNGSCCIADL 381
Cdd:cd05064  80 TMMIVTEYMSNGALDSFLRKheGQLVAGQLMGMLPGLASGMKYL-SEM-------GYVHKGLAAHKVLVNSDLVCKISGF 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 382 GlavKFNSDTNEVdvpLNTRVGTKR---YMAPEvldeSLNKNHFQPyiMADIYSFGLIIWEmarrcitggiVEEY-QLPY 457
Cdd:cd05064 152 R---RLQEDKSEA---IYTTMSGKSpvlWAAPE----AIQYHHFSS--ASDVWSFGIVMWE----------VMSYgERPY 209
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41349437 458 YNMvpsdpSYED-MREVVCVKRLRPIVSnrwnsdeCLRAVLKLMSECWAHNPASRLTALRIKKTLAKMV 525
Cdd:cd05064 210 WDM-----SGQDvIKAVEDGFRLPAPRN-------CPNLLHQLMLDCWQKERGERPRFSQIHSILSKMV 266
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
232-440 7.34e-10

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: 60.21  E-value: 7.34e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 232 KQIQMVRQVGKGRYGEVWMGKWR--GEKVAVK-VFFTTEEASwfRETEIYQTvlMRHENILGFIAADIKGTGSWTQLYL- 307
Cdd:cd14137   4 ISYTIEKVIGSGSFGVVYQAKLLetGEVVAIKkVLQDKRYKN--RELQIMRR--LKHPNIVKLKYFFYSSGEKKDEVYLn 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 308 -ITDYHENgSLYDFLK-----CATLDTRaLLKL-AYSAACGLCHLHTeiygtQGkpaIAHRDLKSKNILI-KKNGSCCIA 379
Cdd:cd14137  80 lVMEYMPE-TLYRVIRhysknKQTIPII-YVKLySYQLFRGLAYLHS-----LG---ICHRDIKPQNLLVdPETGVLKLC 149
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41349437 380 DLGLAVKFNsdTNEvdvPLNTRVGTKRYMAPEVLDESLNKNHfqpyiMADIYSFGLIIWEM 440
Cdd:cd14137 150 DFGSAKRLV--PGE---PNVSYICSRYYRAPELIFGATDYTT-----AIDIWSAGCVLAEL 200
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
237-443 8.27e-10

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: 60.06  E-value: 8.27e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 237 VRQVGKGRYGEVWMGK--WRGEKVAVKVFFTTEEAS---W---FRETEIYQTVlmRHENILGFIAADIKGTGSWtqlyLI 308
Cdd:cd06635  30 LREIGHGSFGAVYFARdvRTSEVVAIKKMSYSGKQSnekWqdiIKEVKFLQRI--KHPNSIEYKGCYLREHTAW----LV 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 309 TDYHEnGSLYDFLKC--ATLDTRALLKLAYSAACGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNGSCCIADLGLAvk 386
Cdd:cd06635 104 MEYCL-GSASDLLEVhkKPLQEIEIAAITHGALQGLAYLHSH--------NMIHRDIKAGNILLTEPGQVKLADFGSA-- 172
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 41349437 387 fnsdtnEVDVPLNTRVGTKRYMAPEVLdESLNKNHFQPYImaDIYSFGLIIWEMARR 443
Cdd:cd06635 173 ------SIASPANSFVGTPYWMAPEVI-LAMDEGQYDGKV--DVWSLGITCIELAER 220
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
235-440 8.68e-10

Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The DMPK-like subfamily is composed of DMPK and DMPK-related cell division control protein 42 (Cdc42) binding kinase (MRCK). DMPK is expressed in skeletal and cardiac muscles, and in central nervous tissues. The functional role of DMPK is not fully understood. It may play a role in the signal transduction and homeostasis of calcium. The DMPK gene is implicated in myotonic dystrophy 1 (DM1), an inherited multisystemic disorder with symptoms that include muscle hyperexcitability, progressive muscle weakness and wasting, cataract development, testicular atrophy, and cardiac conduction defects. The genetic basis for DM1 is the mutational expansion of a CTG repeat in the 3'-UTR of DMPK. MRCK is activated via interaction with the small GTPase Cdc42. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. Three isoforms of MRCK are known, named alpha, beta and gamma. MRCKgamma is expressed in heart and skeletal muscles, unlike MRCKalpha and MRCKbeta, which are expressed ubiquitously. The DMPK-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: 270748 [Multi-domain]  Cd Length: 331  Bit Score: 60.44  E-value: 8.68e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 235 QMVRQVGKGRYGEVWMGKWRG-EKV-AVKVFFTTE-----EASWFRETeiyQTVLmrhenilgfiaadIKGTGSW-TQL- 305
Cdd:cd05597   4 EILKVIGRGAFGEVAVVKLKStEKVyAMKILNKWEmlkraETACFREE---RDVL-------------VNGDRRWiTKLh 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 306 ---------YLITDYHENGSLYDFLkcATLDTRALLKLA--YSAACGLC--HLHTEIYgtqgkpaiAHRDLKSKNILIKK 372
Cdd:cd05597  68 yafqdenylYLVMDYYCGGDLLTLL--SKFEDRLPEEMArfYLAEMVLAidSIHQLGY--------VHRDIKPDNVLLDR 137
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41349437 373 NGSCCIADLGLAVKFNSDTNevdVPLNTRVGTKRYMAPEVLdESLNKNHFQPYIMADIYSFGLIIWEM 440
Cdd:cd05597 138 NGHIRLADFGSCLKLREDGT---VQSSVAVGTPDYISPEIL-QAMEDGKGRYGPECDWWSLGVCMYEM 201
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
239-447 8.92e-10

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: 59.98  E-value: 8.92e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 239 QVGKGRYGEV--WMGKWRGEKVAVKVffTTEEAS------WFRETEIYQTvlMRHENILGF--IAADIKGTGSWTQLYLI 308
Cdd:cd14038   1 RLGTGGFGNVlrWINQETGEQVAIKQ--CRQELSpknrerWCLEIQIMKR--LNHPNVVAArdVPEGLQKLAPNDLPLLA 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 309 TDYHENGSLYDFLK----CATLDTRALLKLAYSAACGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNGSCC---IADL 381
Cdd:cd14038  77 MEYCQGGDLRKYLNqfenCCGLREGAILTLLSDISSALRYLHEN--------RIIHRDLKPENIVLQQGEQRLihkIIDL 148
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41349437 382 GLAVKFNSDTnevdvpLNTR-VGTKRYMAPEVLDEslnknhfQPYIMA-DIYSFGLIIWEmarrCITG 447
Cdd:cd14038 149 GYAKELDQGS------LCTSfVGTLQYLAPELLEQ-------QKYTVTvDYWSFGTLAFE----CITG 199
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
234-521 9.14e-10

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: 59.74  E-value: 9.14e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 234 IQMVRQVGKGRYGEVWMG---KWRGEK--VAVKVFFTTEEASwFRETEIYQTVLMR---HENILGFIaadikGTGSWTQL 305
Cdd:cd05056   8 ITLGRCIGEGQFGDVYQGvymSPENEKiaVAVKTCKNCTSPS-VREKFLQEAYIMRqfdHPHIVKLI-----GVITENPV 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 306 YLITDYHENGSLYDFLKC--ATLDTRALLKLAYSAACGLCHLHTEIYgtqgkpaiAHRDLKSKNILIKKNGSCCIADLGL 383
Cdd:cd05056  82 WIVMELAPLGELRSYLQVnkYSLDLASLILYAYQLSTALAYLESKRF--------VHRDIAARNVLVSSPDCVKLGDFGL 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 384 AVKFNSDT----NEVDVPLntrvgtkRYMAPevldESLNknhFQPYIMA-DIYSFGLIIWEMARRCITggiveeyqlPYY 458
Cdd:cd05056 154 SRYMEDESyykaSKGKLPI-------KWMAP----ESIN---FRRFTSAsDVWMFGVCMWEILMLGVK---------PFQ 210
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41349437 459 NMVPSDpsyedmreVVCV----KRLrPIVSNrwnsdeCLRAVLKLMSECWAHNPASRLTALRIKKTL 521
Cdd:cd05056 211 GVKNND--------VIGRiengERL-PMPPN------CPPTLYSLMTKCWAYDPSKRPRFTELKAQL 262
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
235-440 1.10e-09

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: 59.49  E-value: 1.10e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 235 QMVRQVGKGRYGEVWMGKWRGEK--VAVKVFFTTE------EASWFRETEIyQTVLmRHENILGFIA--ADIKgtgswtQ 304
Cdd:cd14117   9 DIGRPLGKGKFGNVYLAREKQSKfiVALKVLFKSQiekegvEHQLRREIEI-QSHL-RHPNILRLYNyfHDRK------R 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 305 LYLITDYHENGSLYDFL-KCATLDTRALLKLAYSAACGLCHLHteiygtqGKPAIaHRDLKSKNILIKKNGSCCIADLGL 383
Cdd:cd14117  81 IYLILEYAPRGELYKELqKHGRFDEQRTATFMEELADALHYCH-------EKKVI-HRDIKPENLLMGYKGELKIADFGW 152
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 41349437 384 AVKFNSdtnevdVPLNTRVGTKRYMAPEVLDeslNKNHFQPyimADIYSFGLIIWEM 440
Cdd:cd14117 153 SVHAPS------LRRRTMCGTLDYLPPEMIE---GRTHDEK---VDLWCIGVLCYEL 197
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
235-448 1.12e-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: 59.63  E-value: 1.12e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 235 QMVRQVGKGRYGEVWM-----GKWRGEKVAVKVF---FTTEEASWFRETEIYQTVLmRHENILGFIAADIKGTGSWTQLY 306
Cdd:cd05613   3 ELLKVLGTGAYGKVFLvrkvsGHDAGKLYAMKVLkkaTIVQKAKTAEHTRTERQVL-EHIRQSPFLVTLHYAFQTDTKLH 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 307 LITDYHENGSLYDFLKCATLDTRALLKLaYSA--ACGLCHLHteiygtqgKPAIAHRDLKSKNILIKKNGSCCIADLGLA 384
Cdd:cd05613  82 LILDYINGGELFTHLSQRERFTENEVQI-YIGeiVLALEHLH--------KLGIIYRDIKLENILLDSSGHVVLTDFGLS 152
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41349437 385 VKFNSDTNEVDVPLntrVGTKRYMAPEVLdESLNKNHFQPyimADIYSFGLIIWEMarrcITGG 448
Cdd:cd05613 153 KEFLLDENERAYSF---CGTIEYMAPEIV-RGGDSGHDKA---VDWWSLGVLMYEL----LTGA 205
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
237-496 1.17e-09

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: 59.65  E-value: 1.17e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 237 VRQVGKGRYGEVWMGK--WRGEKVAVKVFFTTEEASWFRETEIYQTVL----MRHENILGFIAADIKGTGSWtqlyLITD 310
Cdd:cd06634  20 LREIGHGSFGAVYFARdvRNNEVVAIKKMSYSGKQSNEKWQDIIKEVKflqkLRHPNTIEYRGCYLREHTAW----LVME 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 311 YHEnGSLYDFLKC--ATLDTRALLKLAYSAACGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNGSCCIADLGLAvkfn 388
Cdd:cd06634  96 YCL-GSASDLLEVhkKPLQEVEIAAITHGALQGLAYLHSH--------NMIHRDVKAGNILLTEPGLVKLGDFGSA---- 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 389 sdtnEVDVPLNTRVGTKRYMAPEVLdesLNKNHFQPYIMADIYSFGLIIWEMARRcitggiveeyQLPYYNMVPSDPSYE 468
Cdd:cd06634 163 ----SIMAPANSFVGTPYWMAPEVI---LAMDEGQYDGKVDVWSLGITCIELAER----------KPPLFNMNAMSALYH 225
                       250       260       270
                ....*....|....*....|....*....|....*
gi 41349437 469 dmrevvCVKRLRPIV-SNRWNS------DECLRAV 496
Cdd:cd06634 226 ------IAQNESPALqSGHWSEyfrnfvDSCLQKI 254
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
237-514 1.17e-09

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: 59.36  E-value: 1.17e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 237 VRQVGKGRYGEVWMGKWR--GEKVAVKVFFTTEEASWFRETEIYQTVLM---RHENILGFIAADIKGTgswtQLYLItdy 311
Cdd:cd07861   5 IEKIGEGTYGVVYKGRNKktGQIVAMKKIRLESEEEGVPSTAIREISLLkelQHPNIVCLEDVLMQEN----RLYLV--- 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 312 hengslYDFLKC------------ATLDTRALLKLAYSAACGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNGSCCIA 379
Cdd:cd07861  78 ------FEFLSMdlkkyldslpkgKYMDAELVKSYLYQILQGILFCHSR--------RVLHRDLKPQNLLIDNKGVIKLA 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 380 DLGLAVKFNsdtneVDVPLNT-RVGTKRYMAPEVLDESlnknhfQPYIM-ADIYSFGLIIWEMA-RRCITGGIVEEYQLP 456
Cdd:cd07861 144 DFGLARAFG-----IPVRVYThEVVTLWYRAPEVLLGS------PRYSTpVDIWSIGTIFAEMAtKKPLFHGDSEIDQLF 212
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41349437 457 YYNMVPSDPSYEDMREVVCVKRLRPIVSNrWNSDECLRAV-------LKLMSECWAHNPASRLTA 514
Cdd:cd07861 213 RIFRILGTPTEDIWPGVTSLPDYKNTFPK-WKKGSLRTAVknldedgLDLLEKMLIYDPAKRISA 276
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
336-440 1.18e-09

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: 59.92  E-value: 1.18e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 336 YSA--ACGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNGSCCIADLGLA---VKFNSDTnevdvplNTRVGTKRYMAP 410
Cdd:cd05570 101 YAAeiCLALQFLHER--------GIIYRDLKLDNVLLDAEGHIKIADFGMCkegIWGGNTT-------STFCGTPDYIAP 165
                        90       100       110
                ....*....|....*....|....*....|.
gi 41349437 411 EVLDEslnknhfQPYIMA-DIYSFGLIIWEM 440
Cdd:cd05570 166 EILRE-------QDYGFSvDWWALGVLLYEM 189
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
241-448 1.25e-09

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: 59.73  E-value: 1.25e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 241 GKGRYGEVWM-----GKWRGEKVAVKVFfttEEASWFRETEiyQTVLMRHE-NILG-----FIAADIKGTGSWTQLYLIT 309
Cdd:cd05584   5 GKGGYGKVFQvrkttGSDKGKIFAMKVL---KKASIVRNQK--DTAHTKAErNILEavkhpFIVDLHYAFQTGGKLYLIL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 310 DYHENGSLYDFL--KCATLDTRALLKLAySAACGLCHLHTeiygtQGkpaIAHRDLKSKNILIKKNGSCCIADLGLAvKF 387
Cdd:cd05584  80 EYLSGGELFMHLerEGIFMEDTACFYLA-EITLALGHLHS-----LG---IIYRDLKPENILLDAQGHVKLTDFGLC-KE 149
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41349437 388 NSDTNEVDvplNTRVGTKRYMAPEVLDESlnkNHFQPyimADIYSFGLIIWEMarrcITGG 448
Cdd:cd05584 150 SIHDGTVT---HTFCGTIEYMAPEILTRS---GHGKA---VDWWSLGALMYDM----LTGA 197
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
236-443 1.32e-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: 59.49  E-value: 1.32e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 236 MVRQVGKGRYGEVWMGKWR--GEKVAVK-----VFFTTEEAswFRETEIYQTVLMRHENILGF---------IAADIKGT 299
Cdd:cd13977   4 LIREVGRGSYGVVYEAVVRrtGARVAVKkircnAPENVELA--LREFWALSSIQRQHPNVIQLeecvlqrdgLAQRMSHG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 300 GSWTQLYL-----------------------ITDYHENGSLYDFLKCATLDTRALLKLAYSAACGLCHLHteiygtqgKP 356
Cdd:cd13977  82 SSKSDLYLllvetslkgercfdprsacylwfVMEFCDGGDMNEYLLSRRPDRQTNTSFMLQLSSALAFLH--------RN 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 357 AIAHRDLKSKNILI-KKNGSCC--IADLGLAVKFNSDTNEVDVPLN-------TRVGTKRYMAPEVLDeslnkNHFQPyi 426
Cdd:cd13977 154 QIVHRDLKPDNILIsHKRGEPIlkVADFGLSKVCSGSGLNPEEPANvnkhflsSACGSDFYMAPEVWE-----GHYTA-- 226
                       250
                ....*....|....*..
gi 41349437 427 MADIYSFGLIIWEMARR 443
Cdd:cd13977 227 KADIFALGIIIWAMVER 243
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
272-440 1.41e-09

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: 59.27  E-value: 1.41e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 272 FRETE-IYQTvlMRHENILGFIaadiKGTGSWTQLYLITDYHENGSLYDFL-KCATLDTRALLKLAYSAACGLCHLHTEi 349
Cdd:cd14173  47 FREVEmLYQC--QGHRNVLELI----EFFEEEDKFYLVFEKMRGGSILSHIhRRRHFNELEASVVVQDIASALDFLHNK- 119
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 350 ygtqgkpAIAHRDLKSKNILIKKNGSC-----CIADLGLAVKFNSDTNEVDVP-LNTRVGTKRYMAPEVLdESLNKNHFQ 423
Cdd:cd14173 120 -------GIAHRDLKPENILCEHPNQVspvkiCDFDLGSGIKLNSDCSPISTPeLLTPCGSAEYMAPEVV-EAFNEEASI 191
                       170
                ....*....|....*..
gi 41349437 424 PYIMADIYSFGLIIWEM 440
Cdd:cd14173 192 YDKRCDLWSLGVILYIM 208
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
240-443 1.44e-09

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: 59.69  E-value: 1.44e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 240 VGKGRYGEVWMGKWR--GEKVAVK----VFFTTEEAswfRET--EIYQTVLMRHENILGFIaaDI---KGTGSWTQLYLI 308
Cdd:cd07858  13 IGRGAYGIVCSAKNSetNEKVAIKkianAFDNRIDA---KRTlrEIKLLRHLDHENVIAIK--DImppPHREAFNDVYIV 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 309 -----TDYHE----NGSLYD-----FLkcatldtrallklaYSAACGLCHLHTeiygtqgkPAIAHRDLKSKNILIKKNG 374
Cdd:cd07858  88 yelmdTDLHQiirsSQTLSDdhcqyFL--------------YQLLRGLKYIHS--------ANVLHRDLKPSNLLLNANC 145
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41349437 375 SCCIADLGLAvKFNSDTNEVdvpLNTRVGTKRYMAPEVLdesLNKNHFQPYImaDIYSFGLIIWEMARR 443
Cdd:cd07858 146 DLKICDFGLA-RTTSEKGDF---MTEYVVTRWYRAPELL---LNCSEYTTAI--DVWSVGCIFAELLGR 205
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
235-442 1.53e-09

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: 59.27  E-value: 1.53e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 235 QMVRQVGKGRYGEVWMGKWR--GEKVAVKVFFTTEE---ASWFRETEIYQTVlmRHENILGFIaadikGTGSWT-QLYLI 308
Cdd:cd06644  15 EIIGELGDGAFGKVYKAKNKetGALAAAKVIETKSEeelEDYMVEIEILATC--NHPYIVKLL-----GAFYWDgKLWIM 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 309 TDYHENGSLYDFLkcATLDtRALLKLAYSAAC-----GLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNGSCCIADLGL 383
Cdd:cd06644  88 IEFCPGGAVDAIM--LELD-RGLTEPQIQVICrqmleALQYLHSM--------KIIHRDLKAGNVLLTLDGDIKLADFGV 156
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41349437 384 AVKfNSDTnevdvpLNTR---VGTKRYMAPEVLDESLNKNhfQPY-IMADIYSFGLIIWEMAR 442
Cdd:cd06644 157 SAK-NVKT------LQRRdsfIGTPYWMAPEVVMCETMKD--TPYdYKADIWSLGITLIEMAQ 210
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
233-440 1.66e-09

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: 58.45  E-value: 1.66e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 233 QIQMVRQVGKGRYGEVWM--GKWRGEKVAVKVFFTTEEASWFrETEIYQTVL---MRHENILGFiAADIKGTGswtQLYL 307
Cdd:cd08219   1 QYNVLRVVGEGSFGRALLvqHVNSDQKYAMKEIRLPKSSSAV-EDSRKEAVLlakMKHPNIVAF-KESFEADG---HLYI 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 308 ITDYHENGSLYDFLKC--ATLDTRALLKLAYSAAC-GLCHLHteiygtqgKPAIAHRDLKSKNILIKKNGSCCIADLGLA 384
Cdd:cd08219  76 VMEYCDGGDLMQKIKLqrGKLFPEDTILQWFVQMClGVQHIH--------EKRVLHRDIKSKNIFLTQNGKVKLGDFGSA 147
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 41349437 385 VKFNSdtnevdvPLN---TRVGTKRYMAPEVLdESLNKNHfqpyiMADIYSFGLIIWEM 440
Cdd:cd08219 148 RLLTS-------PGAyacTYVGTPYYVPPEIW-ENMPYNN-----KSDIWSLGCILYEL 193
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
241-443 1.70e-09

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: 58.60  E-value: 1.70e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 241 GKGRYGEVWMG-KWRGEKVAVK-VFFTTeeASWFRETEIYQTV--------LMRHENILGFIAADIKGTgswtQLYLITD 310
Cdd:cd06631  10 GKGAYGTVYCGlTSTGQLIAVKqVELDT--SDKEKAEKEYEKLqeevdllkTLKHVNIVGYLGTCLEDN----VVSIFME 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 311 YHENGSLYDFLK-CATLDTRALLKLAYSAACGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNGSCCIADLGLAVKF-- 387
Cdd:cd06631  84 FVPGGSIASILArFGALEEPVFCRYTKQILEGVAYLHNN--------NVIHRDIKGNNIMLMPNGVIKLIDFGCAKRLci 155
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 41349437 388 -NSDTNEVDVpLNTRVGTKRYMAPEVLDESlnkNHFQPyimADIYSFGLIIWEMARR 443
Cdd:cd06631 156 nLSSGSQSQL-LKSMRGTPYWMAPEVINET---GHGRK---SDIWSIGCTVFEMATG 205
PTKc_TrkB cd05093
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze ...
234-530 1.71e-09

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: 58.90  E-value: 1.71e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 234 IQMVRQVGKGRYGEVWMGKWRG-----EKVAVKVFfTTEEAS------WFRETEIYQTvlMRHENILGFIAADIKGTgsw 302
Cdd:cd05093   7 IVLKRELGEGAFGKVFLAECYNlcpeqDKILVAVK-TLKDASdnarkdFHREAELLTN--LQHEHIVKFYGVCVEGD--- 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 303 tQLYLITDYHENGSLYDFLKC--------------ATLDTRALLKLAYSAACGLCHLHTEIYgtqgkpaiAHRDLKSKNI 368
Cdd:cd05093  81 -PLIMVFEYMKHGDLNKFLRAhgpdavlmaegnrpAELTQSQMLHIAQQIAAGMVYLASQHF--------VHRDLATRNC 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 369 LIKKNGSCCIADLGLAvkfnSDTNEVDVplnTRVGTK-----RYMAPevldESLNKNHFQpyIMADIYSFGLIIWEMarr 443
Cdd:cd05093 152 LVGENLLVKIGDFGMS----RDVYSTDY---YRVGGHtmlpiRWMPP----ESIMYRKFT--TESDVWSLGVVLWEI--- 215
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 444 cITGGIVEEYQLPYYNMVPsdpsyedmrevvCVKRLRPIVSNRwnsdECLRAVLKLMSECWAHNPASRLTALRIKKTLAK 523
Cdd:cd05093 216 -FTYGKQPWYQLSNNEVIE------------CITQGRVLQRPR----TCPKEVYDLMLGCWQREPHMRLNIKEIHSLLQN 278

                ....*..
gi 41349437 524 MVESQDV 530
Cdd:cd05093 279 LAKASPV 285
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
304-440 1.84e-09

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: 59.34  E-value: 1.84e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 304 QLYLITDYHENGSLYDFLKCATLDTRALLKLaYSA--ACGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNGSCCIADL 381
Cdd:cd05582  71 KLYLILDFLRGGDLFTRLSKEVMFTEEDVKF-YLAelALALDHLHSL--------GIIYRDLKPENILLDEDGHIKLTDF 141
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 41349437 382 GLAVKFNSDTNEVdvplNTRVGTKRYMAPEVLDEslnKNHFQpyiMADIYSFGLIIWEM 440
Cdd:cd05582 142 GLSKESIDHEKKA----YSFCGTVEYMAPEVVNR---RGHTQ---SADWWSFGVLMFEM 190
PTKc_Musk cd05050
Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the ...
234-521 2.12e-09

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: 58.69  E-value: 2.12e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 234 IQMVRQVGKGRYGEVWMGKWRG-------EKVAVKVFftTEEAS------WFRETEIYQTvlMRHENILGFIAADIKGTg 300
Cdd:cd05050   7 IEYVRDIGQGAFGRVFQARAPGllpyepfTMVAVKML--KEEASadmqadFQREAALMAE--FDHPNIVKLLGVCAVGK- 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 301 swtQLYLITDYHENGSLYDFL----------------KCAT-------LDTRALLKLAYSAACGLCHLHTEIYgtqgkpa 357
Cdd:cd05050  82 ---PMCLLFEYMAYGDLNEFLrhrspraqcslshstsSARKcglnplpLSCTEQLCIAKQVAAGMAYLSERKF------- 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 358 iAHRDLKSKNILIKKNGSCCIADLGLAVK------FNSDTNEVdVPLntrvgtkRYMAPevldESLNKNHFQpyIMADIY 431
Cdd:cd05050 152 -VHRDLATRNCLVGENMVVKIADFGLSRNiysadyYKASENDA-IPI-------RWMPP----ESIFYNRYT--TESDVW 216
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 432 SFGLIIWEmarrcitggiVEEYQL-PYYNMvpsdpSYEdmrEVVCVKRLRPIVSnrwNSDECLRAVLKLMSECWAHNPAS 510
Cdd:cd05050 217 AYGVVLWE----------IFSYGMqPYYGM-----AHE---EVIYYVRDGNVLS---CPDNCPLELYNLMRLCWSKLPSD 275
                       330
                ....*....|.
gi 41349437 511 RLTALRIKKTL 521
Cdd:cd05050 276 RPSFASINRIL 286
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
340-518 2.33e-09

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: 58.53  E-value: 2.33e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 340 CGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNGSCCIADLGLAVKFNSDtnevDVPLNTRVGTKRYMAPEVLDESLNK 419
Cdd:cd14118 126 LGIEYLHYQ--------KIIHRDIKPSNLLLGDDGHVKIADFGVSNEFEGD----DALLSSTAGTPAFMAPEALSESRKK 193
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 420 NHFQPyimADIYSFGLIIWemarrCITGGiveeyQLPYynmvpSDPSYEDMREVVCVKRLRpiVSNRWNSDECLRAVLKL 499
Cdd:cd14118 194 FSGKA---LDIWAMGVTLY-----CFVFG-----RCPF-----EDDHILGLHEKIKTDPVV--FPDDPVVSEQLKDLILR 253
                       170
                ....*....|....*....
gi 41349437 500 MSEcwaHNPASRLTALRIK 518
Cdd:cd14118 254 MLD---KNPSERITLPEIK 269
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
233-471 2.75e-09

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: 58.99  E-value: 2.75e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 233 QIQMVRQVGKGRYGEVWMGK--WRGEKVAVK----VFFTTEEASW-FRETEIYQTvlMRHENILGfiAADIKGT---GSW 302
Cdd:cd07853   1 DVEPDRPIGYGAFGVVWSVTdpRDGKRVALKkmpnVFQNLVSCKRvFRELKMLCF--FKHDNVLS--ALDILQPphiDPF 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 303 TQLYLITDYHENGSLYDFLKCATLDTRALLKLAYSAACGLCHLHTeiygtqgkPAIAHRDLKSKNILIKKNGSCCIADLG 382
Cdd:cd07853  77 EEIYVVTELMQSDLHKIIVSPQPLSSDHVKVFLYQILRGLKYLHS--------AGILHRDIKPGNLLVNSNCVLKICDFG 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 383 LAVKFNSDTNevdVPLNTRVGTKRYMAPEVLdesLNKNHFQPYImaDIYSFGLIIWEMARRCI---TGGIVEEYQLpYYN 459
Cdd:cd07853 149 LARVEEPDES---KHMTQEVVTQYYRAPEIL---MGSRHYTSAV--DIWSVGCIFAELLGRRIlfqAQSPIQQLDL-ITD 219
                       250
                ....*....|..
gi 41349437 460 MVpSDPSYEDMR 471
Cdd:cd07853 220 LL-GTPSLEAMR 230
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
233-440 3.09e-09

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 58.29  E-value: 3.09e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437  233 QIQMVRQVGKGRYGEVWMGKWR--GEKVAVKVFFTTEEASWFRETEIYQTVL---MRHENILGFiaADIkgTGSWTQLYL 307
Cdd:PLN00009   3 QYEKVEKIGEGTYGVVYKARDRvtNETIALKKIRLEQEDEGVPSTAIREISLlkeMQHGNIVRL--QDV--VHSEKRLYL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437  308 ITDY------HENGSLYDFLKcatlDTRALLKLAYSAACGL--CHLHTeiygtqgkpaIAHRDLKSKNILI-KKNGSCCI 378
Cdd:PLN00009  79 VFEYldldlkKHMDSSPDFAK----NPRLIKTYLYQILRGIayCHSHR----------VLHRDLKPQNLLIdRRTNALKL 144
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41349437  379 ADLGLAVKFNsdtnevdVPLNT---RVGTKRYMAPEVLdesLNKNHFQPYImaDIYSFGLIIWEM 440
Cdd:PLN00009 145 ADFGLARAFG-------IPVRTfthEVVTLWYRAPEIL---LGSRHYSTPV--DIWSVGCIFAEM 197
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
229-442 3.34e-09

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: 58.50  E-value: 3.34e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 229 TIAKQIQMVRQVGKGRYGEVW--MGKWRGEKVAVKVFF-----TTEEASWFRETEIYQTVlmRHENILGFIA--ADIKGT 299
Cdd:cd07876  18 TVLKRYQQLKPIGSGAQGIVCaaFDTVLGINVAVKKLSrpfqnQTHAKRAYRELVLLKCV--NHKNIISLLNvfTPQKSL 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 300 GSWTQLYLITDyhengsLYDFLKCAT----LDTRALLKLAYSAACGLCHLHTeiygtqgkPAIAHRDLKSKNILIKKNGS 375
Cdd:cd07876  96 EEFQDVYLVME------LMDANLCQVihmeLDHERMSYLLYQMLCGIKHLHS--------AGIIHRDLKPSNIVVKSDCT 161
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41349437 376 CCIADLGLAVkfNSDTNEVDVPLntrVGTKRYMAPEVLDESLNKNHfqpyimADIYSFGLIIWEMAR 442
Cdd:cd07876 162 LKILDFGLAR--TACTNFMMTPY---VVTRYYRAPEVILGMGYKEN------VDIWSVGCIMGELVK 217
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
240-519 3.34e-09

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: 57.78  E-value: 3.34e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 240 VGKGRYGEVWMG--KWRGEKVAVKVFFTTEEASWfRETEIYQTVL------------MRHENI---LGFiaadiKGTGSW 302
Cdd:cd06629   9 IGKGTYGRVYLAmnATTGEMLAVKQVELPKTSSD-RADSRQKTVVdalkseidtlkdLDHPNIvqyLGF-----EETEDY 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 303 TQLYLitDYHENGSLYDFL-KCATLD-------TRALLKlaysaacGLCHLHteiygtqgKPAIAHRDLKSKNILIKKNG 374
Cdd:cd06629  83 FSIFL--EYVPGGSIGSCLrKYGKFEedlvrffTRQILD-------GLAYLH--------SKGILHRDLKADNILVDLEG 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 375 SCCIADLGLAVK----FNSDTNevdvplNTRVGTKRYMAPEVLDeslnkNHFQPY-IMADIYSFGLIIWEM--ARRcitg 447
Cdd:cd06629 146 ICKISDFGISKKsddiYGNNGA------TSMQGSVFWMAPEVIH-----SQGQGYsAKVDIWSLGCVVLEMlaGRR---- 210
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41349437 448 giveeyqlPYynmvPSDPSYEDMREVVCVKRLRPIVSNRWNSDEclraVLKLMSECWAHNPASRLTALRIKK 519
Cdd:cd06629 211 --------PW----SDDEAIAAMFKLGNKRSAPPVPEDVNLSPE----ALDFLNACFAIDPRDRPTAAELLS 266
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
238-442 3.47e-09

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: 57.94  E-value: 3.47e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 238 RQVGKGRYGEVWMG--KWRGEKVAVKVFFTTEEASWF-----RETEIYQTVLMRHENILGFIAADIKgtgswtQLYLITD 310
Cdd:cd14097   7 RKLGQGSFGVVIEAthKETQTKWAIKKINREKAGSSAvklleREVDILKHVNHAHIIHLEEVFETPK------RMYLVME 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 311 YHENGSLYDFLK----CATLDTRALLKlaySAACGLCHLHteiygtqgKPAIAHRDLKSKNILIKKNG-------SCCIA 379
Cdd:cd14097  81 LCEDGELKELLLrkgfFSENETRHIIQ---SLASAVAYLH--------KNDIVHRDLKLENILVKSSIidnndklNIKVT 149
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41349437 380 DLGLAVKFNSDTNEVdvpLNTRVGTKRYMAPEVLDeslNKNHFQpyiMADIYSFGLIIWEMAR 442
Cdd:cd14097 150 DFGLSVQKYGLGEDM---LQETCGTPIYMAPEVIS---AHGYSQ---QCDIWSIGVIMYMLLC 203
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
235-440 3.61e-09

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: 57.66  E-value: 3.61e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 235 QMVRQVGKGRYGEVWMGKWR--GEKVAVKVFFTTE------EASWFRETEIYQtvLMRHENILGFIAAdIKGTgswTQLY 306
Cdd:cd14079   5 ILGKTLGVGSFGKVKLAEHEltGHKVAVKILNRQKiksldmEEKIRREIQILK--LFRHPHIIRLYEV-IETP---TDIF 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 307 LITDYHENGSLYDFL----KCATLDTRALLKLAYSAAcGLCHLHTeiygtqgkpaIAHRDLKSKNILIKKNGSCCIADLG 382
Cdd:cd14079  79 MVMEYVSGGELFDYIvqkgRLSEDEARRFFQQIISGV-EYCHRHM----------VVHRDLKPENLLLDSNMNVKIADFG 147
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 41349437 383 LAvKFNSDTNEvdvpLNTRVGTKRYMAPEVLDeslNKNHFQPYImaDIYSFGLIIWEM 440
Cdd:cd14079 148 LS-NIMRDGEF----LKTSCGSPNYAAPEVIS---GKLYAGPEV--DVWSCGVILYAL 195
STKc_WNK2_like cd14032
Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the ...
283-441 3.65e-09

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: 57.78  E-value: 3.65e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 283 MRHENILGFIAADIKGTGSWTQLYLITDYHENGSLYDFLK-CATLDTRALLKLAYSAACGLCHLHTEiygtqgKPAIAHR 361
Cdd:cd14032  57 LQHPNIVRFYDFWESCAKGKRCIVLVTELMTSGTLKTYLKrFKVMKPKVLRSWCRQILKGLLFLHTR------TPPIIHR 130
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 362 DLKSKNILIK-KNGSCCIADLGLA-VKFNSDTNEVdvplntrVGTKRYMAPEVLDESLNKNhfqpyimADIYSFGLIIWE 439
Cdd:cd14032 131 DLKCDNIFITgPTGSVKIGDLGLAtLKRASFAKSV-------IGTPEFMAPEMYEEHYDES-------VDVYAFGMCMLE 196

                ..
gi 41349437 440 MA 441
Cdd:cd14032 197 MA 198
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
235-440 3.81e-09

Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control protein 42 binding kinase (MRCK) beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MRCK-beta is expressed ubiquitously in many tissues. MRCK is activated via interaction with the small GTPase Cdc42. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. The MRCK-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. This alignment model includes the dimerization domain.


Pssm-ID: 270774 [Multi-domain]  Cd Length: 409  Bit Score: 58.87  E-value: 3.81e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 235 QMVRQVGKGRYGEVWMGKWRG-EKV-AVKVFFTTE-----EASWFREteiyqtvlmrHENILgfiaadIKGTGSW----- 302
Cdd:cd05624  75 EIIKVIGRGAFGEVAVVKMKNtERIyAMKILNKWEmlkraETACFRE----------ERNVL------VNGDCQWittlh 138
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 303 ------TQLYLITDYHENGSLYDFLkcATLDTRALLKLA--YSAACGLC--HLHTEIYgtqgkpaiAHRDLKSKNILIKK 372
Cdd:cd05624 139 yafqdeNYLYLVMDYYVGGDLLTLL--SKFEDKLPEDMArfYIGEMVLAihSIHQLHY--------VHRDIKPDNVLLDM 208
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41349437 373 NGSCCIADLGLAVKFNSDTNevdVPLNTRVGTKRYMAPEVL---DESLNKnhFQPyiMADIYSFGLIIWEM 440
Cdd:cd05624 209 NGHIRLADFGSCLKMNDDGT---VQSSVAVGTPDYISPEILqamEDGMGK--YGP--ECDWWSLGVCMYEM 272
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
274-438 3.96e-09

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: 57.73  E-value: 3.96e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 274 ETEIYQTVLMRHENILGFIaadiKGTGSWTQLYLITDYHENGSLYDFLKCATLDT-RALLKLAYSAACGLCHLHteiygt 352
Cdd:cd14184  47 ENEVSILRRVKHPNIIMLI----EEMDTPAELYLVMELVKGGDLFDAITSSTKYTeRDASAMVYNLASALKYLH------ 116
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 353 qgKPAIAHRDLKSKNILI----KKNGSCCIADLGLAVKfnsdtneVDVPLNTRVGTKRYMAPEVLDESlnknhfqPY-IM 427
Cdd:cd14184 117 --GLCIVHRDIKPENLLVceypDGTKSLKLGDFGLATV-------VEGPLYTVCGTPTYVAPEIIAET-------GYgLK 180
                       170
                ....*....|.
gi 41349437 428 ADIYSFGLIIW 438
Cdd:cd14184 181 VDIWAAGVITY 191
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
240-440 4.22e-09

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: 57.54  E-value: 4.22e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 240 VGKGRYGEVWMG--KWRGEKVAVK-VFFTTEEA-----------SWFRETEIYQTvlMRHENILGFIAADIKGTgswtQL 305
Cdd:cd06628   8 IGSGSFGSVYLGmnASSGELMAVKqVELPSVSAenkdrkksmldALQREIALLRE--LQHENIVQYLGSSSDAN----HL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 306 YLITDYHENGSLYDFLKCATLDTRALLK-LAYSAACGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNGSCCIADLGLA 384
Cdd:cd06628  82 NIFLEYVPGGSVATLLNNYGAFEESLVRnFVRQILKGLNYLHNR--------GIIHRDIKGANILVDNKGGIKISDFGIS 153
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41349437 385 VKFNSDTnevdvpLNTRVGTKR--------YMAPEVLDESLNKNHfqpyimADIYSFGLIIWEM 440
Cdd:cd06628 154 KKLEANS------LSTKNNGARpslqgsvfWMAPEVVKQTSYTRK------ADIWSLGCLVVEM 205
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
237-446 5.83e-09

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: 57.05  E-value: 5.83e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 237 VRQVGKGRYGE-------------VWmgkwrgEKVAVKVFFTTEEASWFRETEIYQtvLMRHENILGFIAADIKGTgswt 303
Cdd:cd08221   5 VRVLGRGAFGEavlyrktednslvVW------KEVNLSRLSEKERRDALNEIDILS--LLNHDNIITYYNHFLDGE---- 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 304 QLYLITDYHENGSLYDFL---KCATLDTRALLKLAYSAACGLCHLHteiygtqgKPAIAHRDLKSKNILIKKNGSCCIAD 380
Cdd:cd08221  73 SLFIEMEYCNGGNLHDKIaqqKNQLFPEEVVLWYLYQIVSAVSHIH--------KAGILHRDIKTLNIFLTKADLVKLGD 144
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41349437 381 LGLAVKFNSDTNEVDvplnTRVGTKRYMAPEVLDEslNKNHFQpyimADIYSFGLIIWEMARRCIT 446
Cdd:cd08221 145 FGISKVLDSESSMAE----SIVGTPYYMSPELVQG--VKYNFK----SDIWAVGCVLYELLTLKRT 200
PTKc_PDGFR_alpha cd05105
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor alpha; ...
326-527 5.96e-09

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: 58.11  E-value: 5.96e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 326 LDTRALLKLAYSAACGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNGSCCIADLGLAVKFNSDTNEVD-----VPLnt 400
Cdd:cd05105 234 LTTLDLLSFTYQVARGMEFLASK--------NCVHRDLAARNVLLAQGKIVKICDFGLARDIMHDSNYVSkgstfLPV-- 303
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 401 rvgtkRYMAPEVLDESLNKNhfqpyiMADIYSFGLIIWEMARrciTGGIveeyqlPYYNMVPSDPSYEDMREvvCVKRLR 480
Cdd:cd05105 304 -----KWMAPESIFDNLYTT------LSDVWSYGILLWEIFS---LGGT------PYPGMIVDSTFYNKIKS--GYRMAK 361
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 41349437 481 PivsnrwnsDECLRAVLKLMSECWAHNPASRLTALRIKKTLAKMVES 527
Cdd:cd05105 362 P--------DHATQEVYDIMVKCWNSEPEKRPSFLHLSDIVESLLPS 400
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
305-439 7.38e-09

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: 56.84  E-value: 7.38e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 305 LYLITDYHENGSLYDFLK-CATLDTRA--------LLKLAYsaacglCHLHteiygtqgkpAIAHRDLKSKNILIKKNGS 375
Cdd:cd05579  68 LYLVMEYLPGGDLYSLLEnVGALDEDVariyiaeiVLALEY------LHSH----------GIIHRDLKPDNILIDANGH 131
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41349437 376 CCIADLGLA-VKFNSDTNEVDVPLNTR----------VGTKRYMAPEVLdesLNKNHFQPyimADIYSFGLIIWE 439
Cdd:cd05579 132 LKLTDFGLSkVGLVRRQIKLSIQKKSNgapekedrriVGTPDYLAPEIL---LGQGHGKT---VDWWSLGVILYE 200
PTKc_TrkC cd05094
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze ...
232-524 7.85e-09

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: 56.94  E-value: 7.85e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 232 KQIQMVRQVGKGRYGEVWMGKWRGEK-------VAVKVFFTTEEAS---WFRETEIYQTvlMRHENILGFIAADIKGTgs 301
Cdd:cd05094   5 RDIVLKRELGEGAFGKVFLAECYNLSptkdkmlVAVKTLKDPTLAArkdFQREAELLTN--LQHDHIVKFYGVCGDGD-- 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 302 wtQLYLITDYHENGSLYDFLKC-----------------ATLDTRALLKLAYSAACGLCHLHTEIYgtqgkpaiAHRDLK 364
Cdd:cd05094  81 --PLIMVFEYMKHGDLNKFLRAhgpdamilvdgqprqakGELGLSQMLHIATQIASGMVYLASQHF--------VHRDLA 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 365 SKNILIKKNGSCCIADLGLAVKFNSdTNEVDVPLNTRVGTkRYMAPEvldeSLNKNHFQpyIMADIYSFGLIIWEMarrc 444
Cdd:cd05094 151 TRNCLVGANLLVKIGDFGMSRDVYS-TDYYRVGGHTMLPI-RWMPPE----SIMYRKFT--TESDVWSFGVILWEI---- 218
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 445 ITGGiveeyQLPYYNMVPSDPsyedmreVVCVKRLRPIVSNRWnsdeCLRAVLKLMSECWAHNPASRLTALRIKKTLAKM 524
Cdd:cd05094 219 FTYG-----KQPWFQLSNTEV-------IECITQGRVLERPRV----CPKEVYDIMLGCWQREPQQRLNIKEIYKILHAL 282
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
243-443 9.37e-09

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: 56.85  E-value: 9.37e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 243 GRYGEVWMGKWR--GEKVAVKVFFTTEEASWF-----RETEIyqtvLM--RHENILgfiaaDIK----GTGSwTQLYLIT 309
Cdd:cd07843  16 GTYGVVYRARDKktGEIVALKKLKMEKEKEGFpitslREINI----LLklQHPNIV-----TVKevvvGSNL-DKIYMVM 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 310 DY--HENGSLYDFLK--CATLDTRALLKLAYSaacGLCHLHteiygtqgKPAIAHRDLKSKNILIKKNGSCCIADLGLAV 385
Cdd:cd07843  86 EYveHDLKSLMETMKqpFLQSEVKCLMLQLLS---GVAHLH--------DNWILHRDLKTSNLLLNNRGILKICDFGLAR 154
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 41349437 386 KFNSDTNevdvPLNTRVGTKRYMAPEVLdesLNKNHFQPYImaDIYSFGLIIWEMARR 443
Cdd:cd07843 155 EYGSPLK----PYTQLVVTLWYRAPELL---LGAKEYSTAI--DMWSVGCIFAELLTK 203
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
340-440 1.03e-08

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: 57.01  E-value: 1.03e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 340 CGLCHLHteiygtqgKPAIAHRDLKSKNILIKKNGSCCIADLGLAVKFNSDTNEVDvplnTRVGTKRYMAPEVLdESLNK 419
Cdd:cd05592 107 CGLQFLH--------SRGIIYRDLKLDNVLLDREGHIKIADFGMCKENIYGENKAS----TFCGTPDYIAPEIL-KGQKY 173
                        90       100
                ....*....|....*....|.
gi 41349437 420 NHfqpyiMADIYSFGLIIWEM 440
Cdd:cd05592 174 NQ-----SVDWWSFGVLLYEM 189
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
240-466 1.16e-08

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: 56.17  E-value: 1.16e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 240 VGKGRYGEVWMGKWRGE---KVAVKVF----FTTEEASWFRETEIYQTvlMRHENILGFIaaDIKGTGSwtQLYLITDYH 312
Cdd:cd14201  14 VGHGAFAVVFKGRHRKKtdwEVAIKSInkknLSKSQILLGKEIKILKE--LQHENIVALY--DVQEMPN--SVFLVMEYC 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 313 ENGSLYDFLKC-ATLDTRALLKLAYSAACGLCHLHTEiygtqgkpAIAHRDLKSKNILI----KKNGSCC-----IADLG 382
Cdd:cd14201  88 NGGDLADYLQAkGTLSEDTIRVFLQQIAAAMRILHSK--------GIIHRDLKPQNILLsyasRKKSSVSgirikIADFG 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 383 LAVKFNSDTNEVdvplnTRVGTKRYMAPEVldesLNKNHFQPyiMADIYSFGLIIWEmarrCITGGIVEEYQLP-----Y 457
Cdd:cd14201 160 FARYLQSNMMAA-----TLCGSPMYMAPEV----IMSQHYDA--KADLWSIGTVIYQ----CLVGKPPFQANSPqdlrmF 224
                       250
                ....*....|...
gi 41349437 458 Y----NMVPSDPS 466
Cdd:cd14201 225 YeknkNLQPSIPR 237
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
238-440 1.23e-08

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: 55.98  E-value: 1.23e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 238 RQVGKGRYGEVWMG--KWRGEKVAVKVF--FTTEEASWF-----RETEIYQtvLMRHENILGFIaaDIKGTGSwtQLYLI 308
Cdd:cd14070   8 RKLGEGSFAKVREGlhAVTGEKVAIKVIdkKKAKKDSYVtknlrREGRIQQ--MIRHPNITQLL--DILETEN--SYYLV 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 309 TDYHENGSL----YDFLKCATLDTRALLKLAYSAacgLCHLHteiygtqgKPAIAHRDLKSKNILIKKNGSCCIADLGLA 384
Cdd:cd14070  82 MELCPGGNLmhriYDKKRLEEREARRYIRQLVSA---VEHLH--------RAGVVHRDLKIENLLLDENDNIKLIDFGLS 150
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 41349437 385 VKFNSDTneVDVPLNTRVGTKRYMAPEVldesLNKNHFQPYImaDIYSFGLIIWEM 440
Cdd:cd14070 151 NCAGILG--YSDPFSTQCGSPAYAAPEL----LARKKYGPKV--DVWSIGVNMYAM 198
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
283-441 1.27e-08

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: 56.21  E-value: 1.27e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 283 MRHENILGFIAADIKGTGSWTQLYLITDYHENGSLYDFLK-CATLDTRALLKLAYSAACGLCHLHTEiygtqgKPAIAHR 361
Cdd:cd14030  81 LQHPNIVRFYDSWESTVKGKKCIVLVTELMTSGTLKTYLKrFKVMKIKVLRSWCRQILKGLQFLHTR------TPPIIHR 154
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 362 DLKSKNILIK-KNGSCCIADLGLA-VKFNSDTNEVdvplntrVGTKRYMAPEVLDESLNKNhfqpyimADIYSFGLIIWE 439
Cdd:cd14030 155 DLKCDNIFITgPTGSVKIGDLGLAtLKRASFAKSV-------IGTPEFMAPEMYEEKYDES-------VDVYAFGMCMLE 220

                ..
gi 41349437 440 MA 441
Cdd:cd14030 221 MA 222
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the ...
239-511 1.29e-08

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: 56.12  E-value: 1.29e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 239 QVGKGRYGEVWMGKWRGEK----VAVKVFFTTEEASWFRETEIYQTVLMRHEN------ILGFIAADikgtgSWTqlyLI 308
Cdd:cd05116   2 ELGSGNFGTVKKGYYQMKKvvktVAVKILKNEANDPALKDELLREANVMQQLDnpyivrMIGICEAE-----SWM---LV 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 309 TDYHENGSLYDFL-KCATLDTRALLKLAYSAACGLCHLHTEIYgtqgkpaiAHRDLKSKNILIKKNGSCCIADLGLAVKF 387
Cdd:cd05116  74 MEMAELGPLNKFLqKNRHVTEKNITELVHQVSMGMKYLEESNF--------VHRDLAARNVLLVTQHYAKISDFGLSKAL 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 388 NSDTNEVDVPLNTRVGTKRYmAPEVLdeslnkNHFQPYIMADIYSFGLIIWEmarrCITGGiveeyQLPYYNMVPSDPS- 466
Cdd:cd05116 146 RADENYYKAQTHGKWPVKWY-APECM------NYYKFSSKSDVWSFGVLMWE----AFSYG-----QKPYKGMKGNEVTq 209
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 41349437 467 -YEDMREVVCVKRlrpivsnrwnsdeCLRAVLKLMSECWAHNPASR 511
Cdd:cd05116 210 mIEKGERMECPAG-------------CPPEMYDLMKLCWTYDVDER 242
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
236-440 1.34e-08

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: 55.89  E-value: 1.34e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 236 MVRQVGKGRYGEVWMgkwrgekvaVKVFFTTEEASWFRETEIY-------QTV----------LMRHENILGFIAADIKG 298
Cdd:cd08222   4 VVRKLGSGNFGTVYL---------VSDLKATADEELKVLKEISvgelqpdETVdanreakllsKLDHPAIVKFHDSFVEK 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 299 TgswtQLYLITDYHENGSLYDFLKC-----ATLDTRALLKLAYSAACGLCHLHteiygtqgKPAIAHRDLKSKNILIkKN 373
Cdd:cd08222  75 E----SFCIVTEYCEGGDLDDKISEykksgTTIDENQILDWFIQLLLAVQYMH--------ERRILHRDLKAKNIFL-KN 141
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41349437 374 GSCCIADLGLAVKFNSDTNEVdvplNTRVGTKRYMAPEVLD-ESLNKNhfqpyimADIYSFGLIIWEM 440
Cdd:cd08222 142 NVIKVGDFGISRILMGTSDLA----TTFTGTPYYMSPEVLKhEGYNSK-------SDIWSLGCILYEM 198
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
234-440 1.55e-08

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 56.31  E-value: 1.55e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437  234 IQMVRQVGKGRYGEVW--MGKWRGEKVAVKVF-------FTTEEASWFRETEIYQTVL-----MR---HENILGFIAADI 296
Cdd:PTZ00024  11 IQKGAHLGEGTYGKVEkaYDTLTGKIVAIKKVkiieisnDVTKDRQLVGMCGIHFTTLrelkiMNeikHENIMGLVDVYV 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437  297 KGTgswtQLYLITDYHEngslYDFLKcaTLDTRALLKLAYsAAC-------GLCHLHteiygtqgKPAIAHRDLKSKNIL 369
Cdd:PTZ00024  91 EGD----FINLVMDIMA----SDLKK--VVDRKIRLTESQ-VKCillqilnGLNVLH--------KWYFMHRDLSPANIF 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437  370 IKKNGSCCIADLGLAVKFNSD----------TNEVDVPLNTRVGTKRYMAPEVLDESlNKNHFQpyimADIYSFGLIIWE 439
Cdd:PTZ00024 152 INSKGICKIADFGLARRYGYPpysdtlskdeTMQRREEMTSKVVTLWYRAPELLMGA-EKYHFA----VDMWSVGCIFAE 226

                 .
gi 41349437  440 M 440
Cdd:PTZ00024 227 L 227
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
240-443 1.56e-08

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: 55.60  E-value: 1.56e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 240 VGKGRYGEVW--MGKWRGEKVAVKVFFT-TEEASWFRETEIYQTvlMRHENILGFIAADIKGTgswtQLYLITDYHENGS 316
Cdd:cd14156   1 IGSGFFSKVYkvTHGATGKVMVVKIYKNdVDQHKIVREISLLQK--LSHPNIVRYLGICVKDE----KLHPILEYVSGGC 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 317 LYDFL--KCATLDTRALLKLAYSAACGLCHLHTEiygtqgkpAIAHRDLKSKNILI--KKNG-SCCIADLGLAVKFnsdt 391
Cdd:cd14156  75 LEELLarEELPLSWREKVELACDISRGMVYLHSK--------NIYHRDLNSKNCLIrvTPRGrEAVVTDFGLAREV---- 142
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 41349437 392 neVDVPLN------TRVGTKRYMAPEVLdeslnknHFQPYI-MADIYSFGLIIWEMARR 443
Cdd:cd14156 143 --GEMPANdperklSLVGSAFWMAPEML-------RGEPYDrKVDVFSFGIVLCEILAR 192
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
325-474 1.60e-08

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: 56.22  E-value: 1.60e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 325 TLDTRALLKLAYSAACGLCHLHTEIYgtqgkpaIAHRDLKSKNILIKKNGSCCIADLGLAVKFnsdtneVDVPLNTR-VG 403
Cdd:cd06616 105 VIPEEILGKIAVATVKALNYLKEELK-------IIHRDVKPSNILLDRNGNIKLCDFGISGQL------VDSIAKTRdAG 171
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41349437 404 TKRYMAPEVLDESLNKnhfQPY-IMADIYSFGLIIWEMArrciTGgiveEYQLPYYNMVpsdpsYEDMREVV 474
Cdd:cd06616 172 CRPYMAPERIDPSASR---DGYdVRSDVWSLGITLYEVA----TG----KFPYPKWNSV-----FDQLTQVV 227
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
230-438 1.76e-08

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: 55.77  E-value: 1.76e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 230 IAKQIQMVRQVGKGRYGEVWMGKWR--GEKVAVKVFfttEEASWFR----ETEIYQTVLMRHENILGFiaADIkgTGSWT 303
Cdd:cd14166   1 IRETFIFMEVLGSGAFSEVYLVKQRstGKLYALKCI---KKSPLSRdsslENEIAVLKRIKHENIVTL--EDI--YESTT 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 304 QLYLITDYHENGSLYDFL--------KCATLDTRALLKlaysaacGLCHLHTEiygtqgkpAIAHRDLKSKNILI---KK 372
Cdd:cd14166  74 HYYLVMQLVSGGELFDRIlergvyteKDASRVINQVLS-------AVKYLHEN--------GIVHRDLKPENLLYltpDE 138
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41349437 373 NGSCCIADLGLAvkfNSDTNEVdvpLNTRVGTKRYMAPEVLDEslnknhfQPYIMA-DIYSFGLIIW 438
Cdd:cd14166 139 NSKIMITDFGLS---KMEQNGI---MSTACGTPGYVAPEVLAQ-------KPYSKAvDCWSIGVITY 192
PTKc_Met_Ron cd05058
Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of ...
238-513 1.92e-08

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: 55.56  E-value: 1.92e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 238 RQVGKGRYGEVWMGKW-----RGEKVAVKVF---FTTEEASWFreteIYQTVLMR---HENILGFIAADIKGTGSwtqLY 306
Cdd:cd05058   1 EVIGKGHFGCVYHGTLidsdgQKIHCAVKSLnriTDIEEVEQF----LKEGIIMKdfsHPNVLSLLGICLPSEGS---PL 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 307 LITDYHENGSLYDFLKCATLD--TRALLKLAYSAACGLCHLHTEIYgtqgkpaiAHRDLKSKNILIKKNGSCCIADLGLA 384
Cdd:cd05058  74 VVLPYMKHGDLRNFIRSETHNptVKDLIGFGLQVAKGMEYLASKKF--------VHRDLAARNCMLDESFTVKVADFGLA 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 385 VK-FNSDTNEVDVPLNTRVGTKrYMAPevldESLNKNHFQpyIMADIYSFGLIIWEMARRCITggiveeyqlPYynmvPS 463
Cdd:cd05058 146 RDiYDKEYYSVHNHTGAKLPVK-WMAL----ESLQTQKFT--TKSDVWSFGVLLWELMTRGAP---------PY----PD 205
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 41349437 464 DPSYEDMREVVCVKRLRpivsnrwNSDECLRAVLKLMSECWAHNPASRLT 513
Cdd:cd05058 206 VDSFDITVYLLQGRRLL-------QPEYCPDPLYEVMLSCWHPKPEMRPT 248
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
341-442 2.10e-08

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: 55.52  E-value: 2.10e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 341 GLCHLHTEIygtqgkpaIAHRDLKSKNILIKKNGSCCIADLGLAVKFNSDTnevdvPlNTRVGTKRYMAPEVLDESlnkn 420
Cdd:cd05606 110 GLEHMHNRF--------IVYRDLKPANILLDEHGHVRISDLGLACDFSKKK-----P-HASVGTHGYMAPEVLQKG---- 171
                        90       100
                ....*....|....*....|...
gi 41349437 421 hfQPY-IMADIYSFGLIIWEMAR 442
Cdd:cd05606 172 --VAYdSSADWFSLGCMLYKLLK 192
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
238-474 2.39e-08

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: 55.42  E-value: 2.39e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 238 RQVGKGRYGEVWMGKW--RGEKVAVK------VFFTTEEASWFRETEIYQTvlMRHENILGFIAADIKGTgswtQLYLIT 309
Cdd:cd08229  30 KKIGRGQFSEVYRATCllDGVPVALKkvqifdLMDAKARADCIKEIDLLKQ--LNHPNVIKYYASFIEDN----ELNIVL 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 310 DYHENGSLYDFLKC-----ATLDTRALLKLAYSAACGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNGSCCIADLGLA 384
Cdd:cd08229 104 ELADAGDLSRMIKHfkkqkRLIPEKTVWKYFVQLCSALEHMHSR--------RVMHRDIKPANVFITATGVVKLGDLGLG 175
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 385 VKFNSDTNEVdvplNTRVGTKRYMAPEVLDEslNKNHFQpyimADIYSFGLIIWEMA--RRCITGGIVEEYQLPY----- 457
Cdd:cd08229 176 RFFSSKTTAA----HSLVGTPYYMSPERIHE--NGYNFK----SDIWSLGCLLYEMAalQSPFYGDKMNLYSLCKkieqc 245
                       250
                ....*....|....*...
gi 41349437 458 -YNMVPSDPSYEDMREVV 474
Cdd:cd08229 246 dYPPLPSDHYSEELRQLV 263
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
237-440 2.50e-08

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: 55.18  E-value: 2.50e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 237 VRQVGKGRYGEVWMGKWR--GEKVAVKVFFTTEEASWFRETEI-YQTVLMRHENILGFIAADIKGTGSWTQLYLITDYHE 313
Cdd:cd05611   1 LKPISKGAFGSVYLAKKRstGDYFAIKVLKKSDMIAKNQVTNVkAERAIMMIQGESPYVAKLYYSFQSKDYLYLVMEYLN 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 314 NGSLYDFLK-CATLDTRALLKLAYSAACGLCHLHteiygtqgKPAIAHRDLKSKNILIKKNGSCCIADLGLavkfnSDTN 392
Cdd:cd05611  81 GGDCASLIKtLGGLPEDWAKQYIAEVVLGVEDLH--------QRGIIHRDIKPENLLIDQTGHLKLTDFGL-----SRNG 147
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 41349437 393 EVDVPLNTRVGTKRYMAPEVLdesLNKNHFQpyiMADIYSFGLIIWEM 440
Cdd:cd05611 148 LEKRHNKKFVGTPDYLAPETI---LGVGDDK---MSDWWSLGCVIFEF 189
PTKc_Zap-70 cd05115
Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs ...
239-521 3.02e-08

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: 54.95  E-value: 3.02e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 239 QVGKGRYGEVWMGKWRGEK----VAVKVFFTTEEASwFRETEIYQTVLMrHENILGFIAADIkGTGSWTQLYLITDYHEN 314
Cdd:cd05115  11 ELGSGNFGCVKKGVYKMRKkqidVAIKVLKQGNEKA-VRDEMMREAQIM-HQLDNPYIVRMI-GVCEAEALMLVMEMASG 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 315 GSLYDFL--KCATLDTRALLKLAYSAACGLCHLhteiygtQGKPAIaHRDLKSKNILIKKNGSCCIADLGLAVKFNSDtn 392
Cdd:cd05115  88 GPLNKFLsgKKDEITVSNVVELMHQVSMGMKYL-------EEKNFV-HRDLAARNVLLVNQHYAKISDFGLSKALGAD-- 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 393 evDVPLNTRVGTK---RYMAPEVLdeslnknHFQPY-IMADIYSFGLIIWEmarrCITGGiveeyQLPYYNMV-PSDPSY 467
Cdd:cd05115 158 --DSYYKARSAGKwplKWYAPECI-------NFRKFsSRSDVWSYGVTMWE----AFSYG-----QKPYKKMKgPEVMSF 219
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 41349437 468 -EDMREVVCvkrlrpivsnrwnSDECLRAVLKLMSECWAHNPASRLTALRIKKTL 521
Cdd:cd05115 220 iEQGKRMDC-------------PAECPPEMYALMSDCWIYKWEDRPNFLTVEQRM 261
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
237-440 3.18e-08

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: 55.35  E-value: 3.18e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 237 VRQVGKGRYGEVWM--GKWRGEKVAVKVFfttEEASWFRETEiyQTVLMRHENIL------GFIAADIKGTGSWTQLYLI 308
Cdd:cd05604   1 LKVIGKGSFGKVLLakRKRDGKYYAVKVL---QKKVILNRKE--QKHIMAERNVLlknvkhPFLVGLHYSFQTTDKLYFV 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 309 TDYHENGSLYDFLKCATL--DTRALLKLAySAACGLCHLHTeiygtqgkPAIAHRDLKSKNILIKKNGSCCIADLGLAVK 386
Cdd:cd05604  76 LDFVNGGELFFHLQRERSfpEPRARFYAA-EIASALGYLHS--------INIVYRDLKPENILLDSQGHIVLTDFGLCKE 146
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 41349437 387 --FNSDTNevdvplNTRVGTKRYMAPEVLDEslnknhfQPYI-MADIYSFGLIIWEM 440
Cdd:cd05604 147 giSNSDTT------TTFCGTPEYLAPEVIRK-------QPYDnTVDWWCLGSVLYEM 190
STKc_PINK1 cd14018
Catalytic domain of the Serine/Threonine protein kinase, Pten INduced Kinase 1; STKs catalyze ...
297-440 3.23e-08

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: 55.19  E-value: 3.23e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 297 KGTGSWTQLYLITDYHENgSLYDFLKCATLDTR--ALLKLAYSAACGlcHLHteiygtqgKPAIAHRDLKSKNILIKKNG 374
Cdd:cd14018 107 SGLGHNRTLFLVMKNYPC-TLRQYLWVNTPSYRlaRVMILQLLEGVD--HLV--------RHGIAHRDLKSDNILLELDF 175
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41349437 375 S-----------CCIAD--LGLAVKFNSDtnEVDvplntRVGTKRYMAPEVLDESLNKNHFQPYIMADIYSFGLIIWEM 440
Cdd:cd14018 176 DgcpwlviadfgCCLADdsIGLQLPFSSW--YVD-----RGGNACLMAPEVSTAVPGPGVVINYSKADAWAVGAIAYEI 247
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
238-440 3.76e-08

Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGKs are activated by insulin and growth factors via phosphoinositide 3-kinase and PDK1. They activate ion channels, ion carriers, and the Na-K-ATPase, as well as regulate the activity of enzymes and transcription factors. SGKs play important roles in transport, hormone release, neuroexcitability, cell proliferation, and apoptosis. There are three isoforms of SGK, named SGK1, SGK2, and SGK3 (also called cytokine-independent survival kinase CISK). The SGK 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: 270727 [Multi-domain]  Cd Length: 323  Bit Score: 55.02  E-value: 3.76e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 238 RQVGKGRYGEVWMGKWRGEKV--AVKVFfttEEASWFRETEiyQTVLMRHENIL--------------GFIAADikgtgs 301
Cdd:cd05575   1 KVIGKGSFGKVLLARHKAEGKlyAVKVL---QKKAILKRNE--VKHIMAERNVLlknvkhpflvglhySFQTKD------ 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 302 wtQLYLITDYHENGSLYDFL---KCATlDTRALLklaYSA--ACGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNGSC 376
Cdd:cd05575  70 --KLYFVLDYVNGGELFFHLqreRHFP-EPRARF---YAAeiASALGYLHSL--------NIIYRDLKPENILLDSQGHV 135
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41349437 377 CIADLGLAvKFN---SDTNevdvplNTRVGTKRYMAPEVLdeslnknHFQPYIMA-DIYSFGLIIWEM 440
Cdd:cd05575 136 VLTDFGLC-KEGiepSDTT------STFCGTPEYLAPEVL-------RKQPYDRTvDWWCLGAVLYEM 189
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
360-440 4.43e-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: 54.49  E-value: 4.43e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 360 HRDLKSKNILIKKNGSCCIADLGLAVKFNSDTNEVDV--PLNT------RVGTKRYMAPEVLdeslnknHFQPYI-MADI 430
Cdd:cd14048 141 HRDLKPSNVFFSLDDVVKVGDFGLVTAMDQGEPEQTVltPMPAyakhtgQVGTRLYMSPEQI-------HGNQYSeKVDI 213
                        90
                ....*....|
gi 41349437 431 YSFGLIIWEM 440
Cdd:cd14048 214 FALGLILFEL 223
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
240-441 5.02e-08

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: 54.80  E-value: 5.02e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 240 VGKGRYGEVWMG--KWRGEKVAVKVF----FTTEEASWFRETEIYQTVlmRHENILGFIAADIKGTGSwtQLYLITDYHE 313
Cdd:cd13988   1 LGQGATANVFRGrhKKTGDLYAVKVFnnlsFMRPLDVQMREFEVLKKL--NHKNIVKLFAIEEELTTR--HKVLVMELCP 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 314 NGSLYDFLKCAT----LDTRALLKLAYSAACGLCHLHTEiygtqgkpAIAHRDLKSKNIL--IKKNGSCC--IADLGLAV 385
Cdd:cd13988  77 CGSLYTVLEEPSnaygLPESEFLIVLRDVVAGMNHLREN--------GIVHRDIKPGNIMrvIGEDGQSVykLTDFGAAR 148
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 41349437 386 KFnsdtnEVDVPLNTRVGTKRYMAPEVLDES-LNKNHFQPY-IMADIYSFGLIIWEMA 441
Cdd:cd13988 149 EL-----EDDEQFVSLYGTEEYLHPDMYERAvLRKDHQKKYgATVDLWSIGVTFYHAA 201
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
341-441 5.27e-08

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: 54.36  E-value: 5.27e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 341 GLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNGSCC-IADLGLAVKFNSDTNEVDVPLNTRVGTKRYMAPEVLdeslnk 419
Cdd:cd06630 115 GLAYLHDN--------QIIHRDLKGANLLVDSTGQRLrIADFGAAARLASKGTGAGEFQGQLLGTIAFMAPEVL------ 180
                        90       100
                ....*....|....*....|...
gi 41349437 420 nHFQPYIMA-DIYSFGLIIWEMA 441
Cdd:cd06630 181 -RGEQYGRScDVWSVGCVIIEMA 202
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
240-447 5.32e-08

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: 54.54  E-value: 5.32e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 240 VGKGRYGEVWMGKWR--GEKVAVKV----FFTTEEASWFRETEIYQTvlMRHENI---------LGFIAADIKgtgswtq 304
Cdd:cd14039   1 LGTGGFGNVCLYQNQetGEKIAIKScrleLSVKNKDRWCHEIQIMKK--LNHPNVvkacdvpeeMNFLVNDVP------- 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 305 lYLITDYHENGSLYDFLK----CATLDTRALLKLAYSAACGLCHLHTEiygtqgkpAIAHRDLKSKNILIKK-NGSCC-- 377
Cdd:cd14039  72 -LLAMEYCSGGDLRKLLNkpenCCGLKESQVLSLLSDIGSGIQYLHEN--------KIIHRDLKPENIVLQEiNGKIVhk 142
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41349437 378 IADLGLAVKFNSDTnevdvpLNTR-VGTKRYMAPEVLDeslNKnhfqPY-IMADIYSFGLIIWEmarrCITG 447
Cdd:cd14039 143 IIDLGYAKDLDQGS------LCTSfVGTLQYLAPELFE---NK----SYtVTVDYWSFGTMVFE----CIAG 197
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
240-440 5.43e-08

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: 54.89  E-value: 5.43e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 240 VGKGRYGEVWMGK--WRGEKVAVKVF---FTTEEAS--WFRETEIYQTvlMRHENILGFiaADIKGTGSwTQLYLITDYh 312
Cdd:cd07856  18 VGMGAFGLVCSARdqLTGQNVAVKKImkpFSTPVLAkrTYRELKLLKH--LRHENIISL--SDIFISPL-EDIYFVTEL- 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 313 ENGSLYDFLKCATLDTRALLKLAYSAACGLCHLHTeiygtqgkPAIAHRDLKSKNILIKKNGSCCIADLGLAvkfnsdtN 392
Cdd:cd07856  92 LGTDLHRLLTSRPLEKQFIQYFLYQILRGLKYVHS--------AGVIHRDLKPSNILVNENCDLKICDFGLA-------R 156
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 41349437 393 EVDVPLNTRVGTKRYMAPEVLDEslnknhFQPY-IMADIYSFGLIIWEM 440
Cdd:cd07856 157 IQDPQMTGYVSTRYYRAPEIMLT------WQKYdVEVDIWSAGCIFAEM 199
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
305-440 5.79e-08

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: 54.54  E-value: 5.79e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 305 LYLITDYHENGSL-YDFLKCATLDTRALLKLAYSAACGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNGSCCIADLGL 383
Cdd:cd05619  81 LFFVMEYLNGGDLmFHIQSCHKFDLPRATFYAAEIICGLQFLHSK--------GIVYRDLKLDNILLDKDGHIKIADFGM 152
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 41349437 384 AvkfnSDTNEVDVPLNTRVGTKRYMAPEV-LDESLNKNhfqpyimADIYSFGLIIWEM 440
Cdd:cd05619 153 C----KENMLGDAKTSTFCGTPDYIAPEIlLGQKYNTS-------VDWWSFGVLLYEM 199
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
274-416 5.86e-08

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: 54.18  E-value: 5.86e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 274 ETEIYQTVLMRHENILGFIAAdikgTGSWTQLYLITDYHENGSLYDFLKCATLDTRALLKLAYSAAC-GLCHLHTEiygt 352
Cdd:cd14185  46 ESEILIIKSLSHPNIVKLFEV----YETEKEIYLILEYVRGGDLFDAIIESVKFTEHDAALMIIDLCeALVYIHSK---- 117
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41349437 353 qgkpAIAHRDLKSKNILIKKNG----SCCIADLGLAVkfnsdtnEVDVPLNTRVGTKRYMAPEVLDES 416
Cdd:cd14185 118 ----HIVHRDLKPENLLVQHNPdkstTLKLADFGLAK-------YVTGPIFTVCGTPTYVAPEILSEK 174
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
229-445 6.09e-08

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: 54.71  E-value: 6.09e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 229 TIAKQIQMVRQVGKGRYGEVWMG--KWRGEKVAVKVFFTTEEASWFRETEIYQTVLMR---HENILGF--IAADIKGTGS 301
Cdd:cd07874  14 TVLKRYQNLKPIGSGAQGIVCAAydAVLDRNVAIKKLSRPFQNQTHAKRAYRELVLMKcvnHKNIISLlnVFTPQKSLEE 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 302 WTQLYLITDyhengsLYDFLKCAT----LDTRALLKLAYSAACGLCHLHTeiygtqgkPAIAHRDLKSKNILIKKNGSCC 377
Cdd:cd07874  94 FQDVYLVME------LMDANLCQViqmeLDHERMSYLLYQMLCGIKHLHS--------AGIIHRDLKPSNIVVKSDCTLK 159
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41349437 378 IADLGLAvkfnsDTNEVDVPLNTRVGTKRYMAPEV-LDESLNKNhfqpyimADIYSFGLIIWEMARRCI 445
Cdd:cd07874 160 ILDFGLA-----RTAGTSFMMTPYVVTRYYRAPEViLGMGYKEN-------VDIWSVGCIMGEMVRHKI 216
PTKc_Aatyk3 cd14206
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 3; PTKs ...
237-440 6.43e-08

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: 54.19  E-value: 6.43e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 237 VRQVGKGRYGEVWMGK----WRGEKVAVKVFFTT----EEASWFRETEIYQTvlMRHENILGFIaadikGTGSWTQLYL- 307
Cdd:cd14206   2 LQEIGNGWFGKVILGEifsdYTPAQVVVKELRVSagplEQRKFISEAQPYRS--LQHPNILQCL-----GLCTETIPFLl 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 308 ITDYHENGSLYDFLKCA-----------TLDTRALLKLAYSAACGLCHLHTEIYgtqgkpaiAHRDLKSKNILIKKNGSC 376
Cdd:cd14206  75 IMEFCQLGDLKRYLRAQrkadgmtpdlpTRDLRTLQRMAYEITLGLLHLHKNNY--------IHSDLALRNCLLTSDLTV 146
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41349437 377 CIADLGLA-VKFNSD----TNEVDVPLntrvgtkRYMAPEVLDEsLNKNhfqpYIMAD------IYSFGLIIWEM 440
Cdd:cd14206 147 RIGDYGLShNNYKEDyyltPDRLWIPL-------RWVAPELLDE-LHGN----LIVVDqskesnVWSLGVTIWEL 209
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
232-447 7.22e-08

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: 53.65  E-value: 7.22e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 232 KQIQMVRQVGKGRYGEVWMGKWR--GEKVAVK-VFFTTEEAswfrETEIYQTVLMRHENILGFiaadikgTGSWTQ---- 304
Cdd:cd14047   6 QDFKEIELIGSGGFGQVFKAKHRidGKTYAIKrVKLNNEKA----EREVKALAKLDHPNIVRY-------NGCWDGfdyd 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 305 ---------------LYLITDYHENGSLYDFL---KCATLDTRALLKLAYSAACGLCHLHTEiygtqgkpAIAHRDLKSK 366
Cdd:cd14047  75 petsssnssrsktkcLFIQMEFCEKGTLESWIekrNGEKLDKVLALEIFEQITKGVEYIHSK--------KLIHRDLKPS 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 367 NILIKKNGSCCIADLGLAVkfnSDTNevDVPLNTRVGTKRYMAPevldESLNKNHFQPYImaDIYSFGLIIWEMARRCIT 446
Cdd:cd14047 147 NIFLVDTGKVKIGDFGLVT---SLKN--DGKRTKSKGTLSYMSP----EQISSQDYGKEV--DIYALGLILFELLHVCDS 215

                .
gi 41349437 447 G 447
Cdd:cd14047 216 A 216
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
233-414 7.46e-08

Catalytic domain of Numb-Associated Kinase (NAK)-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 Drosophila melanogaster NAK, human BMP-2-inducible protein kinase (BMP2K or BIKe) and similar vertebrate proteins, as well as the Saccharomyces cerevisiae proteins Prk1, Actin-regulating kinase 1 (Ark1), and Akl1. NAK was the first characterized member of this subfamily. It 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. BMP2K contains a nuclear localization signal and a kinase domain that is capable of phosphorylating itself and myelin basic protein. The expression of the BMP2K gene is increase during BMP-2-induced osteoblast differentiation. It may function to control the rate of differentiation. Prk1, Ark1, and Akl1 comprise a subfamily of yeast proteins that are important regulators of the actin cytoskeleton and endocytosis. They share an N-terminal kinase domain but no significant homology in other regions of their sequences. The NAK-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: 270939 [Multi-domain]  Cd Length: 277  Bit Score: 53.83  E-value: 7.46e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 233 QIQMVRQVGKGRYGEVWMGKWR--GEKVAVKVFFTTEEASWF---RETEIYQTvLMRHENILGFI--AADIKGTGSWtQL 305
Cdd:cd14037   4 HVTIEKYLAEGGFAHVYLVKTSngGNRAALKRVYVNDEHDLNvckREIEIMKR-LSGHKNIVGYIdsSANRSGNGVY-EV 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 306 YLITDYHENGSLYDFLKcATLDTR----ALLKLAYSAACGLCHLHteiygtQGKPAIAHRDLKSKNILIKKNGSCCIADL 381
Cdd:cd14037  82 LLLMEYCKGGGVIDLMN-QRLQTGltesEILKIFCDVCEAVAAMH------YLKPPLIHRDLKVENVLISDSGNYKLCDF 154
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 41349437 382 GLA-VKFNSDTNEVDVPL-------NTrvgTKRYMAPEVLD 414
Cdd:cd14037 155 GSAtTKILPPQTKQGVTYveedikkYT---TLQYRAPEMID 192
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
304-441 8.22e-08

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: 54.28  E-value: 8.22e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 304 QLYLITDYHENGSLYDFLKCATLDTRALL-KLAYSAACGLCHLHTeiygtqgKPAIAHRDLKSKNILIKKNGSCCIADLG 382
Cdd:cd06649  77 EISICMEHMDGGSLDQVLKEAKRIPEEILgKVSIAVLRGLAYLRE-------KHQIMHRDVKPSNILVNSRGEIKLCDFG 149
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 41349437 383 LAVKFnsdtneVDVPLNTRVGTKRYMAPevldESLNKNHFQpyIMADIYSFGLIIWEMA 441
Cdd:cd06649 150 VSGQL------IDSMANSFVGTRSYMSP----ERLQGTHYS--VQSDIWSMGLSLVELA 196
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
274-482 8.25e-08

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: 53.52  E-value: 8.25e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 274 ETEIYQTVLMRHENILGFIAADIK---GTGSWTqLYLITDYHENGSLYDFL-KCATLD-------TRALLKlaysaacGL 342
Cdd:cd14012  46 EKELESLKKLRHPNLVSYLAFSIErrgRSDGWK-VYLLTEYAPGGSLSELLdSVGSVPldtarrwTLQLLE-------AL 117
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 343 CHLHTeiygtQGkpaIAHRDLKSKNILIKKNGSCCIA---DLGLAVKFNSDTNEV--DVPLNTrvgtkRYMAPEVLDESl 417
Cdd:cd14012 118 EYLHR-----NG---VVHKSLHAGNVLLDRDAGTGIVkltDYSLGKTLLDMCSRGslDEFKQT-----YWLPPELAQGS- 183
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41349437 418 nknhFQPYIMADIYSFGLIIWEMarrcITGG-IVEEYQLPYYNMVPSDPSyEDMREVV--CV-----KRLRPI 482
Cdd:cd14012 184 ----KSPTRKTDVWDLGLLFLQM----LFGLdVLEKYTSPNPVLVSLDLS-ASLQDFLskCLsldpkKRPTAL 247
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
240-441 8.55e-08

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: 53.85  E-value: 8.55e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 240 VGKGRYGEVWMGKWR--GEKVAVKVFFTTEEASWFRETEIYQTVLMR---HENILGFIAAdIKGTGswtQLYLITDY--- 311
Cdd:cd07848   9 VGEGAYGVVLKCRHKetKEIVAIKKFKDSEENEEVKETTLRELKMLRtlkQENIVELKEA-FRRRG---KLYLVFEYvek 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 312 --------HENGSLYDFLKCATLDtraLLKlaysaACGLCHlhteiygtqgKPAIAHRDLKSKNILIKKNGSCCIADLGL 383
Cdd:cd07848  85 nmlelleeMPNGVPPEKVRSYIYQ---LIK-----AIHWCH----------KNDIVHRDIKPENLLISHNDVLKLCDFGF 146
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 41349437 384 AVKFNSDTnevDVPLNTRVGTKRYMAPEVLDESlnknhfqPYIMA-DIYSFGLIIWEMA 441
Cdd:cd07848 147 ARNLSEGS---NANYTEYVATRWYRSPELLLGA-------PYGKAvDMWSVGCILGELS 195
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
304-442 1.10e-07

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: 53.90  E-value: 1.10e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 304 QLYLITDYHENGSLYDFLKCATLDTRALLKL-AYSAACGLCHLHTEIygtqgkpaIAHRDLKSKNILIKKNGSCCIADLG 382
Cdd:cd14223  77 KLSFILDLMNGGDLHYHLSQHGVFSEAEMRFyAAEIILGLEHMHSRF--------VVYRDLKPANILLDEFGHVRISDLG 148
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 383 LAVKFNSDTNevdvplNTRVGTKRYMAPEVLDESLNKNHfqpyiMADIYSFGLIIWEMAR 442
Cdd:cd14223 149 LACDFSKKKP------HASVGTHGYMAPEVLQKGVAYDS-----SADWFSLGCMLFKLLR 197
STKc_SRPK cd14136
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze ...
341-441 1.16e-07

Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SRPKs phosphorylate and regulate splicing factors from the SR protein family by specifically phosphorylating multiple serine residues residing in SR/RS dipeptide motifs (also known as RS domains). Phosphorylation of the RS domains enhances interaction with transportin SR and facilitates entry of the SR proteins into the nucleus. SRPKs contain a nonconserved insert domain, within the well-conserved catalytic kinase domain, that regulates their subcellular localization. They play important roles in mediating pre-mRNA processing and mRNA maturation, as well as other cellular functions such as chromatin reorganization, cell cycle and p53 regulation, and metabolic signaling. Vertebrates contain three distinct SRPKs, called SRPK1-3. The SRPK homolog in budding yeast, Sky1p, recognizes and phosphorylates its substrate Npl3p, which lacks a classic RS domain but contains a single RS dipeptide at the C-terminus of its RGG domain. Npl3p is a shuttling heterogeneous nuclear ribonucleoprotein (hnRNP) that exports a distinct class of mRNA from the nucleus to the cytoplasm. The SRPK 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: 271038 [Multi-domain]  Cd Length: 320  Bit Score: 53.73  E-value: 1.16e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 341 GLCHLHTEIygtqgkpAIAHRDLKSKNILIKKNGSCC-IADLGLAV----KFNSDtnevdvplntrVGTKRYMAPEVLde 415
Cdd:cd14136 131 GLDYLHTKC-------GIIHTDIKPENVLLCISKIEVkIADLGNACwtdkHFTED-----------IQTRQYRSPEVI-- 190
                        90       100
                ....*....|....*....|....*.
gi 41349437 416 sLNKNHFQPyimADIYSFGLIIWEMA 441
Cdd:cd14136 191 -LGAGYGTP---ADIWSTACMAFELA 212
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
224-480 1.18e-07

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: 53.47  E-value: 1.18e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 224 LLVQRTIAKQIqMVRQVGKGRYgeVWMGKWRGEKVAVKvfftTEEASWFRETEIYQTVlmRHEnilgFIAADIKGTGSWT 303
Cdd:cd05595   2 LLGKGTFGKVI-LVREKATGRY--YAMKILRKEVIIAK----DEVAHTVTESRVLQNT--RHP----FLTALKYAFQTHD 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 304 QLYLITDYHENGSLYDFLKCATLDTRALLKLaYSA--ACGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNGSCCIADL 381
Cdd:cd05595  69 RLCFVMEYANGGELFFHLSRERVFTEDRARF-YGAeiVSALEYLHSR--------DVVYRDIKLENLMLDKDGHIKITDF 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 382 GLAVKFNSDtnevDVPLNTRVGTKRYMAPEVLDEslnkNHFQPYImaDIYSFGLIIWEMarrcITGgiveeyQLPYYNMv 461
Cdd:cd05595 140 GLCKEGITD----GATMKTFCGTPEYLAPEVLED----NDYGRAV--DWWGLGVVMYEM----MCG------RLPFYNQ- 198
                       250
                ....*....|....*....
gi 41349437 462 psdpSYEDMREVVCVKRLR 480
Cdd:cd05595 199 ----DHERLFELILMEEIR 213
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
239-441 1.36e-07

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: 53.21  E-value: 1.36e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 239 QVGKGRYGEVWMGKWR--GEKVAVKVFFTTEEA-----SWFRETEIYQTvlMRHENILGFIaaDIkgTGSWTQLYLITDY 311
Cdd:cd07839   7 KIGEGTYGTVFKAKNRetHEIVALKRVRLDDDDegvpsSALREICLLKE--LKHKNIVRLY--DV--LHSDKKLTLVFEY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 312 HENGSLYDFLKC-ATLDTRALLKLAYSAACGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNGSCCIADLGLAVKFNsd 390
Cdd:cd07839  81 CDQDLKKYFDSCnGDIDPEIVKSFMFQLLKGLAFCHSH--------NVLHRDLKPQNLLINKNGELKLADFGLARAFG-- 150
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 41349437 391 tnevdVPL---NTRVGTKRYMAPEVLdesLNKNHFQPYImaDIYSFGLIIWEMA 441
Cdd:cd07839 151 -----IPVrcySAEVVTLWYRPPDVL---FGAKLYSTSI--DMWSAGCIFAELA 194
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
239-440 1.36e-07

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: 53.28  E-value: 1.36e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 239 QVGKGRYGEVW--MGKWRGEKVAVK---VFFTTEEASWFRETEIYQTVLMRHENILGFIAAdikgtgsWTQ-----LYL- 307
Cdd:cd14049  13 RLGKGGYGKVYkvRNKLDGQYYAIKkilIKKVTKRDCMKVLREVKVLAGLQHPNIVGYHTA-------WMEhvqlmLYIq 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 308 -----------ITDYHENGSLYDFLKCA--TLDTRALLKLAYSAACGLCHLHTEiygtqgkpAIAHRDLKSKNILIkkNG 374
Cdd:cd14049  86 mqlcelslwdwIVERNKRPCEEEFKSAPytPVDVDVTTKILQQLLEGVTYIHSM--------GIVHRDLKPRNIFL--HG 155
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41349437 375 SCC---IADLGLAVKF----NSDTNEVDvPLN-----TRVGTKRYMAPevldESLNKNHFQPyiMADIYSFGLIIWEM 440
Cdd:cd14049 156 SDIhvrIGDFGLACPDilqdGNDSTTMS-RLNglthtSGVGTCLYAAP----EQLEGSHYDF--KSDMYSIGVILLEL 226
pknD PRK13184
serine/threonine-protein kinase PknD;
235-440 1.46e-07

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 54.39  E-value: 1.46e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437  235 QMVRQVGKGRYGEVWMG--KWRGEKVAVKVFftTEEASwfrETEIYQTVLMRHENIlgfiAADIKGTGSwTQLYLITD-- 310
Cdd:PRK13184   5 DIIRLIGKGGMGEVYLAydPVCSRRVALKKI--REDLS---ENPLLKKRFLREAKI----AADLIHPGI-VPVYSICSdg 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437  311 --------YHENGSLYDFLK----CATL--------DTRALLKLAYSAACGLCHLHTEiygtqgkpAIAHRDLKSKNILI 370
Cdd:PRK13184  75 dpvyytmpYIEGYTLKSLLKsvwqKESLskelaektSVGAFLSIFHKICATIEYVHSK--------GVLHRDLKPDNILL 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437  371 KKNGSCCIADLGLAVKFNSDTNE-VDVPLNTR-------------VGTKRYMAPEVLdeslnKNHfQPYIMADIYSFGLI 436
Cdd:PRK13184 147 GLFGEVVILDWGAAIFKKLEEEDlLDIDVDERnicyssmtipgkiVGTPDYMAPERL-----LGV-PASESTDIYALGVI 220

                 ....
gi 41349437  437 IWEM 440
Cdd:PRK13184 221 LYQM 224
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
229-450 1.53e-07

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: 53.51  E-value: 1.53e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 229 TIAKQIQMVRQVGKGRYGEVWMG--KWRGEKVAVKVFFTTEEASWFRETEIYQTVLMR---HENILGF--IAADIKGTGS 301
Cdd:cd07875  21 TVLKRYQNLKPIGSGAQGIVCAAydAILERNVAIKKLSRPFQNQTHAKRAYRELVLMKcvnHKNIIGLlnVFTPQKSLEE 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 302 WTQLYLITDyhengsLYDFLKCAT----LDTRALLKLAYSAACGLCHLHTeiygtqgkPAIAHRDLKSKNILIKKNGSCC 377
Cdd:cd07875 101 FQDVYIVME------LMDANLCQViqmeLDHERMSYLLYQMLCGIKHLHS--------AGIIHRDLKPSNIVVKSDCTLK 166
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41349437 378 IADLGLAvkfnsDTNEVDVPLNTRVGTKRYMAPEV-LDESLNKNhfqpyimADIYSFGLIIWEMarrcITGGIV 450
Cdd:cd07875 167 ILDFGLA-----RTAGTSFMMTPYVVTRYYRAPEViLGMGYKEN-------VDIWSVGCIMGEM----IKGGVL 224
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
303-413 1.60e-07

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: 52.78  E-value: 1.60e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 303 TQLYLITDYHENGSLYDFLKCATLDTRALLKLaYSA--ACGLCHLHteiygtqgKPAIAHRDLKSKNILIKKNGSCCIAD 380
Cdd:cd05583  72 AKLHLILDYVNGGELFTHLYQREHFTESEVRI-YIGeiVLALEHLH--------KLGIIYRDIKLENILLDSEGHVVLTD 142
                        90       100       110
                ....*....|....*....|....*....|...
gi 41349437 381 LGLAVKFNSDTNEVdvpLNTRVGTKRYMAPEVL 413
Cdd:cd05583 143 FGLSKEFLPGENDR---AYSFCGTIEYMAPEVV 172
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
228-440 1.61e-07

Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ROCK is also referred to as Rho-associated kinase or simply as Rho kinase. It contains an N-terminal extension, a catalytic kinase domain, and a long 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. It is activated via interaction with Rho GTPases and is involved in many cellular functions including contraction, adhesion, migration, motility, proliferation, and apoptosis. The ROCK subfamily consists of two isoforms, ROCK1 and ROCK2, which may be functionally redundant in some systems, but exhibit different tissue distributions. Both isoforms are ubiquitously expressed in most tissues, but ROCK2 is more prominent in brain and skeletal muscle while ROCK1 is more pronounced in the liver, testes, and kidney. Studies in knockout mice result in different phenotypes, suggesting that the two isoforms do not compensate for each other during embryonic development. The ROCK 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: 270747 [Multi-domain]  Cd Length: 352  Bit Score: 53.53  E-value: 1.61e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 228 RTIAKQIQMVRQVGKGRYGEVWM--GKWRGEKVAVKVFFTTE------EASWFRETEIyqtvlMRHEN-----ILGFIAA 294
Cdd:cd05596  22 RMNAEDFDVIKVIGRGAFGEVQLvrHKSTKKVYAMKLLSKFEmikrsdSAFFWEERDI-----MAHANsewivQLHYAFQ 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 295 DIKgtgswtQLYLITDYHENGSL------YDF-LKCATLDTrALLKLAYSAacglchLHTEIYgtqgkpaiAHRDLKSKN 367
Cdd:cd05596  97 DDK------YLYMVMDYMPGGDLvnlmsnYDVpEKWARFYT-AEVVLALDA------IHSMGF--------VHRDVKPDN 155
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41349437 368 ILIKKNGSCCIADLGLAVKFNSDTNevdVPLNTRVGTKRYMAPEVLdesLNKNHFQPY-IMADIYSFGLIIWEM 440
Cdd:cd05596 156 MLLDASGHLKLADFGTCMKMDKDGL---VRSDTAVGTPDYISPEVL---KSQGGDGVYgRECDWWSVGVFLYEM 223
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
230-438 1.61e-07

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: 52.77  E-value: 1.61e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 230 IAKQIQMVRQVGKGRYGEVWMGKWR--GEKVAVKVFFTTEEASWFR--ETEIYQTVLMRHENILGF---IAADIKgtgsw 302
Cdd:cd14078   1 LLKYYELHETIGSGGFAKVKLATHIltGEKVAIKIMDKKALGDDLPrvKTEIEALKNLSHQHICRLyhvIETDNK----- 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 303 tqLYLITDYHENGSLYDFL----KCATLDTRALLKLAYSAacgLCHLHTEIYgtqgkpaiAHRDLKSKNILIKKNGSCCI 378
Cdd:cd14078  76 --IFMVLEYCPGGELFDYIvakdRLSEDEARVFFRQIVSA---VAYVHSQGY--------AHRDLKPENLLLDEDQNLKL 142
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41349437 379 ADLGLAVKfnsDTNEVDVPLNTRVGTKRYMAPEVLDEslnknhfQPYI--MADIYSFGLIIW 438
Cdd:cd14078 143 IDFGLCAK---PKGGMDHHLETCCGSPAYAAPELIQG-------KPYIgsEADVWSMGVLLY 194
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
235-440 1.63e-07

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: 53.38  E-value: 1.63e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 235 QMVRQVGKGRYGEVWM-----GKWRGEKVAVKVF---FTTEEASWFRETEIYQTVLmRHENILGFIAADIKGTGSWTQLY 306
Cdd:cd05614   3 ELLKVLGTGAYGKVFLvrkvsGHDANKLYAMKVLrkaALVQKAKTVEHTRTERNVL-EHVRQSPFLVTLHYAFQTDAKLH 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 307 LITDYHENGSLYDFLKCATLDTRALLKLaYSAAC--GLCHLHteiygtqgKPAIAHRDLKSKNILIKKNGSCCIADLGLA 384
Cdd:cd05614  82 LILDYVSGGELFTHLYQRDHFSEDEVRF-YSGEIilALEHLH--------KLGIVYRDIKLENILLDSEGHVVLTDFGLS 152
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 41349437 385 VKFNSDTNEVDVPLntrVGTKRYMAPEVLDEslNKNHFQpyiMADIYSFGLIIWEM 440
Cdd:cd05614 153 KEFLTEEKERTYSF---CGTIEYMAPEIIRG--KSGHGK---AVDWWSLGILMFEL 200
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
312-513 1.67e-07

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 53.34  E-value: 1.67e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437  312 HENGSLYDFL--KCATLDTRALLKLAYSAACGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNGSCCIADLGlAVKFNs 389
Cdd:PHA03209 138 HYSSDLYTYLtkRSRPLPIDQALIIEKQILEGLRYLHAQ--------RIIHRDVKTENIFINDVDQVCIGDLG-AAQFP- 207
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437  390 dtneVDVPLNTRV-GTKRYMAPEVLDESLNKNHfqpyimADIYSFGLIIWEMarrcitggiveeyqLPYYNMVPSD-PSY 467
Cdd:PHA03209 208 ----VVAPAFLGLaGTVETNAPEVLARDKYNSK------ADIWSAGIVLFEM--------------LAYPSTIFEDpPST 263
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 41349437  468 EDMREVVCVKRLRPIVSnrwnsdeclraVLKLMSECWAHNPASRLT 513
Cdd:PHA03209 264 PEEYVKSCHSHLLKIIS-----------TLKVHPEEFPRDPGSRLV 298
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
273-475 1.71e-07

Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK16 is associated with many names including Myristylated and Palmitylated Serine/threonine Kinase 1 (MPSK1), Kinase related to cerevisiae and thaliana (Krct), and Protein Kinase expressed in day 12 fetal liver (PKL12). It is widely expressed in mammals with highest levels found in liver, testis, and kidney. It is localized in the Golgi but is translocated to the nucleus upon disorganization of the Golgi. STK16 is constitutively active and is capable of phosphorylating itself and other substrates. It may be involved in regulating stromal-epithelial interactions during mammary gland ductal morphogenesis. It may also function as a transcriptional co-activator of type-C natriuretic peptide and VEGF. The STK16 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: 270888 [Multi-domain]  Cd Length: 282  Bit Score: 52.68  E-value: 1.71e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 273 RETEIYQtvLMRHENILGFIAADIKGTGSWTQ-LYLITDYHENGSLYDFL-----KCATLDTRALLKLaYSAAC-GLCHL 345
Cdd:cd13986  46 REIENYR--LFNHPNILRLLDSQIVKEAGGKKeVYLLLPYYKRGSLQDEIerrlvKGTFFPEDRILHI-FLGICrGLKAM 122
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 346 HTeiygtQGKPAIAHRDLKSKNILIKKNGSCCIADLGlavkfnsDTNEVDVPLNTRV------------GTKRYMAPE-- 411
Cdd:cd13986 123 HE-----PELVPYAHRDIKPGNVLLSEDDEPILMDLG-------SMNPARIEIEGRRealalqdwaaehCTMPYRAPElf 190
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 412 ------VLDESlnknhfqpyimADIYSFGLIIWEMA-------RRCITGGIVeeyQLPYYNMV---PSDPSY-EDMREVV 474
Cdd:cd13986 191 dvkshcTIDEK-----------TDIWSLGCTLYALMygespfeRIFQKGDSL---ALAVLSGNysfPDNSRYsEELHQLV 256

                .
gi 41349437 475 C 475
Cdd:cd13986 257 K 257
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
341-518 1.74e-07

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: 52.64  E-value: 1.74e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 341 GLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNGSCCIADLGLAVKFNSDtnevDVPLNTRVGTKRYMAPEVLDESlnKN 420
Cdd:cd14200 136 GIEYLHYQ--------KIVHRDIKPSNLLLGDDGHVKIADFGVSNQFEGN----DALLSSTAGTPAFMAPETLSDS--GQ 201
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 421 HFQPYIMaDIYSFGLIIWemarrCITGG---IVEEYQLPYYNMVPSDP-SYEDMREVvcvkrlrpivsnrwnSDECLRAV 496
Cdd:cd14200 202 SFSGKAL-DVWAMGVTLY-----CFVYGkcpFIDEFILALHNKIKNKPvEFPEEPEI---------------SEELKDLI 260
                       170       180
                ....*....|....*....|..
gi 41349437 497 LKLMSEcwahNPASRLTALRIK 518
Cdd:cd14200 261 LKMLDK----NPETRITVPEIK 278
PTKc_DDR_like cd05097
Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the ...
232-513 2.31e-07

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: 52.67  E-value: 2.31e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 232 KQIQMVRQVGKGRYGEVWMGKWRGEK----------------VAVKVF----FTTEEASWFRETEIYQTvlMRHENILGF 291
Cdd:cd05097   5 QQLRLKEKLGEGQFGEVHLCEAEGLAeflgegapefdgqpvlVAVKMLradvTKTARNDFLKEIKIMSR--LKNPNIIRL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 292 IAADIKGTgswtQLYLITDYHENGSLYDFLkcATLDTRALLKLAYSAAC----GLCHLHTEIygTQGKPAIA-----HRD 362
Cdd:cd05097  83 LGVCVSDD----PLCMITEYMENGDLNQFL--SQREIESTFTHANNIPSvsiaNLLYMAVQI--ASGMKYLAslnfvHRD 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 363 LKSKNILIKKNGSCCIADLGLAVK-FNSDTNEVDvplNTRVGTKRYMAPevldESLNKNHFQpyIMADIYSFGLIIWEMA 441
Cdd:cd05097 155 LATRNCLVGNHYTIKIADFGMSRNlYSGDYYRIQ---GRAVLPIRWMAW----ESILLGKFT--TASDVWAFGVTLWEMF 225
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41349437 442 RRCitggiveeYQLPyYNMVPSDPSYEDMREVVCVKRLRPIVSnrwNSDECLRAVLKLMSECWAHNPASRLT 513
Cdd:cd05097 226 TLC--------KEQP-YSLLSDEQVIENTGEFFRNQGRQIYLS---QTPLCPSPVFKLMMRCWSRDIKDRPT 285
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
232-438 2.69e-07

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: 51.95  E-value: 2.69e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 232 KQIQMVRQV-GKGRYGEVWMGKWRGEKVAVKVFFTTEEASWFRETEIYQTVL----MRHENILGFiaADIKGTGSwtQLY 306
Cdd:cd14167   2 RDIYDFREVlGTGAFSEVVLAEEKRTQKLVAIKCIAKKALEGKETSIENEIAvlhkIKHPNIVAL--DDIYESGG--HLY 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 307 LITDYHENGSLYD-FLKCATLDTRALLKLAYSAACGLCHLHTEiygtqgkpAIAHRDLKSKNIL---IKKNGSCCIADLG 382
Cdd:cd14167  78 LIMQLVSGGELFDrIVEKGFYTERDASKLIFQILDAVKYLHDM--------GIVHRDLKPENLLyysLDEDSKIMISDFG 149
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 41349437 383 LAVKFNSDTnevdvPLNTRVGTKRYMAPEVLDEslnknhfQPYIMA-DIYSFGLIIW 438
Cdd:cd14167 150 LSKIEGSGS-----VMSTACGTPGYVAPEVLAQ-------KPYSKAvDCWSIGVIAY 194
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
304-442 2.86e-07

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK3, also called beta-adrenergic receptor kinase 2 (beta-ARK2), is widely expressed in many tissues. It is involved in modulating the cholinergic response of airway smooth muscles, and also plays a role in dopamine receptor regulation. GRK3-deficient mice show a lack of olfactory receptor desensitization and altered regulation of the M2 muscarinic airway. GRK3 promoter polymorphisms may also be associated with bipolar disorder. GRK3 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. The GRK3 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: 270781 [Multi-domain]  Cd Length: 346  Bit Score: 52.76  E-value: 2.86e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 304 QLYLITDYHENGSL-YDFLKCATLDTRALLKLAYSAACGLCHLHTEIygtqgkpaIAHRDLKSKNILIKKNGSCCIADLG 382
Cdd:cd05633  82 KLCFILDLMNGGDLhYHLSQHGVFSEKEMRFYATEIILGLEHMHNRF--------VVYRDLKPANILLDEHGHVRISDLG 153
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 383 LAVKFNSDTNevdvplNTRVGTKRYMAPEVLDESLNKNHfqpyiMADIYSFGLIIWEMAR 442
Cdd:cd05633 154 LACDFSKKKP------HASVGTHGYMAPEVLQKGTAYDS-----SADWFSLGCMLFKLLR 202
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
235-518 2.91e-07

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: 51.91  E-value: 2.91e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 235 QMVRQVGKGRYG--EVWMGKWRGEKVAVKVFFTTEEASWFRETEIYQTVLMRHENILGFIAADIkgtgSWTQLYLITDYH 312
Cdd:cd14665   3 ELVKDIGSGNFGvaRLMRDKQTKELVAVKYIERGEKIDENVQREIINHRSLRHPNIVRFKEVIL----TPTHLAIVMEYA 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 313 ENGSLYDFL----KCATLDTRALLKLAYSaacGLCHLHTEiygtqgkpAIAHRDLKSKNILIkkNGSCC----IADLGLa 384
Cdd:cd14665  79 AGGELFERIcnagRFSEDEARFFFQQLIS---GVSYCHSM--------QICHRDLKLENTLL--DGSPAprlkICDFGY- 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 385 vkfnSDTNEVDVPLNTRVGTKRYMAPEVldesLNKNHFQPYImADIYSFGLIIWEMarrcitggIVEEYqlPYYNmvPSD 464
Cdd:cd14665 145 ----SKSSVLHSQPKSTVGTPAYIAPEV----LLKKEYDGKI-ADVWSCGVTLYVM--------LVGAY--PFED--PEE 203
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41349437 465 PsyEDMRevvcvKRLRPIVSNRWN-------SDECLRavlkLMSECWAHNPASRLTALRIK 518
Cdd:cd14665 204 P--RNFR-----KTIQRILSVQYSipdyvhiSPECRH----LISRIFVADPATRITIPEIR 253
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
240-440 2.99e-07

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: 52.31  E-value: 2.99e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 240 VGKGRYGEVWMGKWRG--EKVAVKVFfttEEASWFRETEIYQTvlMRHENILG------FIAADIKGTGSWTQLYLITDY 311
Cdd:cd05616   8 LGKGSFGKVMLAERKGtdELYAVKIL---KKDVVIQDDDVECT--MVEKRVLAlsgkppFLTQLHSCFQTMDRLYFVMEY 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 312 HENGSL-YDFLKCATLDTRALLKLAYSAACGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNGSCCIADLGLAVKfnsd 390
Cdd:cd05616  83 VNGGDLmYHIQQVGRFKEPHAVFYAAEIAIGLFFLQSK--------GIIYRDLKLDNVMLDSEGHIKIADFGMCKE---- 150
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 41349437 391 tNEVD-VPLNTRVGTKRYMAPEVLdeslnknHFQPYIMA-DIYSFGLIIWEM 440
Cdd:cd05616 151 -NIWDgVTTKTFCGTPDYIAPEII-------AYQPYGKSvDWWAFGVLLYEM 194
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
283-416 3.05e-07

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: 51.92  E-value: 3.05e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 283 MRHENILGFIaadiKGTGSWTQLYLITDYHENGSLYDFLKCATLDT-RALLKLAYSAACGLCHLHTEiygtqgkpAIAHR 361
Cdd:cd14183  61 VKHPNIVLLI----EEMDMPTELYLVMELVKGGDLFDAITSTNKYTeRDASGMLYNLASAIKYLHSL--------NIVHR 128
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 41349437 362 DLKSKNILIKK----NGSCCIADLGLAVKfnsdtneVDVPLNTRVGTKRYMAPEVLDES 416
Cdd:cd14183 129 DIKPENLLVYEhqdgSKSLKLGDFGLATV-------VDGPLYTVCGTPTYVAPEIIAET 180
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
234-440 3.05e-07

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 52.51  E-value: 3.05e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437  234 IQMVRQVGKGRYGEVWMGKWR--GEKVAVKVFFTTEEASWFRETEIYQTVLMRHENILGFIAADIKGTGSWTQLYLITDY 311
Cdd:PTZ00263  20 FEMGETLGTGSFGRVRIAKHKgtGEYYAIKCLKKREILKMKQVQHVAQEKSILMELSHPFIVNMMCSFQDENRVYFLLEF 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437  312 HENGSLYDFLKCATLDTRALLKLaYSAACGLC--HLHTEiygtqgkpAIAHRDLKSKNILIKKNGSCCIADLGLAVKFNS 389
Cdd:PTZ00263 100 VVGGELFTHLRKAGRFPNDVAKF-YHAELVLAfeYLHSK--------DIIYRDLKPENLLLDNKGHVKVTDFGFAKKVPD 170
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 41349437  390 DTnevdvplNTRVGTKRYMAPEVLDeslNKNHFQPyimADIYSFGLIIWEM 440
Cdd:PTZ00263 171 RT-------FTLCGTPEYLAPEVIQ---SKGHGKA---VDWWTMGVLLYEF 208
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
341-440 3.07e-07

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: 52.19  E-value: 3.07e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 341 GLCHLHteiygtqgKPAIAHRDLKSKNILIKKNGSCCIADLGLAVKFNSDTNEvdvplnTR--VGTKRYMAPEVLDEsln 418
Cdd:cd05608 117 GLEHLH--------QRRIIYRDLKPENVLLDDDGNVRISDLGLAVELKDGQTK------TKgyAGTPGFMAPELLLG--- 179
                        90       100
                ....*....|....*....|...
gi 41349437 419 knhfQPYIMA-DIYSFGLIIWEM 440
Cdd:cd05608 180 ----EEYDYSvDYFTLGVTLYEM 198
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
228-474 3.35e-07

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 52.95  E-value: 3.35e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437  228 RTIAKQIQMVRQVGKGRYGEVWMGKWR--GEKVAVKVFftteEASWFRETEI--------------YQTVLMRHENilgF 291
Cdd:PTZ00283  28 KEQAKKYWISRVLGSGATGTVLCAKRVsdGEPFAVKVV----DMEGMSEADKnraqaevccllncdFFSIVKCHED---F 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437  292 IAADIKGTGSWTQLYLITDYHENGSLYDFLKCATLDTRALLK-----LAYSAACGLCHLHTEiygtqgkpAIAHRDLKSK 366
Cdd:PTZ00283 101 AKKDPRNPENVLMIALVLDYANAGDLRQEIKSRAKTNRTFREheaglLFIQVLLAVHHVHSK--------HMIHRDIKSA 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437  367 NILIKKNGSCCIADLGLAvKFNSDTNEVDVPlNTRVGTKRYMAPEVLDEslnknhfQPYI-MADIYSFGLIIWEM--ARR 443
Cdd:PTZ00283 173 NILLCSNGLVKLGDFGFS-KMYAATVSDDVG-RTFCGTPYYVAPEIWRR-------KPYSkKADMFSLGVLLYELltLKR 243
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 41349437  444 CITGGIVEEYQ----LPYYNMVPSDPSYEdMREVV 474
Cdd:PTZ00283 244 PFDGENMEEVMhktlAGRYDPLPPSISPE-MQEIV 277
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
305-512 3.40e-07

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: 51.84  E-value: 3.40e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 305 LYLITDYHENGSLYDFLKcatldTRALL---KLAYSAAC---GLCHLHTeiygtQGkpaIAHRDLKSKNILIKKNGSCCI 378
Cdd:cd05572  68 LYMLMEYCLGGELWTILR-----DRGLFdeyTARFYTACvvlAFEYLHS-----RG---IIYRDLKPENLLLDSNGYVKL 134
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 379 ADLGLA--VKFNSDTnevdvplNTRVGTKRYMAPEVLdesLNKNHfqpYIMADIYSFGLIIWEMarrcITGGiveeyqLP 456
Cdd:cd05572 135 VDFGFAkkLGSGRKT-------WTFCGTPEYVAPEII---LNKGY---DFSVDYWSLGILLYEL----LTGR------PP 191
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 41349437 457 YYNmvPSDPSYEDMREVvcVKRLRPIVSNRWNSdeclRAVLKLMSECWAHNPASRL 512
Cdd:cd05572 192 FGG--DDEDPMKIYNII--LKGIDKIEFPKYID----KNAKNLIKQLLRRNPEERL 239
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
360-440 3.71e-07

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: 52.32  E-value: 3.71e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 360 HRDLKSKNILIKKNGSCCIADLGLAVKFNSDTNEVDVPLNTRVGTKRYMAPEVLdesLNKNHFQpyiMADIYSFGLIIWE 439
Cdd:cd05598 124 HRDIKPDNILIDRDGHIKLTDFGLCTGFRWTHDSKYYLAHSLVGTPNYIAPEVL---LRTGYTQ---LCDWWSVGVILYE 197

                .
gi 41349437 440 M 440
Cdd:cd05598 198 M 198
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
239-452 3.75e-07

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: 51.93  E-value: 3.75e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 239 QVGKGRYGEVWMG--KWRGEKVAVK-VFFTTEEA---SWFRETEIYQTvlMRHENILGFiaADIKGTGSwtQLYLITDYH 312
Cdd:cd07871  12 KLGEGTYATVFKGrsKLTENLVALKeIRLEHEEGapcTAIREVSLLKN--LKHANIVTL--HDIIHTER--CLTLVFEYL 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 313 ENgSLYDFL-KCATLDTRALLKL-AYSAACGLCHLHteiygtqgKPAIAHRDLKSKNILIKKNGSCCIADLGLAvkfnsd 390
Cdd:cd07871  86 DS-DLKQYLdNCGNLMSMHNVKIfMFQLLRGLSYCH--------KRKILHRDLKPQNLLINEKGELKLADFGLA------ 150
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41349437 391 tNEVDVPLNT---RVGTKRYMAPEVLdesLNKNHFQPYImaDIYSFGLIIWEMA--RRCITGGIVEE 452
Cdd:cd07871 151 -RAKSVPTKTysnEVVTLWYRPPDVL---LGSTEYSTPI--DMWGVGCILYEMAtgRPMFPGSTVKE 211
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
240-436 3.82e-07

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: 51.46  E-value: 3.82e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 240 VGKGRYGEVW--MGKWRGEKVAVKVFFTTEEASW---FRETEIYQTvlMRHENILGFIAA-DIKgtgswTQLYLITDYHE 313
Cdd:cd14103   1 LGRGKFGTVYrcVEKATGKELAAKFIKCRKAKDRedvRNEIEIMNQ--LRHPRLLQLYDAfETP-----REMVLVMEYVA 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 314 NGSLY------DFlkcaTLDTRALLKLAYSAACGLCHLHteiygtqgKPAIAHRDLKSKNIL-IKKNGSCC-IADLGLAV 385
Cdd:cd14103  74 GGELFervvddDF----ELTERDCILFMRQICEGVQYMH--------KQGILHLDLKPENILcVSRTGNQIkIIDFGLAR 141
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 41349437 386 KFNSDTnevdvPLNTRVGTKRYMAPEVLdeslnkNHFQPYIMADIYSFGLI 436
Cdd:cd14103 142 KYDPDK-----KLKVLFGTPEFVAPEVV------NYEPISYATDMWSVGVI 181
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
241-436 3.89e-07

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: 51.50  E-value: 3.89e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 241 GKGRYGEVWMG--KWRGEKVAVKVFFTTEE--ASWFRETEIYQTVlmRHENILGFIAADIKGTGswtqLYLITDYHENGS 316
Cdd:cd14006   2 GRGRFGVVKRCieKATGREFAAKFIPKRDKkkEAVLREISILNQL--QHPRIIQLHEAYESPTE----LVLILELCSGGE 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 317 LYDFL----KCATLDTRALLKLAYSaacGLCHLHTEiygtqgkpAIAHRDLKSKNILI--KKNGSCCIADLGLAVKFNsD 390
Cdd:cd14006  76 LLDRLaergSLSEEEVRTYMRQLLE---GLQYLHNH--------HILHLDLKPENILLadRPSPQIKIIDFGLARKLN-P 143
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 41349437 391 TNEVDVPLntrvGTKRYMAPEVLDeslnknhFQPYIMA-DIYSFGLI 436
Cdd:cd14006 144 GEELKEIF----GTPEFVAPEIVN-------GEPVSLAtDMWSIGVL 179
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
235-480 4.28e-07

Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 binding kinase (MRCK) alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MRCK-alpha is expressed ubiquitously in many tissues. It plays a role in the regulation of peripheral actin reorganization and neurite outgrowth. It may also play a role in the transferrin iron uptake pathway. MRCK is activated via interaction with the small GTPase Cdc42. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. The MRCK-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. This alignment model includes the dimerization domain.


Pssm-ID: 270773 [Multi-domain]  Cd Length: 409  Bit Score: 52.32  E-value: 4.28e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 235 QMVRQVGKGRYGEVWMGKWrgeKVAVKVFFTTEEASWfRETEIYQTVLMRHE-NILgfiaadIKGTGSW----------- 302
Cdd:cd05623  75 EILKVIGRGAFGEVAVVKL---KNADKVFAMKILNKW-EMLKRAETACFREErDVL------VNGDSQWittlhyafqdd 144
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 303 TQLYLITDYHENGSLYDFLkcATLDTRALLKLA--YSAACGLC--HLHTEIYgtqgkpaiAHRDLKSKNILIKKNGSCCI 378
Cdd:cd05623 145 NNLYLVMDYYVGGDLLTLL--SKFEDRLPEDMArfYLAEMVLAidSVHQLHY--------VHRDIKPDNILMDMNGHIRL 214
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 379 ADLGLAVKFNSDTNevdVPLNTRVGTKRYMAPEVLDESLN-KNHFQPyiMADIYSFGLIIWEM--------ARRCIT--G 447
Cdd:cd05623 215 ADFGSCLKLMEDGT---VQSSVAVGTPDYISPEILQAMEDgKGKYGP--ECDWWSLGVCMYEMlygetpfyAESLVEtyG 289
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 41349437 448 GIV---EEYQLPYYNMVPSDPSYEDMREVVCVKRLR 480
Cdd:cd05623 290 KIMnhkERFQFPTQVTDVSENAKDLIRRLICSREHR 325
PHA03210 PHA03210
serine/threonine kinase US3; Provisional
251-440 4.58e-07

serine/threonine kinase US3; Provisional


Pssm-ID: 165476 [Multi-domain]  Cd Length: 501  Bit Score: 52.39  E-value: 4.58e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437  251 GKWRGEKVAVKVFFTTEEASWFRETEIYQTVLMRHENILGFiaADIKGTGSWTqlYLITDYHENgSLYDFLKCATLD--- 327
Cdd:PHA03210 188 GKPKCERLIAKRVKAGSRAAIQLENEILALGRLNHENILKI--EEILRSEANT--YMITQKYDF-DLYSFMYDEAFDwkd 262
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437  328 ------TRALLKlaySAACGLCHLHTEIygtqgkpaIAHRDLKSKNILIKKNGSCCIADLGLAVKFNSDTNEVDVPLntr 401
Cdd:PHA03210 263 rpllkqTRAIMK---QLLCAVEYIHDKK--------LIHRDIKLENIFLNCDGKIVLGDFGTAMPFEKEREAFDYGW--- 328
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 41349437  402 VGTKRYMAPEVLDESlnknhfqPYI-MADIYSFGLIIWEM 440
Cdd:PHA03210 329 VGTVATNSPEILAGD-------GYCeITDIWSCGLILLDM 361
PTKc_HER4 cd05110
Catalytic domain of the Protein Tyrosine Kinase, HER4; PTKs catalyze the transfer of the ...
233-440 4.67e-07

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: 51.61  E-value: 4.67e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 233 QIQMVRQVGKGRYGEVWMGKWRGE----KVAVKVFFTTEEASWFRETEIYQTVL----MRHENILGFIAADIKGTgswtq 304
Cdd:cd05110   8 ELKRVKVLGSGAFGTVYKGIWVPEgetvKIPVAIKILNETTGPKANVEFMDEALimasMDHPHLVRLLGVCLSPT----- 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 305 LYLITDYHENGSLYDFLK--CATLDTRALLKLAYSAACGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNGSCCIADLG 382
Cdd:cd05110  83 IQLVTQLMPHGCLLDYVHehKDNIGSQLLLNWCVQIAKGMMYLEER--------RLVHRDLAARNVLVKSPNHVKITDFG 154
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41349437 383 LAVKFNSDTNEVDVPlntrvGTK---RYMAPEVLdeslnknHFQPYI-MADIYSFGLIIWEM 440
Cdd:cd05110 155 LARLLEGDEKEYNAD-----GGKmpiKWMALECI-------HYRKFThQSDVWSYGVTIWEL 204
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
241-474 5.02e-07

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: 51.29  E-value: 5.02e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 241 GKGRYGEV--WMGKWRGEKVAVK---VFFTTEEAS---WFRETEIYQTvlMRHENILGFiaadiKGTGSWTQLYLITD-- 310
Cdd:cd13989   2 GSGGFGYVtlWKHQDTGEYVAIKkcrQELSPSDKNrerWCLEVQIMKK--LNHPNVVSA-----RDVPPELEKLSPNDlp 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 311 -----YHENGSLYDFLK----CATL---DTRALLKlaySAACGLCHLHteiygtqgKPAIAHRDLKSKNILIKKNGSCCI 378
Cdd:cd13989  75 llameYCSGGDLRKVLNqpenCCGLkesEVRTLLS---DISSAISYLH--------ENRIIHRDLKPENIVLQQGGGRVI 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 379 ---ADLGLAVKFnsDTNEVDVPLntrVGTKRYMAPEVLDEslnknhfQPY-IMADIYSFGLIIWEmarrCITGgiveeYQ 454
Cdd:cd13989 144 yklIDLGYAKEL--DQGSLCTSF---VGTLQYLAPELFES-------KKYtCTVDYWSFGTLAFE----CITG-----YR 202
                       250       260       270
                ....*....|....*....|....*....|...
gi 41349437 455 --LPYYNMVP-------SDPS----YEDMREVV 474
Cdd:cd13989 203 pfLPNWQPVQwhgkvkqKKPEhicaYEDLTGEV 235
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
274-513 5.57e-07

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: 50.75  E-value: 5.57e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 274 ETEIYQTVlmRHENILGFIaaDIKgtgsWTQ--LYLITDYHENGSLYDFLKC-ATLDTRALLKLAYSAACGLCHLHTEiy 350
Cdd:cd14121  45 EIELLKKL--KHPHIVELK--DFQ----WDEehIYLIMEYCSGGDLSRFIRSrRTLPESTVRRFLQQLASALQFLREH-- 114
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 351 gtqgkpAIAHRDLKSKNILI--KKNGSCCIADLGLAVKFNSDtnevDVPLNTRvGTKRYMAPEVLdesLNKnHFQPyiMA 428
Cdd:cd14121 115 ------NISHMDLKPQNLLLssRYNPVLKLADFGFAQHLKPN----DEAHSLR-GSPLYMAPEMI---LKK-KYDA--RV 177
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 429 DIYSFGLIIWEmarrCITGgiveeyQLPYynmvpSDPSYEDMREVvcVKRLRPIV--SNRWNSDECLRAVLKLMsecwAH 506
Cdd:cd14121 178 DLWSVGVILYE----CLFG------RAPF-----ASRSFEELEEK--IRSSKPIEipTRPELSADCRDLLLRLL----QR 236

                ....*..
gi 41349437 507 NPASRLT 513
Cdd:cd14121 237 DPDRRIS 243
PTKc_CSF-1R cd05106
Catalytic domain of the Protein Tyrosine Kinase, Colony-Stimulating Factor-1 Receptor; PTKs ...
326-525 5.83e-07

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: 51.77  E-value: 5.83e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 326 LDTRALLKLAYSAACGLCHLHTeiygtqgKPAIaHRDLKSKNILIKKNGSCCIADLGLAVKFNSDTNEVdVPLNTRVGTK 405
Cdd:cd05106 209 LDLDDLLRFSSQVAQGMDFLAS-------KNCI-HRDVAARNVLLTDGRVAKICDFGLARDIMNDSNYV-VKGNARLPVK 279
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 406 rYMAPEVLDESLNKnhfqpyIMADIYSFGLIIWEMarrcitggiveeYQL---PYYNMVPSDPSYEDMREvvCVKRLRPi 482
Cdd:cd05106 280 -WMAPESIFDCVYT------VQSDVWSYGILLWEI------------FSLgksPYPGILVNSKFYKMVKR--GYQMSRP- 337
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 41349437 483 vsnrwnsDECLRAVLKLMSECWAHNPASRLTALRIKKTLAKMV 525
Cdd:cd05106 338 -------DFAPPEIYSIMKMCWNLEPTERPTFSQISQLIQRQL 373
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
329-459 6.16e-07

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: 51.22  E-value: 6.16e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 329 RALLKLAYSAACGLCHLHTeiygtqgKPAIAHRDLKSKNILIKKNGSCCIADLGLAVKFnsdtneVDVPLNTR-VGTKRY 407
Cdd:cd06618 114 DILGKMTVSIVKALHYLKE-------KHGVIHRDVKPSNILLDESGNVKLCDFGISGRL------VDSKAKTRsAGCAAY 180
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 41349437 408 MAPEVLDESLNKNHfqpYIMADIYSFGLIIWEMArrciTGgiveeyQLPYYN 459
Cdd:cd06618 181 MAPERIDPPDNPKY---DIRADVWSLGISLVELA----TG------QFPYRN 219
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
241-382 6.19e-07

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: 48.59  E-value: 6.19e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 241 GKGRYGEVWM--GKWRGEKVAVKVF--FTTEEASWF-RETEIYQtVLMRHE-NILGFIAADIKGTGSWtqlyLITDYHEN 314
Cdd:cd13968   2 GEGASAKVFWaeGECTTIGVAVKIGddVNNEEGEDLeSEMDILR-RLKGLElNIPKVLVTEDVDGPNI----LLMELVKG 76
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41349437 315 GSLYDFLKCATLDTRALLKLAYSAACGLCHLHTEIYGtqgkpaiaHRDLKSKNILIKKNGSCCIADLG 382
Cdd:cd13968  77 GTLIAYTQEEELDEKDVESIMYQLAECMRLLHSFHLI--------HRDLNNDNILLSEDGNVKLIDFG 136
TFP_LU_ECD_ALK5 cd23537
extracellular domain (ECD) found in activin receptor-like kinase 5 (ALK-5) and similar ...
59-131 6.43e-07

extracellular domain (ECD) found in activin receptor-like kinase 5 (ALK-5) and similar proteins; ALK-5 (EC 2.7.11.30, also called TGF-beta receptor type-1 (TGFR-1), or activin A receptor type II-like protein kinase of 53kD, or serine/threonine-protein kinase receptor R4 (SKR4), or TGF-beta type I receptor, or transforming growth factor-beta receptor type I (TGFBR1), or TGF-beta receptor type I (TbetaR-I)) is the transmembrane serine/threonine kinase forming with the TGF-beta type II serine/threonine kinase receptor, TGFBR2, the non-promiscuous receptor for the TGF-beta cytokines TGFB1, TGFB2, and TGFB3. It transduces the TGFB1, TGFB2, and TGFB3 signal from the cell surface to the cytoplasm and is thus regulating a plethora of physiological and pathological processes including cell cycle arrest in epithelial and hematopoietic cells, control of mesenchymal cell proliferation and differentiation, wound healing, extracellular matrix production, immunosuppression, and carcinogenesis. This model corresponds to the extracellular domain (ECD) of ALK-5, which belongs to Ly-6 antigen/uPA receptor-like (LU) superfamily and exhibits a snake toxin-like fold (also known as three-finger toxin/3FTx fold or three-fingered protein/TFP domain fold).


Pssm-ID: 467067  Cd Length: 74  Bit Score: 47.02  E-value: 6.43e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41349437  59 LKCYCSgHCPDdaiNNTCITNGHCFAIIEEDDqGETTLASGCMKYE-----GSDFQCKDSPKAQLRRTIECCRTNLCN 131
Cdd:cd23537   1 LQCYCH-LCTK---NFTCVTDGLCFVSVTRST-DKVIHNSMCIAEIdliprDRPFVCAPSSKDGSSTHPYCCNTDHCN 73
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
241-436 7.81e-07

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: 50.45  E-value: 7.81e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 241 GKGRYGEVWMGKWR--GEKVAVKVF----FTTEEASWfrETEIyqTVL--MRHENILGFIaaDIkgTGSWTQLYLITDYH 312
Cdd:cd14083  12 GTGAFSEVVLAEDKatGKLVAIKCIdkkaLKGKEDSL--ENEI--AVLrkIKHPNIVQLL--DI--YESKSHLYLVMELV 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 313 ENGSLYDFL---KCAT-LDTRALLKLAYSAacgLCHLHTeiygtQGkpaIAHRDLKSKNILI---KKNGSCCIADLGLav 385
Cdd:cd14083  84 TGGELFDRIvekGSYTeKDASHLIRQVLEA---VDYLHS-----LG---IVHRDLKPENLLYyspDEDSKIMISDFGL-- 150
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 41349437 386 kfnSDTNEVDVpLNTRVGTKRYMAPEVLDEslnknhfQPYIMA-DIYSFGLI 436
Cdd:cd14083 151 ---SKMEDSGV-MSTACGTPGYVAPEVLAQ-------KPYGKAvDCWSIGVI 191
TFP_LU_ECD_sma6 cd23586
extracellular domain (ECD) found in Caenorhabditis elegans serine/threonine-protein kinase ...
59-132 8.35e-07

extracellular domain (ECD) found in Caenorhabditis elegans serine/threonine-protein kinase receptor sma-6 and similar proteins; Sma-6 (EC 2.7.11.30) is serine/threonine-protein kinase receptor that binds transforming growth factor-beta (TGF-beta)-like ligands dbl-1 and perhaps daf-7. Upon ligand binding, it probably activates a TGF-beta-like signaling pathway. Sma-6 contains an extracellular domain (ECD), which belongs to Ly-6 antigen/uPA receptor-like (LU) superfamily and exhibits a snake toxin-like fold (also known as three-finger toxin/3FTx fold or three-fingered protein/TFP domain fold).


Pssm-ID: 467116  Cd Length: 78  Bit Score: 46.63  E-value: 8.35e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437  59 LKCYC--SGHCPddAINNTCITNGHCFAIIEEDD--QGETTLASGCMKYE--GSDFQCKDspKAQLRRTIECC-RTNLCN 131
Cdd:cd23586   1 LICYCtpSDHCP--NGNKTCTTTAGCFHSIEIDGnkRMETLEQFGCFSNDrgGSHLTCNA--KRPTPSSIKCCyNGDFCN 76

                .
gi 41349437 132 Q 132
Cdd:cd23586  77 R 77
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
303-441 8.95e-07

Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phototropins are blue-light receptors that control responses such as phototropism, stromatal opening, and chloroplast movement in order to optimize the photosynthetic efficiency of plants. They are light-activated STKs that contain an N-terminal photosensory domain and a C-terminal catalytic domain. The N-terminal domain contains two LOV (Light, Oxygen or Voltage) domains that binds FMN. Photoexcitation of the LOV domains results in autophosphorylation at multiple sites and activation of the catalytic domain. In addition to plant phototropins, included in this subfamily are predominantly uncharacterized fungal STKs whose catalytic domains resemble the phototropin kinase domain. One protein from Neurospora crassa is called nrc-2, which plays a role in growth and development by controlling entry into the conidiation program. The phototropin-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: 270726 [Multi-domain]  Cd Length: 316  Bit Score: 50.70  E-value: 8.95e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 303 TQLYLITDYHENGSLYDFLKcatldTRALLKLAYSAA--------CGLCHLHTeiygtQGkpaIAHRDLKSKNILIKKNG 374
Cdd:cd05574  74 THLCFVMDYCPGGELFRLLQ-----KQPGKRLPEEVArfyaaevlLALEYLHL-----LG---FVYRDLKPENILLHESG 140
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 375 SCCIADLGLAV--------------------KFNSDTNE-VDVPLNTR----VGTKRYMAPEVldesLNKNHFQPYImaD 429
Cdd:cd05574 141 HIMLTDFDLSKqssvtpppvrkslrkgsrrsSVKSIEKEtFVAEPSARsnsfVGTEEYIAPEV----IKGDGHGSAV--D 214
                       170
                ....*....|..
gi 41349437 430 IYSFGLIIWEMA 441
Cdd:cd05574 215 WWTLGILLYEML 226
PTKc_EGFR cd05108
Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs ...
233-511 9.31e-07

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: 50.79  E-value: 9.31e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 233 QIQMVRQVGKGRYGEVWMGKW--RGEK----VAVKVF--FTTEEASWFRETEIYQTVLMRHENILGFIAADIKGTgswtq 304
Cdd:cd05108   8 EFKKIKVLGSGAFGTVYKGLWipEGEKvkipVAIKELreATSPKANKEILDEAYVMASVDNPHVCRLLGICLTST----- 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 305 LYLITDYHENGSLYDFLK--CATLDTRALLKLAYSAACGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNGSCCIADLG 382
Cdd:cd05108  83 VQLITQLMPFGCLLDYVRehKDNIGSQYLLNWCVQIAKGMNYLEDR--------RLVHRDLAARNVLVKTPQHVKITDFG 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 383 LAVKFNSDTNEV-----DVPLntrvgtkRYMApevLDESLNKNHFQpyiMADIYSFGLIIWEMArrcitggiveEYQLPY 457
Cdd:cd05108 155 LAKLLGAEEKEYhaeggKVPI-------KWMA---LESILHRIYTH---QSDVWSYGVTVWELM----------TFGSKP 211
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 458 YNMVPSdpsyedmREVVCV----KRL--RPIvsnrwnsdeCLRAVLKLMSECWAHNPASR 511
Cdd:cd05108 212 YDGIPA-------SEISSIlekgERLpqPPI---------CTIDVYMIMVKCWMIDADSR 255
PTKc_PDGFR_beta cd05107
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor beta; ...
360-504 9.78e-07

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: 51.16  E-value: 9.78e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 360 HRDLKSKNILIKKNGSCCIADLGLAVKFNSDTNEVD-----VPLntrvgtkRYMAPEVLDESLNKNhfqpyiMADIYSFG 434
Cdd:cd05107 262 HRDLAARNVLICEGKLVKICDFGLARDIMRDSNYISkgstfLPL-------KWMAPESIFNNLYTT------LSDVWSFG 328
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 435 LIIWEMArrcITGGIveeyqlPYynmvPSDPSYEDMREVvcVKRLRPIVSNRWNSDEclraVLKLMSECW 504
Cdd:cd05107 329 ILLWEIF---TLGGT------PY----PELPMNEQFYNA--IKRGYRMAKPAHASDE----IYEIMQKCW 379
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
233-440 1.02e-06

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 51.66  E-value: 1.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437   233 QIQMVRQVGKGRYGEVWMGKWRgekvAVKVFFTTEEASW--FRETEIYQTVL-------MRHENILGFIAADIKGTGSwt 303
Cdd:PTZ00266   14 EYEVIKKIGNGRFGEVFLVKHK----RTQEFFCWKAISYrgLKEREKSQLVIevnvmreLKHKNIVRYIDRFLNKANQ-- 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437   304 QLYLITDYHENGSL-YDFLKC----ATLDTRALLKLAYSAACGLCHLHTEIYGTQGKpAIAHRDLKSKNILIKK------ 372
Cdd:PTZ00266   88 KLYILMEFCDAGDLsRNIQKCykmfGKIEEHAIVDITRQLLHALAYCHNLKDGPNGE-RVLHRDLKPQNIFLSTgirhig 166
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41349437   373 ---------NGS--CCIADLGLavkfnSDTNEVDVPLNTRVGTKRYMAPEVLDESLNKNHFQpyimADIYSFGLIIWEM 440
Cdd:PTZ00266  167 kitaqannlNGRpiAKIGDFGL-----SKNIGIESMAHSCVGTPYYWSPELLLHETKSYDDK----SDMWALGCIIYEL 236
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
360-441 1.06e-06

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: 50.48  E-value: 1.06e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 360 HRDLKSKNILIKKNGSCCIADLGLAVKFNSDTnevdvplNTRVGTKRYMAPEVLdesLNKnhfqPYIMA-DIYSFGLIIW 438
Cdd:cd14209 124 YRDLKPENLLIDQQGYIKVTDFGFAKRVKGRT-------WTLCGTPEYLAPEII---LSK----GYNKAvDWWALGVLIY 189

                ...
gi 41349437 439 EMA 441
Cdd:cd14209 190 EMA 192
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
233-440 1.09e-06

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: 50.55  E-value: 1.09e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 233 QIQMVrqVGKGRYGEVWMGKWR--GEKVAVK----VFFTTEEAS-WFRETEIYQtvLMRHENILgfiaaDIKgtgswtQL 305
Cdd:cd07859   3 KIQEV--IGKGSYGVVCSAIDThtGEKVAIKkindVFEHVSDATrILREIKLLR--LLRHPDIV-----EIK------HI 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 306 YLITDYHENGSLYDFLKCATLDTRALLK------------LAYSAACGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKN 373
Cdd:cd07859  68 MLPPSRREFKDIYVVFELMESDLHQVIKanddltpehhqfFLYQLLRALKYIHTA--------NVFHRDLKPKNILANAD 139
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41349437 374 GSCCIADLGLA-VKFNsdtnevDVPLNT----RVGTKRYMAPEVLDESLNKnhFQPYImaDIYSFGLIIWEM 440
Cdd:cd07859 140 CKLKICDFGLArVAFN------DTPTAIfwtdYVATRWYRAPELCGSFFSK--YTPAI--DIWSIGCIFAEV 201
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
303-440 1.12e-06

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: 50.04  E-value: 1.12e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 303 TQLYLITDYHENGSLYDFLKCATL----DTRALLKLAYSaacGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNGSCC- 377
Cdd:cd14106  81 SELILILELAAGGELQTLLDEEEClteaDVRRLMRQILE---GVQYLHER--------NIVHLDLKPQNILLTSEFPLGd 149
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41349437 378 --IADLGLAVKFNSDTNEVDVplntrVGTKRYMAPEVLdeslnknHFQPYIMA-DIYSFGLIIWEM 440
Cdd:cd14106 150 ikLCDFGISRVIGEGEEIREI-----LGTPDYVAPEIL-------SYEPISLAtDMWSIGVLTYVL 203
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
358-518 1.14e-06

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: 50.35  E-value: 1.14e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 358 IAHRDLKSKNILIKKNGSCCIADLGLAVKFNSDtnevDVPLNTRVGTKRYMAPEVLDESlnKNHFQPYIMaDIYSFGLII 437
Cdd:cd14199 147 IIHRDVKPSNLLVGEDGHIKIADFGVSNEFEGS----DALLTNTVGTPAFMAPETLSET--RKIFSGKAL-DVWAMGVTL 219
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 438 WemarrCITGG---IVEEYQLPYYNMVPSDP-SYEDMREVvcvkrlrpivsnrwnSDECLRAVLKLMSEcwahNPASRLT 513
Cdd:cd14199 220 Y-----CFVFGqcpFMDERILSLHSKIKTQPlEFPDQPDI---------------SDDLKDLLFRMLDK----NPESRIS 275

                ....*
gi 41349437 514 ALRIK 518
Cdd:cd14199 276 VPEIK 280
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
238-440 1.16e-06

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: 50.02  E-value: 1.16e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 238 RQVGKGRYGEVWM--GKWRGEKVAVK-VFF------TTEEASWFrETEIYQTVLMRHENILGFIAADIKGTGSwtQLYLI 308
Cdd:cd06653   8 KLLGRGAFGEVYLcyDADTGRELAVKqVPFdpdsqeTSKEVNAL-ECEIQLLKNLRHDRIVQYYGCLRDPEEK--KLSIF 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 309 TDYHENGSLYDFLKC-ATLDTRALLKLAYSAACGLCHLHTEIygtqgkpaIAHRDLKSKNILIKKNGSCCIADLGLAVKF 387
Cdd:cd06653  85 VEYMPGGSVKDQLKAyGALTENVTRRYTRQILQGVSYLHSNM--------IVHRDIKGANILRDSAGNVKLGDFGASKRI 156
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 41349437 388 NSDTNEvDVPLNTRVGTKRYMAPEVLD-ESLNKNhfqpyimADIYSFGLIIWEM 440
Cdd:cd06653 157 QTICMS-GTGIKSVTGTPYWMSPEVISgEGYGRK-------ADVWSVACTVVEM 202
TFP_LU_ECD_ALK2 cd23535
extracellular domain (ECD) found in activin receptor-like kinase 2 (ALK-2) and similar ...
59-132 1.21e-06

extracellular domain (ECD) found in activin receptor-like kinase 2 (ALK-2) and similar proteins; ALK-2 (EC 2.7.11.30, also called ACVRLK2, or activin receptor type-1 (ACVR1), or activin receptor type I (ACTR-I), or serine/threonine-protein kinase receptor R1 (SKR1), or TGF-B superfamily receptor type I (TSR-I)) is bone morphogenetic protein (BMP) type I receptor that is involved in a wide variety of biological processes, including bone, heart, cartilage, nervous, and reproductive system development and regulation. As a type I receptor, ALK-2 forms heterotetrameric receptor complexes with the type II receptors AMHR2, ACVR2A, or ACVR2B. Upon binding of ligands such as BMP7 or GDF2/BMP9 to the heteromeric complexes, type II receptors transphosphorylate ACVR1 intracellular domain. In turn, ACVR1 kinase domain is activated and subsequently phosphorylates SMAD1/5/8 proteins that transduce the signal. In addition to its role in mediating BMP pathway-specific signaling, ALK-2 suppresses TGFbeta/activin pathway signaling by interfering with the binding of activin to its type II receptor. Besides canonical SMAD signaling, it can activate non-canonical pathways such as p38 mitogen-activated protein kinases/MAPKs. This model corresponds to the extracellular domain (ECD) of ALK-2, which belongs to Ly-6 antigen/uPA receptor-like (LU) superfamily and exhibits a snake toxin-like fold (also known as three-finger toxin/3FTx fold or three-fingered protein/TFP domain fold).


Pssm-ID: 467065  Cd Length: 71  Bit Score: 46.22  E-value: 1.21e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41349437  59 LKCYCSG-HCPDDainNTCitNGH-CFAIIEEDDQGETtLASGCMK-YEGSDFQCKDSPkaQLRRTIECCRTNLCNQ 132
Cdd:cd23535   1 FECVCEGsSCPGG---DRC--EGQqCFSSLSVEDGGAV-VQKGCLEgEEQGRMTCKTPP--SPDLAVECCSGHLCNA 69
PTKc_VEGFR1 cd14207
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
360-511 1.37e-06

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: 50.39  E-value: 1.37e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 360 HRDLKSKNILIKKNGSCCIADLGLAVKFNSDTNEVdvplntRVGTKR----YMAPE-VLDESLNKNhfqpyimADIYSFG 434
Cdd:cd14207 203 HRDLAARNILLSENNVVKICDFGLARDIYKNPDYV------RKGDARlplkWMAPEsIFDKIYSTK-------SDVWSYG 269
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41349437 435 LIIWEmarrcitggIVEEYQLPYYNMVPSDPSYEDMREVVcvkRLRPivsnrwnSDECLRAVLKLMSECWAHNPASR 511
Cdd:cd14207 270 VLLWE---------IFSLGASPYPGVQIDEDFCSKLKEGI---RMRA-------PEFATSEIYQIMLDCWQGDPNER 327
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
358-459 1.37e-06

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: 50.43  E-value: 1.37e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 358 IAHRDLKSKNILIKKNGSCCIADLGLA---VKFNSDTnevdvplNTRVGTKRYMAPEVLDESlnknhfqPYIMA-DIYSF 433
Cdd:cd05571 116 IVYRDLKLENLLLDKDGHIKITDFGLCkeeISYGATT-------KTFCGTPEYLAPEVLEDN-------DYGRAvDWWGL 181
                        90       100
                ....*....|....*....|....*.
gi 41349437 434 GLIIWEMarrcITGgiveeyQLPYYN 459
Cdd:cd05571 182 GVVMYEM----MCG------RLPFYN 197
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
228-440 1.38e-06

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: 50.77  E-value: 1.38e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 228 RTIAKQIQMVRQVGKGRYGEVWMGKWRGEK--VAVKVFFTTE-----EASWFREteiyqtvlmrHENILGFiaadikGTG 300
Cdd:cd05622  69 RMKAEDYEVVKVIGRGAFGEVQLVRHKSTRkvYAMKLLSKFEmikrsDSAFFWE----------ERDIMAF------ANS 132
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 301 SWT-----------QLYLITDYHENGSLYDFLkcATLDTRALLKLAYSA--ACGLCHLHTEiygtqgkpAIAHRDLKSKN 367
Cdd:cd05622 133 PWVvqlfyafqddrYLYMVMEYMPGGDLVNLM--SNYDVPEKWARFYTAevVLALDAIHSM--------GFIHRDVKPDN 202
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41349437 368 ILIKKNGSCCIADLGLAVKFNSDTNevdVPLNTRVGTKRYMAPEVLDESLNKNHFQPyiMADIYSFGLIIWEM 440
Cdd:cd05622 203 MLLDKSGHLKLADFGTCMKMNKEGM---VRCDTAVGTPDYISPEVLKSQGGDGYYGR--ECDWWSVGVFLYEM 270
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
232-440 1.39e-06

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: 49.91  E-value: 1.39e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 232 KQIQMVRQVGKGRYGEVWmgKWRGEK---VAVKVFFTTEE-----ASWFRETEIYQTvlMRHE-NILGFIAADIkgTGSW 302
Cdd:cd14131   1 KPYEILKQLGKGGSSKVY--KVLNPKkkiYALKRVDLEGAdeqtlQSYKNEIELLKK--LKGSdRIIQLYDYEV--TDED 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 303 TQLYLITDYHEnGSLYDFLK---CATLDtRALLKLAYS---AACGLCHLHteiygtqgkpAIAHRDLKSKNILIKKnGSC 376
Cdd:cd14131  75 DYLYMVMECGE-IDLATILKkkrPKPID-PNFIRYYWKqmlEAVHTIHEE----------GIVHSDLKPANFLLVK-GRL 141
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41349437 377 CIADLGLAVKFNSDTneVDVPLNTRVGTKRYMAPEVLDESLNKNHFQPYIM----ADIYSFGLIIWEM 440
Cdd:cd14131 142 KLIDFGIAKAIQNDT--TSIVRDSQVGTLNYMSPEAIKDTSASGEGKPKSKigrpSDVWSLGCILYQM 207
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
235-515 1.40e-06

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: 50.39  E-value: 1.40e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 235 QMVRQVGKGRYGEVWMGKWR--GEKVAVKVFFTTEEASWF-----RETEIYQtvLMRHENILGFIAADI----KGTGSWT 303
Cdd:cd07866  11 EILGKLGEGTFGEVYKARQIktGRVVALKKILMHNEKDGFpitalREIKILK--KLKHPNVVPLIDMAVerpdKSKRKRG 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 304 QLYLITDYHE---NGSLYD--------FLKCATLDtraLLKlaysaacGLCHLHteiygtqgKPAIAHRDLKSKNILIKK 372
Cdd:cd07866  89 SVYMVTPYMDhdlSGLLENpsvkltesQIKCYMLQ---LLE-------GINYLH--------ENHILHRDIKAANILIDN 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 373 NGSCCIADLGLAVKF--NSDTNEVDVPLNTR-----VGTKRYMAPEVLdesLNKNHFQPYImaDIYSFGLIIWEM-ARRC 444
Cdd:cd07866 151 QGILKIADFGLARPYdgPPPNPKGGGGGGTRkytnlVVTRWYRPPELL---LGERRYTTAV--DIWGIGCVFAEMfTRRP 225
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 445 ITGGIVEEYQLPY-YNMVPSdPSYEDM---------REVVCVKRLRPIVSNRWNSdeCLRAVLKLMSECWAHNPASRLTA 514
Cdd:cd07866 226 ILQGKSDIDQLHLiFKLCGT-PTEETWpgwrslpgcEGVHSFTNYPRTLEERFGK--LGPEGLDLLSKLLSLDPYKRLTA 302

                .
gi 41349437 515 L 515
Cdd:cd07866 303 S 303
PTKc_VEGFR2 cd05103
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; ...
360-440 1.53e-06

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: 50.36  E-value: 1.53e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 360 HRDLKSKNILIKKNGSCCIADLGLAVKFNSDTNEVdvplntRVGTKR----YMAPEVLDESLNKnhfqpyIMADIYSFGL 435
Cdd:cd05103 202 HRDLAARNILLSENNVVKICDFGLARDIYKDPDYV------RKGDARlplkWMAPETIFDRVYT------IQSDVWSFGV 269

                ....*
gi 41349437 436 IIWEM 440
Cdd:cd05103 270 LLWEI 274
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
240-440 1.60e-06

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: 49.94  E-value: 1.60e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 240 VGKGRYGEVWMG--KWRGEKVAVK-----VFFTTEEASWfreTEIYQTVL-MRHENilGFIAADIKGTGSWTQLYLITDY 311
Cdd:cd05620   3 LGKGSFGKVLLAelKGKGEYFAVKalkkdVVLIDDDVEC---TMVEKRVLaLAWEN--PFLTHLYCTFQTKEHLFFVMEF 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 312 HENGSL-YDFLKCATLDTRALLKLAYSAACGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNGSCCIADLGLAVKFNSD 390
Cdd:cd05620  78 LNGGDLmFHIQDKGRFDLYRATFYAAEIVCGLQFLHSK--------GIIYRDLKLDNVMLDRDGHIKIADFGMCKENVFG 149
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 41349437 391 TNEVdvplNTRVGTKRYMAPEVLdeslnkNHFQPYIMADIYSFGLIIWEM 440
Cdd:cd05620 150 DNRA----STFCGTPDYIAPEIL------QGLKYTFSVDWWSFGVLLYEM 189
PTKc_VEGFR3 cd05102
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; ...
360-513 1.72e-06

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: 49.98  E-value: 1.72e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 360 HRDLKSKNILIKKNGSCCIADLGLAVKFNSDTNEVdvplntRVGTKR----YMAPEVLDESLNKNHfqpyimADIYSFGL 435
Cdd:cd05102 195 HRDLAARNILLSENNVVKICDFGLARDIYKDPDYV------RKGSARlplkWMAPESIFDKVYTTQ------SDVWSFGV 262
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41349437 436 IIWEmarrcitggIVEEYQLPYynmvpsdPSYEdMREVVCvKRLRPIVSNRwNSDECLRAVLKLMSECWAHNPASRLT 513
Cdd:cd05102 263 LLWE---------IFSLGASPY-------PGVQ-INEEFC-QRLKDGTRMR-APEYATPEIYRIMLSCWHGDPKERPT 321
STKc_CDC2L6 cd07867
Catalytic domain of Serine/Threonine Kinase, Cell Division Cycle 2-like 6; STKs catalyze the ...
239-440 1.82e-06

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: 50.07  E-value: 1.82e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 239 QVGKGRYGEVWMGKWRGEKVAVKVFFTTEEASWFRETEIYQTVLMR---HENILGFIAADIkgTGSWTQLYLITDY--HE 313
Cdd:cd07867   9 KVGRGTYGHVYKAKRKDGKDEKEYALKQIEGTGISMSACREIALLRelkHPNVIALQKVFL--SHSDRKVWLLFDYaeHD 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 314 NGSLYDFLKCATLDT------RALLK-LAYSAACGLCHLHTEiygtqgkpAIAHRDLKSKNILI----KKNGSCCIADLG 382
Cdd:cd07867  87 LWHIIKFHRASKANKkpmqlpRSMVKsLLYQILDGIHYLHAN--------WVLHRDLKPANILVmgegPERGRVKIADMG 158
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 41349437 383 LAVKFNSDTNEVdVPLNTRVGTKRYMAPEVLdesLNKNHFQPYImaDIYSFGLIIWEM 440
Cdd:cd07867 159 FARLFNSPLKPL-ADLDPVVVTFWYRAPELL---LGARHYTKAI--DIWAIGCIFAEL 210
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
256-440 1.88e-06

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 50.40  E-value: 1.88e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437  256 EKVAVK-VFFTTEEASWFRETEIYQTVLMRHENILGFIAaDIKgtgSWTQLYLITDYHENGSLYDFLKcATLDTRALLK- 333
Cdd:PTZ00267  94 EKVVAKfVMLNDERQAAYARSELHCLAACDHFGIVKHFD-DFK---SDDKLLLIMEYGSGGDLNKQIK-QRLKEHLPFQe 168
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437  334 -----LAYSAACGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNGSCCIADLGLAVKFnSDTNEVDVPlNTRVGTKRYM 408
Cdd:PTZ00267 169 yevglLFYQIVLALDEVHSR--------KMMHRDLKSANIFLMPTGIIKLGDFGFSKQY-SDSVSLDVA-SSFCGTPYYL 238
                        170       180       190
                 ....*....|....*....|....*....|..
gi 41349437  409 APEVLDEslnKNHFQPyimADIYSFGLIIWEM 440
Cdd:PTZ00267 239 APELWER---KRYSKK---ADMWSLGVILYEL 264
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
239-413 2.05e-06

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: 49.68  E-value: 2.05e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 239 QVGKGRYGEVWMGKWR--GEKVAVKVFFTTEEASWFRET---EIYQTVLMRHENILGFIAADIKGTgswtQLYLITDYHE 313
Cdd:cd07847   8 KIGEGSYGVVFKCRNRetGQIVAIKKFVESEDDPVIKKIalrEIRMLKQLKHPNLVNLIEVFRRKR----KLHLVFEYCD 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 314 NGSLYDFLKCAT-LDTRALLKLAYSAACGL--CHLHTEIygtqgkpaiaHRDLKSKNILIKKNGSCCIADLGLAVKFNSD 390
Cdd:cd07847  84 HTVLNELEKNPRgVPEHLIKKIIWQTLQAVnfCHKHNCI----------HRDVKPENILITKQGQIKLCDFGFARILTGP 153
                       170       180
                ....*....|....*....|...
gi 41349437 391 TNEvdvpLNTRVGTKRYMAPEVL 413
Cdd:cd07847 154 GDD----YTDYVATRWYRAPELL 172
PTKc_VEGFR cd05054
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
360-526 2.24e-06

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: 49.41  E-value: 2.24e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 360 HRDLKSKNILIKKNGSCCIADLGLAVKFNSDTNEVdvplntRVGTKR----YMAPEVLDESLNKNHfqpyimADIYSFGL 435
Cdd:cd05054 161 HRDLAARNILLSENNVVKICDFGLARDIYKDPDYV------RKGDARlplkWMAPESIFDKVYTTQ------SDVWSFGV 228
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 436 IIWEmarrCITGGiveeyQLPYYNMVPSDPSYEDMREVVcvkRLRpivSNRWNSDEclraVLKLMSECWAHNPASRltal 515
Cdd:cd05054 229 LLWE----IFSLG-----ASPYPGVQMDEEFCRRLKEGT---RMR---APEYTTPE----IYQIMLDCWHGEPKER---- 285
                       170
                ....*....|.
gi 41349437 516 rikKTLAKMVE 526
Cdd:cd05054 286 ---PTFSELVE 293
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
235-519 2.47e-06

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: 49.00  E-value: 2.47e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 235 QMVRQVGKGRYG--EVWMGKWRGEKVAVKVFFTTEEASWFRETEIYQTVLMRHENILGFIAADIKGTgswtQLYLITDYH 312
Cdd:cd14662   3 ELVKDIGSGNFGvaRLMRNKETKELVAVKYIERGLKIDENVQREIINHRSLRHPNIIRFKEVVLTPT----HLAIVMEYA 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 313 ENGSLYDFLKCATLDTRALLKLAYSA-ACGLCHLHTEiygtqgkpAIAHRDLKSKNILIkkNGSCC----IADLGLavkf 387
Cdd:cd14662  79 AGGELFERICNAGRFSEDEARYFFQQlISGVSYCHSM--------QICHRDLKLENTLL--DGSPAprlkICDFGY---- 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 388 nSDTNEVDVPLNTRVGTKRYMAPEVLD--ESLNKnhfqpyiMADIYSFGLIIWEMarrcitggIVEEYqlPYYNmvPSDP 465
Cdd:cd14662 145 -SKSSVLHSQPKSTVGTPAYIAPEVLSrkEYDGK-------VADVWSCGVTLYVM--------LVGAY--PFED--PDDP 204
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41349437 466 syEDMRevvcvKRLRPIVSNRWN-------SDECLRavlkLMSECWAHNPASRLTALRIKK 519
Cdd:cd14662 205 --KNFR-----KTIQRIMSVQYKipdyvrvSQDCRH----LLSRIFVANPAKRITIPEIKN 254
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
235-438 2.68e-06

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: 49.34  E-value: 2.68e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 235 QMVRQVGKGRYGEV--WMGKWRGEKVAVKVFFTTEEAS-----WFRETEIYQtvLMRHENILGfIAADIKGTGSWtqlYL 307
Cdd:cd14086   4 DLKEELGKGAFSVVrrCVQKSTGQEFAAKIINTKKLSArdhqkLEREARICR--LLKHPNIVR-LHDSISEEGFH---YL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 308 ITDYHENGSLYDflkcaTLDTRALLKLAYSAAC------GLCHLHTEiygtqgkpAIAHRDLKSKNILI---KKNGSCCI 378
Cdd:cd14086  78 VFDLVTGGELFE-----DIVAREFYSEADASHCiqqileSVNHCHQN--------GIVHRDLKPENLLLaskSKGAAVKL 144
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41349437 379 ADLGLAVkfnsdtnEVDVPLNTR---VGTKRYMAPEVLDEslnknhfQPYIMA-DIYSFGLIIW 438
Cdd:cd14086 145 ADFGLAI-------EVQGDQQAWfgfAGTPGYLSPEVLRK-------DPYGKPvDIWACGVILY 194
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
238-440 2.71e-06

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: 49.52  E-value: 2.71e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 238 RQVGKGRYGEVWMGKWR--GEKVAVKVFfttEEASWFRETEIYQTvlMRHENILG------FIAADIKGTGSWTQLYLIT 309
Cdd:cd05590   1 RVLGKGSFGKVMLARLKesGRLYAVKVL---KKDVILQDDDVECT--MTEKRILSlarnhpFLTQLYCCFQTPDRLFFVM 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 310 DYHENGSL-YDFLKCATLDTRALLKLAYSAACGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNGSCCIADLGLAVK-- 386
Cdd:cd05590  76 EFVNGGDLmFHIQKSRRFDEARARFYAAEITSALMFLHDK--------GIIYRDLKLDNVLLDHEGHCKLADFGMCKEgi 147
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 41349437 387 FNSDTNevdvplNTRVGTKRYMAPEVLDESLnknhFQPYImaDIYSFGLIIWEM 440
Cdd:cd05590 148 FNGKTT------STFCGTPDYIAPEILQEML----YGPSV--DWWAMGVLLYEM 189
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
240-436 2.94e-06

Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PSKH1 is an autophosphorylating STK that is expressed ubiquitously and exhibits multiple intracellular localizations including the centrosome, Golgi apparatus, and splice factor compartments. It contains a catalytic kinase domain and an N-terminal SH4-like motif that is acylated to facilitate membrane attachment. PSKH1 plays a rile in the maintenance of the Golgi apparatus, an important organelle within the secretory pathway. It may also function as a novel splice factor and a regulator of prostate cancer cell growth. The PSKH1 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: 270989 [Multi-domain]  Cd Length: 259  Bit Score: 48.68  E-value: 2.94e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 240 VGKGRYGEVWMGKWRGEK--VAVKVFFTTEEASWFRETEIYQTVLMRHENILGFIAAdikgTGSWTQLYLITDYHENGSL 317
Cdd:cd14087   9 IGRGSFSRVVRVEHRVTRqpYAIKMIETKCRGREVCESELNVLRRVRHTNIIQLIEV----FETKERVYMVMELATGGEL 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 318 YDFL----KCATLDTRALLKLAYSaacGLCHLHTeiygtqgkPAIAHRDLKSKNILIKKNGS---CCIADLGLAVKFNSD 390
Cdd:cd14087  85 FDRIiakgSFTERDATRVLQMVLD---GVKYLHG--------LGITHRDLKPENLLYYHPGPdskIMITDFGLASTRKKG 153
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 41349437 391 TNEVdvpLNTRVGTKRYMAPEVLdesLNKnhfqPYIMA-DIYSFGLI 436
Cdd:cd14087 154 PNCL---MKTTCGTPEYIAPEIL---LRK----PYTQSvDMWAVGVI 190
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
227-480 3.00e-06

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: 49.31  E-value: 3.00e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 227 QRTIAKQIQMVRQVGKGRYGEVWM------GKWRGEKVAVK--VFFTTEEASWFRETEIYQTVlmRHEnilgFIAADIKG 298
Cdd:cd05593  10 KRKTMNDFDYLKLLGKGTFGKVILvrekasGKYYAMKILKKevIIAKDEVAHTLTESRVLKNT--RHP----FLTSLKYS 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 299 TGSWTQLYLITDYHENGSLYDFLKCATLDTRALLKLaYSA--ACGLCHLHTeiygtqGKpaIAHRDLKSKNILIKKNGSC 376
Cdd:cd05593  84 FQTKDRLCFVMEYVNGGELFFHLSRERVFSEDRTRF-YGAeiVSALDYLHS------GK--IVYRDLKLENLMLDKDGHI 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 377 CIADLGLAVKFNSDTnevdVPLNTRVGTKRYMAPEVLDEslnkNHFQPYImaDIYSFGLIIWEMarrcITGgiveeyQLP 456
Cdd:cd05593 155 KITDFGLCKEGITDA----ATMKTFCGTPEYLAPEVLED----NDYGRAV--DWWGLGVVMYEM----MCG------RLP 214
                       250       260
                ....*....|....*....|....
gi 41349437 457 YYNMvpsdpSYEDMREVVCVKRLR 480
Cdd:cd05593 215 FYNQ-----DHEKLFELILMEDIK 233
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
281-440 3.19e-06

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: 48.86  E-value: 3.19e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 281 VLMR---HENILGFiaADIKGTGSWtqLYLITDYHENGSLYD-FLKCATLDTRALLKLAYSAACGLCHLHTEiygtqgkp 356
Cdd:cd14177  50 ILMRygqHPNIITL--KDVYDDGRY--VYLVTELMKGGELLDrILRQKFFSEREASAVLYTITKTVDYLHCQ-------- 117
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 357 AIAHRDLKSKNILIKKNG----SCCIADLGLAVKFNSDTNEVDVPLNtrvgTKRYMAPEVLDEslnknhfQPYIMA-DIY 431
Cdd:cd14177 118 GVVHRDLKPSNILYMDDSanadSIRICDFGFAKQLRGENGLLLTPCY----TANFVAPEVLMR-------QGYDAAcDIW 186

                ....*....
gi 41349437 432 SFGLIIWEM 440
Cdd:cd14177 187 SLGVLLYTM 195
PTKc_DDR2 cd05095
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze ...
232-521 3.34e-06

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: 48.84  E-value: 3.34e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 232 KQIQMVRQVGKGRYGEVWMGKWRG-EK-----------------VAVKVFFT----TEEASWFRETEIYQTvlMRHENIL 289
Cdd:cd05095   5 KLLTFKEKLGEGQFGEVHLCEAEGmEKfmdkdfalevsenqpvlVAVKMLRAdankNARNDFLKEIKIMSR--LKDPNII 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 290 GFIAADIKGTgswtQLYLITDYHENGSLYDFL-----KCATLDTRALLKLAYSaacGLCHLHTEIygTQGKPAIA----- 359
Cdd:cd05095  83 RLLAVCITDD----PLCMITEYMENGDLNQFLsrqqpEGQLALPSNALTVSYS---DLRFMAAQI--ASGMKYLSslnfv 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 360 HRDLKSKNILIKKNGSCCIADLGLAVK-FNSDTNEVDvplNTRVGTKRYMAPevldESLNKNHFQpyIMADIYSFGLIIW 438
Cdd:cd05095 154 HRDLATRNCLVGKNYTIKIADFGMSRNlYSGDYYRIQ---GRAVLPIRWMSW----ESILLGKFT--TASDVWAFGVTLW 224
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 439 EMARRCitggiveeYQLPYYNMvpSDPS--------YEDMREVVCVKrlRPIVsnrwnsdeCLRAVLKLMSECWAHNPAS 510
Cdd:cd05095 225 ETLTFC--------REQPYSQL--SDEQvientgefFRDQGRQTYLP--QPAL--------CPDSVYKLMLSCWRRDTKD 284
                       330
                ....*....|.
gi 41349437 511 RLTALRIKKTL 521
Cdd:cd05095 285 RPSFQEIHTLL 295
PK_NRBP1_like cd13984
Pseudokinase domain of Nuclear Receptor Binding Protein 1 and similar proteins; The ...
285-441 3.98e-06

Pseudokinase domain of Nuclear Receptor Binding Protein 1 and similar proteins; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. This subfamily is composed of NRBP1, also called MLF1-adaptor molecule (MADM), and MADML. NRBP1 was originally named based on the presence of nuclear binding and localization motifs prior to functional analyses. It is expressed ubiquitously and is found to localize in the cytoplasm, not the nucleus. NRBP1 is an adaptor protein that interacts with myeloid leukemia factor 1 (MLF1), an oncogene that enhances myeloid development of hematopoietic cells. It also interacts with the small GTPase Rac3. NRBP1 may also be involved in Golgi to ER trafficking. MADML (for MADM-Like) has been shown to be expressed throughout development in Xenopus laevis with highest expression found in the developing lens and retina. The NRBP1-like 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: 270886 [Multi-domain]  Cd Length: 256  Bit Score: 48.30  E-value: 3.98e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 285 HENILGF--IAADIKGTGswTQLYLITDYHENGSLYDFLK-----CATLDTRALLKLAYSAACGLCHLHTeiygtqGKPA 357
Cdd:cd13984  54 HPNIVKFhrYWTDVQEEK--ARVIFITEYMSSGSLKQFLKktkknHKTMNEKSWKRWCTQILSALSYLHS------CDPP 125
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 358 IAHRDLKSKNILIKKNGSCCIAdlglAVKFNSDTNEVDVPLNTRvGTKRYMAPEVLDeslnKNHFQPYImaDIYSFGLII 437
Cdd:cd13984 126 IIHGNLTCDTIFIQHNGLIKIG----SVAPDAIHNHVKTCREEH-RNLHFFAPEYGY----LEDVTTAV--DIYSFGMCA 194

                ....
gi 41349437 438 WEMA 441
Cdd:cd13984 195 LEMA 198
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
235-440 4.01e-06

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: 48.45  E-value: 4.01e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 235 QMVRQVGKGRYGEV--WMGKWRGEKVAVKVFFTTEEASWF------RETEIYQTvlMRHENILGFIAADIKGTGswtQLY 306
Cdd:cd14163   3 QLGKTIGEGTYSKVkeAFSKKHQRKVAIKIIDKSGGPEEFiqrflpRELQIVER--LDHKNIIHVYEMLESADG---KIY 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 307 LITDYHENGSLYDFL---------KCATLDTRALLKLAYSAACGlchlhteiygtqgkpaIAHRDLKSKNILIkKNGSCC 377
Cdd:cd14163  78 LVMELAEDGDVFDCVlhggplpehRAKALFRQLVEAIRYCHGCG----------------VAHRDLKCENALL-QGFTLK 140
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41349437 378 IADLGLAVKFNSDTNEVDvplNTRVGTKRYMAPEVLDESLNKNHfqpyiMADIYSFGLIIWEM 440
Cdd:cd14163 141 LTDFGFAKQLPKGGRELS---QTFCGSTAYAAPEVLQGVPHDSR-----KGDIWSMGVVLYVM 195
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
358-457 4.12e-06

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 49.41  E-value: 4.12e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437  358 IAHRDLKSKNILIKKNGSCCIADLGLAVKFNS----DTNEVdvplntrVGTKRYMAPE-----VLDESlnknhfqpyimA 428
Cdd:NF033483 128 IVHRDIKPQNILITKDGRVKVTDFGIARALSSttmtQTNSV-------LGTVHYLSPEqarggTVDAR-----------S 189
                         90       100
                 ....*....|....*....|....*....
gi 41349437  429 DIYSFGLIIWEMarrcITGgiveeyQLPY 457
Cdd:NF033483 190 DIYSLGIVLYEM----LTG------RPPF 208
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
336-440 4.14e-06

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: 48.84  E-value: 4.14e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 336 YSAAC---GLCHLHteiygtqgKPAIAHRDLKSKNILIKKNGSCCIADLGL---AVKFNSDTnevdvplNTRVGTKRYMA 409
Cdd:cd05589 105 FYAACvvlGLQFLH--------EHKIVYRDLKLDNLLLDTEGYVKIADFGLckeGMGFGDRT-------STFCGTPEFLA 169
                        90       100       110
                ....*....|....*....|....*....|..
gi 41349437 410 PEVLDESlnknhfqPYIMA-DIYSFGLIIWEM 440
Cdd:cd05589 170 PEVLTDT-------SYTRAvDWWGLGVLIYEM 194
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
333-517 4.23e-06

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: 48.42  E-value: 4.23e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 333 KLAYSAACGLCHLHteiygtqgKPAIAHRDLKSKNILI-----KKNGSCCIADLGLAVK-FNSDTNEVDvplntrvGTKR 406
Cdd:cd14067 118 KIAYQIAAGLAYLH--------KKNIIFCDLKSDNILVwsldvQEHINIKLSDYGISRQsFHEGALGVE-------GTPG 182
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 407 YMAPEVldeslnknhfQPYIM----ADIYSFGLIIWEM--ARRCITGgiveEYQLPYYNMVPsdpsyedmrevvcvKRLR 480
Cdd:cd14067 183 YQAPEI----------RPRIVydekVDMFSYGMVLYELlsGQRPSLG----HHQLQIAKKLS--------------KGIR 234
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 41349437 481 PIVSNrwNSDECLRAVLKLMSECWAHNPASRLTALRI 517
Cdd:cd14067 235 PVLGQ--PEEVQFFRLQALMMECWDTKPEKRPLACSV 269
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
227-480 4.26e-06

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: 48.87  E-value: 4.26e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 227 QRTIAKQIQMVRQVGKGRYGEVWMGKWR--GEKVAVKVF------FTTEEASWFRETEIYQTvlMRHEnilgFIAADIKG 298
Cdd:cd05594  20 HKVTMNDFEYLKLLGKGTFGKVILVKEKatGRYYAMKILkkevivAKDEVAHTLTENRVLQN--SRHP----FLTALKYS 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 299 TGSWTQLYLITDYHENGSLYDFLKCATLDTRALLKLaYSA--ACGLCHLHTEiygtqgkPAIAHRDLKSKNILIKKNGSC 376
Cdd:cd05594  94 FQTHDRLCFVMEYANGGELFFHLSRERVFSEDRARF-YGAeiVSALDYLHSE-------KNVVYRDLKLENLMLDKDGHI 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 377 CIADLGLAVKFNSDtnevDVPLNTRVGTKRYMAPEVLDEslnkNHFQPYImaDIYSFGLIIWEMarrcITGgiveeyQLP 456
Cdd:cd05594 166 KITDFGLCKEGIKD----GATMKTFCGTPEYLAPEVLED----NDYGRAV--DWWGLGVVMYEM----MCG------RLP 225
                       250       260
                ....*....|....*....|....
gi 41349437 457 YYNMvpsdpSYEDMREVVCVKRLR 480
Cdd:cd05594 226 FYNQ-----DHEKLFELILMEEIR 244
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
304-440 4.59e-06

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: 48.84  E-value: 4.59e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 304 QLYLITDYHENGSL-YDFLKCATLDTRALLKLAYSAACGLCHLHteiygtqgKPAIAHRDLKSKNILIKKNGSCCIADLG 382
Cdd:cd05615  85 RLYFVMEYVNGGDLmYHIQQVGKFKEPQAVFYAAEISVGLFFLH--------KKGIIYRDLKLDNVMLDSEGHIKIADFG 156
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 41349437 383 LAVKFNSDtnevDVPLNTRVGTKRYMAPEVLdeslnknHFQPYIMA-DIYSFGLIIWEM 440
Cdd:cd05615 157 MCKEHMVE----GVTTRTFCGTPDYIAPEII-------AYQPYGRSvDWWAYGVLLYEM 204
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
336-440 4.91e-06

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: 48.54  E-value: 4.91e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 336 YSA--ACGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNGSCCIADLGLAVKFNSDtnevDVPLNTRVGTKRYMAPEVL 413
Cdd:cd05587 102 YAAeiAVGLFFLHSK--------GIIYRDLKLDNVMLDAEGHIKIADFGMCKEGIFG----GKTTRTFCGTPDYIAPEII 169
                        90       100
                ....*....|....*....|....*...
gi 41349437 414 deslnknHFQPY-IMADIYSFGLIIWEM 440
Cdd:cd05587 170 -------AYQPYgKSVDWWAYGVLLYEM 190
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
239-468 5.23e-06

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: 48.46  E-value: 5.23e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 239 QVGKGRYGEVWMGKWR--GEKVAVK-VFFTTEEA---SWFRETEIYQTvlMRHENILGFiaADIKGTGSwtQLYLITDYH 312
Cdd:cd07873   9 KLGEGTYATVYKGRSKltDNLVALKeIRLEHEEGapcTAIREVSLLKD--LKHANIVTL--HDIIHTEK--SLTLVFEYL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 313 ENgSLYDFLK-CATLDTRALLKL-AYSAACGLCHLHteiygtqgKPAIAHRDLKSKNILIKKNGSCCIADLGLAVKFNSD 390
Cdd:cd07873  83 DK-DLKQYLDdCGNSINMHNVKLfLFQLLRGLAYCH--------RRKVLHRDLKPQNLLINERGELKLADFGLARAKSIP 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 391 TNEVDvplnTRVGTKRYMAPEVLdesLNKNHFQPYImaDIYSFGLIIWEMA--RRCITGGIVEEyQLPYYNMVPSDPSYE 468
Cdd:cd07873 154 TKTYS----NEVVTLWYRPPDIL---LGSTDYSTQI--DMWGVGCIFYEMStgRPLFPGSTVEE-QLHFIFRILGTPTEE 223
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
235-440 6.09e-06

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: 48.04  E-value: 6.09e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 235 QMVRQVGKGRYGEVWMGKWR--GEKVAVK----VFFTTEEASWFRETEiyqtvLMR----HENILGFIAA--DIKgTGSw 302
Cdd:cd07831   2 KILGKIGEGTFSEVLKAQSRktGKYYAIKcmkkHFKSLEQVNNLREIQ-----ALRrlspHPNILRLIEVlfDRK-TGR- 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 303 tqLYLITDYHEnGSLYDFLKCAT--LDTRALLKLAYSAACGLCHLHteiygtqgKPAIAHRDLKSKNILIKKN------- 373
Cdd:cd07831  75 --LALVFELMD-MNLYELIKGRKrpLPEKRVKNYMYQLLKSLDHMH--------RNGIFHRDIKPENILIKDDilkladf 143
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41349437 374 GSCCiadlGLAVKfnsdtnevdVPLNTRVGTKRYMAPEVLdesLNKNHFQPYImaDIYSFGLIIWEM 440
Cdd:cd07831 144 GSCR----GIYSK---------PPYTEYISTRWYRAPECL---LTDGYYGPKM--DIWAVGCVFFEI 192
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
240-440 6.11e-06

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: 48.26  E-value: 6.11e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 240 VGKGRYGEVWMGKWRG--EKVAVKVFfttEEASWFRETEIYQTvlMRHENILG------FIAADIKGTGSWTQLYLITDY 311
Cdd:cd05591   3 LGKGSFGKVMLAERKGtdEVYAIKVL---KKDVILQDDDVDCT--MTEKRILAlaakhpFLTALHSCFQTKDRLFFVMEY 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 312 HENGSL-YDFLKCATLDTRALLKLAYSAACGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNGSCCIADLGLAVKFNSD 390
Cdd:cd05591  78 VNGGDLmFQIQRARKFDEPRARFYAAEVTLALMFLHRH--------GVIYRDLKLDNILLDAEGHCKLADFGMCKEGILN 149
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 41349437 391 tnevDVPLNTRVGTKRYMAPEVLDEslnknhfQPY-IMADIYSFGLIIWEM 440
Cdd:cd05591 150 ----GKTTTTFCGTPDYIAPEILQE-------LEYgPSVDWWALGVLMYEM 189
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
274-440 6.44e-06

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: 48.01  E-value: 6.44e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 274 ETEIyqtvLMR---HENILGFIAADIKGTgswtQLYLITDYHENGSLYDFL---KCAT-LDTRALLKLAYSAacgLCHLH 346
Cdd:cd14091  43 EIEI----LLRygqHPNIITLRDVYDDGN----SVYLVTELLRGGELLDRIlrqKFFSeREASAVMKTLTKT---VEYLH 111
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 347 TeiygtQGkpaIAHRDLKSKNILIKKNG----SCCIADLGLAVKFNSDtNEVdvpLNTRVGTKRYMAPEVLDEslnknhf 422
Cdd:cd14091 112 S-----QG---VVHRDLKPSNILYADESgdpeSLRICDFGFAKQLRAE-NGL---LMTPCYTANFVAPEVLKK------- 172
                       170
                ....*....|....*....
gi 41349437 423 QPYIMA-DIYSFGLIIWEM 440
Cdd:cd14091 173 QGYDAAcDIWSLGVLLYTM 191
PHA02988 PHA02988
hypothetical protein; Provisional
251-460 6.61e-06

hypothetical protein; Provisional


Pssm-ID: 165291 [Multi-domain]  Cd Length: 283  Bit Score: 47.81  E-value: 6.61e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437  251 GKWRGEKVAVKVF--FTTEEASWFR--ETEIYQTVLMRHENILGFIAADIKGTGSWTQLYLITDYHENGSLYDFL-KCAT 325
Cdd:PHA02988  39 GIFNNKEVIIRTFkkFHKGHKVLIDitENEIKNLRRIDSNNILKIYGFIIDIVDDLPRLSLILEYCTRGYLREVLdKEKD 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437  326 LDTRALLKLAYSAACGLCHLHTEIygtqGKPaiaHRDLKSKNILIKKNGSCCIADLGLavkfnsdTNEVDVPLNTRVGTK 405
Cdd:PHA02988 119 LSFKTKLDMAIDCCKGLYNLYKYT----NKP---YKNLTSVSFLVTENYKLKIICHGL-------EKILSSPPFKNVNFM 184
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 41349437  406 RYMAPEVLdeslnKNHFQPY-IMADIYSFGLIIWEMARRCItggiveeyqlPYYNM 460
Cdd:PHA02988 185 VYFSYKML-----NDIFSEYtIKDDIYSLGVVLWEIFTGKI----------PFENL 225
PTKc_HER2 cd05109
Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the ...
233-440 6.65e-06

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: 48.10  E-value: 6.65e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 233 QIQMVRQVGKGRYGEVWMGKW--RGEK----VAVKVFftTEEASWFRETEIYQTVLMRhENILGFIAADIKGTGSWTQLY 306
Cdd:cd05109   8 ELKKVKVLGSGAFGTVYKGIWipDGENvkipVAIKVL--RENTSPKANKEILDEAYVM-AGVGSPYVCRLLGICLTSTVQ 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 307 LITDYHENGSLYDFLK--CATLDTRALLKLAYSAACGLCHLHteiygtqgKPAIAHRDLKSKNILIKKNGSCCIADLGLA 384
Cdd:cd05109  85 LVTQLMPYGCLLDYVRenKDRIGSQDLLNWCVQIAKGMSYLE--------EVRLVHRDLAARNVLVKSPNHVKITDFGLA 156
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41349437 385 VKFNSDTNEV-----DVPLntrvgtkRYMAPevldESLNKNHFQPyiMADIYSFGLIIWEM 440
Cdd:cd05109 157 RLLDIDETEYhadggKVPI-------KWMAL----ESILHRRFTH--QSDVWSYGVTVWEL 204
STKc_CDK8 cd07868
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 8; STKs ...
239-440 9.33e-06

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: 47.75  E-value: 9.33e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 239 QVGKGRYGEVWMGKWRGEKVAVKVFFTTEEASWFRETEIYQTVLMR---HENILGFIAADIKGTGSwtQLYLITDY--HE 313
Cdd:cd07868  24 KVGRGTYGHVYKAKRKDGKDDKDYALKQIEGTGISMSACREIALLRelkHPNVISLQKVFLSHADR--KVWLLFDYaeHD 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 314 NGSLYDFLKCATLDT------RALLK-LAYSAACGLCHLHTEiygtqgkpAIAHRDLKSKNILI----KKNGSCCIADLG 382
Cdd:cd07868 102 LWHIIKFHRASKANKkpvqlpRGMVKsLLYQILDGIHYLHAN--------WVLHRDLKPANILVmgegPERGRVKIADMG 173
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 41349437 383 LAVKFNSDTNEVdVPLNTRVGTKRYMAPEVLdesLNKNHFQPYImaDIYSFGLIIWEM 440
Cdd:cd07868 174 FARLFNSPLKPL-ADLDPVVVTFWYRAPELL---LGARHYTKAI--DIWAIGCIFAEL 225
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
232-400 9.48e-06

Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like kinase (also called greatwall kinase); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MASTL kinases in this group carry only a catalytic domain, which contains a long insertion relative to MAST kinases. MASTL, also called greatwall kinase (Gwl), is involved in the regulation of mitotic entry, which is controlled by the coordinated activities of protein kinases and opposing protein phosphatases (PPs). The cyclin B/CDK1 complex induces entry into M-phase while PP2A-B55 shows anti-mitotic activity. MASTL/Gwl is activated downstream of cyclin B/CDK1 and indirectly inhibits PP2A-B55 by phosphorylating the small protein alpha-endosulfine (Ensa) or the cAMP-regulated phosphoprotein 19 (Arpp19), resulting in M-phase progression. Gwl kinase may also play roles in mRNA stabilization and DNA checkpoint recovery. The human MASTL gene has also been named FLJ14813; a missense mutation in FLJ14813 is associated with autosomal dominant thrombocytopenia. The MASTL 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: 270761 [Multi-domain]  Cd Length: 349  Bit Score: 47.95  E-value: 9.48e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 232 KQIQMVRQVGKGRYGEVWMG--KWRGEKVAVKVfftTEEASWFRETEIYQTVLMRHENILG---FIAADIKGTGSWTQLY 306
Cdd:cd05610   4 EEFVIVKPISRGAFGKVYLGrkKNNSKLYAVKV---VKKADMINKNMVHQVQAERDALALSkspFIVHLYYSLQSANNVY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 307 LITDYHENGSLYDFLKC-ATLDTRALLKLAYSAACGLCHLHteiygtqgKPAIAHRDLKSKNILIKKNGSCCIADLGLA- 384
Cdd:cd05610  81 LVMEYLIGGDVKSLLHIyGYFDEEMAVKYISEVALALDYLH--------RHGIIHRDLKPDNMLISNEGHIKLTDFGLSk 152
                       170
                ....*....|....*.
gi 41349437 385 VKFNSDTNEVDVpLNT 400
Cdd:cd05610 153 VTLNRELNMMDI-LTT 167
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
358-441 9.89e-06

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 48.07  E-value: 9.89e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437  358 IAHRDLKSKNILIKKNGSCCIADLGLAVKfnsdtnEVDVPLNTR---VGTKRYMAPEVLDESlnknhfqPYIMA-DIYSF 433
Cdd:PHA03212 203 IIHRDIKAENIFINHPGDVCLGDFGAACF------PVDINANKYygwAGTIATNAPELLARD-------PYGPAvDIWSA 269

                 ....*...
gi 41349437  434 GLIIWEMA 441
Cdd:PHA03212 270 GIVLFEMA 277
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
341-513 1.03e-05

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: 47.23  E-value: 1.03e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 341 GLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNGSCCIADLGLAVKFNSdtneVDVPLNTRVGTKRYMAPEVLdesLNKN 420
Cdd:cd14189 113 GLKYLHLK--------GILHRDLKLGNFFINENMELKVGDFGLAARLEP----PEQRKKTICGTPNYLAPEVL---LRQG 177
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 421 HFQPyimADIYSFGLIIwemarrcitggiveeyqlpyYNMVPSDPSYE--DMREVV-CVKRLRPIVSNRWNSdeclrAVL 497
Cdd:cd14189 178 HGPE---SDVWSLGCVM--------------------YTLLCGNPPFEtlDLKETYrCIKQVKYTLPASLSL-----PAR 229
                       170
                ....*....|....*.
gi 41349437 498 KLMSECWAHNPASRLT 513
Cdd:cd14189 230 HLLAGILKRNPGDRLT 245
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
281-519 1.08e-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: 47.33  E-value: 1.08e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 281 VLMR---HENILGFiaADIKGTGSwtQLYLITDYHENGSLYD-FLKCATLDTRALLKLAYSAACGLCHLHTeiygtQGkp 356
Cdd:cd14175  47 ILLRygqHPNIITL--KDVYDDGK--HVYLVTELMRGGELLDkILRQKFFSEREASSVLHTICKTVEYLHS-----QG-- 115
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 357 aIAHRDLKSKNIL-IKKNG---SCCIADLGLAVKFNSDTNEVDVPLNtrvgTKRYMAPEVLDEslnknhfQPYIMA-DIY 431
Cdd:cd14175 116 -VVHRDLKPSNILyVDESGnpeSLRICDFGFAKQLRAENGLLMTPCY----TANFVAPEVLKR-------QGYDEGcDIW 183
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 432 SFGLIIWEMARRCItggiveeyqlPYYNMvPSDPSYEDMREVVCVKrlRPIVSNRWNSdecLRAVLK-LMSECWAHNPAS 510
Cdd:cd14175 184 SLGILLYTMLAGYT----------PFANG-PSDTPEEILTRIGSGK--FTLSGGNWNT---VSDAAKdLVSKMLHVDPHQ 247

                ....*....
gi 41349437 511 RLTALRIKK 519
Cdd:cd14175 248 RLTAKQVLQ 256
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
240-447 1.11e-05

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: 47.57  E-value: 1.11e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 240 VGKGRYGEVwMGKWRGEKVAVKVFFTTEEASWFRETEIY-----QTVLMRHENilGFIAADIKGTGSWTQLYLITDYHEN 314
Cdd:cd05585   2 IGKGSFGKV-MQVRKKDTSRIYALKTIRKAHIVSRSEVThtlaeRTVLAQVDC--PFIVPLKFSFQSPEKLYLVLAFING 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 315 GSLYDFL-KCATLD-TRALLklaYSAA--CGLCHLHteiygtqgKPAIAHRDLKSKNILIKKNGSCCIADLGLAvKFN-S 389
Cdd:cd05585  79 GELFHHLqREGRFDlSRARF---YTAEllCALECLH--------KFNVIYRDLKPENILLDYTGHIALCDFGLC-KLNmK 146
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 41349437 390 DTNEVdvplNTRVGTKRYMAPEVLDEslnknhfQPYIMA-DIYSFGLIIWEMarrcITG 447
Cdd:cd05585 147 DDDKT----NTFCGTPEYLAPELLLG-------HGYTKAvDWWTLGVLLYEM----LTG 190
PK_GC-2D cd14043
Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-2D; The pseudokinase domain ...
283-517 1.30e-05

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: 47.02  E-value: 1.30e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 283 MRHENI---LG-FIAADIKGtgswtqlyLITDYHENGSLYDFLKCA--TLDTRALLKLAYSAACGLCHLHTeiygtqgkP 356
Cdd:cd14043  53 LRHENVnlfLGlFVDCGILA--------IVSEHCSRGSLEDLLRNDdmKLDWMFKSSLLLDLIKGMRYLHH--------R 116
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 357 AIAHRDLKSKNILIKKNGSCCIADLGLAVKFNSDTnevdVPLNTRVGTKRY-MAPEVL-DESLNKNHFQPyimADIYSFG 434
Cdd:cd14043 117 GIVHGRLKSRNCVVDGRFVLKITDYGYNEILEAQN----LPLPEPAPEELLwTAPELLrDPRLERRGTFP---GDVFSFA 189
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 435 LIIWEMARRCitggiveeyqLPYYNMvpSDPSYEDMREV-----VCvkrlRPIVSnrwnSDECLRAVLKLMSECWAHNPA 509
Cdd:cd14043 190 IIMQEVIVRG----------APYCML--GLSPEEIIEKVrspppLC----RPSVS----MDQAPLECIQLMKQCWSEAPE 249

                ....*...
gi 41349437 510 SRLTALRI 517
Cdd:cd14043 250 RRPTFDQI 257
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
239-436 1.40e-05

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: 46.81  E-value: 1.40e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 239 QVGKGRYGEVWMGKWRGEK--VAVKVF----FTTEEAswFRETEIYQTVLMRHENILGFiaADIKGTGswTQLYLITDYH 312
Cdd:cd14169  10 KLGEGAFSEVVLAQERGSQrlVALKCIpkkaLRGKEA--MVENEIAVLRRINHENIVSL--EDIYESP--THLYLAMELV 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 313 ENGSLYD-FLKCATLDTRALLKLAYSAACGLCHLHteiygtqgKPAIAHRDLKSKNILIK---KNGSCCIADLGLAvKFn 388
Cdd:cd14169  84 TGGELFDrIIERGSYTEKDASQLIGQVLQAVKYLH--------QLGIVHRDLKPENLLYAtpfEDSKIMISDFGLS-KI- 153
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 41349437 389 sdtnEVDVPLNTRVGTKRYMAPEVLDEslnknhfQPYIMA-DIYSFGLI 436
Cdd:cd14169 154 ----EAQGMLSTACGTPGYVAPELLEQ-------KPYGKAvDVWAIGVI 191
PHA03211 PHA03211
serine/threonine kinase US3; Provisional
256-441 1.44e-05

serine/threonine kinase US3; Provisional


Pssm-ID: 223009 [Multi-domain]  Cd Length: 461  Bit Score: 47.58  E-value: 1.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437  256 EKVAVKvfftteeASWFRETeIYQTVLMR---HENILGFIaaDIKGTGSWTQLYLiTDYHENgsLYDFL--KCATLDTRA 330
Cdd:PHA03211 195 QRVVVK-------AGWYASS-VHEARLLRrlsHPAVLALL--DVRVVGGLTCLVL-PKYRSD--LYTYLgaRLRPLGLAQ 261
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437  331 LLKLAYSAACGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNGSCCIADLGLAVkFNSDTNEVDVPLNTrVGTKRYMAP 410
Cdd:PHA03211 262 VTAVARQLLSAIDYIHGE--------GIIHRDIKTENVLVNGPEDICLGDFGAAC-FARGSWSTPFHYGI-AGTVDTNAP 331
                        170       180       190
                 ....*....|....*....|....*....|..
gi 41349437  411 EVLDESlnknhfqPYIMA-DIYSFGLIIWEMA 441
Cdd:PHA03211 332 EVLAGD-------PYTPSvDIWSAGLVIFEAA 356
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
237-440 1.48e-05

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: 46.88  E-value: 1.48e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 237 VRQVGKGRYGEVWMGKWR--GEKVAVKVF-FTTEEASWFreTEIYQTVLMR---HENILgfIAADIKGTGSwtQLYLITD 310
Cdd:cd07870   5 LEKLGEGSYATVYKGISRinGQLVALKVIsMKTEEGVPF--TAIREASLLKglkHANIV--LLHDIIHTKE--TLTFVFE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 311 Y-HENGSLYDFLKCATLDTRALLKLAYSAACGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNGSCCIADLGLAvkfns 389
Cdd:cd07870  79 YmHTDLAQYMIQHPGGLHPYNVRLFMFQLLRGLAYIHGQ--------HILHRDLKPQNLLISYLGELKLADFGLA----- 145
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 41349437 390 dtNEVDVPLNT---RVGTKRYMAPEVLdesLNKNHFQPYImaDIYSFGLIIWEM 440
Cdd:cd07870 146 --RAKSIPSQTyssEVVTLWYRPPDVL---LGATDYSSAL--DIWGAGCIFIEM 192
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
240-440 1.49e-05

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: 46.58  E-value: 1.49e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 240 VGKGRYGEVWM--GKWRGEKVAVK-VFF------TTEEASWFrETEIYQTVLMRHENILGFIAAdIKGTGSWTqLYLITD 310
Cdd:cd06652  10 LGQGAFGRVYLcyDADTGRELAVKqVQFdpespeTSKEVNAL-ECEIQLLKNLLHERIVQYYGC-LRDPQERT-LSIFME 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 311 YHENGSLYDFLKC-ATLDTRALLKLAYSAACGLCHLHTEIygtqgkpaIAHRDLKSKNILIKKNGSCCIADLGLAVKFN- 388
Cdd:cd06652  87 YMPGGSIKDQLKSyGALTENVTRKYTRQILEGVHYLHSNM--------IVHRDIKGANILRDSVGNVKLGDFGASKRLQt 158
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 41349437 389 ---SDTNEVDVplntrVGTKRYMAPEVLD-ESLNKNhfqpyimADIYSFGLIIWEM 440
Cdd:cd06652 159 iclSGTGMKSV-----TGTPYWMSPEVISgEGYGRK-------ADIWSVGCTVVEM 202
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
237-413 1.51e-05

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: 46.45  E-value: 1.51e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 237 VRQVGKGRYGEVWMG---------KWRGEKVAVK-VFFTTEEASWFRETEIYQtVLMRHENILGFIAADIKGTgswtQLY 306
Cdd:cd14019   6 IEKIGEGTFSSVYKAedklhdlydRNKGRLVALKhIYPTSSPSRILNELECLE-RLGGSNNVSGLITAFRNED----QVV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 307 LITDYHENGSLYDFLKCATL-DTRALLKLAYSAacgLCHLHteiygtqgKPAIAHRDLKSKNILI-KKNGSCCIADLGLA 384
Cdd:cd14019  81 AVLPYIEHDDFRDFYRKMSLtDIRIYLRNLFKA---LKHVH--------SFGIIHRDVKPGNFLYnRETGKGVLVDFGLA 149
                       170       180
                ....*....|....*....|....*....
gi 41349437 385 VKFnSDTNEVDVPlntRVGTKRYMAPEVL 413
Cdd:cd14019 150 QRE-EDRPEQRAP---RAGTRGFRAPEVL 174
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
231-440 2.10e-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: 46.92  E-value: 2.10e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 231 AKQIQMVRQVGKGRYGEVWMGKWRG-EKV-AVKVFFTTE-----EASWFREteiyqtvlmrHENILGFiaadikGTGSWT 303
Cdd:cd05621  51 AEDYDVVKVIGRGAFGEVQLVRHKAsQKVyAMKLLSKFEmikrsDSAFFWE----------ERDIMAF------ANSPWV 114
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 304 -----------QLYLITDYHENGSLYDFLkcATLDTRALLKLAYSA--ACGLCHLHTEiygtqgkpAIAHRDLKSKNILI 370
Cdd:cd05621 115 vqlfcafqddkYLYMVMEYMPGGDLVNLM--SNYDVPEKWAKFYTAevVLALDAIHSM--------GLIHRDVKPDNMLL 184
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 371 KKNGSCCIADLGLAVKFNSDTNevdVPLNTRVGTKRYMAPEVLDESLNKNHFQPyiMADIYSFGLIIWEM 440
Cdd:cd05621 185 DKYGHLKLADFGTCMKMDETGM---VHCDTAVGTPDYISPEVLKSQGGDGYYGR--ECDWWSVGVFLFEM 249
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
255-477 2.13e-05

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated protein kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK-activated protein kinase 5 (MAPKAP5 or MK5) is also called PRAK (p38-regulated/activated protein kinase). It contains 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. 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: 271073 [Multi-domain]  Cd Length: 289  Bit Score: 46.30  E-value: 2.13e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 255 GEKVAVKVFFTTEEAswfrETEIYQTVLMR-HENILGFI---AADIKGTG---SWTQLYLITDYHENGSLYDFL-KCATL 326
Cdd:cd14171  31 GERFALKILLDRPKA----RTEVRLHMMCSgHPNIVQIYdvyANSVQFPGessPRARLLIVMELMEGGELFDRIsQHRHF 106
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 327 DTRALLKLAYSAACGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNG---SCCIADLGLAVKFNSDtnevdvpLNTRVG 403
Cdd:cd14171 107 TEKQAAQYTKQIALAVQHCHSL--------NIAHRDLKPENLLLKDNSedaPIKLCDFGFAKVDQGD-------LMTPQF 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 404 TKRYMAPEVLDESLNKN--------HFQPYIM---ADIYSFGLIIW--------------------EMARRCITGgiveE 452
Cdd:cd14171 172 TPYYVAPQVLEAQRRHRkersgiptSPTPYTYdksCDMWSLGVIIYimlcgyppfysehpsrtitkDMKRKIMTG----S 247
                       250       260
                ....*....|....*....|....*..
gi 41349437 453 YQLPY--YNMVpSDPSYEDMREVVCVK 477
Cdd:cd14171 248 YEFPEeeWSQI-SEMAKDIVRKLLCVD 273
PK_MADML cd14035
Pseudokinase domain of MLF1-ADaptor Molecule-Like; The pseudokinase domain shows similarity to ...
261-441 2.29e-05

Pseudokinase domain of MLF1-ADaptor Molecule-Like; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. MADML has been shown to be expressed throughout development in Xenopus laevis with highest expression found in the developing lens and retina. It may play an important role in embryonic eye development. The MADML 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: 270937 [Multi-domain]  Cd Length: 263  Bit Score: 46.07  E-value: 2.29e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 261 KVFFTTEEASwfrETEIYQTVLMRHENILGFIAADIKGTGSWTQLYLITDYHENGSLYDFLKCATLDTRALLKLAYSAAC 340
Cdd:cd14035  33 KAFKAHEDKI---KTMFENLTLVDHPNIVKFHKYWLDVKDNHARVVFITEYVSSGSLKQFLKKTKKNHKTMNARAWKRWC 109
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 341 -----GLCHLHTeiygtqGKPAIAHRDLKSKNILIKKNGSCCIAdlglAVKFNSDTNEVDVP-LNTRVGTKRymapevlD 414
Cdd:cd14035 110 tqilsALSYLHS------CEPPIIHGNLTSDTIFIQHNGLIKIG----SVWHRLFVNVLPEGgVRGPLRQER-------E 172
                       170       180       190
                ....*....|....*....|....*....|....
gi 41349437 415 ESLNKNHFQPY-------IMADIYSFGLIIWEMA 441
Cdd:cd14035 173 ELRNLHFFPPEygscedgTAVDIFSFGMCALEMA 206
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
241-441 2.32e-05

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: 46.22  E-value: 2.32e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 241 GKGRYGEVWMGKWR--GEKVAVKVF-FTTEEASWF---RETEIYQTvlMRHENILgfIAADIKGTGSWTQL---YLITD- 310
Cdd:cd07844   9 GEGSYATVYKGRSKltGQLVALKEIrLEHEEGAPFtaiREASLLKD--LKHANIV--TLHDIIHTKKTLTLvfeYLDTDl 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 311 --YHEN-GSLYDfLKCATLDTRALLK-LAYsaacglCHlhteiygtqgKPAIAHRDLKSKNILIKKNGSCCIADLGLAvK 386
Cdd:cd07844  85 kqYMDDcGGGLS-MHNVRLFLFQLLRgLAY------CH----------QRRVLHRDLKPQNLLISERGELKLADFGLA-R 146
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 41349437 387 FNSdtnevdVPLNT---RVGTKRYMAPEVLdesLNKNHFQPYImaDIYSFGLIIWEMA 441
Cdd:cd07844 147 AKS------VPSKTysnEVVTLWYRPPDVL---LGSTEYSTSL--DMWGVGCIFYEMA 193
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
358-440 2.55e-05

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: 46.08  E-value: 2.55e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 358 IAHRDLKSKNILIKKNGSCCIADLGLAVKFNSDTNevdvPLNTRVGTKRYMAPEVLDEslnKNH-FQpyimADIYSFGLI 436
Cdd:cd14187 128 VIHRDLKLGNLFLNDDMEVKIGDFGLATKVEYDGE----RKKTLCGTPNYIAPEVLSK---KGHsFE----VDIWSIGCI 196

                ....
gi 41349437 437 IWEM 440
Cdd:cd14187 197 MYTL 200
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
360-440 2.73e-05

Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NDR kinases regulate mitosis, cell growth, embryonic development, and neurological processes. They are also required for proper centrosome duplication. Higher eukaryotes contain two NDR isoforms, NDR1 and NDR2. This subfamily also contains fungal NDR-like kinases. NDR kinase contains an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Like many other AGC kinases, NDR kinase requires phosphorylation at two sites, the activation loop (A-loop) and the hydrophobic motif (HM), for activity. The NDR 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: 270750 [Multi-domain]  Cd Length: 324  Bit Score: 46.45  E-value: 2.73e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 360 HRDLKSKNILIKKNGSCCIADLGLAVKFnsdtnEVDVPLNTRVGTKRYMAPEVLDESlnknhfqPYIM-ADIYSFGLIIW 438
Cdd:cd05599 124 HRDIKPDNLLLDARGHIKLSDFGLCTGL-----KKSHLAYSTVGTPDYIAPEVFLQK-------GYGKeCDWWSLGVIMY 191

                ..
gi 41349437 439 EM 440
Cdd:cd05599 192 EM 193
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
358-441 2.86e-05

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: 46.02  E-value: 2.86e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 358 IAHRDLKSKNILIKKNGSCCIADLGLAvkfnsdTNEVDVPLNTRVGTKRYMAPE-VLDEslnknhfQPYIMADIYSFGLI 436
Cdd:cd06619 116 ILHRDVKPSNMLVNTRGQVKLCDFGVS------TQLVNSIAKTYVGTNAYMAPErISGE-------QYGIHSDVWSLGIS 182

                ....*
gi 41349437 437 IWEMA 441
Cdd:cd06619 183 FMELA 187
PK_STRAD cd08216
Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows ...
258-462 3.19e-05

Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. STRAD forms a complex with the scaffolding protein MO25, and the serine/threonine kinase (STK), LKB1, resulting in the activation of the kinase. In the complex, LKB1 phosphorylates and activates adenosine monophosphate-activated protein kinases (AMPKs), which regulate cell energy metabolism and cell polarity. LKB1 is a tumor suppressor linked to the rare inherited disease, Peutz-Jeghers syndrome, which is characterized by a predisposition to benign polyps and hyperpigmentation of the buccal mucosa. There are two forms of STRAD, alpha and beta, that complex with LKB1 and MO25. The structure of STRAD-alpha is available and shows that this protein binds ATP, has an ordered activation loop, and adopts a closed conformation typical of fully active protein kinases. It does not possess activity due to nonconservative substitutions of essential catalytic residues. ATP binding enhances the affinity of STRAD for MO25. The conformation of STRAD-alpha stabilized through ATP and MO25 may be needed to activate LKB1. The STRAD 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: 270856 [Multi-domain]  Cd Length: 315  Bit Score: 46.13  E-value: 3.19e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 258 VAVKVFF----TTEEASWFREtEIYQTVLMRHENILGFIAADIKGTgswtQLYLITDYHENGSLYDFLK---CATLDTRA 330
Cdd:cd08216  28 VAVKKINlesdSKEDLKFLQQ-EILTSRQLQHPNILPYVTSFVVDN----DLYVVTPLMAYGSCRDLLKthfPEGLPELA 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 331 LLKLAYSAACGLCHLHTEIYgtqgkpaiAHRDLKSKNILIKKNGSCCIADLGLAVKFNSDTNEV----DVPLNTrVGTKR 406
Cdd:cd08216 103 IAFILRDVLNALEYIHSKGY--------IHRSVKASHILISGDGKVVLSGLRYAYSMVKHGKRQrvvhDFPKSS-EKNLP 173
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 41349437 407 YMAPEVLDESLnknhfQPY-IMADIYSFGLIIWEMArrcitGGIVeeyqlPYYNMVP 462
Cdd:cd08216 174 WLSPEVLQQNL-----LGYnEKSDIYSVGITACELA-----NGVV-----PFSDMPA 215
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
233-408 3.23e-05

Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK1 phosphorylates a variety of substrates including enzymes, transcription and splice factors, cytoskeletal proteins, viral oncogenes, receptors, and membrane-associated proteins. There are mutliple isoforms of CK1 and in mammals, seven isoforms (alpha, beta, gamma1-3, delta, and epsilon) have been characterized. These isoforms differ mainly in the length and structure of their C-terminal non-catalytic region. Some isoforms have several splice variants such as the long (L) and short (S) variants of CK1alpha. CK1 proteins are involved in the regulation of many cellular processes including membrane transport processes, circadian rhythm, cell division, apoptosis, and the development of cancer and neurodegenerative diseases. The CK1 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: 270918 [Multi-domain]  Cd Length: 266  Bit Score: 45.53  E-value: 3.23e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 233 QIQMVRQVGKGRYGEVWMGK--WRGEKVAVKVFFTTEEAS-WFRETEIYQTVlmrhENILGFiaADIKGTGSW-TQLYLI 308
Cdd:cd14016   1 RYKLVKKIGSGSFGEVYLGIdlKTGEEVAIKIEKKDSKHPqLEYEAKVYKLL----QGGPGI--PRLYWFGQEgDYNVMV 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 309 TDYHenG-SLYD-FLKC-ATLDTRALLKLAYSAACGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNGSC---CIADLG 382
Cdd:cd14016  75 MDLL--GpSLEDlFNKCgRKFSLKTVLMLADQMISRLEYLHSK--------GYIHRDIKPENFLMGLGKNSnkvYLIDFG 144
                       170       180       190
                ....*....|....*....|....*....|
gi 41349437 383 LAVKF-NSDTNEvDVPLNTR---VGTKRYM 408
Cdd:cd14016 145 LAKKYrDPRTGK-HIPYREGkslTGTARYA 173
PTKc_DDR1 cd05096
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 1; PTKs catalyze ...
305-511 3.52e-05

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: 45.70  E-value: 3.52e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 305 LYLITDYHENGSLYDFLKCATLDTRA------------LLKLAYSAacgLCHLHTEIygTQGKPAIA-----HRDLKSKN 367
Cdd:cd05096  94 LCMITEYMENGDLNQFLSSHHLDDKEengndavppahcLPAISYSS---LLHVALQI--ASGMKYLSslnfvHRDLATRN 168
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 368 ILIKKNGSCCIADLGLAVK-FNSDTNEVDvplNTRVGTKRYMAPEVLdeslnknhfqpyIM------ADIYSFGLIIWEM 440
Cdd:cd05096 169 CLVGENLTIKIADFGMSRNlYAGDYYRIQ---GRAVLPIRWMAWECI------------LMgkfttaSDVWAFGVTLWEI 233
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41349437 441 ARRCitggiveeYQLPYYNMVPSD------PSYEDMREVVCVKRLRPivsnrwnsdeCLRAVLKLMSECWAHNPASR 511
Cdd:cd05096 234 LMLC--------KEQPYGELTDEQvienagEFFRDQGRQVYLFRPPP----------CPQGLYELMLQCWSRDCRER 292
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
358-440 3.67e-05

C-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: 270994 [Multi-domain]  Cd Length: 311  Bit Score: 45.75  E-value: 3.67e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 358 IAHRDLKSKNIL---IKKNGSCCIADLGLA-VKFNSdtnevdVPLNTRVGTKRYMAPEVLDESLNKNHFQPyiMADIYSF 433
Cdd:cd14092 120 VVHRDLKPENLLftdEDDDAEIKIVDFGFArLKPEN------QPLKTPCFTLPYAAPEVLKQALSTQGYDE--SCDLWSL 191

                ....*..
gi 41349437 434 GLIIWEM 440
Cdd:cd14092 192 GVILYTM 198
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
281-519 3.68e-05

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: 45.78  E-value: 3.68e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 281 VLMR---HENILGFiaADIKGTGSWtqLYLITDYHENGSLYD-FLKCATLDTRALLKLAYSAACGLCHLHTEiygtqgkp 356
Cdd:cd14176  65 ILLRygqHPNIITL--KDVYDDGKY--VYVVTELMKGGELLDkILRQKFFSEREASAVLFTITKTVEYLHAQ-------- 132
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 357 AIAHRDLKSKNIL-IKKNG---SCCIADLGLAVKFNSDTNEVDVPLNtrvgTKRYMAPEVLDEslnknhfQPYIMA-DIY 431
Cdd:cd14176 133 GVVHRDLKPSNILyVDESGnpeSIRICDFGFAKQLRAENGLLMTPCY----TANFVAPEVLER-------QGYDAAcDIW 201
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 432 SFGLIIWEMarrcITGgiveeyQLPYYNMvPSDPSYEDMREVVCVKrlRPIVSNRWNSdeCLRAVLKLMSECWAHNPASR 511
Cdd:cd14176 202 SLGVLLYTM----LTG------YTPFANG-PDDTPEEILARIGSGK--FSLSGGYWNS--VSDTAKDLVSKMLHVDPHQR 266

                ....*...
gi 41349437 512 LTALRIKK 519
Cdd:cd14176 267 LTAALVLR 274
PK_STRAD_alpha cd08227
Pseudokinase domain of STE20-related kinase adapter protein alpha; The pseudokinase domain ...
255-441 3.98e-05

Pseudokinase domain of STE20-related kinase adapter protein alpha; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. The structure of STRAD-alpha is available and shows that this protein binds ATP, has an ordered activation loop, and adopts a closed conformation typical of fully active protein kinases. It does not possess activity due to nonconservative substitutions of essential catalytic residues. ATP binding enhances the affinity of STRAD for MO25. The conformation of STRAD-alpha, stabilized through ATP and MO25, may be needed to activate LKB1. A mutation which results in a truncation of a C-terminal part of the human STRAD-alpha pseudokinase domain and disrupts its association with LKB1, leads to PMSE (polyhydramnios, megalencephaly, symptomatic epilepsy) syndrome. Several splice variants of STRAD-alpha exist which exhibit different effects on the localization and activation of LKB1. STRAD forms a complex with the scaffolding protein MO25, and the serine/threonine kinase (STK), LKB1, resulting in the activation of the kinase. In the complex, LKB1 phosphorylates and activates adenosine monophosphate-activated protein kinases (AMPKs), which regulate cell energy metabolism and cell polarity. The STRAD alpha 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: 173767 [Multi-domain]  Cd Length: 327  Bit Score: 45.70  E-value: 3.98e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 255 GEKVAVK---VFFTTEEASWFRETEIYQTVLMRHENILGFIAADIKGTgswtQLYLITDYHENGSLYDFLKCATLDTRAL 331
Cdd:cd08227  25 GEYVTVRrinLEACTNEMVTFLQGELHVSKLFNHPNIVPYRATFIADN----ELWVVTSFMAYGSAKDLICTHFMDGMSE 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 332 LKLAY---SAACGLCHLHTEIYgtqgkpaiAHRDLKSKNILIKKNGSCCIADLGLAVKFNSDTNEV----DVPLNTrVGT 404
Cdd:cd08227 101 LAIAYilqGVLKALDYIHHMGY--------VHRSVKASHILISVDGKVYLSGLRSNLSMINHGQRLrvvhDFPKYS-VKV 171
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 41349437 405 KRYMAPEVLDESLnknhfQPY-IMADIYSFGLIIWEMA 441
Cdd:cd08227 172 LPWLSPEVLQQNL-----QGYdAKSDIYSVGITACELA 204
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
237-452 4.43e-05

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: 45.75  E-value: 4.43e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 237 VRQVGKGRYGEVWMG--KWRGEKVAVK-VFFTTEEA---SWFRETEIYQTvlMRHENILGFiaADIKGTGSwtQLYLITD 310
Cdd:cd07872  11 LEKLGEGTYATVFKGrsKLTENLVALKeIRLEHEEGapcTAIREVSLLKD--LKHANIVTL--HDIVHTDK--SLTLVFE 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 311 YHENGSLYDFLKCATLDTRALLKL-AYSAACGLCHLHteiygtqgKPAIAHRDLKSKNILIKKNGSCCIADLGLAvkfns 389
Cdd:cd07872  85 YLDKDLKQYMDDCGNIMSMHNVKIfLYQILRGLAYCH--------RRKVLHRDLKPQNLLINERGELKLADFGLA----- 151
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41349437 390 dtNEVDVPLNT---RVGTKRYMAPEVLdesLNKNHFQPYImaDIYSFGLIIWEMA--RRCITGGIVEE 452
Cdd:cd07872 152 --RAKSVPTKTysnEVVTLWYRPPDVL---LGSSEYSTQI--DMWGVGCIFFEMAsgRPLFPGSTVED 212
PK_NRBP1 cd14034
Pseudokinase domain of Nuclear Receptor Binding Protein 1; The pseudokinase domain shows ...
281-447 4.66e-05

Pseudokinase domain of Nuclear Receptor Binding Protein 1; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. NRBP1, also called MLF1-adaptor molecule (MADM), was originally named based on the presence of nuclear binding and localization motifs prior to functional analyses. It is expressed ubiquitously and is found to localize in the cytoplasm, not the nucleus. NRBP1 is an adaptor protein that interacts with myeloid leukemia factor 1 (MLF1), an oncogene that enhances myeloid development of hematopoietic cells. It also interacts with the small GTPase Rac3. NRBP1 may also be involved in Golgi to ER trafficking and actin dynamics. The NRBP1-like 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: 270936 [Multi-domain]  Cd Length: 277  Bit Score: 45.51  E-value: 4.66e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 281 VLMRHENILGF--IAADIKGTGSwtQLYLITDYHENGSLYDFLKCATLDTRALLKLAYSAAC-----GLCHLHTeiygtq 353
Cdd:cd14034  65 IQLEHLNIVKFhkYWADVKENRA--RVIFITEYMSSGSLKQFLKKTKKNHKTMNEKAWKRWCtqilsALSYLHS------ 136
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 354 GKPAIAHRDLKSKNILIKKNGSCCIADLGlavkfnSDTnevdvpLNTRVGTKRymapevlDESLNKNHFQP--------Y 425
Cdd:cd14034 137 CDPPIIHGNLTCDTIFIQHNGLIKIGSVA------PDT------INNHVKTCR-------EEQKNLHFFAPeygevanvT 197
                       170       180
                ....*....|....*....|..
gi 41349437 426 IMADIYSFGLIIWEMARRCITG 447
Cdd:cd14034 198 TAVDIYSFGMCALEMAVLEIQG 219
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
231-440 5.09e-05

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: 45.45  E-value: 5.09e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 231 AKQIQMVRQVGKGRYGEVWMGKWR--GEKVAVKVFFTTEEA----SWFRETEIYQTvlMRHENILgfIAADIKGTGSwtQ 304
Cdd:cd07869   4 ADSYEKLEKLGEGSYATVYKGKSKvnGKLVALKVIRLQEEEgtpfTAIREASLLKG--LKHANIV--LLHDIIHTKE--T 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 305 LYLITDY-HENGSLYDFLKCATLDTRALLKLAYSAACGLCHLHTEIygtqgkpaIAHRDLKSKNILIKKNGSCCIADLGL 383
Cdd:cd07869  78 LTLVFEYvHTDLCQYMDKHPGGLHPENVKLFLFQLLRGLSYIHQRY--------ILHRDLKPQNLLISDTGELKLADFGL 149
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 384 AvkfnsdtNEVDVPLNT---RVGTKRYMAPEVLdesLNKNHFQPYImaDIYSFGLIIWEM 440
Cdd:cd07869 150 A-------RAKSVPSHTysnEVVTLWYRPPDVL---LGSTEYSTCL--DMWGVGCIFVEM 197
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
305-440 5.26e-05

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: 45.00  E-value: 5.26e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 305 LYLITDYHENGSLYDFLKCATL----DTRALLKLAYSaacGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNGSCCIAD 380
Cdd:cd14188  76 IYILLEYCSRRSMAHILKARKVltepEVRYYLRQIVS---GLKYLHEQ--------EILHRDLKLGNFFINENMELKVGD 144
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41349437 381 LGLAVKFNsdtnevdvPLNTR----VGTKRYMAPEVLDESLNKNHfqpyimADIYSFGLIIWEM 440
Cdd:cd14188 145 FGLAARLE--------PLEHRrrtiCGTPNYLSPEVLNKQGHGCE------SDIWALGCVMYTM 194
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
358-438 5.37e-05

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: 44.97  E-value: 5.37e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 358 IAHRDLKSKNILIKKNGSCCI---ADLGLAVKFNSdtnevDVPLNTRVGTKRYMAPEVLD-ESLNKNhfqpyimADIYSF 433
Cdd:cd14089 121 IAHRDLKPENLLYSSKGPNAIlklTDFGFAKETTT-----KKSLQTPCYTPYYVAPEVLGpEKYDKS-------CDMWSL 188

                ....*
gi 41349437 434 GLIIW 438
Cdd:cd14089 189 GVIMY 193
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
240-440 6.12e-05

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: 45.07  E-value: 6.12e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 240 VGKGRYGEVWM------GKwrgEKVAVKVFF------TTEEASWFrETEIYQTVLMRHENILGFIAAdIKGTGSWTqLYL 307
Cdd:cd06651  15 LGQGAFGRVYLcydvdtGR---ELAAKQVQFdpespeTSKEVSAL-ECEIQLLKNLQHERIVQYYGC-LRDRAEKT-LTI 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 308 ITDYHENGSLYDFLKC-ATLDTRALLKLAYSAACGLCHLHTEIygtqgkpaIAHRDLKSKNILIKKNGSCCIADLGLAVK 386
Cdd:cd06651  89 FMEYMPGGSVKDQLKAyGALTESVTRKYTRQILEGMSYLHSNM--------IVHRDIKGANILRDSAGNVKLGDFGASKR 160
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 41349437 387 FNSDTNEvDVPLNTRVGTKRYMAPEVLD-ESLNKNhfqpyimADIYSFGLIIWEM 440
Cdd:cd06651 161 LQTICMS-GTGIRSVTGTPYWMSPEVISgEGYGRK-------ADVWSLGCTVVEM 207
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
341-438 6.98e-05

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: 44.53  E-value: 6.98e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 341 GLCHLHteiygtqgKPAIAHRDLKSKNIL---IKKNGSCCIADLGLAVKFNSDTNevdvpLNTRVGTKRYMAPEVLDesl 417
Cdd:cd14198 122 GVYYLH--------QNNIVHLDLKPQNILlssIYPLGDIKIVDFGMSRKIGHACE-----LREIMGTPEYLAPEILN--- 185
                        90       100
                ....*....|....*....|..
gi 41349437 418 nknhFQPYIMA-DIYSFGLIIW 438
Cdd:cd14198 186 ----YDPITTAtDMWNIGVIAY 203
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
273-438 7.16e-05

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: 44.56  E-value: 7.16e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 273 RETEIYQTVLmrHENILGFiaADIKGTGswTQLYLITDYHENGSLYDFL-KCATLDTRALLKLAYSAACGLCHLHTEiyg 351
Cdd:cd14196  57 REVSILRQVL--HPNIITL--HDVYENR--TDVVLILELVSGGELFDFLaQKESLSEEEATSFIKQILDGVNYLHTK--- 127
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 352 tqgkpAIAHRDLKSKNI-LIKKNGSCC---IADLGLAVKFnsdtnEVDVPLNTRVGTKRYMAPEVLDeslnknhFQPY-I 426
Cdd:cd14196 128 -----KIAHFDLKPENImLLDKNIPIPhikLIDFGLAHEI-----EDGVEFKNIFGTPEFVAPEIVN-------YEPLgL 190
                       170
                ....*....|..
gi 41349437 427 MADIYSFGLIIW 438
Cdd:cd14196 191 EADMWSIGVITY 202
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
344-452 7.42e-05

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: 44.70  E-value: 7.42e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 344 HLHTeiYGtqgkpaIAHRDLKSKNILIKKNGSCCIADLGLAvK---FNSDTN------EVDVPL---NTRVGTKRYMAPE 411
Cdd:cd05609 115 YLHS--YG------IVHRDLKPDNLLITSMGHIKLTDFGLS-KiglMSLTTNlyeghiEKDTREfldKQVCGTPEYIAPE 185
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 41349437 412 VLdesLNKNHFQPyimADIYSFGLIIWEMARRCIT--GGIVEE 452
Cdd:cd05609 186 VI---LRQGYGKP---VDWWAMGIILYEFLVGCVPffGDTPEE 222
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
239-412 7.63e-05

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: 44.42  E-value: 7.63e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 239 QVGKGRYGEVWMG-------KWRGEKVAVKVFFTTEEASWF-----RETEIYQTVlmrhenilgfiaadikGTGSWTQLY 306
Cdd:cd13991  13 RIGRGSFGEVHRMedkqtgfQCAVKKVRLEVFRAEELMACAgltspRVVPLYGAV----------------REGPWVNIF 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 307 LitDYHENGSLYDFLK---CATLDtRALLKLAySAACGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNGS-CCIADLG 382
Cdd:cd13991  77 M--DLKEGGSLGQLIKeqgCLPED-RALHYLG-QALEGLEYLHSR--------KILHGDVKADNVLLSSDGSdAFLCDFG 144
                       170       180       190
                ....*....|....*....|....*....|.
gi 41349437 383 LAVKFNSDTNEVDVPLNTRV-GTKRYMAPEV 412
Cdd:cd13991 145 HAECLDPDGLGKSLFTGDYIpGTETHMAPEV 175
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
230-438 1.07e-04

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: 44.27  E-value: 1.07e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 230 IAKQIQMVRQVGKGRYGEVWMGKWR--GEKVAVKVF----FTTEEASWfrETEIYQTVLMRHENILGFiaADIkgTGSWT 303
Cdd:cd14168   8 IKKIFEFKEVLGTGAFSEVVLAEERatGKLFAVKCIpkkaLKGKESSI--ENEIAVLRKIKHENIVAL--EDI--YESPN 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 304 QLYLITDYHENGSLYDFL--------KCATLDTRALLKLAYsaacglcHLHTEiygtqgkpAIAHRDLKSKNILI---KK 372
Cdd:cd14168  82 HLYLVMQLVSGGELFDRIvekgfyteKDASTLIRQVLDAVY-------YLHRM--------GIVHRDLKPENLLYfsqDE 146
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41349437 373 NGSCCIADLGLAVKfnSDTNEVdvpLNTRVGTKRYMAPEVLDEslnknhfQPYIMA-DIYSFGLIIW 438
Cdd:cd14168 147 ESKIMISDFGLSKM--EGKGDV---MSTACGTPGYVAPEVLAQ-------KPYSKAvDCWSIGVIAY 201
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
255-440 1.24e-04

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: 44.38  E-value: 1.24e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 255 GEKVAVKVFFTTEEASW---FRETEIYQTvlMRHENILGFIaaDIKGTGSWTQLYLITDYHENGSLYDFLKCATLDTRAL 331
Cdd:cd07854  30 DKRVAVKKIVLTDPQSVkhaLREIKIIRR--LDHDNIVKVY--EVLGPSGSDLTEDVGSLTELNSVYIVQEYMETDLANV 105
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 332 LK-----------LAYSAACGLCHLHTeiygtqgkPAIAHRDLKSKNILIKKNGSCC-IADLGLAVKFNSDTNEVDVpLN 399
Cdd:cd07854 106 LEqgplseeharlFMYQLLRGLKYIHS--------ANVLHRDLKPANVFINTEDLVLkIGDFGLARIVDPHYSHKGY-LS 176
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 41349437 400 TRVGTKRYMAPEVLdesLNKNHFQPYImaDIYSFGLIIWEM 440
Cdd:cd07854 177 EGLVTKWYRSPRLL---LSPNNYTKAI--DMWAAGCIFAEM 212
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
358-445 1.30e-04

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: 43.69  E-value: 1.30e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 358 IAHRDLKSKNILIKKNG-SCCIADLGLAvKFNSDTNEVDvplNTRVGTKRYMAPEVLDESlnknhfqPY--IMADIYSFG 434
Cdd:cd14164 121 IVHRDLKCENILLSADDrKIKIADFGFA-RFVEDYPELS---TTFCGSRAYTPPEVILGT-------PYdpKKYDVWSLG 189
                        90
                ....*....|.
gi 41349437 435 LIIWEMARRCI 445
Cdd:cd14164 190 VVLYVMVTGTM 200
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
305-456 1.63e-04

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: 43.31  E-value: 1.63e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 305 LYLITDYHENGSLYDFLK-----CATLDTRALLKlaySAACGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNGSCCIA 379
Cdd:cd14186  76 VYLVLEMCHNGEMSRYLKnrkkpFTEDEARHFMH---QIVTGMLYLHSH--------GILHRDLTLSNLLLTRNMNIKIA 144
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 380 DLGLAVKFNSdTNEVDVplnTRVGTKRYMAPEVLDESlnkNHFQPyimADIYSFGLIIW-----------EMARRCITGG 448
Cdd:cd14186 145 DFGLATQLKM-PHEKHF---TMCGTPNYISPEIATRS---AHGLE---SDVWSLGCMFYtllvgrppfdtDTVKNTLNKV 214

                ....*...
gi 41349437 449 IVEEYQLP 456
Cdd:cd14186 215 VLADYEMP 222
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
358-440 1.96e-04

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: 43.27  E-value: 1.96e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 358 IAHRDLKSKNILIKKNGSCCIADLGLAVKFNSDTNEvdvPLNTRVGTKRYMAPEVLDESLNKNhfqpyiMADIYSFGLII 437
Cdd:cd14111 120 VLHLDIKPDNIMVTNLNAIKIVDFGSAQSFNPLSLR---QLGRRTGTLEYMAPEMVKGEPVGP------PADIWSIGVLT 190

                ...
gi 41349437 438 WEM 440
Cdd:cd14111 191 YIM 193
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
281-440 2.32e-04

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: 43.08  E-value: 2.32e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 281 VLMR---HENILGFiaADIKGTGSWtqLYLITDYHENGSLYDflkcatldtRALLKLAYS---AACGLCHLH--TEIYGT 352
Cdd:cd14178  49 ILLRygqHPNIITL--KDVYDDGKF--VYLVMELMRGGELLD---------RILRQKCFSereASAVLCTITktVEYLHS 115
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 353 QGkpaIAHRDLKSKNIL-IKKNG---SCCIADLGLAVKFNSDTNEVDVPLNtrvgTKRYMAPEVLDEslnknhfQPYIMA 428
Cdd:cd14178 116 QG---VVHRDLKPSNILyMDESGnpeSIRICDFGFAKQLRAENGLLMTPCY----TANFVAPEVLKR-------QGYDAA 181
                       170
                ....*....|...
gi 41349437 429 -DIYSFGLIIWEM 440
Cdd:cd14178 182 cDIWSLGILLYTM 194
TFP_LU_ECD_ALK4 cd23536
extracellular domain (ECD) found in activin receptor-like kinase 4 (ALK-4) and similar ...
59-131 2.99e-04

extracellular domain (ECD) found in activin receptor-like kinase 4 (ALK-4) and similar proteins; ALK-4 (EC 2.7.11.30, also called ACVRLK4, or activin receptor type-1B (ACVR1B), or activin receptor type IB (ACTR-IB), or serine/threonine-protein kinase receptor R2 (SKR2)) is the transmembrane serine/threonine kinase activin type-1 receptor forming an activin receptor complex with activin receptor type-2 (ACVR2A or ACVR2B). It transduces the activin signal from the cell surface to the cytoplasm and is thus regulating many physiological and pathological processes including neuronal differentiation and neuronal survival, hair follicle development and cycling, FSH production by the pituitary gland, wound healing, extracellular matrix production, immunosuppression, and carcinogenesis. This model corresponds to the extracellular domain (ECD) of ALK-4, which belongs to Ly-6 antigen/uPA receptor-like (LU) superfamily and exhibits a snake toxin-like fold (also known as three-finger toxin/3FTx fold or three-fingered protein/TFP domain fold).


Pssm-ID: 467066  Cd Length: 77  Bit Score: 39.28  E-value: 2.99e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41349437  59 LKCYCSgHCPDdaiNNTCITNGHCFAIIEEDDQGETTLASGCMKYE-----GSDFQCKDSPKAQLRRTIECCR-TNLCN 131
Cdd:cd23536   3 LKCVCS-DCTN---NGTCETDGYCLVSITIDKDGEIKIRRTCIDKDklfppGRPFFCLSSEDLLHNSNVHCCNdEDFCN 77
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
273-438 3.34e-04

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; 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. DAPK2 is also called DAPK-related protein 1 (DRP-1), while DAPK3 has also been named DAP-like kinase (DLK) and zipper-interacting protein kinase (ZIPk). These proteins are ubiquitously expressed in adult tissues, are capable of cross talk with each other, and may act synergistically in regulating cell death. The DAPK 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: 271007 [Multi-domain]  Cd Length: 269  Bit Score: 42.47  E-value: 3.34e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 273 RETEIYQTVlmRHENILGFiaADIkgTGSWTQLYLITDYHENGSLYDFL---KCATL-DTRALLKLAYSaacGLCHLHTE 348
Cdd:cd14105  57 REVSILRQV--LHPNIITL--HDV--FENKTDVVLILELVAGGELFDFLaekESLSEeEATEFLKQILD---GVNYLHTK 127
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 349 iygtqgkpAIAHRDLKSKNI-LIKKN---GSCCIADLGLAVKFnsdtnEVDVPLNTRVGTKRYMAPEVLDeslnknhFQP 424
Cdd:cd14105 128 --------NIAHFDLKPENImLLDKNvpiPRIKLIDFGLAHKI-----EDGNEFKNIFGTPEFVAPEIVN-------YEP 187
                       170
                ....*....|....*
gi 41349437 425 Y-IMADIYSFGLIIW 438
Cdd:cd14105 188 LgLEADMWSIGVITY 202
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
303-440 4.57e-04

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: 42.23  E-value: 4.57e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 303 TQLYLITDYHENGSLYDflKCAT--------LDTRALLKLAYSaacGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKN- 373
Cdd:cd14197  82 SEMILVLEYAAGGEIFN--QCVAdreeafkeKDVKRLMKQILE---GVSFLHNN--------NVVHLDLKPQNILLTSEs 148
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41349437 374 --GSCCIADLGLA--VKFNSDTNEVdvplntrVGTKRYMAPEVLDeslnknhFQPYIMA-DIYSFGLIIWEM 440
Cdd:cd14197 149 plGDIKIVDFGLSriLKNSEELREI-------MGTPEYVAPEILS-------YEPISTAtDMWSIGVLAYVM 206
TFP cd00117
three-fingered protein (TFP) fold found in Ly6/uPAR (LU) and snake toxin superfamily; The LU ...
59-131 4.74e-04

three-fingered protein (TFP) fold found in Ly6/uPAR (LU) and snake toxin superfamily; The LU (also known as Ly-6 antigen/uPA receptor)-like extracellular domain (ECD) occurs singly in GPI-linked cell-surface glycoproteins (Ly-6 family, CD59, thymocyte B cell antigen, Sgp-2) or as three-fold repeated domain in urokinase-type plasminogen activator receptor. It is a structural domain involved in protein-protein interactions, tolerating an unusual degree of variation and binding with high specificity to a broad spectrum of targets. The snake toxin domain is present in short and long neurotoxins, cytotoxins, and short toxins, and in other miscellaneous venom peptides. The toxin acts by binding to the nicotinic acetylcholine receptors in the postsynaptic membrane of skeletal muscles and preventing the binding of acetylcholine, thereby blocking the excitation of muscles. Both the LU-like ECD and the snake toxin domain belong to three-fingered protein (TFP) fold, which is characterized by containing 70 to 100 amino acids including eight to ten cysteine residues spaced at conserved distances.


Pssm-ID: 467060  Cd Length: 81  Bit Score: 39.01  E-value: 4.74e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437  59 LKCY------CSGHCPDDAINNTCITNG-HCFAIIEEDDQGETTLASGCMKY-EGSDFQCKDSPKAQLRRTIECCRTNLC 130
Cdd:cd00117   1 LKCYqcnssnDPNCCNSSPTLVTCSSPEtFCRKIVGKVGGGETLVIRGCATEcECGCTECCSGTGTSGTTCTSCCDTDLC 80

                .
gi 41349437 131 N 131
Cdd:cd00117  81 N 81
PHA03207 PHA03207
serine/threonine kinase US3; Provisional
233-446 5.03e-04

serine/threonine kinase US3; Provisional


Pssm-ID: 165473 [Multi-domain]  Cd Length: 392  Bit Score: 42.52  E-value: 5.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437  233 QIQMVRQVGKGRYGEVWMGKWRGE----KVAVKVffTTEEASWFRETEIYQTvlMRHENILGFIAAdikgtGSWTQLYLI 308
Cdd:PHA03207  93 QYNILSSLTPGSEGEVFVCTKHGDeqrkKVIVKA--VTGGKTPGREIDILKT--ISHRAIINLIHA-----YRWKSTVCM 163
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437  309 TDYHENGSLYDF--------LKCATLDTRALLKlaysaacGLCHLHteiygtqGKpAIAHRDLKSKNILIKKNGSCCIAD 380
Cdd:PHA03207 164 VMPKYKCDLFTYvdrsgplpLEQAITIQRRLLE-------ALAYLH-------GR-GIIHRDVKTENIFLDEPENAVLGD 228
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41349437  381 LGLAVKFnsdTNEVDVPLNTR-VGTKRYMAPEVLdeslnknHFQPYIM-ADIYSFGLIIWEMARRCIT 446
Cdd:PHA03207 229 FGAACKL---DAHPDTPQCYGwSGTLETNSPELL-------ALDPYCAkTDIWSAGLVLFEMSVKNVT 286
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
303-438 5.85e-04

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: 41.93  E-value: 5.85e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 303 TQLYLITDYHENGSLYDFL-KCATLDTRALLKLAYSAACGLCHLHTEiygtqgkpAIAHRDLKSKNI-LIKKNG---SCC 377
Cdd:cd14194  81 TDVILILELVAGGELFDFLaEKESLTEEEATEFLKQILNGVYYLHSL--------QIAHFDLKPENImLLDRNVpkpRIK 152
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41349437 378 IADLGLAVKFNSDTNEVDVplntrVGTKRYMAPEVLDeslnknhFQPY-IMADIYSFGLIIW 438
Cdd:cd14194 153 IIDFGLAHKIDFGNEFKNI-----FGTPEFVAPEIVN-------YEPLgLEADMWSIGVITY 202
KIND smart00750
kinase non-catalytic C-lobe domain; It is an interaction domain identified as being similar to ...
315-529 6.27e-04

kinase non-catalytic C-lobe domain; It is an interaction domain identified as being similar to the C-terminal protein kinase catalytic fold (C lobe). Its presence at the N terminus of signalling proteins and the absence of the active-site residues in the catalytic and activation loops suggest that it folds independently and is likely to be non-catalytic. The occurrence of KIND only in metazoa implies that it has evolved from the catalytic protein kinase domain into an interaction domain possibly by keeping the substrate-binding features


Pssm-ID: 214801  Cd Length: 176  Bit Score: 40.85  E-value: 6.27e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437    315 GSLYDFLKC--ATLDTRALLKLAYSAACGLCHLHteiygtqgKPAIAHRDLKSKNILIKKNGSCCIADlglavkfnsdtn 392
Cdd:smart00750   1 VSLADILEVrgRPLNEEEIWAVCLQCLGALRELH--------RQAKSGNILLTWDGLLKLDGSVAFKT------------ 60
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437    393 evdvPLNTRVGTKrYMAPEVLDEslnknhfQPYI-MADIYSFGLIIWEMArrcitggiveEYQLPYYNMVPSDPSYED-- 469
Cdd:smart00750  61 ----PEQSRPDPY-FMAPEVIQG-------QSYTeKADIYSLGITLYEAL----------DYELPYNEERELSAILEIll 118
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41349437    470 --MREVVCVKRLRPivsnrwNSDECLRAVLKLMSECWAHNPASRLTALRIKKTL-AKMVESQD 529
Cdd:smart00750 119 ngMPADDPRDRSNL------EGVSAARSFEDFMRLCASRLPQRREAANHYLAHCrALFAETLE 175
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
317-514 8.26e-04

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: 41.48  E-value: 8.26e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 317 LYDFLKCAT---LDTRALLKLAYSAACGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNGSCCIA--DLGLAVkFNSDT 391
Cdd:cd14133  87 LYEFLKQNKfqyLSLPRIRKIAQQILEALVFLHSL--------GLIHCDLKPENILLASYSRCQIKiiDFGSSC-FLTQR 157
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 392 nevdvpLNTRVGTKRYMAPEVLdesLNknhfQPYIMA-DIYSFGLIIWEMarrcITGgiveeyqlpyYNMVPSDPSYEDM 470
Cdd:cd14133 158 ------LYSYIQSRYYRAPEVI---LG----LPYDEKiDMWSLGCILAEL----YTG----------EPLFPGASEVDQL 210
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 41349437 471 REVVCVKRLRP--IVSNRWNSDECLravLKLMSECWAHNPASRLTA 514
Cdd:cd14133 211 ARIIGTIGIPPahMLDQGKADDELF---VDFLKKLLEIDPKERPTA 253
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
358-438 1.36e-03

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: 40.74  E-value: 1.36e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 358 IAHRDLKSKNILI---KKNGSCCIADLGLAvKFNSDTNevdvPLNTRVGTKRYMAPEVLD-ESLNKNhfqpyimADIYSF 433
Cdd:cd14172 124 IAHRDVKPENLLYtskEKDAVLKLTDFGFA-KETTVQN----ALQTPCYTPYYVAPEVLGpEKYDKS-------CDMWSL 191

                ....*
gi 41349437 434 GLIIW 438
Cdd:cd14172 192 GVIMY 196
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
358-440 1.49e-03

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: 40.79  E-value: 1.49e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 358 IAHRDLKSKNILI---KKNGSCCIADLGLAvKFNSDTNEvdvPLNTRVGTKRYMAPEVldesLNKNHFQPyiMADIYSFG 434
Cdd:cd14179 123 VVHRDLKPENLLFtdeSDNSEIKIIDFGFA-RLKPPDNQ---PLKTPCFTLHYAAPEL----LNYNGYDE--SCDLWSLG 192

                ....*.
gi 41349437 435 LIIWEM 440
Cdd:cd14179 193 VILYTM 198
QVR pfam17064
Sleepless protein; In Drosophila QUIVER (also known as SLEEPLESS protein) is required for ...
59-131 1.74e-03

Sleepless protein; In Drosophila QUIVER (also known as SLEEPLESS protein) is required for homoeostatic regulation of sleep under normal conditions and following sleep deprivation. It is a novel potassium channel subunit that modulates the Shaker potassium channel which regulates the sleep.


Pssm-ID: 435716  Cd Length: 85  Bit Score: 37.58  E-value: 1.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437    59 LKCY-CSG----HCPDDAINNT-------CitNGHCFAIIEEDDQGETTLASGCMKYEGSDF--QCKDSPKAQLrRTIEC 124
Cdd:pfam17064   1 IKCYsCNSsddpGCGDPFPFNSssiklvdC--DGGCVKIKTKGSGGSTRVTRGCGPELTEDIkdGCSSSSSGGG-GTITC 77

                  ....*...
gi 41349437   125 -CRTNLCN 131
Cdd:pfam17064  78 fCNTDLCN 85
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
360-439 1.92e-03

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: 40.38  E-value: 1.92e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 360 HRDLKSKNILIKKNGSCCIADLGLAVKFNSDTNEVDVPLNTRVG-------TKRYMAPEVLdesLNKNHFqpyIMADIYS 432
Cdd:cd14011 138 HGNICPESVVINSNGEWKLAGFDFCISSEQATDQFPYFREYDPNlpplaqpNLNYLAPEYI---LSKTCD---PASDMFS 211

                ....*..
gi 41349437 433 FGLIIWE 439
Cdd:cd14011 212 LGVLIYA 218
PK_STRAD_beta cd08226
Pseudokinase domain of STE20-related kinase adapter protein beta; The pseudokinase domain ...
255-442 2.36e-03

Pseudokinase domain of STE20-related kinase adapter protein beta; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity.STRAD-beta is also referred to as ALS2CR2 (Amyotrophic lateral sclerosis 2 chromosomal region candidate gene 2 protein), since the human gene encoding it is located within the juvenile ALS2 critical region on chromosome 2q33-q34. It is not linked to the development of ALS2. STRAD forms a complex with the scaffolding protein MO25, and the serine/threonine kinase (STK), LKB1, resulting in the activation of the kinase. In the complex, LKB1 phosphorylates and activates adenosine monophosphate-activated protein kinases (AMPKs), which regulate cell energy metabolism and cell polarity. LKB1 is a tumor suppressor linked to the rare inherited disease, Peutz-Jeghers syndrome, which is characterized by a predisposition to benign polyps and hyperpigmentation of the buccal mucosa. The STRAD-beta 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: 270864 [Multi-domain]  Cd Length: 328  Bit Score: 40.24  E-value: 2.36e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 255 GEKVAVKVF---FTTEEASWFRETEIYQTVLMRHENILGFIAadIKGTGSWtqLYLITDYHENGSLYDFLKCATLD--TR 329
Cdd:cd08226  25 GTLVTVKITnldNCSEEHLKALQNEVVLSHFFRHPNIMTHWT--VFTEGSW--LWVISPFMAYGSARGLLKTYFPEgmNE 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 330 ALLK-LAYSAACGLCHLHTEIYgtqgkpaiAHRDLKSKNILIKKNGS---------CCIADLGLAVKFNSDTNEVDVPLn 399
Cdd:cd08226 101 ALIGnILYGAIKALNYLHQNGC--------IHRSVKASHILISGDGLvslsglshlYSMVTNGQRSKVVYDFPQFSTSV- 171
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 41349437 400 trvgtKRYMAPEVLDESLNKNHfqpyIMADIYSFGLIIWEMAR 442
Cdd:cd08226 172 -----LPWLSPELLRQDLHGYN----VKSDIYSVGITACELAR 205
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
240-438 4.11e-03

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: 39.13  E-value: 4.11e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 240 VGKGRYGEV--WMGKWRGEKVAVKVFFT-----TEEAswfrETEIYQTVLMRHENILGFIAAdikgTGSWTQLYLITDYH 312
Cdd:cd14193  12 LGGGRFGQVhkCEEKSSGLKLAAKIIKArsqkeKEEV----KNEIEVMNQLNHANLIQLYDA----FESRNDIVLVMEYV 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 313 ENGSLYDFL-----KCATLDTRALLKLAYSaacGLCHLHtEIYgtqgkpaIAHRDLKSKNILI--KKNGSCCIADLGLAV 385
Cdd:cd14193  84 DGGELFDRIidenyNLTELDTILFIKQICE---GIQYMH-QMY-------ILHLDLKPENILCvsREANQVKIIDFGLAR 152
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 41349437 386 KFNSDTNevdvpLNTRVGTKRYMAPEVLdeslnkNHFQPYIMADIYSFGLIIW 438
Cdd:cd14193 153 RYKPREK-----LRVNFGTPEFLAPEVV------NYEFVSFPTDMWSLGVIAY 194
STKc_Vps15 cd13980
Catalytic domain of the Serine/Threonine kinase, Vacuolar protein sorting-associated protein ...
238-440 4.19e-03

Catalytic domain of the Serine/Threonine kinase, Vacuolar protein sorting-associated protein 15; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Vps15 is a large protein consisting of an N-terminal kinase domain, a C-terminal WD-repeat containing domain, and an intermediate bridge domain that contain HEAT repeats. The kinase domain is necessary for the signaling functions of Vps15. Human Vps15 was previously called p150. It associates and regulates Vps34, also called Class III phosphoinositide 3-kinase (PI3K), which catalyzes the phosphorylation of D-myo-phosphatidylinositol (PtdIns). Vps34 is the only PI3K present in yeast. It plays an important role in the regulation of protein and vesicular trafficking and sorting, autophagy, trimeric G-protein signaling, and phagocytosis. The Vps15 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 PI3K.


Pssm-ID: 270882 [Multi-domain]  Cd Length: 278  Bit Score: 39.16  E-value: 4.19e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 238 RQVGKGRYGEVWMGKWRGEKVAVKVFFTTEEA----SWFRETEIYQTVLMRHENILGFIAADIKGTGSwtqlYLITDYHE 313
Cdd:cd13980   6 KSLGSTRFLKVARARHDEGLVVVKVFVKPDPAlplrSYKQRLEEIRDRLLELPNVLPFQKVIETDKAA----YLIRQYVK 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 314 NgSLYDflkcaTLDTRALLKL------AYSAACGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNGSCCIADlglavkF 387
Cdd:cd13980  82 Y-NLYD-----RISTRPFLNLiekkwiAFQLLHALNQCHKR--------GVCHGDIKTENVLVTSWNWVYLTD------F 141
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41349437 388 NS------------------DTNEvdvplnTRVGtkrYMAPE--------VLDESLNKNHFQPyiMADIYSFGLIIWEM 440
Cdd:cd13980 142 ASfkptylpednpadfsyffDTSR------RRTC---YIAPErfvdaltlDAESERRDGELTP--AMDIFSLGCVIAEL 209
TGF_beta_GS pfam08515
Transforming growth factor beta type I GS-motif; This motif is found in the transforming ...
205-232 6.04e-03

Transforming growth factor beta type I GS-motif; This motif is found in the transforming growth factor beta (TGF-beta) type I which regulates cell growth and differentiation. The name of the GS motif comes from its highly conserved GSGSGLP signature in the cytoplasmic juxtamembrane region immediately preceding the protein's kinase domain. Point mutations in the GS motif modify the signaling ability of the type I receptor.


Pssm-ID: 462503  Cd Length: 28  Bit Score: 34.49  E-value: 6.04e-03
                          10        20
                  ....*....|....*....|....*...
gi 41349437   205 SLKDLIDQSQSSGSGSGLPLLVQRTIAK 232
Cdd:pfam08515   1 TLKDLIDESCTSGSGSGLPLLVQRTIAR 28
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
350-440 7.02e-03

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: 38.45  E-value: 7.02e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 350 YGTQGKPAIAHRDLKSKNILI---KKNGSCCIADLGLAVKFNSDTNEVDVPLNTR--VGTKRYMAPEVLDesLNKNhfQP 424
Cdd:cd13990 120 YLNEIKPPIIHYDLKPGNILLhsgNVSGEIKITDFGLSKIMDDESYNSDGMELTSqgAGTYWYLPPECFV--VGKT--PP 195
                        90
                ....*....|....*...
gi 41349437 425 YIMA--DIYSFGLIIWEM 440
Cdd:cd13990 196 KISSkvDVWSVGVIFYQM 213
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
238-413 8.59e-03

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: 38.27  E-value: 8.59e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 238 RQVGKGRYGEVWMGKWRG--EKVAVKVFFTTEEASWFReTEIyqTVLMR--HENILGFIaaDIKGTGswTQLYLITDYHE 313
Cdd:cd14085   9 SELGRGATSVVYRCRQKGtqKPYAVKKLKKTVDKKIVR-TEI--GVLLRlsHPNIIKLK--EIFETP--TEISLVLELVT 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41349437 314 NGSLYDflkcatldtRALLKLAYS----AAC------GLCHLHteiygtqgKPAIAHRDLKSKNILIKKNGSCC---IAD 380
Cdd:cd14085  82 GGELFD---------RIVEKGYYSerdaADAvkqileAVAYLH--------ENGIVHRDLKPENLLYATPAPDAplkIAD 144
                       170       180       190
                ....*....|....*....|....*....|...
gi 41349437 381 LGLavkfnSDTNEVDVPLNTRVGTKRYMAPEVL 413
Cdd:cd14085 145 FGL-----SKIVDQQVTMKTVCGTPGYCAPEIL 172
 
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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