NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1370461664|ref|XP_024304706|]
View 

anti-Muellerian hormone type-2 receptor isoform X8 [Homo sapiens]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
PKc_like super family cl21453
Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the ...
208-414 1.72e-94

Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the catalytic domains of serine/threonine-specific and tyrosine-specific protein kinases. It also includes RIO kinases, which are atypical serine protein kinases, aminoglycoside phosphotransferases, and choline kinases. These proteins catalyze the transfer of the gamma-phosphoryl group from ATP to hydroxyl groups in specific substrates such as serine, threonine, or tyrosine residues of proteins.


The actual alignment was detected with superfamily member cd14054:

Pssm-ID: 473864 [Multi-domain]  Cd Length: 300  Bit Score: 288.11  E-value: 1.72e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 208 QVIREGGHAVVWAGQLQGKLVAIKAFPPRSVAQFQAERALYELPGLQHDHIVRFITASRGGPGRLLSGPLLVLELHPKGS 287
Cdd:cd14054     1 QLIGQGRYGTVWKGSLDERPVAVKVFPARHRQNFQNEKDIYELPLMEHSNILRFIGADERPTADGRMEYLLVLEYAPKGS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 288 LCHYLTQYTSDWGSSLRMALSLAQGLAFLHEERWQNGQYKPGIAHRDLSSQNVLIREDGSCAIGDLGLALVLPGLTQPpa 367
Cdd:cd14054    81 LCSYLRENTLDWMSSCRMALSLTRGLAYLHTDLRRGDQYKPAIAHRDLNSRNVLVKADGSCVICDFGLAMVLRGSSLV-- 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 368 WTPTQPQGPAAIME------------------------------------------------------------------ 381
Cdd:cd14054   159 RGRPGAAENASISEvgtlrymapevlegavnlrdcesalkqvdvyalglvlweiamrcsdlypgesvppyqmpyeaelgn 238
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370461664 382 -----------------------------DPDGLRELLEDCWDADPEARLTAECVQQRLAAL 414
Cdd:cd14054   239 hptfedmqllvsrekarpkfpdawkenslAVRSLKETIEDCWDQDAEARLTALCVEERLAEL 300
TFP_LU_ECD_AMHR2 cd23616
extracellular domain (ECD) found in anti-Muellerian hormone type-2 receptor (AMHR2) and ...
22-121 3.06e-30

extracellular domain (ECD) found in anti-Muellerian hormone type-2 receptor (AMHR2) and similar proteins; AMHR2 (EC 2.7.11.30, also called anti-Muellerian hormone type II receptor (MISRII), or AMH type II receptor, or MIS type II receptor, or MRII, 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. AMHR2 is the receptor for anti-Muellerian hormone. This model corresponds to the extracellular domain (ECD) of AMHR2, 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: 467136  Cd Length: 89  Bit Score: 112.83  E-value: 3.06e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664  22 RTCVFFEAPGVRGSTKTLGelldtgTELPRAIRCLYSRCCFGIWNLTQDRAQVEMQGCRDSdEPGCESLHCDPSPRAHPS 101
Cdd:cd23616     1 RTCVFYVSPSNRGSLRAAG------NVSGSVQRCENTQCCVGIWNIINGQLQVDLLGCWVS-EASCPSATCKPSPRFNPN 73
                          90       100
                  ....*....|....*....|
gi 1370461664 102 pgstLFTCSCGTDFCNANYS 121
Cdd:cd23616    74 ----YIKCVCNTDLCNGNIT 89
 
Name Accession Description Interval E-value
STKc_BMPR2_AMHR2 cd14054
Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and ...
208-414 1.72e-94

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: 288.11  E-value: 1.72e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 208 QVIREGGHAVVWAGQLQGKLVAIKAFPPRSVAQFQAERALYELPGLQHDHIVRFITASRGGPGRLLSGPLLVLELHPKGS 287
Cdd:cd14054     1 QLIGQGRYGTVWKGSLDERPVAVKVFPARHRQNFQNEKDIYELPLMEHSNILRFIGADERPTADGRMEYLLVLEYAPKGS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 288 LCHYLTQYTSDWGSSLRMALSLAQGLAFLHEERWQNGQYKPGIAHRDLSSQNVLIREDGSCAIGDLGLALVLPGLTQPpa 367
Cdd:cd14054    81 LCSYLRENTLDWMSSCRMALSLTRGLAYLHTDLRRGDQYKPAIAHRDLNSRNVLVKADGSCVICDFGLAMVLRGSSLV-- 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 368 WTPTQPQGPAAIME------------------------------------------------------------------ 381
Cdd:cd14054   159 RGRPGAAENASISEvgtlrymapevlegavnlrdcesalkqvdvyalglvlweiamrcsdlypgesvppyqmpyeaelgn 238
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370461664 382 -----------------------------DPDGLRELLEDCWDADPEARLTAECVQQRLAAL 414
Cdd:cd14054   239 hptfedmqllvsrekarpkfpdawkenslAVRSLKETIEDCWDQDAEARLTALCVEERLAEL 300
TFP_LU_ECD_AMHR2 cd23616
extracellular domain (ECD) found in anti-Muellerian hormone type-2 receptor (AMHR2) and ...
22-121 3.06e-30

extracellular domain (ECD) found in anti-Muellerian hormone type-2 receptor (AMHR2) and similar proteins; AMHR2 (EC 2.7.11.30, also called anti-Muellerian hormone type II receptor (MISRII), or AMH type II receptor, or MIS type II receptor, or MRII, 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. AMHR2 is the receptor for anti-Muellerian hormone. This model corresponds to the extracellular domain (ECD) of AMHR2, 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: 467136  Cd Length: 89  Bit Score: 112.83  E-value: 3.06e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664  22 RTCVFFEAPGVRGSTKTLGelldtgTELPRAIRCLYSRCCFGIWNLTQDRAQVEMQGCRDSdEPGCESLHCDPSPRAHPS 101
Cdd:cd23616     1 RTCVFYVSPSNRGSLRAAG------NVSGSVQRCENTQCCVGIWNIINGQLQVDLLGCWVS-EASCPSATCKPSPRFNPN 73
                          90       100
                  ....*....|....*....|
gi 1370461664 102 pgstLFTCSCGTDFCNANYS 121
Cdd:cd23616    74 ----YIKCVCNTDLCNGNIT 89
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
208-409 1.63e-18

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: 84.91  E-value: 1.63e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664  208 QVIREGGHAVVWAGQLQGKL------VAIKAfpPRSVAQFQAERALYE----LPGLQHDHIVRFITASRGGPGrllsgPL 277
Cdd:smart00221   5 KKLGEGAFGEVYKGTLKGKGdgkeveVAVKT--LKEDASEQQIEEFLReariMRKLDHPNIVKLLGVCTEEEP-----LM 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664  278 LVLELHPKGSLCHYLTQYTSDWGSS---LRMALSLAQGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDLG 354
Cdd:smart00221  78 IVMEYMPGGDLLDYLRKNRPKELSLsdlLSFALQIARGMEYLESKN---------FIHRDLAARNCLVGENLVVKISDFG 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664  355 LALVLPGLTQ--------PPAWTP--------------------------TQPQGPAAIMED------------------ 382
Cdd:smart00221 149 LSRDLYDDDYykvkggklPIRWMApeslkegkftsksdvwsfgvllweifTLGEEPYPGMSNaevleylkkgyrlpkppn 228
                          250       260
                   ....*....|....*....|....*....
gi 1370461664  383 -PDGLRELLEDCWDADPEARLT-AECVQQ 409
Cdd:smart00221 229 cPPELYKLMLQCWAEDPEDRPTfSELVEI 257
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
208-365 1.72e-18

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 87.76  E-value: 1.72e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 208 QVIREGGHAVVWAG--QLQGKLVAIK------AFPPRSVAQFQAERALyeLPGLQHDHIVRFITASRGGPGrllsgPLLV 279
Cdd:COG0515    13 RLLGRGGMGVVYLArdLRLGRPVALKvlrpelAADPEARERFRREARA--LARLNHPNIVRVYDVGEEDGR-----PYLV 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 280 LELHPKGSLCHYLTQYTS-DWGSSLRMALSLAQGLAFLHEErwqngqykpGIAHRDLSSQNVLIREDGSCAIGDLGLALV 358
Cdd:COG0515    86 MEYVEGESLADLLRRRGPlPPAEALRILAQLAEALAAAHAA---------GIVHRDIKPANILLTPDGRVKLIDFGIARA 156

                  ....*....
gi 1370461664 359 LPG--LTQP 365
Cdd:COG0515   157 LGGatLTQT 165
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
208-411 1.66e-16

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: 79.08  E-value: 1.66e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 208 QVIREGGHAVVWAGQLQGK------LVAIKAFPP----RSVAQFQAERALyeLPGLQHDHIVRFITA-SRGGPgrllsgP 276
Cdd:pfam07714   5 EKLGEGAFGEVYKGTLKGEgentkiKVAVKTLKEgadeEEREDFLEEASI--MKKLDHPNIVKLLGVcTQGEP------L 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 277 LLVLELHPKGSLCHYLTQYTSDWGSS--LRMALSLAQGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDLG 354
Cdd:pfam07714  77 YIVTEYMPGGDLLDFLRKHKRKLTLKdlLSMALQIAKGMEYLESKN---------FVHRDLAARNCLVSENLVVKISDFG 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 355 LALVLP---------GLTQPPAWTPtqpqgPAAIMED------------------------------------------- 382
Cdd:pfam07714 148 LSRDIYdddyyrkrgGGKLPIKWMA-----PESLKDGkftsksdvwsfgvllweiftlgeqpypgmsneevlefledgyr 222
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1370461664 383 -------PDGLRELLEDCWDADPEARLTAECVQQRL 411
Cdd:pfam07714 223 lpqpencPDELYDLMKQCWAYDPEDRPTFSELVEDL 258
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
250-356 3.40e-04

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 42.94  E-value: 3.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 250 LPGLQHDHIVRFITAsrggpgrLLSGPLLVLEL-HPKGSLCHYLTQYTS--DWGSSLRMALSLAQGLAFLHEERwqngqy 326
Cdd:PHA03209  111 LQNVNHPSVIRMKDT-------LVSGAITCMVLpHYSSDLYTYLTKRSRplPIDQALIIEKQILEGLRYLHAQR------ 177
                          90       100       110
                  ....*....|....*....|....*....|
gi 1370461664 327 kpgIAHRDLSSQNVLIREDGSCAIGDLGLA 356
Cdd:PHA03209  178 ---IIHRDVKTENIFINDVDQVCIGDLGAA 204
 
Name Accession Description Interval E-value
STKc_BMPR2_AMHR2 cd14054
Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and ...
208-414 1.72e-94

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: 288.11  E-value: 1.72e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 208 QVIREGGHAVVWAGQLQGKLVAIKAFPPRSVAQFQAERALYELPGLQHDHIVRFITASRGGPGRLLSGPLLVLELHPKGS 287
Cdd:cd14054     1 QLIGQGRYGTVWKGSLDERPVAVKVFPARHRQNFQNEKDIYELPLMEHSNILRFIGADERPTADGRMEYLLVLEYAPKGS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 288 LCHYLTQYTSDWGSSLRMALSLAQGLAFLHEERWQNGQYKPGIAHRDLSSQNVLIREDGSCAIGDLGLALVLPGLTQPpa 367
Cdd:cd14054    81 LCSYLRENTLDWMSSCRMALSLTRGLAYLHTDLRRGDQYKPAIAHRDLNSRNVLVKADGSCVICDFGLAMVLRGSSLV-- 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 368 WTPTQPQGPAAIME------------------------------------------------------------------ 381
Cdd:cd14054   159 RGRPGAAENASISEvgtlrymapevlegavnlrdcesalkqvdvyalglvlweiamrcsdlypgesvppyqmpyeaelgn 238
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370461664 382 -----------------------------DPDGLRELLEDCWDADPEARLTAECVQQRLAAL 414
Cdd:cd14054   239 hptfedmqllvsrekarpkfpdawkenslAVRSLKETIEDCWDQDAEARLTALCVEERLAEL 300
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
208-414 1.73e-53

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: 181.48  E-value: 1.73e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 208 QVIREGGHAVVWAGQLQGKLVAIKAFPPRSVAQFQAERALYELPGLQHDHIVRFITASRGGPGrLLSGPLLVLELHPKGS 287
Cdd:cd13998     1 EVIGKGRFGEVWKASLKNEPVAVKIFSSRDKQSWFREKEIYRTPMLKHENILQFIAADERDTA-LRTELWLVTAFHPNGS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 288 LCHYLTQYTSDWGSSLRMALSLAQGLAFLHEERWQNGQYKPGIAHRDLSSQNVLIREDGSCAIGDLGLALVLPGLT---- 363
Cdd:cd13998    80 L*DYLSLHTIDWVSLCRLALSVARGLAHLHSEIPGCTQGKPAIAHRDLKSKNILVKNDGTCCIADFGLAVRLSPSTgeed 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 364 -----------------------------------------------------------QPPAWT-----PT-------- 371
Cdd:cd13998   160 nanngqvgtkrymapevlegainlrdfesfkrvdiyamglvlwemasrctdlfgiveeyKPPFYSevpnhPSfedmqevv 239
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1370461664 372 -----QPQGPAAIMEDPD--GLRELLEDCWDADPEARLTAECVQQRLAAL 414
Cdd:cd13998   240 vrdkqRPNIPNRWLSHPGlqSLAETIEECWDHDAEARLTAQCIEERLSEF 289
STKc_ACVR2 cd14053
Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the ...
218-416 6.93e-50

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: 172.13  E-value: 6.93e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 218 VWAGQLQGKLVAIKAFPPRSVAQFQAERALYELPGLQHDHIVRFITASRGGPGrLLSGPLLVLELHPKGSLCHYLTQYTS 297
Cdd:cd14053    11 VWKAQYLNRLVAVKIFPLQEKQSWLTEREIYSLPGMKHENILQFIGAEKHGES-LEAEYWLITEFHERGSLCDYLKGNVI 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 298 DWGSSLRMALSLAQGLAFLHEER-WQNGQYKPGIAHRDLSSQNVLIREDGSCAIGDLGLAL------------------- 357
Cdd:cd14053    90 SWNELCKIAESMARGLAYLHEDIpATNGGHKPSIAHRDFKSKNVLLKSDLTACIADFGLALkfepgkscgdthgqvgtrr 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 358 -----VLPGLTQ--PPA-------------W--------------------------TPT-------------QPQGPAA 378
Cdd:cd14053   170 ymapeVLEGAINftRDAflridmyamglvlWellsrcsvhdgpvdeyqlpfeeevgqHPTledmqecvvhkklRPQIRDE 249
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1370461664 379 IMEDPdGLREL---LEDCWDADPEARLTAECVQQRLAALAH 416
Cdd:cd14053   250 WRKHP-GLAQLcetIEECWDHDAEARLSAGCVEERLSQLSR 289
STKc_TGFbR2_like cd14055
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II ...
208-415 4.16e-37

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: 137.89  E-value: 4.16e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 208 QVIREGGHAVVWAGQL------QGKLVAIKAFPPRSVAQFQAERALYELPGLQHDHIVRFITAS--RGGPGRLLsgpLLV 279
Cdd:cd14055     1 KLVGKGRFAEVWKAKLkqnasgQYETVAVKIFPYEEYASWKNEKDIFTDASLKHENILQFLTAEerGVGLDRQY---WLI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 280 LELHPKGSLCHYLTQYTSDWGSSLRMALSLAQGLAFLHEERWQNGQYKPGIAHRDLSSQNVLIREDGSCAIGDLGLALVL 359
Cdd:cd14055    78 TAYHENGSLQDYLTRHILSWEDLCKMAGSLARGLAHLHSDRTPCGRPKIPIAHRDLKSSNILVKNDGTCVLADFGLALRL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 360 -PGLT-------------------------------------------------------------QPPAWTPTQPQGPA 377
Cdd:cd14055   158 dPSLSvdelansgqvgtarymapealesrvnledlesfkqidvysmalvlwemasrceasgevkpyELPFGSKVRERPCV 237
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1370461664 378 AIMED-----------PDG---------LRELLEDCWDADPEARLTAECVQQRLAALA 415
Cdd:cd14055   238 ESMKDlvlrdrgrpeiPDSwlthqgmcvLCDTITECWDHDPEARLTASCVAERFNELK 295
STKc_TGFbR_I cd14056
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type ...
218-358 3.88e-35

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: 132.40  E-value: 3.88e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 218 VWAGQLQGKLVAIKAFPPRSVAQFQAERALYELPGLQHDHIVRFITASRGGPG---RLLsgplLVLELHPKGSLCHYLTQ 294
Cdd:cd14056    11 VWLGKYRGEKVAVKIFSSRDEDSWFRETEIYQTVMLRHENILGFIAADIKSTGswtQLW----LITEYHEHGSLYDYLQR 86
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370461664 295 YTSDWGSSLRMALSLAQGLAFLHEERWQNgQYKPGIAHRDLSSQNVLIREDGSCAIGDLGLALV 358
Cdd:cd14056    87 NTLDTEEALRLAYSAASGLAHLHTEIVGT-QGKPAIAHRDLKSKNILVKRDGTCCIADLGLAVR 149
STKc_TGFbR1_ACVR1b_ACVR1c cd14143
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta Type I ...
208-357 6.81e-33

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: 126.40  E-value: 6.81e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 208 QVIREGGHAVVWAGQLQGKLVAIKAFPPRSVAQFQAERALYELPGLQHDHIVRFITASRGGPGrLLSGPLLVLELHPKGS 287
Cdd:cd14143     1 ESIGKGRFGEVWRGRWRGEDVAVKIFSSREERSWFREAEIYQTVMLRHENILGFIAADNKDNG-TWTQLWLVSDYHEHGS 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 288 LCHYLTQYTSDWGSSLRMALSLAQGLAFLHEErWQNGQYKPGIAHRDLSSQNVLIREDGSCAIGDLGLAL 357
Cdd:cd14143    80 LFDYLNRYTVTVEGMIKLALSIASGLAHLHME-IVGTQGKPAIAHRDLKSKNILVKKNGTCCIADLGLAV 148
STKc_ACVR2b cd14140
Catalytic domain of the Serine/Threonine Kinase, Activin Type IIB Receptor; STKs catalyze the ...
208-414 7.72e-33

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: 126.30  E-value: 7.72e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 208 QVIREGGHAVVWAGQLQGKLVAIKAFPPRSVAQFQAERALYELPGLQHDHIVRFITASRGGpGRLLSGPLLVLELHPKGS 287
Cdd:cd14140     1 EIKARGRFGCVWKAQLMNEYVAVKIFPIQDKQSWQSEREIFSTPGMKHENLLQFIAAEKRG-SNLEMELWLITAFHDKGS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 288 LCHYLTQYTSDWGSSLRMALSLAQGLAFLHEE-RWQNGQ-YKPGIAHRDLSSQNVLIREDGSCAIGDLGLALVL-PGltQ 364
Cdd:cd14140    80 LTDYLKGNIVSWNELCHIAETMARGLSYLHEDvPRCKGEgHKPAIAHRDFKSKNVLLKNDLTAVLADFGLAVRFePG--K 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 365 PPAWTPTQ--------PQ------------------------------------GPA---------AIMEDPD------- 384
Cdd:cd14140   158 PPGDTHGQvgtrrymaPEvlegainfqrdsflridmyamglvlwelvsrckaadGPVdeymlpfeeEIGQHPSledlqev 237
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1370461664 385 ------------------GLREL---LEDCWDADPEARLTAECVQQRLAAL 414
Cdd:cd14140   238 vvhkkmrpvfkdhwlkhpGLAQLcvtIEECWDHDAEARLSAGCVEERISQI 288
TFP_LU_ECD_AMHR2 cd23616
extracellular domain (ECD) found in anti-Muellerian hormone type-2 receptor (AMHR2) and ...
22-121 3.06e-30

extracellular domain (ECD) found in anti-Muellerian hormone type-2 receptor (AMHR2) and similar proteins; AMHR2 (EC 2.7.11.30, also called anti-Muellerian hormone type II receptor (MISRII), or AMH type II receptor, or MIS type II receptor, or MRII, 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. AMHR2 is the receptor for anti-Muellerian hormone. This model corresponds to the extracellular domain (ECD) of AMHR2, 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: 467136  Cd Length: 89  Bit Score: 112.83  E-value: 3.06e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664  22 RTCVFFEAPGVRGSTKTLGelldtgTELPRAIRCLYSRCCFGIWNLTQDRAQVEMQGCRDSdEPGCESLHCDPSPRAHPS 101
Cdd:cd23616     1 RTCVFYVSPSNRGSLRAAG------NVSGSVQRCENTQCCVGIWNIINGQLQVDLLGCWVS-EASCPSATCKPSPRFNPN 73
                          90       100
                  ....*....|....*....|
gi 1370461664 102 pgstLFTCSCGTDFCNANYS 121
Cdd:cd23616    74 ----YIKCVCNTDLCNGNIT 89
STKc_BMPR1 cd14144
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type I Receptor; ...
208-356 3.27e-27

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: 110.64  E-value: 3.27e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 208 QVIREGGHAVVWAGQLQGKLVAIKAFPPRSVAQFQAERALYELPGLQHDHIVRFITASRGGPGRLlSGPLLVLELHPKGS 287
Cdd:cd14144     1 RSVGKGRYGEVWKGKWRGEKVAVKIFFTTEEASWFRETEIYQTVLMRHENILGFIAADIKGTGSW-TQLYLITDYHENGS 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370461664 288 LCHYLTQYTSDWGSSLRMALSLAQGLAFLHEERWQNgQYKPGIAHRDLSSQNVLIREDGSCAIGDLGLA 356
Cdd:cd14144    80 LYDFLRGNTLDTQSMLKLAYSAACGLAHLHTEIFGT-QGKPAIAHRDIKSKNILVKKNGTCCIADLGLA 147
STKc_ACVR1_ALK1 cd14142
Catalytic domain of the Serine/Threonine Kinases, Activin Type I Receptor and Activin ...
208-356 1.17e-26

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: 109.07  E-value: 1.17e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 208 QVIREGGHAVVWAGQLQGKLVAIKAFPPRSVAQFQAERALYELPGLQHDHIVRFIT---ASRGGPGRLLsgplLVLELHP 284
Cdd:cd14142    11 ECIGKGRYGEVWRGQWQGESVAVKIFSSRDEKSWFRETEIYNTVLLRHENILGFIAsdmTSRNSCTQLW----LITHYHE 86
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370461664 285 KGSLCHYLTQYTSDWGSSLRMALSLAQGLAFLHEERWQNgQYKPGIAHRDLSSQNVLIREDGSCAIGDLGLA 356
Cdd:cd14142    87 NGSLYDYLQRTTLDHQEMLRLALSAASGLVHLHTEIFGT-QGKPAIAHRDLKSKNILVKSNGQCCIADLGLA 157
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
210-401 3.11e-26

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: 106.85  E-value: 3.11e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 210 IREGGHAVVWAGQLQGKLVAIKAFPPRS-----VAQFQAERALyeLPGLQHDHIVRFITASRGGPgrllsgPL-LVLELH 283
Cdd:cd13999     1 IGSGSFGEVYKGKWRGTDVAIKKLKVEDdndelLKEFRREVSI--LSKLRHPNIVQFIGACLSPP------PLcIVTEYM 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 284 PKGSLCHYLT--QYTSDWGSSLRMALSLAQGLAFLHEerwqngqykPGIAHRDLSSQNVLIREDGSCAIGDLGLALVLPG 361
Cdd:cd13999    73 PGGSLYDLLHkkKIPLSWSLRLKIALDIARGMNYLHS---------PPIIHRDLKSLNILLDENFTVKIADFGLSRIKNS 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 362 LTQP-------PAW-------------------------------TPTQPQGPAAIMED--------------PDGLREL 389
Cdd:cd13999   144 TTEKmtgvvgtPRWmapevlrgepytekadvysfgivlwelltgeVPFKELSPIQIAAAvvqkglrppippdcPPELSKL 223
                         250
                  ....*....|..
gi 1370461664 390 LEDCWDADPEAR 401
Cdd:cd13999   224 IKRCWNEDPEKR 235
STKc_BMPR1a cd14220
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IA Receptor; ...
210-357 8.12e-26

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: 106.66  E-value: 8.12e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 210 IREGGHAVVWAGQLQGKLVAIKAFPPRSVAQFQAERALYELPGLQHDHIVRFITASRGGPGRLlSGPLLVLELHPKGSLC 289
Cdd:cd14220     3 IGKGRYGEVWMGKWRGEKVAVKVFFTTEEASWFRETEIYQTVLMRHENILGFIAADIKGTGSW-TQLYLITDYHENGSLY 81
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370461664 290 HYLTQYTSDWGSSLRMALSLAQGLAFLHEERWQNgQYKPGIAHRDLSSQNVLIREDGSCAIGDLGLAL 357
Cdd:cd14220    82 DFLKCTTLDTRALLKLAYSAACGLCHLHTEIYGT-QGKPAIAHRDLKSKNILIKKNGTCCIADLGLAV 148
STKc_ACVR2a cd14141
Catalytic domain of the Serine/Threonine Kinase, Activin Type IIA Receptor; STKs catalyze the ...
208-357 1.02e-25

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: 106.28  E-value: 1.02e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 208 QVIREGGHAVVWAGQLQGKLVAIKAFPPRSVAQFQAERALYELPGLQHDHIVRFITASRGGPGrLLSGPLLVLELHPKGS 287
Cdd:cd14141     1 EIKARGRFGCVWKAQLLNEYVAVKIFPIQDKLSWQNEYEIYSLPGMKHENILQFIGAEKRGTN-LDVDLWLITAFHEKGS 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370461664 288 LCHYLTQYTSDWGSSLRMALSLAQGLAFLHEE--RWQNGqYKPGIAHRDLSSQNVLIREDGSCAIGDLGLAL 357
Cdd:cd14141    80 LTDYLKANVVSWNELCHIAQTMARGLAYLHEDipGLKDG-HKPAIAHRDIKSKNVLLKNNLTACIADFGLAL 150
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
210-411 3.36e-25

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: 103.12  E-value: 3.36e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 210 IREGGHAVVWAGQLQ--GKLVAIKAFPPRSVaQFQAERALYE---LPGLQHDHIVRFITASRGGPGRLLsgpllVLELHP 284
Cdd:cd00180     1 LGKGSFGKVYKARDKetGKKVAVKVIPKEKL-KKLLEELLREieiLKKLNHPNIVKLYDVFETENFLYL-----VMEYCE 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 285 KGSLCHYLTQYTS--DWGSSLRMALSLAQGLAFLHEErwqngqykpGIAHRDLSSQNVLIREDGSCAIGDLGLALVL--P 360
Cdd:cd00180    75 GGSLKDLLKENKGplSEEEALSILRQLLSALEYLHSN---------GIIHRDLKPENILLDSDGTVKLADFGLAKDLdsD 145
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 361 GLTQPPAWTPTQPQGPAAIMEDP-------------------DGLRELLEDCWDADPEARLTAECVQQRL 411
Cdd:cd00180   146 DSLLKTTGGTTPPYYAPPELLGGryygpkvdiwslgvilyelEELKDLIRRMLQYDPKKRPSAKELLEHL 215
STKc_BMPR1b cd14219
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IB; STKs ...
210-357 1.89e-23

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: 100.51  E-value: 1.89e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 210 IREGGHAVVWAGQLQGKLVAIKAFPPRSVAQFQAERALYELPGLQHDHIVRFITASRGGPGRLlSGPLLVLELHPKGSLC 289
Cdd:cd14219    13 IGKGRYGEVWMGKWRGEKVAVKVFFTTEEASWFRETEIYQTVLMRHENILGFIAADIKGTGSW-TQLYLITDYHENGSLY 91
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370461664 290 HYLTQYTSDWGSSLRMALSLAQGLAFLHEERWQNgQYKPGIAHRDLSSQNVLIREDGSCAIGDLGLAL 357
Cdd:cd14219    92 DYLKSTTLDTKAMLKLAYSSVSGLCHLHTEIFST-QGKPAIAHRDLKSKNILVKKNGTCCIADLGLAV 158
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
207-365 8.13e-20

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: 88.80  E-value: 8.13e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 207 QQVIREGGHAVVWAG--QLQGKLVAIKAFPP------RSVAQFQAE-RALYELpglQHDHIVRFITAsrggpGRLLSGPL 277
Cdd:cd14014     5 VRLLGRGGMGEVYRArdTLLGRPVAIKVLRPelaedeEFRERFLREaRALARL---SHPNIVRVYDV-----GEDDGRPY 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 278 LVLELHPKGSLCHYLTQYTS-DWGSSLRMALSLAQGLAFLHEErwqngqykpGIAHRDLSSQNVLIREDGSCAIGDLGLA 356
Cdd:cd14014    77 IVMEYVEGGSLADLLRERGPlPPREALRILAQIADALAAAHRA---------GIVHRDIKPANILLTEDGRVKLTDFGIA 147
                         170
                  ....*....|.
gi 1370461664 357 LVL--PGLTQP 365
Cdd:cd14014   148 RALgdSGLTQT 158
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
210-360 1.34e-19

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: 88.48  E-value: 1.34e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 210 IREGGHAVVWAGQLQ-GKLVAIKAFPPRSVA----QFQAEraLYELPGLQHDHIVRFITASRGGpgrllSGPLLVLELHP 284
Cdd:cd14066     1 IGSGGFGTVYKGVLEnGTVVAVKRLNEMNCAaskkEFLTE--LEMLGRLRHPNLVRLLGYCLES-----DEKLLVYEYMP 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 285 KGSLCHYLTQYTS----DWGSSLRMALSLAQGLAFLHEErwqngqYKPGIAHRDLSSQNVLIREDGSCAIGDLGLALVLP 360
Cdd:cd14066    74 NGSLEDRLHCHKGspplPWPQRLKIAKGIARGLEYLHEE------CPPPIIHGDIKSSNILLDEDFEPKLTDFGLARLIP 147
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
208-409 1.63e-18

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: 84.91  E-value: 1.63e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664  208 QVIREGGHAVVWAGQLQGKL------VAIKAfpPRSVAQFQAERALYE----LPGLQHDHIVRFITASRGGPGrllsgPL 277
Cdd:smart00221   5 KKLGEGAFGEVYKGTLKGKGdgkeveVAVKT--LKEDASEQQIEEFLReariMRKLDHPNIVKLLGVCTEEEP-----LM 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664  278 LVLELHPKGSLCHYLTQYTSDWGSS---LRMALSLAQGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDLG 354
Cdd:smart00221  78 IVMEYMPGGDLLDYLRKNRPKELSLsdlLSFALQIARGMEYLESKN---------FIHRDLAARNCLVGENLVVKISDFG 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664  355 LALVLPGLTQ--------PPAWTP--------------------------TQPQGPAAIMED------------------ 382
Cdd:smart00221 149 LSRDLYDDDYykvkggklPIRWMApeslkegkftsksdvwsfgvllweifTLGEEPYPGMSNaevleylkkgyrlpkppn 228
                          250       260
                   ....*....|....*....|....*....
gi 1370461664  383 -PDGLRELLEDCWDADPEARLT-AECVQQ 409
Cdd:smart00221 229 cPPELYKLMLQCWAEDPEDRPTfSELVEI 257
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
208-365 1.72e-18

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 87.76  E-value: 1.72e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 208 QVIREGGHAVVWAG--QLQGKLVAIK------AFPPRSVAQFQAERALyeLPGLQHDHIVRFITASRGGPGrllsgPLLV 279
Cdd:COG0515    13 RLLGRGGMGVVYLArdLRLGRPVALKvlrpelAADPEARERFRREARA--LARLNHPNIVRVYDVGEEDGR-----PYLV 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 280 LELHPKGSLCHYLTQYTS-DWGSSLRMALSLAQGLAFLHEErwqngqykpGIAHRDLSSQNVLIREDGSCAIGDLGLALV 358
Cdd:COG0515    86 MEYVEGESLADLLRRRGPlPPAEALRILAQLAEALAAAHAA---------GIVHRDIKPANILLTPDGRVKLIDFGIARA 156

                  ....*....
gi 1370461664 359 LPG--LTQP 365
Cdd:COG0515   157 LGGatLTQT 165
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
208-409 2.36e-18

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 84.50  E-value: 2.36e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664  208 QVIREGGHAVVWAGQLQGKL------VAIKAfpPRSVAQFQAERALYE----LPGLQHDHIVRFITASRGGPGrllsgPL 277
Cdd:smart00219   5 KKLGEGAFGEVYKGKLKGKGgkkkveVAVKT--LKEDASEQQIEEFLReariMRKLDHPNVVKLLGVCTEEEP-----LY 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664  278 LVLELHPKGSLCHYLTQYTSDWGSS--LRMALSLAQGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDLGL 355
Cdd:smart00219  78 IVMEYMEGGDLLSYLRKNRPKLSLSdlLSFALQIARGMEYLESKN---------FIHRDLAARNCLVGENLVVKISDFGL 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664  356 ALVLP--------GLTQPPAWTP--------------------------TQPQGPAAIMED------------------- 382
Cdd:smart00219 149 SRDLYdddyyrkrGGKLPIRWMApeslkegkftsksdvwsfgvllweifTLGEQPYPGMSNeevleylkngyrlpqppnc 228
                          250       260
                   ....*....|....*....|....*...
gi 1370461664  383 PDGLRELLEDCWDADPEARLT-AECVQQ 409
Cdd:smart00219 229 PPELYDLMLQCWAEDPEDRPTfSELVEI 256
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
208-411 1.66e-16

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: 79.08  E-value: 1.66e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 208 QVIREGGHAVVWAGQLQGK------LVAIKAFPP----RSVAQFQAERALyeLPGLQHDHIVRFITA-SRGGPgrllsgP 276
Cdd:pfam07714   5 EKLGEGAFGEVYKGTLKGEgentkiKVAVKTLKEgadeEEREDFLEEASI--MKKLDHPNIVKLLGVcTQGEP------L 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 277 LLVLELHPKGSLCHYLTQYTSDWGSS--LRMALSLAQGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDLG 354
Cdd:pfam07714  77 YIVTEYMPGGDLLDFLRKHKRKLTLKdlLSMALQIAKGMEYLESKN---------FVHRDLAARNCLVSENLVVKISDFG 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 355 LALVLP---------GLTQPPAWTPtqpqgPAAIMED------------------------------------------- 382
Cdd:pfam07714 148 LSRDIYdddyyrkrgGGKLPIKWMA-----PESLKDGkftsksdvwsfgvllweiftlgeqpypgmsneevlefledgyr 222
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1370461664 383 -------PDGLRELLEDCWDADPEARLTAECVQQRL 411
Cdd:pfam07714 223 lpqpencPDELYDLMKQCWAYDPEDRPTFSELVEDL 258
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
208-417 4.60e-16

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 77.96  E-value: 4.60e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664  208 QVIREGGHAVVWAGQLQ--GKLVAIKAFPPRS----VAQFQAERALYELpgLQHDHIVRFITASRGgPGRLLsgplLVLE 281
Cdd:smart00220   5 EKLGEGSFGKVYLARDKktGKLVAIKVIKKKKikkdRERILREIKILKK--LKHPNIVRLYDVFED-EDKLY----LVME 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664  282 LHPKGSLCHYLTQY---TSDWgsSLRMALSLAQGLAFLHEErwqngqykpGIAHRDLSSQNVLIREDGSCAIGDLGLALV 358
Cdd:smart00220  78 YCEGGDLFDLLKKRgrlSEDE--ARFYLRQILSALEYLHSK---------GIVHRDLKPENILLDEDGHVKLADFGLARQ 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664  359 LPG----------------------------------------LT-QPPAWTPTQPQ--------GPAAIMEDPDG---- 385
Cdd:smart00220 147 LDPgeklttfvgtpeymapevllgkgygkavdiwslgvilyelLTgKPPFPGDDQLLelfkkigkPKPPFPPPEWDispe 226
                          250       260       270
                   ....*....|....*....|....*....|..
gi 1370461664  386 LRELLEDCWDADPEARLTAEcvqqrlAALAHP 417
Cdd:smart00220 227 AKDLIRKLLVKDPEKRLTAE------EALQHP 252
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
224-360 5.38e-16

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: 78.19  E-value: 5.38e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 224 QGKLVAIKAFPPRSVAQFQA--ERALYELPGLQHDHIVRFITASRGgPGRLlsGPLLVLELHPKGSLCHYL--TQYTSDW 299
Cdd:cd05038    32 TGEQVAVKSLQPSGEEQHMSdfKREIEILRTLDHEYIVKYKGVCES-PGRR--SLRLIMEYLPSGSLRDYLqrHRDQIDL 108
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370461664 300 GSSLRMALSLAQGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDLGLALVLP 360
Cdd:cd05038   109 KRLLLFASQICKGMEYLGSQR---------YIHRDLAARNILVESEDLVKISDFGLAKVLP 160
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
217-356 1.15e-14

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: 73.73  E-value: 1.15e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 217 VVWAGQLQGK-----LVAIKAfpPRSVAQFQAERALYE----LPGLQHDHIVRFI-TASRGGPgrllsgPLLVLELHPKG 286
Cdd:cd00192    10 EVYKGKLKGGdgktvDVAVKT--LKEDASESERKDFLKearvMKKLGHPNVVRLLgVCTEEEP------LYLVMEYMEGG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 287 SLCHYLTQYTSDWGSS----------LRMALSLAQGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDLGLA 356
Cdd:cd00192    82 DLLDFLRKSRPVFPSPepstlslkdlLSFAIQIAKGMEYLASKK---------FVHRDLAARNCLVGEDLVVKISDFGLS 152
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
218-411 2.34e-14

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: 72.70  E-value: 2.34e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 218 VWAGQLQGKL-VAIKAFPP--RSVAQFQAERALyeLPGLQHDHIVR-FITASRGGPgrllsgPLLVLELHPKGSLCHYLT 293
Cdd:cd05034    11 VWMGVWNGTTkVAVKTLKPgtMSPEAFLQEAQI--MKKLRHDKLVQlYAVCSDEEP------IYIVTELMSKGSLLDYLR 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 294 qytSDWGSSLR------MALSLAQGLAFLHEERWqngqykpgiAHRDLSSQNVLIREDGSCAIGDLGLALVLP------- 360
Cdd:cd05034    83 ---TGEGRALRlpqlidMAAQIASGMAYLESRNY---------IHRDLAARNILVGENNVCKVADFGLARLIEddeytar 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 361 -GLTQPPAWT-P-------------------------TQPQGPAAIMED-------------------PDGLRELLEDCW 394
Cdd:cd05034   151 eGAKFPIKWTaPeaalygrftiksdvwsfgillyeivTYGRVPYPGMTNrevleqvergyrmpkppgcPDELYDIMLQCW 230
                         250
                  ....*....|....*..
gi 1370461664 395 DADPEARLTAECVQQRL 411
Cdd:cd05034   231 KKEPEERPTFEYLQSFL 247
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
193-414 5.33e-14

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: 71.61  E-value: 5.33e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 193 WSVELQELPELcfsqQVIREGGHAVVWAGQLQGKLVAIKAFPPRSVA--QFQAERALyeLPGLQHDHIVRFITASrggpg 270
Cdd:cd05039     1 WAINKKDLKLG----ELIGKGEFGDVMLGDYRGQKVAVKCLKDDSTAaqAFLAEASV--MTTLRHPNLVQLLGVV----- 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 271 rLLSGPL-LVLELHPKGSLCHYLTQYtsdwGSS-------LRMALSLAQGLAFLHEERwqngqykpgIAHRDLSSQNVLI 342
Cdd:cd05039    70 -LEGNGLyIVTEYMAKGSLVDYLRSR----GRAvitrkdqLGFALDVCEGMEYLESKK---------FVHRDLAARNVLV 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 343 REDGSCAIGDLGLA----LVLPGLTQPPAWTptqpqGPAAI--------------------------------------- 379
Cdd:cd05039   136 SEDNVAKVSDFGLAkeasSNQDGGKLPIKWT-----APEALrekkfstksdvwsfgillweiysfgrvpypriplkdvvp 210
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1370461664 380 -------MEDPDG----LRELLEDCWDADPEARLTAECVQQRLAAL 414
Cdd:cd05039   211 hvekgyrMEAPEGcppeVYKVMKNCWELDPAKRPTFKQLREKLEHI 256
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
213-417 1.79e-13

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: 70.33  E-value: 1.79e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 213 GGHAVVWAG--QLQGKLVAIKAF-----PPRSVAQFQAERALyeLPGLQHDHIVRFITASRGGpgRLLSgplLVLELHPK 285
Cdd:cd06627    11 GAFGSVYKGlnLNTGEFVAIKQIslekiPKSDLKSVMGEIDL--LKKLNHPNIVKYIGSVKTK--DSLY---IILEYVEN 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 286 GSLCHYLTQYtSDWGSSLrMALSLAQ---GLAFLHEErwqngqykpGIAHRDLSSQNVLIREDGSCAIGDLGLALVLPGL 362
Cdd:cd06627    84 GSLASIIKKF-GKFPESL-VAVYIYQvleGLAYLHEQ---------GVIHRDIKGANILTTKDGLVKLADFGVATKLNEV 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 363 TQP---PAWTP-------------------------------TQP----QGPAA----IMEDP---------DGLRELLE 391
Cdd:cd06627   153 EKDensVVGTPywmapeviemsgvttasdiwsvgctvielltGNPpyydLQPMAalfrIVQDDhpplpenisPELRDFLL 232
                         250       260
                  ....*....|....*....|....*.
gi 1370461664 392 DCWDADPEARLTAEcvqqrlAALAHP 417
Cdd:cd06627   233 QCFQKDPTLRPSAK------ELLKHP 252
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
210-356 5.32e-13

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: 69.06  E-value: 5.32e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 210 IREGGHAVVWAGQL-QGKLVAIKAFPPRSVA----QFQAEraLYELPGLQHDHIVRFitasRGgpgrLLSGP---LLVLE 281
Cdd:cd14664     1 IGRGGAGTVYKGVMpNGTLVAVKRLKGEGTQggdhGFQAE--IQTLGMIRHRNIVRL----RG----YCSNPttnLLVYE 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 282 LHPKGSLCHYL-----TQYTSDWGSSLRMALSLAQGLAFLHEErwqngqYKPGIAHRDLSSQNVLIREDGSCAIGDLGLA 356
Cdd:cd14664    71 YMPNGSLGELLhsrpeSQPPLDWETRQRIALGSARGLAYLHHD------CSPLIIHRDVKSNNILLDEEFEAHVADFGLA 144
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
212-356 7.95e-13

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: 68.68  E-value: 7.95e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 212 EGGHAVVWAGQLQGKLVAIKAFPPRSVAQFQAERALYE-----LPGLQHDHIVRFITASRGGPGrllsgPLLVLELHPKG 286
Cdd:cd14158    25 EGGFGVVFKGYINDKNVAVKKLAAMVDISTEDLTKQFEqeiqvMAKCQHENLVELLGYSCDGPQ-----LCLVYTYMPNG 99
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370461664 287 SL-----CHYLTQYTSdWGSSLRMALSLAQGLAFLHEErwqngqykpGIAHRDLSSQNVLIREDGSCAIGDLGLA 356
Cdd:cd14158   100 SLldrlaCLNDTPPLS-WHMRCKIAQGTANGINYLHEN---------NHIHRDIKSANILLDETFVPKISDFGLA 164
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
202-359 1.25e-12

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: 67.79  E-value: 1.25e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 202 ELCFsQQVIREGGHAVVWAGQLQGKLVAIKAFPPR-----SVAQFQAER-ALYelpgLQHDHIVRFITASRGGPGRllSG 275
Cdd:cd13979     4 PLRL-QEPLGSGGFGSVYKATYKGETVAVKIVRRRrknraSRQSFWAELnAAR----LRHENIVRVLAAETGTDFA--SL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 276 PLLVLELHPKGSLCHYLTQYTSDWGSSLRM--ALSLAQGLAFLHEErwqngqykpGIAHRDLSSQNVLIREDGSCAIGDL 353
Cdd:cd13979    77 GLIIMEYCGNGTLQQLIYEGSEPLPLAHRIliSLDIARALRFCHSH---------GIVHLDVKPANILISEQGVCKLCDF 147

                  ....*.
gi 1370461664 354 GLALVL 359
Cdd:cd13979   148 GCSVKL 153
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
208-356 1.62e-12

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: 67.55  E-value: 1.62e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 208 QVIREGGHAVVWAGQ--LQGKLVAIK-----AFPPRSVAQFQAERALyeLPGLQHDHIVRFITASRGGPGRLLsgpllVL 280
Cdd:cd06606     6 ELLGKGSFGSVYLALnlDTGELMAVKevelsGDSEEELEALEREIRI--LSSLKHPNIVRYLGTERTENTLNI-----FL 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370461664 281 ELHPKGSLCHYLTQYTSDWGSSLRM-ALSLAQGLAFLHEErwqngqykpGIAHRDLSSQNVLIREDGSCAIGDLGLA 356
Cdd:cd06606    79 EYVPGGSLASLLKKFGKLPEPVVRKyTRQILEGLEYLHSN---------GIVHRDIKGANILVDSDGVVKLADFGCA 146
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
193-360 4.55e-12

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: 66.05  E-value: 4.55e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 193 WSVELQELPelcfSQQVIREGGHAVVWAGQLQGKLVAIKAFPPRSVAQ-FQAERALyeLPGLQHDHIVRFItasrggpGR 271
Cdd:cd05083     1 WLLNLQKLT----LGEIIGEGEFGAVLQGEYMGQKVAVKNIKCDVTAQaFLEETAV--MTKLQHKNLVRLL-------GV 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 272 LL-SGPLLVLELHPKGSLCHYLT---QYTSDWGSSLRMALSLAQGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGS 347
Cdd:cd05083    68 ILhNGLYIVMELMSKGNLVNFLRsrgRALVPVIQLLQFSLDVAEGMEYLESKK---------LVHRDLAARNILVSEDGV 138
                         170
                  ....*....|...
gi 1370461664 348 CAIGDLGLALVLP 360
Cdd:cd05083   139 AKISDFGLAKVGS 151
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
212-359 6.03e-12

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: 65.92  E-value: 6.03e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 212 EGGHAVVWAGQLQGKL-VAIKAFPPRSVA---QFQAEraLYELPGLQHDHIVR-FITASRGGPgrllsgPLLVLELHPKG 286
Cdd:cd05148    16 SGYFGEVWEGLWKNRVrVAIKILKSDDLLkqqDFQKE--VQALKRLRHKHLISlFAVCSVGEP------VYIITELMEKG 87
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370461664 287 SLCHYLTqytSDWGSSLR------MALSLAQGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDLGLALVL 359
Cdd:cd05148    88 SLLAFLR---SPEGQVLPvaslidMACQVAEGMAYLEEQN---------SIHRDLAARNILVGEDLVCKVADFGLARLI 154
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
225-360 8.84e-12

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: 65.81  E-value: 8.84e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 225 GKLVAIKAFPPRSVAQFQA-ERALYELPGLQHDHIVRFITASRGGPGRLLSgplLVLELHPKGSLCHYLTQYTS--DWGS 301
Cdd:cd14205    33 GEVVAVKKLQHSTEEHLRDfEREIEILKSLQHDNIVKYKGVCYSAGRRNLR---LIMEYLPYGSLRDYLQKHKEriDHIK 109
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1370461664 302 SLRMALSLAQGLAFLHEERWqngqykpgiAHRDLSSQNVLIREDGSCAIGDLGLALVLP 360
Cdd:cd14205   110 LLQYTSQICKGMEYLGTKRY---------IHRDLATRNILVENENRVKIGDFGLTKVLP 159
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
193-411 1.47e-11

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: 64.62  E-value: 1.47e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 193 WSVELQELPelcfSQQVIREGGHAVVWAGQLQGKLVAIKAFPPRSVAQ-FQAERALyeLPGLQHDHIVRFITASRGGPGR 271
Cdd:cd05082     1 WALNMKELK----LLQTIGKGEFGDVMLGDYRGNKVAVKCIKNDATAQaFLAEASV--MTQLRHSNLVQLLGVIVEEKGG 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 272 LLsgplLVLELHPKGSLCHYL-TQYTSDWGSS--LRMALSLAQGLAFLHEERWqngqykpgiAHRDLSSQNVLIREDGSC 348
Cdd:cd05082    75 LY----IVTEYMAKGSLVDYLrSRGRSVLGGDclLKFSLDVCEAMEYLEGNNF---------VHRDLAARNVLVSEDNVA 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 349 AIGDLGLALVLPGlTQPPAWTPTQPQGPAAI----------------------------------------------MED 382
Cdd:cd05082   142 KVSDFGLTKEASS-TQDTGKLPVKWTAPEALrekkfstksdvwsfgillweiysfgrvpypriplkdvvprvekgykMDA 220
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1370461664 383 PDG----LRELLEDCWDADPEARLTAECVQQRL 411
Cdd:cd05082   221 PDGcppaVYDVMKNCWHLDAAMRPSFLQLREQL 253
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
225-360 2.52e-11

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: 64.15  E-value: 2.52e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 225 GKLVAIKAFPPRSVAQFQA--ERALYELPGLQHDHIVRFITASRGGPGRLLsgpLLVLELHPKGSLCHYLTQYTSDWGSS 302
Cdd:cd05080    33 GEMVAVKALKADCGPQHRSgwKQEIDILKTLYHENIVKYKGCCSEQGGKSL---QLIMEYVPLGSLRDYLPKHSIGLAQL 109
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1370461664 303 LRMALSLAQGLAFLHEERWqngqykpgiAHRDLSSQNVLIREDGSCAIGDLGLALVLP 360
Cdd:cd05080   110 LLFAQQICEGMAYLHSQHY---------IHRDLAARNVLLDNDRLVKIGDFGLAKAVP 158
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
210-358 2.97e-11

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: 63.89  E-value: 2.97e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 210 IREGGHAVVW-AGQLQ-GKLVAIKAFPPRSVAQFQAERALYELPGLQ----HDHIVRFITASRGGpgrllSGPLLVLELH 283
Cdd:cd07832     8 IGEGAHGIVFkAKDREtGETVALKKVALRKLEGGIPNQALREIKALQacqgHPYVVKLRDVFPHG-----TGFVLVFEYM 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 284 PkGSLCHYLTQY-----TSDWGSSLRMALslaQGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDLGLALV 358
Cdd:cd07832    83 L-SSLSEVLRDEerpltEAQVKRYMRMLL---KGVAYMHANR---------IMHRDLKPANLLISSTGVLKIADFGLARL 149
TFP_LU_ECD_BMPR2_like cd23533
extracellular domain (ECD) found in the bone morphogenetic protein receptor type-2 (BMPR2) ...
22-119 3.37e-11

extracellular domain (ECD) found in the bone morphogenetic protein receptor type-2 (BMPR2)-like family; The BMPR2-like family includes BMPR2, activin receptor type-2A (ACTR-IIA), activin receptor type-2B (ACTR-IIB), and anti-Muellerian hormone type-2 receptor (AMHR2). On ligand binding, 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. BMPR2 binds to BMP7, BMP2, and less efficiently, BMP4. ACTR-IIA is the receptor for activin A, activin B, and inhibin A. It also interacts with type I receptor ACVR1 and bone morphogenetic protein 7 (BMP7). ACTR-IIB interacts with vacuolar protein sorting 39 (Vps39), dynein light chain Tctex-type 1 (DYNLT1), bone morphogenetic protein 2 (BMP2), and bone morphogenetic protein 3 (BMP3). AMHR2 is the receptor for anti-Muellerian hormone. 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: 467063  Cd Length: 93  Bit Score: 59.56  E-value: 3.37e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664  22 RTCVFFEAPGVRGSTKTlgellDTGTELPRAIRCLY-SRCCFGIWNLT-QDRAQVEMQGCRDSDEP-GCESLHCDPSPRa 98
Cdd:cd23533     1 IKCAYYKSSVSLSSTDE-----SDITSCNTTETCKSgSSYCFALWREDsNGNIEILLQGCWDSSGPnECDSSECIASKS- 74
                          90       100
                  ....*....|....*....|.
gi 1370461664  99 hpSPGSTLFTCSCGTDFCNAN 119
Cdd:cd23533    75 --PSLNNTKFCCCSGDLCNAN 93
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
221-360 5.90e-11

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: 62.99  E-value: 5.90e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 221 GQLQGKLVAIKAFPPRSVAQFQA-ERALYELPGLQHDHIVRFitasRG---GPGRllSGPLLVLELHPKGSLCHYLTQYT 296
Cdd:cd05081    29 GDNTGALVAVKQLQHSGPDQQRDfQREIQILKALHSDFIVKY----RGvsyGPGR--RSLRLVMEYLPSGCLRDFLQRHR 102
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370461664 297 SDWGSS--LRMALSLAQGLAFLHEERWqngqykpgiAHRDLSSQNVLIREDGSCAIGDLGLALVLP 360
Cdd:cd05081   103 ARLDASrlLLYSSQICKGMEYLGSRRC---------VHRDLAARNILVESEAHVKIADFGLAKLLP 159
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
257-356 1.12e-10

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: 62.36  E-value: 1.12e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 257 HIVRFI-TASRGGPgrllsgPLLVLELHPKGSLCHYLTQYTSD-----------WGSSLRMALSLAQGLAFLHEERwqng 324
Cdd:cd05032    70 HVVRLLgVVSTGQP------TLVVMELMAKGDLKSYLRSRRPEaennpglgpptLQKFIQMAAEIADGMAYLAAKK---- 139
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1370461664 325 qykpgIAHRDLSSQNVLIREDGSCAIGDLGLA 356
Cdd:cd05032   140 -----FVHRDLAARNCMVAEDLTVKIGDFGMT 166
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
210-354 1.68e-10

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: 61.39  E-value: 1.68e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 210 IREGGHAVVWAGQLQGKLVAIK-----AFPPRS-VAQFQAERALyeLPGLQHDHIVRFITASRGGPGRLLsgplLVLELH 283
Cdd:cd14064     1 IGSGSFGKVYKGRCRNKIVAIKryranTYCSKSdVDMFCREVSI--LCRLNHPCVIQFVGACLDDPSQFA----IVTQYV 74
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370461664 284 PKGSLCHYL--TQYTSDWGSSLRMALSLAQGLAFLHEERwqngqyKPgIAHRDLSSQNVLIREDGSCAIGDLG 354
Cdd:cd14064    75 SGGSLFSLLheQKRVIDLQSKLIIAVDVAKGMEYLHNLT------QP-IIHRDLNSHNILLYEDGHAVVADFG 140
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
221-355 4.18e-10

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: 60.71  E-value: 4.18e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 221 GQLQGKLVAIKAFPPRSVAQFQAE--RALYELPGLQHDHIVRF--ITASRGGpgrllSGPLLVLELHPKGSLCHYLTQYT 296
Cdd:cd05079    29 GDNTGEQVAVKSLKPESGGNHIADlkKEIEILRNLYHENIVKYkgICTEDGG-----NGIKLIMEFLPSGSLKEYLPRNK 103
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370461664 297 S--DWGSSLRMALSLAQGLAFLHEErwqngQYkpgiAHRDLSSQNVLIREDGSCAIGDLGL 355
Cdd:cd05079   104 NkiNLKQQLKYAVQICKGMDYLGSR-----QY----VHRDLAARNVLVESEHQVKIGDFGL 155
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
278-411 4.88e-10

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: 60.11  E-value: 4.88e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 278 LVLELHPKGSLCHYLtqytSDWGSSLR------MALSLAQGLAFLHEerwQNgqykpgIAHRDLSSQNVLIREDGSCAIG 351
Cdd:cd05068    80 IITELMKHGSLLEYL----QGKGRSLQlpqlidMAAQVASGMAYLES---QN------YIHRDLAARNVLVGENNICKVA 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 352 DLGLALVL---------PGLTQPPAWTP--------------------------TQPQGPAAIMED-------------- 382
Cdd:cd05068   147 DFGLARVIkvedeyearEGAKFPIKWTApeaanynrfsiksdvwsfgillteivTYGRIPYPGMTNaevlqqvergyrmp 226
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1370461664 383 -----PDGLRELLEDCWDADPEARLTAECVQQRL 411
Cdd:cd05068   227 cppncPPQLYDIMLECWKADPMERPTFETLQWKL 260
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
253-372 5.54e-10

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: 60.21  E-value: 5.54e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 253 LQHDHIVRFItasrggpGRLLSGPLL--VLELHPKGSLCHYLTQYTS--DWGSSLRMALSLAQGLAFLHEErwqngqykp 328
Cdd:cd14154    47 LDHPNVLKFI-------GVLYKDKKLnlITEYIPGGTLKDVLKDMARplPWAQRVRFAKDIASGMAYLHSM--------- 110
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1370461664 329 GIAHRDLSSQNVLIREDGSCAIGDLGLA-LVLPGLTQPPAWTPTQ 372
Cdd:cd14154   111 NIIHRDLNSHNCLVREDKTVVVADFGLArLIVEERLPSGNMSPSE 155
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
222-360 5.89e-10

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: 60.13  E-value: 5.89e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 222 QLQGKLVAIKAFPPRSVAQFQAERALYELPGLQ------HDHIVRFITASRGGpGRLLsgplLVLELHPKGSLCHYLTQY 295
Cdd:cd14052    23 VPTGKVYAVKKLKPNYAGAKDRLRRLEEVSILReltldgHDNIVQLIDSWEYH-GHLY----IQTELCENGSLDVFLSEL 97
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 296 T-----SDWgSSLRMALSLAQGLAFLHEErwqngqykpGIAHRDLSSQNVLIREDGSCAIGDLGLALVLP 360
Cdd:cd14052    98 GllgrlDEF-RVWKILVELSLGLRFIHDH---------HFVHLDLKPANVLITFEGTLKIGDFGMATVWP 157
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
218-411 6.98e-10

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: 59.52  E-value: 6.98e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 218 VWAGQLQG-KLVAIKAFPP--RSVAQFQAERALyeLPGLQHDHIVRFITASRGGPgrllsgPLLVLELHPKGSLCHYLTq 294
Cdd:cd05067    23 VWMGYYNGhTKVAIKSLKQgsMSPDAFLAEANL--MKQLQHQRLVRLYAVVTQEP------IYIITEYMENGSLVDFLK- 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 295 ytSDWGSSLR------MALSLAQGLAFLHEERWqngqykpgiAHRDLSSQNVLIREDGSCAIGDLGLALVL--------P 360
Cdd:cd05067    94 --TPSGIKLTinklldMAAQIAEGMAFIEERNY---------IHRDLRAANILVSDTLSCKIADFGLARLIedneytarE 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 361 GLTQPPAWTPTQP---------------------------------QGPAAI--------MEDPDG----LRELLEDCWD 395
Cdd:cd05067   163 GAKFPIKWTAPEAinygtftiksdvwsfgillteivthgripypgmTNPEVIqnlergyrMPRPDNcpeeLYQLMRLCWK 242
                         250
                  ....*....|....*.
gi 1370461664 396 ADPEARLTAECVQQRL 411
Cdd:cd05067   243 ERPEDRPTFEYLRSVL 258
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
210-359 9.60e-10

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: 59.24  E-value: 9.60e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 210 IREGGHAVV-----WAgQLQGKLVAIKAFPPR---SVAQFQAERALYE---LPGLQHDHIVR----FITASRGGpgrlls 274
Cdd:cd13994     1 IGKGATSVVrivtkKN-PRSGVLYAVKEYRRRddeSKRKDYVKRLTSEyiiSSKLHHPNIVKvldlCQDLHGKW------ 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 275 gpLLVLELHPKGSLCHYLTQYTS-DWGSSLRMALSLAQGLAFLHEErwqngqykpGIAHRDLSSQNVLIREDGSCAIGDL 353
Cdd:cd13994    74 --CLVMEYCPGGDLFTLIEKADSlSLEEKDCFFKQILRGVAYLHSH---------GIAHRDLKPENILLDEDGVLKLTDF 142

                  ....*.
gi 1370461664 354 GLALVL 359
Cdd:cd13994   143 GTAEVF 148
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
218-379 1.34e-09

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: 58.90  E-value: 1.34e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 218 VWAGQLQGKL-VAIKAFPP--RSVAQFQAERALyeLPGLQHDHIVR-FITASRGGPgrllsgPLLVLELHPKGSLCHYLT 293
Cdd:cd05072    23 VWMGYYNNSTkVAVKTLKPgtMSVQAFLEEANL--MKTLQHDKLVRlYAVVTKEEP------IYIITEYMAKGSLLDFLK 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 294 qytSDWGSSLRM------ALSLAQGLAFLHEERWqngqykpgiAHRDLSSQNVLIREDGSCAIGDLGLALVL-------- 359
Cdd:cd05072    95 ---SDEGGKVLLpklidfSAQIAEGMAYIERKNY---------IHRDLRAANVLVSESLMCKIADFGLARVIedneytar 162
                         170       180
                  ....*....|....*....|
gi 1370461664 360 PGLTQPPAWTptqpqGPAAI 379
Cdd:cd05072   163 EGAKFPIKWT-----APEAI 177
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
213-356 2.39e-09

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: 57.83  E-value: 2.39e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 213 GGHAVVWAGQLQGKLVAIKAFPPRSVaQFQAERALYELPGLQHDHIVRFITASRGGpgrllSGPLLVLELHPKGSLCHYL 292
Cdd:cd14058     4 GSFGVVCKARWRNQIVAVKIIESESE-KKAFEVEVRQLSRVDHPNIIKLYGACSNQ-----KPVCLVMEYAEGGSLYNVL 77
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370461664 293 ------TQYTSdwGSSLRMALSLAQGLAFLHeerwqNGQYKPgIAHRDLSSQNVLIREDGS-CAIGDLGLA 356
Cdd:cd14058    78 hgkepkPIYTA--AHAMSWALQCAKGVAYLH-----SMKPKA-LIHRDLKPPNLLLTNGGTvLKICDFGTA 140
PTK_HER3 cd05111
Pseudokinase domain of the Protein Tyrosine Kinase, HER3; HER3 (ErbB3) is a member of the EGFR ...
228-360 2.64e-09

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: 58.04  E-value: 2.64e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 228 VAIKAFPPRSVAQ-FQA-ERALYELPGLQHDHIVRFITASrggPGRLLSgplLVLELHPKGSLCHYLTQYTSDWGSS--L 303
Cdd:cd05111    39 VAIKVIQDRSGRQsFQAvTDHMLAIGSLDHAYIVRLLGIC---PGASLQ---LVTQLLPLGSLLDHVRQHRGSLGPQllL 112
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1370461664 304 RMALSLAQGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDLGLALVLP 360
Cdd:cd05111   113 NWCVQIAKGMYYLEEHR---------MVHRNLAARNVLLKSPSQVQVADFGVADLLY 160
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
228-361 3.37e-09

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: 57.81  E-value: 3.37e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 228 VAIKAFPPRSVAQFQAE--RALYELPGLQHDHIVRFITASrggpgrLLSGPLLVLELHPKGSLCHYLTQYTSDWGSS--L 303
Cdd:cd05057    39 VAIKVLREETGPKANEEilDEAYVMASVDHPHLVRLLGIC------LSSQVQLITQLMPLGCLLDYVRNHRDNIGSQllL 112
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1370461664 304 RMALSLAQGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDLGLALVLPG 361
Cdd:cd05057   113 NWCVQIAKGMSYLEEKR---------LVHRDLAARNVLVKTPNHVKITDFGLAKLLDV 161
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
210-360 4.12e-09

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: 57.23  E-value: 4.12e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 210 IREGGHAVVWAG--QLQGKLVAIKAFP-----PRSVAQFQAERALyeLPGLQHDHIVRFITASRGgPGRLLsgplLVLEL 282
Cdd:cd14009     1 IGRGSFATVWKGrhKQTGEVVAIKEISrkklnKKLQENLESEIAI--LKSIKHPNIVRLYDVQKT-EDFIY----LVLEY 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 283 HPKGSLCHYLTQY---TSDwgSSLRMALSLAQGLAFLHEErwqngqykpGIAHRDLSSQNVLIREDGSCA---IGDLGLA 356
Cdd:cd14009    74 CAGGDLSQYIRKRgrlPEA--VARHFMQQLASGLKFLRSK---------NIIHRDLKPQNLLLSTSGDDPvlkIADFGFA 142

                  ....
gi 1370461664 357 LVLP 360
Cdd:cd14009   143 RSLQ 146
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
209-417 6.12e-09

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: 56.47  E-value: 6.12e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 209 VIREGGHAVVWAGQ--LQGKLVAIKAFPPRSVAQFQAER---ALYEL-PGLQHDHIVR---FITASRGGpgrllsGPLLV 279
Cdd:cd05118     6 KIGEGAFGTVWLARdkVTGEKVAIKKIKNDFRHPKAALReikLLKHLnDVEGHPNIVKlldVFEHRGGN------HLCLV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 280 LEL-HPkgSLCHYLTQYTSDWGSSL--RMALSLAQGLAFLHEErwqngqykpGIAHRDLSSQNVLIREDGS-CAIGDLGL 355
Cdd:cd05118    80 FELmGM--NLYELIKDYPRGLPLDLikSYLYQLLQALDFLHSN---------GIIHRDLKPENILINLELGqLKLADFGL 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 356 ALVL--PGLTQPPA---------------WTPT----------------QPQGP--------AAIME--DPDGLRELLED 392
Cdd:cd05118   149 ARSFtsPPYTPYVAtrwyrapevllgakpYGSSidiwslgcilaelltgRPLFPgdsevdqlAKIVRllGTPEALDLLSK 228
                         250       260
                  ....*....|....*....|....*
gi 1370461664 393 CWDADPEARLTAEcvqqrlAALAHP 417
Cdd:cd05118   229 MLKYDPAKRITAS------QALAHP 247
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
212-356 7.94e-09

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: 56.62  E-value: 7.94e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 212 EGGHAVVWAGQ--LQGKLVAIKA--FPPRSVAQFQAERALYELPGLQHDHIVRF--ITASRggpgRLLSgplLVLE-LHP 284
Cdd:cd07844    10 EGSYATVYKGRskLTGQLVALKEirLEHEEGAPFTAIREASLLKDLKHANIVTLhdIIHTK----KTLT---LVFEyLDT 82
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370461664 285 KgslchyLTQYTSDWGSSLRMA------LSLAQGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDLGLA 356
Cdd:cd07844    83 D------LKQYMDDCGGGLSMHnvrlflFQLLRGLAYCHQRR---------VLHRDLKPQNLLISERGELKLADFGLA 145
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
213-342 8.44e-09

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: 56.47  E-value: 8.44e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 213 GGHAVVWAGQLQGKLVAIKAF---PPRSVAQFQAERALYELPG-------------------LQHDHIVRFITASrggpg 270
Cdd:cd14000     5 GGFGSVYRASYKGEPVAVKIFnkhTSSNFANVPADTMLRHLRAtdamknfrllrqeltvlshLHHPSIVYLLGIG----- 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370461664 271 rllSGPL-LVLELHPKGSLCHYLTQYTSDWGSSLRM-----ALSLAQGLAFLHEERwqngqykpgIAHRDLSSQNVLI 342
Cdd:cd14000    80 ---IHPLmLVLELAPLGSLDHLLQQDSRSFASLGRTlqqriALQVADGLRYLHSAM---------IIYRDLKSHNVLV 145
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
278-403 8.81e-09

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: 56.31  E-value: 8.81e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 278 LVLELHPKGSLCHYLTQYTSD--WGSSLRMALSLAQGLAFLHEERwqngqykPGIAHRDLSSQNVLIREDGSCAIGDLGL 355
Cdd:cd13978    69 LVMEYMENGSLKSLLEREIQDvpWSLRFRIIHEIALGMNFLHNMD-------PPLLHHDLKPENILLDNHFHVKISDFGL 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 356 ALV------------LPGLTQPPAWTP------------------------------TQP----QGPAAIM--------- 380
Cdd:cd13978   142 SKLgmksisanrrrgTENLGGTPIYMApeafddfnkkptsksdvysfaiviwavltrKEPfenaINPLLIMqivskgdrp 221
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1370461664 381 -----------EDPDGLRELLEDCWDADPEARLT 403
Cdd:cd13978   222 slddigrlkqiENVQELISLMIRCWDGNPDARPT 255
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
211-359 8.98e-09

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: 56.08  E-value: 8.98e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 211 REGGHAVVWaGQLQgklvaIKAFPPRSVAQFQAERALyeLPGLQHDHIVRFITASRGGPGRLLsgpLLVLELHPKGSLCH 290
Cdd:cd13983    23 TEEGIEVAW-NEIK-----LRKLPKAERQRFKQEIEI--LKSLKHPNIIKFYDSWESKSKKEV---IFITELMTSGTLKQ 91
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370461664 291 YLTQYT-------SDWGsslRMALslaQGLAFLHEErwqngqyKPGIAHRDLSSQNVLIR-EDGSCAIGDLGLALVL 359
Cdd:cd13983    92 YLKRFKrlklkviKSWC---RQIL---EGLNYLHTR-------DPPIIHRDLKCDNIFINgNTGEVKIGDLGLATLL 155
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
228-355 9.46e-09

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: 56.20  E-value: 9.46e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 228 VAIKAFPPRSVAQFQAE--RALYELPGLQHDHIVRFITASRGGPgrllsgPLLVLELHPKGSLCHYLTQYTSDWGSSLR- 304
Cdd:cd05060    26 VAVKTLKQEHEKAGKKEflREASVMAQLDHPCIVRLIGVCKGEP------LMLVMELAPLGPLLKYLKKRREIPVSDLKe 99
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1370461664 305 MALSLAQGLAFLHEERWqngqykpgiAHRDLSSQNVLIREDGSCAIGDLGL 355
Cdd:cd05060   100 LAHQVAMGMAYLESKHF---------VHRDLAARNVLLVNRHQAKISDFGM 141
PK_ILK cd14057
Pseudokinase domain of Integrin Linked Kinase; The pseudokinase domain shows similarity to ...
219-394 1.11e-08

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: 55.96  E-value: 1.11e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 219 WAGQLQG-----KLVAIKAFPPRSVAQFQAEralyeLPGLQ---HDHIVRFITASRGGPGrllsgPLLVLELHPKGSLCH 290
Cdd:cd14057    12 WKGRWQGndivaKILKVRDVTTRISRDFNEE-----YPRLRifsHPNVLPVLGACNSPPN-----LVVISQYMPYGSLYN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 291 YL---TQYTSDWGSSLRMALSLAQGLAFLHeerwqngQYKPGIAHRDLSSQNVLIREDGSCAI--GDLGLALVLPGLTQP 365
Cdd:cd14057    82 VLhegTGVVVDQSQAVKFALDIARGMAFLH-------TLEPLIPRHHLNSKHVMIDEDMTARInmADVKFSFQEPGKMYN 154
                         170       180
                  ....*....|....*....|....*....
gi 1370461664 366 PAWTptqpqGPAAIMEDPDGLRELLEDCW 394
Cdd:cd14057   155 PAWM-----APEALQKKPEDINRRSADMW 178
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
209-366 1.40e-08

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: 55.79  E-value: 1.40e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 209 VIREGGHAVVWAGQLQ--GKLVAIKAFPPRSVAQFQAERALYE---LPGLQHDHIVRFITASRGGpGRLLsgplLVLELH 283
Cdd:cd07833     8 VVGEGAYGVVLKCRNKatGEIVAIKKFKESEDDEDVKKTALREvkvLRQLRHENIVNLKEAFRRK-GRLY----LVFEYV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 284 PKgSLCHYLTQYTSDWGSSL--RMALSLAQGLAFLHeerwqngqyKPGIAHRDLSSQNVLIREDGSCAIGDLGLALVLPG 361
Cdd:cd07833    83 ER-TLLELLEASPGGLPPDAvrSYIWQLLQAIAYCH---------SHNIIHRDIKPENILVSESGVLKLCDFGFARALTA 152

                  ....*
gi 1370461664 362 LTQPP 366
Cdd:cd07833   153 RPASP 157
PTKc_HER4 cd05110
Catalytic domain of the Protein Tyrosine Kinase, HER4; PTKs catalyze the transfer of the ...
235-361 1.63e-08

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: 55.84  E-value: 1.63e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 235 PRSVAQFQAERALyeLPGLQHDHIVRFItasrggpGRLLSGPL-LVLELHPKGSLCHYLTQYTSDWGSSLRM--ALSLAQ 311
Cdd:cd05110    50 PKANVEFMDEALI--MASMDHPHLVRLL-------GVCLSPTIqLVTQLMPHGCLLDYVHEHKDNIGSQLLLnwCVQIAK 120
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1370461664 312 GLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDLGLALVLPG 361
Cdd:cd05110   121 GMMYLEERR---------LVHRDLAARNVLVKSPNHVKITDFGLARLLEG 161
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
236-356 1.77e-08

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: 55.39  E-value: 1.77e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 236 RSVAQFQAERALYE---LPGLQHDHIVRFITASRGgpgrLLSGP---LLVLELHPKGSLCHYLTQYTSDWGSSL-RMALS 308
Cdd:cd14033    37 RKLSKGERQRFSEEvemLKGLQHPNIVRFYDSWKS----TVRGHkciILVTELMTSGTLKTYLKRFREMKLKLLqRWSRQ 112
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1370461664 309 LAQGLAFLHEErwqngqyKPGIAHRDLSSQNVLIR-EDGSCAIGDLGLA 356
Cdd:cd14033   113 ILKGLHFLHSR-------CPPILHRDLKCDNIFITgPTGSVKIGDLGLA 154
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
223-360 2.19e-08

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: 55.08  E-value: 2.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 223 LQGKLVAIKafppRSVAQF----QAERALYELPGL----QHDHIVRFITASRGGpGRLLsgplLVLELHPKGSLchylTQ 294
Cdd:cd13997    23 VDGCLYAVK----KSKKPFrgpkERARALREVEAHaalgQHPNIVRYYSSWEEG-GHLY----IQMELCENGSL----QD 89
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370461664 295 YTSDWGSS--------LRMALSLAQGLAFLHEErwqngqykpGIAHRDLSSQNVLIREDGSCAIGDLGLALVLP 360
Cdd:cd13997    90 ALEELSPIsklseaevWDLLLQVALGLAFIHSK---------GIVHLDIKPDNIFISNKGTCKIGDFGLATRLE 154
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
214-356 2.27e-08

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: 55.07  E-value: 2.27e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 214 GHAVVWAGQLQGKLVAIKAFPPRSvAQFQAERALYE---LPGLQHDHIVRFITAsrggpgRLLSGPLLV-LELHPKGSLC 289
Cdd:cd14046    20 GQVVKVRNKLDGRYYAIKKIKLRS-ESKNNSRILREvmlLSRLNHQHVVRYYQA------WIERANLYIqMEYCEKSTLR 92
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370461664 290 H----YLTQYTSD-WgsslRMALSLAQGLAFLHEErwqngqykpGIAHRDLSSQNVLIREDGSCAIGDLGLA 356
Cdd:cd14046    93 DlidsGLFQDTDRlW----RLFRQILEGLAYIHSQ---------GIIHRDLKPVNIFLDSNGNVKIGDFGLA 151
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
209-356 2.33e-08

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: 54.90  E-value: 2.33e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 209 VIREGGHAVVWAGQ--LQGKLVAIKAFPPRSVAQFQ---AERALyeLPGLQHDHIVRFITASrggpgrLLSGPL-LVLEL 282
Cdd:cd05122     7 KIGKGGFGVVYKARhkKTGQIVAIKKINLESKEKKEsilNEIAI--LKKCKHPNIVKYYGSY------LKKDELwIVMEF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 283 HPKGSLchyltqytSDWGSSLRMALSLAQ----------GLAFLHEErwqngqykpGIAHRDLSSQNVLIREDGSCAIGD 352
Cdd:cd05122    79 CSGGSL--------KDLLKNTNKTLTEQQiayvckevlkGLEYLHSH---------GIIHRDIKAANILLTSDGEVKLID 141

                  ....
gi 1370461664 353 LGLA 356
Cdd:cd05122   142 FGLS 145
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
299-360 2.76e-08

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: 54.79  E-value: 2.76e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370461664 299 WGSSLRMALSLAQGLAFLHEErwqngqykpGIAHRDLSSQNVLIR--EDGSCAI-GDLGLALVLP 360
Cdd:cd14155    87 WTVRVKLALDIARGLSYLHSK---------GIFHRDLTSKNCLIKrdENGYTAVvGDFGLAEKIP 142
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
212-356 2.94e-08

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: 54.89  E-value: 2.94e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 212 EGGHAVVWAGQ--LQGKLVAIKAFP--PRSVAQ----FQAERALYELPGLQHDHIVRFITASrgGPGRLLSgplLVLELH 283
Cdd:cd07841    10 EGTYAVVYKARdkETGRIVAIKKIKlgERKEAKdginFTALREIKLLQELKHPNIIGLLDVF--GHKSNIN---LVFEFM 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 284 PkGSL-------CHYLTQytSDWGSSLRMALslaQGLAFLHEeRWqngqykpgIAHRDLSSQNVLIREDGSCAIGDLGLA 356
Cdd:cd07841    85 E-TDLekvikdkSIVLTP--ADIKSYMLMTL---RGLEYLHS-NW--------ILHRDLKPNNLLIASDGVLKLADFGLA 149
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
225-359 3.75e-08

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: 54.32  E-value: 3.75e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 225 GKLVAIKAFPPRSVAQFQAERALYE---LPGLQHDHIVRFITASrggpgrLLSGPL-LVLELHPKGSLCHYLTQYTSD-- 298
Cdd:cd08530    25 NQVYALKEVNLGSLSQKEREDSVNEirlLASVNHPNIIRYKEAF------LDGNRLcIVMEYAPFGDLSKLISKRKKKrr 98
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370461664 299 -------WgsslRMALSLAQGLAFLHEErwqngqykpGIAHRDLSSQNVLIREDGSCAIGDLGLALVL 359
Cdd:cd08530    99 lfpeddiW----RIFIQMLRGLKALHDQ---------KILHRDLKSANILLSAGDLVKIGDLGISKVL 153
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
208-356 4.10e-08

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: 54.14  E-value: 4.10e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 208 QVIREGGHAVVWAGQ--LQGKLVAIKAFpprSVAQFQAERALYE---LPGLQHDHIVRFITASrggpgrLLSGPL-LVLE 281
Cdd:cd06614     6 EKIGEGASGEVYKATdrATGKEVAIKKM---RLRKQNKELIINEiliMKECKHPNIVDYYDSY------LVGDELwVVME 76
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370461664 282 LHPKGSLCHYLTQYTSDWGSSlRMA---LSLAQGLAFLHeerwqngqyKPGIAHRDLSSQNVLIREDGSCAIGDLGLA 356
Cdd:cd06614    77 YMDGGSLTDIITQNPVRMNES-QIAyvcREVLQGLEYLH---------SQNVIHRDIKSDNILLSKDGSVKLADFGFA 144
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
253-366 4.85e-08

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: 54.19  E-value: 4.85e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 253 LQHDHIVRFItasrggpGRLLSGPLL--VLELHPKGSLCHYLTQYTSD--WGSSLRMALSLAQGLAFLHEERwqngqykp 328
Cdd:cd14221    47 LEHPNVLKFI-------GVLYKDKRLnfITEYIKGGTLRGIIKSMDSHypWSQRVSFAKDIASGMAYLHSMN-------- 111
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1370461664 329 gIAHRDLSSQNVLIREDGSCAIGDLGLALVLPGLTQPP 366
Cdd:cd14221   112 -IIHRDLNSHNCLVRENKSVVVADFGLARLMVDEKTQP 148
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
210-359 5.11e-08

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: 53.95  E-value: 5.11e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 210 IREGGHAVVWAG--QLQGKLVAIKAFPPRSVAQFQAERALYE---LPGLQHDHIVRFITAsrggpgrLLSGPLL--VLEL 282
Cdd:cd08529     8 LGKGSFGVVYKVvrKVDGRVYALKQIDISRMSRKMREEAIDEarvLSKLNSPYVIKYYDS-------FVDKGKLniVMEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 283 HPKGSLCHYLTQYTsdwGSSL------RMALSLAQGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDLGLA 356
Cdd:cd08529    81 AENGDLHSLIKSQR---GRPLpedqiwKFFIQTLLGLSHLHSKK---------ILHRDIKSMNIFLDKGDNVKIGDLGVA 148

                  ...
gi 1370461664 357 LVL 359
Cdd:cd08529   149 KIL 151
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
218-411 5.92e-08

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: 53.77  E-value: 5.92e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 218 VWAGQLQGKL-VAIKAFPPRSVA--QFQAERALYELpgLQHDHIVRFITASRGGPgrllsgPLLVLELHPKGSLCHYLTQ 294
Cdd:cd14203    11 VWMGTWNGTTkVAIKTLKPGTMSpeAFLEEAQIMKK--LRHDKLVQLYAVVSEEP------IYIVTEFMSKGSLLDFLKD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 295 YTsdwGSSLR------MALSLAQGLAFLHEERWqngqykpgiAHRDLSSQNVLIREDGSCAIGDLGLALVLP-------- 360
Cdd:cd14203    83 GE---GKYLKlpqlvdMAAQIASGMAYIERMNY---------IHRDLRAANILVGDNLVCKIADFGLARLIEdneytarq 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 361 GLTQPPAWTPTQPQ--GPAAIMED-------------------------------------------PDGLRELLEDCWD 395
Cdd:cd14203   151 GAKFPIKWTAPEAAlyGRFTIKSDvwsfgilltelvtkgrvpypgmnnrevleqvergyrmpcppgcPESLHELMCQCWR 230
                         250
                  ....*....|....*.
gi 1370461664 396 ADPEARLTAECVQQRL 411
Cdd:cd14203   231 KDPEERPTFEYLQSFL 246
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
209-356 6.16e-08

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: 53.88  E-value: 6.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 209 VIREGGHAVVWAGQLQ--GKLVAIKA---FPPRSVAQFQAERALY-ELPglQHDHIVRFI-TASRGGPGRllSGPLLVLE 281
Cdd:cd13985     7 QLGEGGFSYVYLAHDVntGRRYALKRmyfNDEEQLRVAIKEIEIMkRLC--GHPNIVQYYdSAILSSEGR--KEVLLLME 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 282 LHPkGSLCHYL-----TQYTSDwgSSLRMALSLAQGLAFLHeerwqngQYKPGIAHRDLSSQNVLIREDGSCAIGDLGLA 356
Cdd:cd13985    83 YCP-GSLVDILeksppSPLSEE--EVLRIFYQICQAVGHLH-------SQSPPIIHRDIKIENILFSNTGRFKLCDFGSA 152
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
253-371 8.32e-08

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: 53.41  E-value: 8.32e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 253 LQHDHIVRFItasrggpGRLLSGPLLVL--ELHPKGSLCHYLTQYTS-DWGSSLRMALSLAQGLAFLHEErwqngqykpG 329
Cdd:cd14222    47 LDHPNVLKFI-------GVLYKDKRLNLltEFIEGGTLKDFLRADDPfPWQQKVSFAKGIASGMAYLHSM---------S 110
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1370461664 330 IAHRDLSSQNVLIREDGSCAIGDLGLA-LVLPGLTQPPAWTPT 371
Cdd:cd14222   111 IIHRDLNSHNCLIKLDKTVVVADFGLSrLIVEEKKKPPPDKPT 153
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
212-342 8.82e-08

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: 53.03  E-value: 8.82e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 212 EGGHAVVWAGQLQGKLVAIKAFPPRSVAQFqAERALYELPGLQHDHIVRFITASrggpgrlLSGPLLVLELHPKGSLCHY 291
Cdd:cd14068     4 DGGFGSVYRAVYRGEDVAVKIFNKHTSFRL-LRQELVVLSHLHHPSLVALLAAG-------TAPRMLVMELAPKGSLDAL 75
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1370461664 292 LTQYTSDWGSSL--RMALSLAQGLAFLHEERwqngqykpgIAHRDLSSQNVLI 342
Cdd:cd14068    76 LQQDNASLTRTLqhRIALHVADGLRYLHSAM---------IIYRDLKPHNVLL 119
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
243-350 8.85e-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: 53.13  E-value: 8.85e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 243 AERALYELPGLQHDHIVRFITASRGGPGRLLSGPL-LVLELHPKGSLCHYLTQYTS-DWGSSLRMALSLAQGLAFLHeer 320
Cdd:cd14012    45 LEKELESLKKLRHPNLVSYLAFSIERRGRSDGWKVyLLTEYAPGGSLSELLDSVGSvPLDTARRWTLQLLEALEYLH--- 121
                          90       100       110
                  ....*....|....*....|....*....|
gi 1370461664 321 wqngqyKPGIAHRDLSSQNVLIREDGSCAI 350
Cdd:cd14012   122 ------RNGVVHKSLHAGNVLLDRDAGTGI 145
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
224-354 9.53e-08

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: 53.04  E-value: 9.53e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 224 QGKLVAIKAFpprsvaqFQAERALYELPGLQHDHIVRFItasrggpGRLLSGP--LLVLELHPKGSLCHYLTQYTS---D 298
Cdd:cd14060    17 QDKEVAVKKL-------LKIEKEAEILSVLSHRNIIQFY-------GAILEAPnyGIVTEYASYGSLFDYLNSNESeemD 82
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1370461664 299 WGSSLRMALSLAQGLAFLHEErwqngqyKP-GIAHRDLSSQNVLIREDGSCAIGDLG 354
Cdd:cd14060    83 MDQIMTWATDIAKGMHYLHME-------APvKVIHRDLKSRNVVIAADGVLKICDFG 132
PK_GC cd13992
Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows ...
217-373 9.66e-08

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: 53.16  E-value: 9.66e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 217 VVWAGQLQGKLVAIKAFPPRSVAQFQAERALYELPGLQHDHIVRFItasrggpGRLLSGPLL--VLELHPKGSLCHYL-- 292
Cdd:cd13992    17 VKKVGVYGGRTVAIKHITFSRTEKRTILQELNQLKELVHDNLNKFI-------GICINPPNIavVTEYCTRGSLQDVLln 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 293 TQYTSDWGSSLRMALSLAQGLAFLHEErwqngqykPGIAHRDLSSQNVLIREDGSCAIGDLGLALVLPGLTQPPAWTPTQ 372
Cdd:cd13992    90 REIKMDWMFKSSFIKDIVKGMNYLHSS--------SIGYHGRLKSSNCLVDSRWVVKLTDFGLRNLLEEQTNHQLDEDAQ 161

                  .
gi 1370461664 373 P 373
Cdd:cd13992   162 H 162
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
240-359 9.91e-08

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: 53.19  E-value: 9.91e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 240 QFQAERALyeLPGLQHDHIVRFITASRGgpgrLLSGP---LLVLELHPKGSLCHYLTQYTSDWGSSLR-MALSLAQGLAF 315
Cdd:cd14031    55 RFKEEAEM--LKGLQHPNIVRFYDSWES----VLKGKkciVLVTELMTSGTLKTYLKRFKVMKPKVLRsWCRQILKGLQF 128
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1370461664 316 LHEErwqngqyKPGIAHRDLSSQNVLIR-EDGSCAIGDLGLALVL 359
Cdd:cd14031   129 LHTR-------TPPIIHRDLKCDNIFITgPTGSVKIGDLGLATLM 166
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
212-359 1.03e-07

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: 52.94  E-value: 1.03e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 212 EGGHAVVWAGQLQ--GKLVAIKAFP------PRSVAQFQAERALYElpGLQHDHIVRFITASRGGpgrllSGPLLVLELH 283
Cdd:cd14099    11 KGGFAKCYEVTDMstGKVYAGKVVPkssltkPKQREKLKSEIKIHR--SLKHPNIVKFHDCFEDE-----ENVYILLELC 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 284 PKGSLCHYLTQytsdwgsslRMALS----------LAQGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDL 353
Cdd:cd14099    84 SNGSLMELLKR---------RKALTepevryfmrqILSGVKYLHSNR---------IIHRDLKLGNLFLDENMNVKIGDF 145

                  ....*.
gi 1370461664 354 GLALVL 359
Cdd:cd14099   146 GLAARL 151
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
209-362 1.84e-07

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: 52.41  E-value: 1.84e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 209 VIREGGHAVVWAGQ-LQGKL-VAIKAFPPRSVAQFQA---ERALYElpGLQHDHIVRFITA-SRGGPGRLlsgpllVLEL 282
Cdd:cd06624    15 VLGKGTFGVVYAARdLSTQVrIAIKEIPERDSREVQPlheEIALHS--RLSHKNIVQYLGSvSEDGFFKI------FMEQ 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 283 HPKGSLCHYLTqytSDWGSSLR----MALSLAQ---GLAFLHEERwqngqykpgIAHRDLSSQNVLIRE-DGSCAIGDLG 354
Cdd:cd06624    87 VPGGSLSALLR---SKWGPLKDnentIGYYTKQileGLKYLHDNK---------IVHRDIKGDNVLVNTySGVVKISDFG 154

                  ....*...
gi 1370461664 355 LALVLPGL 362
Cdd:cd06624   155 TSKRLAGI 162
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
234-356 3.10e-07

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: 51.73  E-value: 3.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 234 PPRSvaqfQAERALYE----LPGLQHDHIVRFItasrggpGRLLSGP--LLVLELHPKGSLCHYLTQYTSDWGSSLRMAL 307
Cdd:cd14027    29 PNCI----EHNEALLEegkmMNRLRHSRVVKLL-------GVILEEGkySLVMEYMEKGNLMHVLKKVSVPLSVKGRIIL 97
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1370461664 308 SLAQGLAFLHEErwqngqykpGIAHRDLSSQNVLIREDGSCAIGDLGLA 356
Cdd:cd14027    98 EIIEGMAYLHGK---------GVIHKDLKPENILVDNDFHIKIADLGLA 137
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
253-356 3.80e-07

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: 51.27  E-value: 3.80e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 253 LQHDHIVRFItasrggpGRLLSGPL-LVLELHPKGSLCHYLTQYtSDWGSSLRM---ALSLAQGLAFLHEERWqngqykp 328
Cdd:cd05056    64 FDHPHIVKLI-------GVITENPVwIVMELAPLGELRSYLQVN-KYSLDLASLilyAYQLSTALAYLESKRF------- 128
                          90       100
                  ....*....|....*....|....*...
gi 1370461664 329 giAHRDLSSQNVLIREDGSCAIGDLGLA 356
Cdd:cd05056   129 --VHRDIAARNVLVSSPDCVKLGDFGLS 154
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
250-356 4.94e-07

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: 51.20  E-value: 4.94e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 250 LPGLQHDHIVRFITaSRGGPGRLLSGPLLVLELHPKGSLCHYLTQYTSDWGSSLR-MALSLAQGLAFLHEErwqngqyKP 328
Cdd:cd14030    78 LKGLQHPNIVRFYD-SWESTVKGKKCIVLVTELMTSGTLKTYLKRFKVMKIKVLRsWCRQILKGLQFLHTR-------TP 149
                          90       100
                  ....*....|....*....|....*....
gi 1370461664 329 GIAHRDLSSQNVLIR-EDGSCAIGDLGLA 356
Cdd:cd14030   150 PIIHRDLKCDNIFITgPTGSVKIGDLGLA 178
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
225-359 5.33e-07

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: 50.92  E-value: 5.33e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 225 GKLVAIKAFPPRSVAQFQAERALYE---LPGLQHDHIVRFITASRGGpGRLlsgpLLVLELHPKGSLCHYLTQYTSDwGS 301
Cdd:cd08215    25 GKLYVLKEIDLSNMSEKEREEALNEvklLSKLKHPNIVKYYESFEEN-GKL----CIVMEYADGGDLAQKIKKQKKK-GQ 98
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370461664 302 S------LRMALSLAQGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDLGLALVL 359
Cdd:cd08215    99 PfpeeqiLDWFVQICLALKYLHSRK---------ILHRDLKTQNIFLTKDGVVKLGDFGISKVL 153
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
226-358 5.86e-07

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: 50.79  E-value: 5.86e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 226 KLVAIKAFPPRSVAQFQAERALYELpgLQHDHIVRFITASRGGPGRLLsgpllVLELHPKGSLchyLTQYTSDWGsslrM 305
Cdd:cd14069    32 KFVDMKRAPGDCPENIKKEVCIQKM--LSHKNVVRFYGHRREGEFQYL-----FLEYASGGEL---FDKIEPDVG----M 97
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370461664 306 ALSLAQ--------GLAFLHEErwqngqykpGIAHRDLSSQNVLIREDGSCAIGDLGLALV 358
Cdd:cd14069    98 PEDVAQfyfqqlmaGLKYLHSC---------GITHRDIKPENLLLDENDNLKISDFGLATV 149
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
209-356 5.90e-07

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: 50.85  E-value: 5.90e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 209 VIREGGHAVVWAGQLQGKLVAIKAF-------PPRSVAQFQAERALYELpgLQHDHIVrfitASRG---GPGRLLsgplL 278
Cdd:cd14061     1 VIGVGGFGKVYRGIWRGEEVAVKAArqdpdedISVTLENVRQEARLFWM--LRHPNII----ALRGvclQPPNLC----L 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 279 VLELHPKGSLCHYLTQYTSDWGSSLRMALSLAQGLAFLHEERwqngqyKPGIAHRDLSSQNVLIRE--------DGSCAI 350
Cdd:cd14061    71 VMEYARGGALNRVLAGRKIPPHVLVDWAIQIARGMNYLHNEA------PVPIIHRDLKSSNILILEaienedleNKTLKI 144

                  ....*.
gi 1370461664 351 GDLGLA 356
Cdd:cd14061   145 TDFGLA 150
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
208-359 5.96e-07

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: 50.86  E-value: 5.96e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 208 QVIREGGHAVVWAG--QLQGKLVAIKAFP--------PRSVAQFQAERALyeLPGLQHDHIVRFITASRggpgrlLSGPL 277
Cdd:cd06632     6 QLLGSGSFGSVYEGfnGDTGDFFAVKEVSlvdddkksRESVKQLEQEIAL--LSKLRHPNIVQYYGTER------EEDNL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 278 LV-LELHPKGSLCHYLTQYTSDWGSSLRM-ALSLAQGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDLGL 355
Cdd:cd06632    78 YIfLEYVPGGSIHKLLQRYGAFEEPVIRLyTRQILSGLAYLHSRN---------TVHRDIKGANILVDTNGVVKLADFGM 148

                  ....
gi 1370461664 356 ALVL 359
Cdd:cd06632   149 AKHV 152
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
208-411 6.71e-07

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: 50.52  E-value: 6.71e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 208 QVIREGGHAVVWAGQLQGK--LVAIKA----FPPRSVAQF-QAERALyelpgLQHDH--IVRFITASrggpgrLLSGPLL 278
Cdd:cd05041     1 EKIGRGNFGDVYRGVLKPDntEVAVKTcretLPPDLKRKFlQEARIL-----KQYDHpnIVKLIGVC------VQKQPIM 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 279 -VLELHPKGSLCHYLTQYTSDW--GSSLRMALSLAQGLAFLhEERwqngqykpGIAHRDLSSQNVLIREDGSCAIGDLGL 355
Cdd:cd05041    70 iVMELVPGGSLLTFLRKKGARLtvKQLLQMCLDAAAGMEYL-ESK--------NCIHRDLAARNCLVGENNVLKISDFGM 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 356 A--------LVLPGLTQ-PPAWTP--------------------------TQPQGPAAIMED------------------ 382
Cdd:cd05041   141 SreeedgeyTVSDGLKQiPIKWTApealnygrytsesdvwsfgillweifSLGATPYPGMSNqqtreqiesgyrmpapel 220
                         250       260       270
                  ....*....|....*....|....*....|
gi 1370461664 383 -PDGLRELLEDCWDADPEARLTAECVQQRL 411
Cdd:cd05041   221 cPEAVYRLMLQCWAYDPENRPSFSEIYNEL 250
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
212-360 6.88e-07

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: 50.42  E-value: 6.88e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 212 EGGHAVVWAG---QLQGKL--VAIKAFPPRSVAQFQA-ERALYE---LPGLQHDHIVRFItasrggpGRLLSGPL-LVLE 281
Cdd:cd05040     5 DGSFGVVRRGewtTPSGKViqVAVKCLKSDVLSQPNAmDDFLKEvnaMHSLDHPNLIRLY-------GVVLSSPLmMVTE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 282 LHPKGSLC--------HYLTQYTSDWgsslrmALSLAQGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDL 353
Cdd:cd05040    78 LAPLGSLLdrlrkdqgHFLISTLCDY------AVQIANGMAYLESKR---------FIHRDLAARNILLASKDKVKIGDF 142

                  ....*..
gi 1370461664 354 GLALVLP 360
Cdd:cd05040   143 GLMRALP 149
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
207-356 8.19e-07

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: 50.17  E-value: 8.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 207 QQVIREGGHAVVWAG--QLQGKLVAIKAFPPRSVAQFQAERALYE---LPGLQHDHIVRFI----TasrggPGRLLsgpl 277
Cdd:cd05117     5 GKVLGRGSFGVVRLAvhKKTGEEYAVKIIDKKKLKSEDEEMLRREieiLKRLDHPNIVKLYevfeD-----DKNLY---- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 278 LVLELHPKGSLCHYLTQYTSDwgsSLRMAL----SLAQGLAFLHEErwqngqykpGIAHRDLSSQNVLI---REDGSCAI 350
Cdd:cd05117    76 LVMELCTGGELFDRIVKKGSF---SEREAAkimkQILSAVAYLHSQ---------GIVHRDLKPENILLaskDPDSPIKI 143

                  ....*.
gi 1370461664 351 GDLGLA 356
Cdd:cd05117   144 IDFGLA 149
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
207-356 8.34e-07

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: 50.56  E-value: 8.34e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 207 QQVIREGGHAVVWAGQ--LQGKLVAIKAFP--------PRSvaqfqaerALYE---LPGLQHDHIVRFITASRGgPGRLL 273
Cdd:cd07829     4 LEKLGEGTYGVVYKAKdkKTGEIVALKKIRldneeegiPST--------ALREislLKELKHPNIVKLLDVIHT-ENKLY 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 274 sgplLVLELHPKgSLCHYLTQYTSdwGSSLRMALSLA----QGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCA 349
Cdd:cd07829    75 ----LVFEYCDQ-DLKKYLDKRPG--PLPPNLIKSIMyqllRGLAYCHSHR---------ILHRDLKPQNLLINRDGVLK 138

                  ....*..
gi 1370461664 350 IGDLGLA 356
Cdd:cd07829   139 LADFGLA 145
STKc_WNK2_like cd14032
Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the ...
236-356 9.38e-07

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: 50.08  E-value: 9.38e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 236 RSVAQFQAERALYE---LPGLQHDHIVRFIT--ASRGGPGRLLsgpLLVLELHPKGSLCHYLTQYTSDWGSSLR-MALSL 309
Cdd:cd14032    37 RKLTKVERQRFKEEaemLKGLQHPNIVRFYDfwESCAKGKRCI---VLVTELMTSGTLKTYLKRFKVMKPKVLRsWCRQI 113
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1370461664 310 AQGLAFLHEErwqngqyKPGIAHRDLSSQNVLIR-EDGSCAIGDLGLA 356
Cdd:cd14032   114 LKGLLFLHTR-------TPPIIHRDLKCDNIFITgPTGSVKIGDLGLA 154
PTKc_EGFR cd05108
Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs ...
228-359 1.39e-06

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: 50.02  E-value: 1.39e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 228 VAIK----AFPPRSVAQFQAERalYELPGLQHDHIVRFITASrggpgrLLSGPLLVLELHPKGSLCHYLTQYTSDWGSS- 302
Cdd:cd05108    39 VAIKelreATSPKANKEILDEA--YVMASVDNPHVCRLLGIC------LTSTVQLITQLMPFGCLLDYVREHKDNIGSQy 110
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1370461664 303 -LRMALSLAQGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDLGLALVL 359
Cdd:cd05108   111 lLNWCVQIAKGMNYLEDRR---------LVHRDLAARNVLVKTPQHVKITDFGLAKLL 159
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
225-377 1.43e-06

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: 49.60  E-value: 1.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 225 GKLVAIKAFPPRsVAQFQAERALYE---LPGLQHDHIVRFITAsrggpgRLLSGPLLV-LELHPKGSLCHYLTQYTS--- 297
Cdd:cd13996    31 GVTYAIKKIRLT-EKSSASEKVLREvkaLAKLNHPNIVRYYTA------WVEEPPLYIqMELCEGGTLRDWIDRRNSssk 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 298 -DWGSSLRMALSLAQGLAFLHEErwqngqykpGIAHRDLSSQNVLI-REDGSCAIGDLGLALVLpGLTQPPAWTPTQPQG 375
Cdd:cd13996   104 nDRKLALELFKQILKGVSYIHSK---------GIVHRDLKPSNIFLdNDDLQVKIGDFGLATSI-GNQKRELNNLNNNNN 173

                  ..
gi 1370461664 376 PA 377
Cdd:cd13996   174 GN 175
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
193-379 1.66e-06

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: 49.64  E-value: 1.66e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 193 WSVELQELPELCFS-QQVIREGGHAVVWAGQLQGKL-VAIKAFPP--RSVAQFQAERALyeLPGLQHDHIVRFITASRGG 268
Cdd:cd05073     1 WEKDAWEIPRESLKlEKKLGAGQFGEVWMATYNKHTkVAVKTMKPgsMSVEAFLAEANV--MKTLQHDKLVKLHAVVTKE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 269 PgrllsgPLLVLELHPKGSLCHYLTqytSDWGSSLRM------ALSLAQGLAFLHEERWqngqykpgiAHRDLSSQNVLI 342
Cdd:cd05073    79 P------IYIITEFMAKGSLLDFLK---SDEGSKQPLpklidfSAQIAEGMAFIEQRNY---------IHRDLRAANILV 140
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1370461664 343 REDGSCAIGDLGLALVL--------PGLTQPPAWTptqpqGPAAI 379
Cdd:cd05073   141 SASLVCKIADFGLARVIedneytarEGAKFPIKWT-----APEAI 180
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
212-356 1.70e-06

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: 49.57  E-value: 1.70e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 212 EGGHAVVWAG--QLQGKLVAIKAFPPRSV--AQFQAERALYELPGLQHDHIVRF--ITASRggpgrllSGPLLVLElHPK 285
Cdd:cd07870    10 EGSYATVYKGisRINGQLVALKVISMKTEegVPFTAIREASLLKGLKHANIVLLhdIIHTK-------ETLTFVFE-YMH 81
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370461664 286 GSLCHYLTQYTSDWGS-SLRMAL-SLAQGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDLGLA 356
Cdd:cd07870    82 TDLAQYMIQHPGGLHPyNVRLFMfQLLRGLAYIHGQH---------ILHRDLKPQNLLISYLGELKLADFGLA 145
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
207-359 1.79e-06

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: 49.42  E-value: 1.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 207 QQVIREGGHAVVWAGQLQ--GKLVAIKafpprSVAQ---FQaERALYELPGLQHDHIVR----FITASRGGPGRLLSgpl 277
Cdd:cd14137     9 EKVIGSGSFGVVYQAKLLetGEVVAIK-----KVLQdkrYK-NRELQIMRRLKHPNIVKlkyfFYSSGEKKDEVYLN--- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 278 LVLELHPKgSLCHYLTQYtsdWGSSLRMALS--------LAQGLAFLHeerwqngqyKPGIAHRDLSSQNVLI-REDGSC 348
Cdd:cd14137    80 LVMEYMPE-TLYRVIRHY---SKNKQTIPIIyvklysyqLFRGLAYLH---------SLGICHRDIKPQNLLVdPETGVL 146
                         170
                  ....*....|.
gi 1370461664 349 AIGDLGLALVL 359
Cdd:cd14137   147 KLCDFGSAKRL 157
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
212-411 2.08e-06

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: 49.30  E-value: 2.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 212 EGGHAVVWAGQLQGKL-VAIKAFPPRSVAQFQAERALYELPGLQHDHIVRFITASRGGPgrllsgPLLVLELHPKGSLCH 290
Cdd:cd05069    22 QGCFGEVWMGTWNGTTkVAIKTLKPGTMMPEAFLQEAQIMKKLRHDKLVPLYAVVSEEP------IYIVTEFMGKGSLLD 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 291 YLTQYTsdwGSSLR------MALSLAQGLAFLHEERWqngqykpgiAHRDLSSQNVLIREDGSCAIGDLGLALVLP---- 360
Cdd:cd05069    96 FLKEGD---GKYLKlpqlvdMAAQIADGMAYIERMNY---------IHRDLRAANILVGDNLVCKIADFGLARLIEdney 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 361 ----GLTQPPAWTPTQPQ--GPAAIMED-------------------------------------------PDGLRELLE 391
Cdd:cd05069   164 tarqGAKFPIKWTAPEAAlyGRFTIKSDvwsfgilltelvtkgrvpypgmvnrevleqvergyrmpcpqgcPESLHELMK 243
                         250       260
                  ....*....|....*....|
gi 1370461664 392 DCWDADPEARLTAECVQQRL 411
Cdd:cd05069   244 LCWKKDPDERPTFEYIQSFL 263
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
210-371 2.24e-06

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: 49.06  E-value: 2.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 210 IREGGHAVVWAGQLQ--GKLVAIKAFPPRSVAQFQAER-ALYELPGLQHDHiVRFITA---SRGGPGRLLsgplLVLELH 283
Cdd:cd05577     1 LGRGGFGEVCACQVKatGKMYACKKLDKKRIKKKKGETmALNEKIILEKVS-SPFIVSlayAFETKDKLC----LVLTLM 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 284 PKGSLCHYLTQYTSDWGSSLRMALSLAQ---GLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDLGLALVLP 360
Cdd:cd05577    76 NGGDLKYHIYNVGTRGFSEARAIFYAAEiicGLEHLHNRF---------IVYRDLKPENILLDDHGHVRISDLGLAVEFK 146
                         170
                  ....*....|.
gi 1370461664 361 GLTQPPAWTPT 371
Cdd:cd05577   147 GGKKIKGRVGT 157
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
253-360 2.35e-06

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: 49.03  E-value: 2.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 253 LQHDHIVRFITASRGgPGRLLsgplLVLELHPKGSLCHYLTQYTS--DWGSSLRMALSLAQGLAFLHEERwqngqykpgI 330
Cdd:cd14065    45 LSHPNILRFIGVCVK-DNKLN----FITEYVNGGTLEELLKSMDEqlPWSQRVSLAKDIASGMAYLHSKN---------I 110
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1370461664 331 AHRDLSSQNVLIREDG---SCAIGDLGLALVLP 360
Cdd:cd14065   111 IHRDLNSKNCLVREANrgrNAVVADFGLAREMP 143
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
278-371 2.64e-06

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: 48.86  E-value: 2.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 278 LVLELHPKGSLCHYLTQ---YTSDWGSslRMALSLAQGLAFLHEErwqngqykpGIAHRDLSSQNVLIREDG----SCAI 350
Cdd:cd14095    75 LVMELVKGGDLFDAITSstkFTERDAS--RMVTDLAQALKYLHSL---------SIVHRDIKPENLLVVEHEdgskSLKL 143
                          90       100
                  ....*....|....*....|.
gi 1370461664 351 GDLGLALVLPGLTQPPAWTPT 371
Cdd:cd14095   144 ADFGLATEVKEPLFTVCGTPT 164
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
208-356 2.78e-06

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: 48.72  E-value: 2.78e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 208 QVIREGGHAVVWAGQ--LQGKLVAIK--AFPPRSVAQFQAERALYELPGLQHDHIVRFITASRGGPGRLLSGPL------ 277
Cdd:cd14048    12 QCLGRGGFGVVFEAKnkVDDCNYAVKriRLPNNELAREKVLREVRALAKLDHPGIVRYFNAWLERPPEGWQEKMdevyly 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 278 LVLELHPKGSLCHYL----TQYTSDWGSSLRMALSLAQGLAFLHEErwqngqykpGIAHRDLSSQNVLIREDGSCAIGDL 353
Cdd:cd14048    92 IQMQLCRKENLKDWMnrrcTMESRELFVCLNIFKQIASAVEYLHSK---------GLIHRDLKPSNVFFSLDDVVKVGDF 162

                  ...
gi 1370461664 354 GLA 356
Cdd:cd14048   163 GLV 165
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
212-356 3.14e-06

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: 48.63  E-value: 3.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 212 EGGHAVVWAGQ--LQGKLVAIKafpprsVAQFQAE--------RALYELPGLQHDHIVRFI----TASRggpgrllsgPL 277
Cdd:cd07836    10 EGTYATVYKGRnrTTGEIVALK------EIHLDAEegtpstaiREISLMKELKHENIVRLHdvihTENK---------LM 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 278 LVLElHPKGSLCHYLTQYTSDWGSSLRMALS----LAQGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDL 353
Cdd:cd07836    75 LVFE-YMDKDLKKYMDTHGVRGALDPNTVKSftyqLLKGIAFCHENR---------VLHRDLKPQNLLINKRGELKLADF 144

                  ...
gi 1370461664 354 GLA 356
Cdd:cd07836   145 GLA 147
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
201-414 3.61e-06

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: 48.52  E-value: 3.61e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 201 PELCFSQQVIREGGHAVVWAGQLQ--GK---LVAIKAFPPRSVAQFQAErALYE---LPGLQHDHIVRF---ITASRggp 269
Cdd:cd05033     3 ASYVTIEKVIGGGEFGEVCSGSLKlpGKkeiDVAIKTLKSGYSDKQRLD-FLTEasiMGQFDHPNVIRLegvVTKSR--- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 270 grllsgPLL-VLELHPKGSLCHYLTQYTSD--WGSSLRMALSLAQGLAFLHEErwqngqykpGIAHRDLSSQNVLIREDG 346
Cdd:cd05033    79 ------PVMiVTEYMENGSLDKFLRENDGKftVTQLVGMLRGIASGMKYLSEM---------NYVHRDLAARNILVNSDL 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 347 SCAIGDLGLALVLPGL---------------TQP------------------------------PAWTPTQPQGPAAIME 381
Cdd:cd05033   144 VCKVSDFGLSRRLEDSeatyttkggkipirwTAPeaiayrkftsasdvwsfgivmwevmsygerPYWDMSNQDVIKAVED 223
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1370461664 382 D---------PDGLRELLEDCWDADPEARLTAECVQQRLAAL 414
Cdd:cd05033   224 GyrlpppmdcPSALYQLMLDCWQKDRNERPTFSQIVSTLDKM 265
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
193-411 3.77e-06

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: 48.53  E-value: 3.77e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 193 WSVELQELpelcFSQQVIREGGHAVVWAGQLQGKL-VAIKAFPPRSVAQFQAERALYELPGLQHDHIVRFITASRGGPgr 271
Cdd:cd05070     4 WEIPRESL----QLIKRLGNGQFGEVWMGTWNGNTkVAIKTLKPGTMSPESFLEEAQIMKKLKHDKLVQLYAVVSEEP-- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 272 llsgPLLVLELHPKGSLCHYLTQYTsdwGSSLR------MALSLAQGLAFLHEERWqngqykpgiAHRDLSSQNVLIRED 345
Cdd:cd05070    78 ----IYIVTEYMSKGSLLDFLKDGE---GRALKlpnlvdMAAQVAAGMAYIERMNY---------IHRDLRSANILVGNG 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 346 GSCAIGDLGLALVLP--------GLTQPPAWTP--------------------------TQPQGPAAIMED--------- 382
Cdd:cd05070   142 LICKIADFGLARLIEdneytarqGAKFPIKWTApeaalygrftiksdvwsfgilltelvTKGRVPYPGMNNrevleqver 221
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1370461664 383 ----------PDGLRELLEDCWDADPEARLTAECVQQRL 411
Cdd:cd05070   222 gyrmpcpqdcPISLHELMIHCWKKDPEERPTFEYLQGFL 260
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
207-360 3.92e-06

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: 48.27  E-value: 3.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 207 QQVIREGGHAVVWAGQ--LQGKLVAIKAF----PPRSVAQFQAERALYELPGlqHDHIVRFITASRGGP---GRLLSGPL 277
Cdd:cd14036     5 KRVIAEGGFAFVYEAQdvGTGKEYALKRLlsneEEKNKAIIQEINFMKKLSG--HPNIVQFCSAASIGKeesDQGQAEYL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 278 LVLELhPKGSLCHYLTQYTSDWGSS----LRMALSLAQGLAFLHEErwqngqyKPGIAHRDLSSQNVLIREDGSCAIGDL 353
Cdd:cd14036    83 LLTEL-CKGQLVDFVKKVEAPGPFSpdtvLKIFYQTCRAVQHMHKQ-------SPPIIHRDLKIENLLIGNQGQIKLCDF 154

                  ....*..
gi 1370461664 354 GLALVLP 360
Cdd:cd14036   155 GSATTEA 161
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
212-356 4.11e-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: 4.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 212 EGGHAVVWAG--QLQGKLVAIKA--FPPRSVAQFQAERALYELPGLQHDHIVRF--ITASRggpgRLLSgplLVLELHPK 285
Cdd:cd07873    12 EGTYATVYKGrsKLTDNLVALKEirLEHEEGAPCTAIREVSLLKDLKHANIVTLhdIIHTE----KSLT---LVFEYLDK 84
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370461664 286 GslchyLTQYTSDWGSSLRM------ALSLAQGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDLGLA 356
Cdd:cd07873    85 D-----LKQYLDDCGNSINMhnvklfLFQLLRGLAYCHRRK---------VLHRDLKPQNLLINERGELKLADFGLA 147
PTKc_InsR cd05061
Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer ...
250-355 4.40e-06

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: 48.43  E-value: 4.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 250 LPGLQHDHIVRFI-TASRGGPgrllsgPLLVLELHPKGSLCHYLTQYTSDWGSS-----------LRMALSLAQGLAFLH 317
Cdd:cd05061    63 MKGFTCHHVVRLLgVVSKGQP------TLVVMELMAHGDLKSYLRSLRPEAENNpgrppptlqemIQMAAEIADGMAYLN 136
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1370461664 318 EERWqngqykpgiAHRDLSSQNVLIREDGSCAIGDLGL 355
Cdd:cd05061   137 AKKF---------VHRDLAARNCMVAHDFTVKIGDFGM 165
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
209-356 5.23e-06

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: 48.11  E-value: 5.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 209 VIREGGHAVVWAGQLQGKLVAIKAF---PPRSVA----QFQAERALYELpgLQHDHIVRFitasrggPGRLLSGP--LLV 279
Cdd:cd14146     1 IIGVGGFGKVYRATWKGQEVAVKAArqdPDEDIKataeSVRQEAKLFSM--LRHPNIIKL-------EGVCLEEPnlCLV 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 280 LELHPKGSLCHYLTQYTSDWGSS----------LRMALSLAQGLAFLHEErwqngQYKPgIAHRDLSSQNVLIRE----D 345
Cdd:cd14146    72 MEFARGGTLNRALAAANAAPGPRrarripphilVNWAVQIARGMLYLHEE-----AVVP-ILHRDLKSSNILLLEkiehD 145
                         170
                  ....*....|....*
gi 1370461664 346 GSC----AIGDLGLA 356
Cdd:cd14146   146 DICnktlKITDFGLA 160
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
212-356 5.91e-06

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: 48.08  E-value: 5.91e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 212 EGGHAVVWAG--QLQGKLVAIKA--FPPRSVAQFQAERALYELPGLQHDHIVRF--ITASRggpgRLLSgplLVLELhpk 285
Cdd:cd07871    15 EGTYATVFKGrsKLTENLVALKEirLEHEEGAPCTAIREVSLLKNLKHANIVTLhdIIHTE----RCLT---LVFEY--- 84
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370461664 286 gsLCHYLTQYTSDWGSSLRM------ALSLAQGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDLGLA 356
Cdd:cd07871    85 --LDSDLKQYLDNCGNLMSMhnvkifMFQLLRGLSYCHKRK---------ILHRDLKPQNLLINEKGELKLADFGLA 150
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
278-396 6.57e-06

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: 47.72  E-value: 6.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 278 LVLELHPKGSLCHYLT---QYTSDWGSSlrMALSLAQGLAFLHeerwqngqyKPGIAHRDLSSQNVLIRE--DG--SCAI 350
Cdd:cd14184    76 LVMELVKGGDLFDAITsstKYTERDASA--MVYNLASALKYLH---------GLCIVHRDIKPENLLVCEypDGtkSLKL 144
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1370461664 351 GDLGLALVLPGLTQPPAWTPTQpQGPAAIMEDPDGLRellEDCWDA 396
Cdd:cd14184   145 GDFGLATVVEGPLYTVCGTPTY-VAPEIIAETGYGLK---VDIWAA 186
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
278-417 6.96e-06

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: 47.73  E-value: 6.96e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 278 LVLELHPKGSLCHYLTQ-YTSDWGSSLRMALSLAQGLAFLHeerwqngqyKPGIAHRDLSSQNVLIREDGSCAIGDLGLA 356
Cdd:cd14093    86 LVFELCRKGELFDYLTEvVTLSEKKTRRIMRQLFEAVEFLH---------SLNIVHRDLKPENILLDDNLNVKISDFGFA 156
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 357 LVL-----------------------------PGLTQ------------------PPAWTPTQPQGPAAIME------DP 383
Cdd:cd14093   157 TRLdegeklrelcgtpgylapevlkcsmydnaPGYGKevdmwacgvimytllagcPPFWHRKQMVMLRNIMEgkyefgSP 236
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1370461664 384 ------DGLRELLEDCWDADPEARLTAEcvqqrlAALAHP 417
Cdd:cd14093   237 ewddisDTAKDLISKLLVVDPKKRLTAE------EALEHP 270
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
209-356 7.60e-06

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: 47.53  E-value: 7.60e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 209 VIREGGHAVVWAG--QLQGKLVAIKA--FPPRSVAQFQAERALYE--------LPGLQHDHIVRFITASrggpgrlLSGP 276
Cdd:cd06628     7 LIGSGSFGSVYLGmnASSGELMAVKQveLPSVSAENKDRKKSMLDalqreialLRELQHENIVQYLGSS-------SDAN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 277 LL--VLELHPKGSLCHYLTQYTSDWGSSLR-MALSLAQGLAFLHEErwqngqykpGIAHRDLSSQNVLIREDGSCAIGDL 353
Cdd:cd06628    80 HLniFLEYVPGGSVATLLNNYGAFEESLVRnFVRQILKGLNYLHNR---------GIIHRDIKGANILVDNKGGIKISDF 150

                  ...
gi 1370461664 354 GLA 356
Cdd:cd06628   151 GIS 153
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
225-359 7.88e-06

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: 47.20  E-value: 7.88e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 225 GKLVAIK--AFPPRSVAQFQAERALYELPGLQHDHIVRFITA-SRGGPgrlLSgplLVLELHPKGSLcHYLTQYTSDWGS 301
Cdd:cd06623    26 GKIYALKkiHVDGDEEFRKQLLRELKTLRSCESPYVVKCYGAfYKEGE---IS---IVLEYMDGGSL-ADLLKKVGKIPE 98
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 302 SLRMALS--LAQGLAFLHEERwqngqykpGIAHRDLSSQNVLIREDGSCAIGDLGLALVL 359
Cdd:cd06623    99 PVLAYIArqILKGLDYLHTKR--------HIIHRDIKPSNLLINSKGEVKIADFGISKVL 150
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
250-354 8.08e-06

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: 47.38  E-value: 8.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 250 LPGLQHDHIVRFITASRGGpgRLLSgplLVLELHPKGSLCHYLTQYTSDWGSSLRMALS-LAQGLAFLHeerwqngqyKP 328
Cdd:cd06629    62 LKDLDHPNIVQYLGFEETE--DYFS---IFLEYVPGGSIGSCLRKYGKFEEDLVRFFTRqILDGLAYLH---------SK 127
                          90       100
                  ....*....|....*....|....*.
gi 1370461664 329 GIAHRDLSSQNVLIREDGSCAIGDLG 354
Cdd:cd06629   128 GILHRDLKADNILVDLEGICKISDFG 153
PTKc_HER2 cd05109
Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the ...
261-359 8.29e-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: 47.33  E-value: 8.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 261 FITASRGGP--GRLL-----SGPLLVLELHPKGSLCHYLTQYTSDWGSS--LRMALSLAQGLAFLHEERwqngqykpgIA 331
Cdd:cd05109    61 YVMAGVGSPyvCRLLgicltSTVQLVTQLMPYGCLLDYVRENKDRIGSQdlLNWCVQIAKGMSYLEEVR---------LV 131
                          90       100
                  ....*....|....*....|....*...
gi 1370461664 332 HRDLSSQNVLIREDGSCAIGDLGLALVL 359
Cdd:cd05109   132 HRDLAARNVLVKSPNHVKITDFGLARLL 159
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
207-355 9.17e-06

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: 47.27  E-value: 9.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 207 QQVIREGGHAVVWAGQ--LQGKLVAIKafpprSVAQF------QAERALYE---LPGLQHDHIVRFITAsrggpgrLLSG 275
Cdd:cd08224     5 EKKIGKGQFSVVYRARclLDGRLVALK-----KVQIFemmdakARQDCLKEidlLQQLNHPNIIKYLAS-------FIEN 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 276 PLL--VLELHPKGSLCHYLTQYTSD---------WgsslRMALSLAQGLAFLHEERwqngqykpgIAHRDLSSQNVLIRE 344
Cdd:cd08224    73 NELniVLELADAGDLSRLIKHFKKQkrlipertiW----KYFVQLCSALEHMHSKR---------IMHRDIKPANVFITA 139
                         170
                  ....*....|.
gi 1370461664 345 DGSCAIGDLGL 355
Cdd:cd08224   140 NGVVKLGDLGL 150
PTKc_TrkA cd05092
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze ...
227-356 9.67e-06

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: 47.27  E-value: 9.67e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 227 LVAIKAFPPRSVA---QFQAERALyeLPGLQHDHIVRFITASRggPGRLLsgpLLVLELHPKGSLCHYLTQYTSD----- 298
Cdd:cd05092    37 LVAVKALKEATESarqDFQREAEL--LTVLQHQHIVRFYGVCT--EGEPL---IMVFEYMRHGDLNRFLRSHGPDakild 109
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370461664 299 -----------WGSSLRMALSLAQGLAFLHEERWqngqykpgiAHRDLSSQNVLIREDGSCAIGDLGLA 356
Cdd:cd05092   110 ggegqapgqltLGQMLQIASQIASGMVYLASLHF---------VHRDLATRNCLVGQGLVVKIGDFGMS 169
TFP_LU_ECD_Wit cd23618
extracellular domain (ECD) found in Drosophila melanogaster Wishful thinking (Wit) and similar ...
61-122 1.00e-05

extracellular domain (ECD) found in Drosophila melanogaster Wishful thinking (Wit) and similar proteins; Wit is the Drosophila homolog to the mammalian bone morphogenetic protein (BMP) type II receptor, BMPRII. It is essential for nervous system development in Drosophila. It is necessary for BMP signaling and required for eggshell patterning. Wit 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: 467138  Cd Length: 103  Bit Score: 44.36  E-value: 1.00e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370461664  61 CFGIWNLTQDR--AQVEMQGCRDSDEPGCESLHCDPSPRahPSPGSTLFTCSCGTDFCNANYSH 122
Cdd:cd23618    42 CFTLWKNTSNNggISIIKQGCWINSPGDCNTSECVSSSP--TKDNNTSYFCCCSGHMCNANFSD 103
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
192-358 1.01e-05

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: 46.98  E-value: 1.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 192 DWsvelqELPELCFS-QQVIREGGHAVVWAGQLQG----KLVAIKAFPPRSVAQFQAERALyeLPGLQHDHIVRFITASr 266
Cdd:cd14151     2 DW-----EIPDGQITvGQRIGSGSFGTVYKGKWHGdvavKMLNVTAPTPQQLQAFKNEVGV--LRKTRHVNILLFMGYS- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 267 ggpgrllSGPLL--VLELHPKGSLCHYL--TQYTSDWGSSLRMALSLAQGLAFLHEErwqngqykpGIAHRDLSSQNVLI 342
Cdd:cd14151    74 -------TKPQLaiVTQWCEGSSLYHHLhiIETKFEMIKLIDIARQTAQGMDYLHAK---------SIIHRDLKSNNIFL 137
                         170
                  ....*....|....*.
gi 1370461664 343 REDGSCAIGDLGLALV 358
Cdd:cd14151   138 HEDLTVKIGDFGLATV 153
PKc_TOPK cd14001
Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer ...
303-382 1.25e-05

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: 47.01  E-value: 1.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 303 LRMALSLAQGLAFLHEERWqngqykpgIAHRDLSSQNVLIRED-GSCAIGDLGLALVLP----GLTQPPA-WTPTQPQGP 376
Cdd:cd14001   113 LKVALSIARALEYLHNEKK--------ILHGDIKSGNVLIKGDfESVKLCDFGVSLPLTenleVDSDPKAqYVGTEPWKA 184

                  ....*.
gi 1370461664 377 AAIMED 382
Cdd:cd14001   185 KEALEE 190
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
225-356 1.34e-05

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: 46.36  E-value: 1.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 225 GKLVAIKAFPPRS------VAQFQAERALyeLPGLQHDHIVR----FITasrggPGRLLsgplLVLELHPKGSLCHYLTQ 294
Cdd:cd05123    18 GKLYAMKVLRKKEiikrkeVEHTLNERNI--LERVNHPFIVKlhyaFQT-----EEKLY----LVLDYVPGGELFSHLSK 86
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370461664 295 YTS-DWGSSLRMALSLAQGLAFLHEErwqngqykpGIAHRDLSSQNVLIREDGSCAIGDLGLA 356
Cdd:cd05123    87 EGRfPEERARFYAAEIVLALEYLHSL---------GIIYRDLKPENILLDSDGHIKLTDFGLA 140
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
207-382 1.36e-05

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: 46.89  E-value: 1.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 207 QQVIREGGHAVVWAGQL--QGKLVAIK--AFPPRSVAQ-FQAE-RALYELPGlqHDHIVRFI--TASRGGPGRLLSgpLL 278
Cdd:cd14037     8 EKYLAEGGFAHVYLVKTsnGGNRAALKrvYVNDEHDLNvCKREiEIMKRLSG--HKNIVGYIdsSANRSGNGVYEV--LL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 279 VLELHPKGSLCHYLTQYTSDWGSS---LRMALSLAQGLAFLHeerwqngQYKPGIAHRDLSSQNVLIREDGSCAIGDLGL 355
Cdd:cd14037    84 LMEYCKGGGVIDLMNQRLQTGLTEseiLKIFCDVCEAVAAMH-------YLKPPLIHRDLKVENVLISDSGNYKLCDFGS 156
                         170       180
                  ....*....|....*....|....*..
gi 1370461664 356 AlvlpgltQPPAWTPTQPQGPAAIMED 382
Cdd:cd14037   157 A-------TTKILPPQTKQGVTYVEED 176
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
225-356 1.40e-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: 46.46  E-value: 1.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 225 GKLVAIKAFPPRSVAQ-FQAERALYELP---GLQHDHIVRFITASRGGpgrllSGPLLVLELHPKGSLCHYLTQYTSDWG 300
Cdd:cd14189    26 NKTYAVKVIPHSRVAKpHQREKIVNEIElhrDLHHKHVVKFSHHFEDA-----ENIYIFLELCSRKSLAHIWKARHTLLE 100
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1370461664 301 SSLRMAL-SLAQGLAFLHEErwqngqykpGIAHRDLSSQNVLIREDGSCAIGDLGLA 356
Cdd:cd14189   101 PEVRYYLkQIISGLKYLHLK---------GILHRDLKLGNFFINENMELKVGDFGLA 148
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
310-365 1.42e-05

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: 46.62  E-value: 1.42e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370461664 310 AQGLAFLHEErwqngqykpGIAHRDLSSQNVLIREDGSCAIGDLGLALV------LPGLTQP 365
Cdd:cd14062    99 AQGMDYLHAK---------NIIHRDLKSNNIFLHEDLTVKIGDFGLATVktrwsgSQQFEQP 151
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
214-356 1.53e-05

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: 46.67  E-value: 1.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 214 GHAVVWAGQLQGKLVAIKAFPPR-SVAQFQAERALYE---LPGLQHDHIVRFITASRG----GPGRLlsgPLLVLELHPK 285
Cdd:cd13989     7 GYVTLWKHQDTGEYVAIKKCRQElSPSDKNRERWCLEvqiMKKLNHPNVVSARDVPPEleklSPNDL---PLLAMEYCSG 83
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370461664 286 GSLCHYLTQYTSDWG---SSLRMALS-LAQGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIG---DLGLA 356
Cdd:cd13989    84 GDLRKVLNQPENCCGlkeSEVRTLLSdISSAISYLHENR---------IIHRDLKPENIVLQQGGGRVIYkliDLGYA 152
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
212-356 1.78e-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: 46.61  E-value: 1.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 212 EGGHAVVWAGQ--LQGKLVAIKA--FPPRSVAQFQAERALYELPGLQHDHIVRF--ITASRggpgrllSGPLLVLElHPK 285
Cdd:cd07869    15 EGSYATVYKGKskVNGKLVALKVirLQEEEGTPFTAIREASLLKGLKHANIVLLhdIIHTK-------ETLTLVFE-YVH 86
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370461664 286 GSLCHYLTQYTSDWG-SSLRMAL-SLAQGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDLGLA 356
Cdd:cd07869    87 TDLCQYMDKHPGGLHpENVKLFLfQLLRGLSYIHQRY---------ILHRDLKPQNLLISDTGELKLADFGLA 150
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
205-360 2.01e-05

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: 46.17  E-value: 2.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 205 FSQ-QVIREGGHAVVWAGQLQ--GKLVAIKAFPPRSVAQFQAER-ALYELPGLQHDHiVRFITaSRGGPGRLLSGPLLVL 280
Cdd:cd05630     2 FRQyRVLGKGGFGEVCACQVRatGKMYACKKLEKKRIKKRKGEAmALNEKQILEKVN-SRFVV-SLAYAYETKDALCLVL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 281 ELHPKGSL---CHYLTQYTSDWGSSLRMALSLAQGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDLGLAL 357
Cdd:cd05630    80 TLMNGGDLkfhIYHMGQAGFPEARAVFYAAEICCGLEDLHRER---------IVYRDLKPENILLDDHGHIRISDLGLAV 150

                  ...
gi 1370461664 358 VLP 360
Cdd:cd05630   151 HVP 153
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
210-356 2.08e-05

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: 46.34  E-value: 2.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 210 IREGGHAVVWAGQ--LQGKLVAIKAFPPRSVAQFQAERALYE---LPGLQHDHIVRFITASRGgPGRLLsgplLVLELhp 284
Cdd:cd07860     8 IGEGTYGVVYKARnkLTGEVVALKKIRLDTETEGVPSTAIREislLKELNHPNIVKLLDVIHT-ENKLY----LVFEF-- 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370461664 285 kgsLCHYLTQYT-SDWGSSLRMAL------SLAQGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDLGLA 356
Cdd:cd07860    81 ---LHQDLKKFMdASALTGIPLPLiksylfQLLQGLAFCHSHR---------VLHRDLKPQNLLINTEGAIKLADFGLA 147
TFP_LU_ECD_BMPR2 cd23614
extracellular domain (ECD) found in bone morphogenetic protein receptor type-2 (BMPR-2) and ...
53-121 2.14e-05

extracellular domain (ECD) found in bone morphogenetic protein receptor type-2 (BMPR-2) and similar proteins; BMPR2 (EC 2.7.11.30, also called BMP type-2 receptor, or bone morphogenetic protein receptor type II (BMPR-II), or BMP type II receptor) 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. BMPR2 binds to BMP7, BMP2, and less efficiently, BMP4. The binding is weak, but enhanced by the presence of type I receptors for BMPs. It also mediates the induction of adipogenesis by GDF6. This model corresponds to the extracellular domain (ECD) of BMPR2, 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: 467134  Cd Length: 101  Bit Score: 43.23  E-value: 2.14e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370461664  53 IRCLYSRCCFGIWNLTQD-RAQVEMQGC--RDSDEPGCESLHCDPSprAHPSP--GSTLFTCSCGTDFCNANYS 121
Cdd:cd23614    27 ILCVKGSQCYGLWEKTKEgEIRLVKQGCwsHIGDPQECHSEECVVT--TTPSSiqNGTYRFCCCSTDMCNVNFT 98
PTKc_c-ros cd05044
Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the ...
239-411 2.22e-05

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: 45.87  E-value: 2.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 239 AQFQAERALyeLPGLQHDHIVRFITASrggpgrLLSGP-LLVLELHPKGSLCHYL--TQYTSDWGSSL------RMALSL 309
Cdd:cd05044    44 AEFLKEAHL--MSNFKHPNILKLLGVC------LDNDPqYIILELMEGGDLLSYLraARPTAFTPPLLtlkdllSICVDV 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 310 AQGLAFLHEERWqngqykpgiAHRDLSSQNVLIREDGSC----AIGDLGLAL--------------VLP----------- 360
Cdd:cd05044   116 AKGCVYLEDMHF---------VHRDLAARNCLVSSKDYRervvKIGDFGLARdiykndyyrkegegLLPvrwmapeslvd 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 361 GL--TQPPAW--------TPTQPQGPAAIMED-------------------PDGLRELLEDCWDADPEARLTAECVQQRL 411
Cdd:cd05044   187 GVftTQSDVWafgvlmweILTLGQQPYPARNNlevlhfvraggrldqpdncPDDLYELMLRCWSTDPEERPSFARILEQL 266
PTKc_FGFR4 cd05099
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs ...
191-356 2.68e-05

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: 46.11  E-value: 2.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 191 RDWSVELQELPELCFSQqVIREGGHAVVWAGQLQGKLVAIKAFPP----RSVAQFQAERALYELPGlQHDHIVRFITASR 266
Cdd:cd05099    11 RDRLVLGKPLGEGCFGQ-VVRAEAYGIDKSRPDQTVTVAVKMLKDnatdKDLADLISEMELMKLIG-KHKNIINLLGVCT 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 267 GgpgrllSGPLLVL-ELHPKGSLCHYL-------TQYTSDWGSSLRMALS----------LAQGLAFLHEERwqngqykp 328
Cdd:cd05099    89 Q------EGPLYVIvEYAAKGNLREFLrarrppgPDYTFDITKVPEEQLSfkdlvscayqVARGMEYLESRR-------- 154
                         170       180
                  ....*....|....*....|....*...
gi 1370461664 329 gIAHRDLSSQNVLIREDGSCAIGDLGLA 356
Cdd:cd05099   155 -CIHRDLAARNVLVTEDNVMKIADFGLA 181
PTKc_Trk cd05049
Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze ...
227-356 2.92e-05

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: 45.92  E-value: 2.92e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 227 LVAIKAFPPRSVAQ----FQAERALyeLPGLQHDHIVRFI-TASRGGPgrllsgPLLVLELHPKGSLCHYLTQYTSD--- 298
Cdd:cd05049    37 LVAVKTLKDASSPDarkdFEREAEL--LTNLQHENIVKFYgVCTEGDP------LLMVFEYMEHGDLNKFLRSHGPDaaf 108
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 299 ------------WGSSLRMALSLAQGLAFLHEERWqngqykpgiAHRDLSSQNVLIREDGSCAIGDLGLA 356
Cdd:cd05049   109 lasedsapgeltLSQLLHIAVQIASGMVYLASQHF---------VHRDLATRNCLVGTNLVVKIGDFGMS 169
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
208-356 2.95e-05

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: 46.20  E-value: 2.95e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 208 QVIREGGHAVVWAG--QLQGKLVAIKAFPPRSVAQFQAERALYELPGLQ---HDHIVRFITASRG-GPGRLLSGPLLVLE 281
Cdd:cd07855    11 ETIGSGAYGVVCSAidTKSGQKVAIKKIPNAFDVVTTAKRTLRELKILRhfkHDNIIAIRDILRPkVPYADFKDVYVVLD 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 282 L---------HPKGSL-----CHYLTQytsdwgsslrmalsLAQGLAFLHEerwqngqykPGIAHRDLSSQNVLIREDGS 347
Cdd:cd07855    91 LmesdlhhiiHSDQPLtlehiRYFLYQ--------------LLRGLKYIHS---------ANVIHRDLKPSNLLVNENCE 147

                  ....*....
gi 1370461664 348 CAIGDLGLA 356
Cdd:cd07855   148 LKIGDFGMA 156
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
209-414 3.11e-05

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: 45.36  E-value: 3.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 209 VIREGGHAVVWAGQLQGKLVAIKAF---PPRSVA----QFQAERALYELpgLQHDHIVRFitasrggPGRLLSGP--LLV 279
Cdd:cd14148     1 IIGVGGFGKVYKGLWRGEEVAVKAArqdPDEDIAvtaeNVRQEARLFWM--LQHPNIIAL-------RGVCLNPPhlCLV 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 280 LELHPKGSLCHYLTQYTSDWGSSLRMALSLAQGLAFLHeerwqNGQYKPgIAHRDLSSQNVLIRE--------DGSCAIG 351
Cdd:cd14148    72 MEYARGGALNRALAGKKVPPHVLVNWAVQIARGMNYLH-----NEAIVP-IIHRDLKSSNILILEpienddlsGKTLKIT 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 352 DLGLALVLPGLTQPPAWTPTQPQGPAAIMED------------------------------------------------- 382
Cdd:cd14148   146 DFGLAREWHKTTKMSAAGTYAWMAPEVIRLSlfskssdvwsfgvllwelltgevpyreidalavaygvamnkltlpipst 225
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1370461664 383 -PDGLRELLEDCWDADPEARLTAECVQQRLAAL 414
Cdd:cd14148   226 cPEPFARLLEECWDPDPHGRPDFGSILKRLEDI 258
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
254-356 4.53e-05

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: 45.10  E-value: 4.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 254 QHDHIVRFITASRGGpgrllsGPL-LVLELHPKGSLCHYL-------TQYTSDWGSSLR----------MALSLAQGLAF 315
Cdd:cd05053    75 KHKNIINLLGACTQD------GPLyVVVEYASKGNLREFLrarrppgEEASPDDPRVPEeqltqkdlvsFAYQVARGMEY 148
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1370461664 316 LHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDLGLA 356
Cdd:cd05053   149 LASKK---------CIHRDLAARNVLVTEDNVMKIADFGLA 180
PTKc_IGF-1R cd05062
Catalytic domain of the Protein Tyrosine Kinase, Insulin-like Growth Factor-1 Receptor; PTKs ...
257-355 5.06e-05

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: 45.02  E-value: 5.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 257 HIVRFI-TASRGGPgrllsgPLLVLELHPKGSLCHYLTQYTSDWGSS-----------LRMALSLAQGLAFLHEERWqng 324
Cdd:cd05062    70 HVVRLLgVVSQGQP------TLVIMELMTRGDLKSYLRSLRPEMENNpvqappslkkmIQMAGEIADGMAYLNANKF--- 140
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1370461664 325 qykpgiAHRDLSSQNVLIREDGSCAIGDLGL 355
Cdd:cd05062   141 ------VHRDLAARNCMVAEDFTVKIGDFGM 165
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
210-361 5.15e-05

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: 44.67  E-value: 5.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 210 IREGGHAVVWAGQLQGK---LVAIKAFPPRSVAQFQA--ERALYELPGLQHDHIVRFITASRggpgrLLSGPLLVLELHP 284
Cdd:cd14120     1 IGHGAFAVVFKGRHRKKpdlPVAIKCITKKNLSKSQNllGKEIKILKELSHENVVALLDCQE-----TSSSVYLVMEYCN 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 285 KGSLCHYLTQYTSDWGSSLRMAL-SLAQGLAFLHEErwqngqykpGIAHRDLSSQNVLIREDGSCA---------IGDLG 354
Cdd:cd14120    76 GGDLADYLQAKGTLSEDTIRVFLqQIAAAMKALHSK---------GIVHRDLKPQNILLSHNSGRKpspndirlkIADFG 146

                  ....*..
gi 1370461664 355 LALVLPG 361
Cdd:cd14120   147 FARFLQD 153
PTKc_Ror1 cd05090
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
221-380 5.15e-05

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: 45.00  E-value: 5.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 221 GQLQGKLVAIKAFP----PRSVAQFQAERALyeLPGLQHDHIVRFITA-SRGGPGRLLsgpllvLELHPKGSLCHYL--- 292
Cdd:cd05090    30 GMDHAQLVAIKTLKdynnPQQWNEFQQEASL--MTELHHPNIVCLLGVvTQEQPVCML------FEFMNQGDLHEFLimr 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 293 ---------------TQYTSDWGSSLRMALSLAQGLAFLHEERWqngqykpgiAHRDLSSQNVLIREDGSCAIGDLGLAL 357
Cdd:cd05090   102 sphsdvgcssdedgtVKSSLDHGDFLHIAIQIAAGMEYLSSHFF---------VHKDLAARNILVGEQLHVKISDLGLSR 172
                         170       180
                  ....*....|....*....|....*..
gi 1370461664 358 VLPG----LTQPPAWTPTQPQGPAAIM 380
Cdd:cd05090   173 EIYSsdyyRVQNKSLLPIRWMPPEAIM 199
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
207-356 6.02e-05

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: 44.43  E-value: 6.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 207 QQVIREGGHAVVWAGQ--LQGKLVAIKAFPPRSVAQFQAERALYE---LPGLQHDHIVRF----ITasrggPGRLLsgpl 277
Cdd:cd14003     5 GKTLGEGSFGKVKLARhkLTGEKVAIKIIDKSKLKEEIEEKIKREieiMKLLNHPNIIKLyeviET-----ENKIY---- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 278 LVLELHPKGSLCHYLTQYTsdwgsslRMALSLAQ--------GLAFLHeerwqngqyKPGIAHRDLSSQNVLIREDGSCA 349
Cdd:cd14003    76 LVMEYASGGELFDYIVNNG-------RLSEDEARrffqqlisAVDYCH---------SNGIVHRDLKLENILLDKNGNLK 139

                  ....*..
gi 1370461664 350 IGDLGLA 356
Cdd:cd14003   140 IIDFGLS 146
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
277-361 6.59e-05

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: 44.47  E-value: 6.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 277 LLVLELHPKGSLC-----HYLTQYTSDwgSSLRMALSLAQGLAFLHEErwqngqykpGIAHRDLSSQNVLIREDGSCAIG 351
Cdd:cd14008    82 YLVLEYCEGGPVMeldsgDRVPPLPEE--TARKYFRDLVLGLEYLHEN---------GIVHRDIKPENLLLTADGTVKIS 150
                          90
                  ....*....|
gi 1370461664 352 DLGLALVLPG 361
Cdd:cd14008   151 DFGVSEMFED 160
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
199-408 6.75e-05

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: 44.68  E-value: 6.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 199 ELPELCFSQQV-IREGGHAVVWAGQLQGKL-VAIKAFPPRSVAQFQAERALYELPGLQHDHIVRFITASRGGPgrllsgP 276
Cdd:cd05071     5 EIPRESLRLEVkLGQGCFGEVWMGTWNGTTrVAIKTLKPGTMSPEAFLQEAQVMKKLRHEKLVQLYAVVSEEP------I 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 277 LLVLELHPKGSLCHYLTqytSDWGSSLR------MALSLAQGLAFLHEERWqngqykpgiAHRDLSSQNVLIREDGSCAI 350
Cdd:cd05071    79 YIVTEYMSKGSLLDFLK---GEMGKYLRlpqlvdMAAQIASGMAYVERMNY---------VHRDLRAANILVGENLVCKV 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 351 GDLGLALVLP--------GLTQPPAWTP--------------------------TQPQGPAAIM---------------- 380
Cdd:cd05071   147 ADFGLARLIEdneytarqGAKFPIKWTApeaalygrftiksdvwsfgillteltTKGRVPYPGMvnrevldqvergyrmp 226
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1370461664 381 ---EDPDGLRELLEDCWDADPEARLTAECVQ 408
Cdd:cd05071   227 cppECPESLHDLMCQCWRKEPEERPTFEYLQ 257
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
202-356 6.93e-05

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: 44.36  E-value: 6.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 202 ELCFSQQvIREGGHAVVWAGQLQGKL-VAIKAFPPRSVAQ--FQAERALyeLPGLQHDHIVR-FITASRGGPGRLlsgpl 277
Cdd:cd05059     5 ELTFLKE-LGSGQFGVVHLGKWRGKIdVAIKMIKEGSMSEddFIEEAKV--MMKLSHPKLVQlYGVCTKQRPIFI----- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 278 lVLELHPKGSLCHYLTQYTSDWGSS--LRMALSLAQGLAFLHEErwqngqykpGIAHRDLSSQNVLIREDGSCAIGDLGL 355
Cdd:cd05059    77 -VTEYMANGCLLNYLRERRGKFQTEqlLEMCKDVCEAMEYLESN---------GFIHRDLAARNCLVGEQNVVKVSDFGL 146

                  .
gi 1370461664 356 A 356
Cdd:cd05059   147 A 147
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
279-380 7.58e-05

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: 44.51  E-value: 7.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 279 VLELHPKGSLCHYLTQYTS-DWGSSLRMALSLAQGLAFLHEErwqngqykpGIAHRDLSSQNVLIREDGSCAIGDLGLAL 357
Cdd:cd05581    79 VLEYAPNGDLLEYIRKYGSlDEKCTRFYTAEIVLALEYLHSK---------GIIHRDLKPENILLDEDMHIKITDFGTAK 149
                          90       100
                  ....*....|....*....|...
gi 1370461664 358 VLPGlTQPPAWTPTQPQGPAAIM 380
Cdd:cd05581   150 VLGP-DSSPESTKGDADSQIAYN 171
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
213-354 8.30e-05

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: 44.02  E-value: 8.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 213 GGHAVVWAGQLQGKLVAIKAfpprsvAQFQAERALYELPGLQHDHIVRFitasrggPGRLLSGPL--LVLELHPKGSLCH 290
Cdd:cd14059     4 GAQGAVFLGKFRGEEVAVKK------VRDEKETDIKHLRKLNHPNIIKF-------KGVCTQAPCycILMEYCPYGQLYE 70
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370461664 291 YLTQ-------YTSDWgsslrmALSLAQGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDLG 354
Cdd:cd14059    71 VLRAgreitpsLLVDW------SKQIASGMNYLHLHK---------IIHRDLKSPNVLVTYNDVLKISDFG 126
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
309-356 9.47e-05

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: 44.20  E-value: 9.47e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1370461664 309 LAQGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDLGLA 356
Cdd:cd07835   108 LLQGIAFCHSHR---------VLHRDLKPQNLLIDTEGALKLADFGLA 146
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
309-356 1.03e-04

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: 44.09  E-value: 1.03e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1370461664 309 LAQGLAFLHEErwqngqykpGIAHRDLSSQNVLIREDGSCAIGDLGLA 356
Cdd:cd07840   113 LLEGLQYLHSN---------GILHRDIKGSNILINNDGVLKLADFGLA 151
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
210-360 1.10e-04

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: 43.82  E-value: 1.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 210 IREGGHAVVWAGQLQG--KLVAIKafpprSVAQFQAERALYELP---GLQHDHIVRFI----TasrggpgrllSGPL-LV 279
Cdd:cd14010     8 IGRGKHSVVYKGRRKGtiEFVAIK-----CVDKSKRPEVLNEVRlthELKHPNVLKFYewyeT----------SNHLwLV 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 280 LELHPKGSLCHYLTQYTSDWGSSLRM-ALSLAQGLAFLHeerwqngqyKPGIAHRDLSSQNVLIREDGSCAIGDLGLALV 358
Cdd:cd14010    73 VEYCTGGDLETLLRQDGNLPESSVRKfGRDLVRGLHYIH---------SKGIIYCDLKPSNILLDGNGTLKLSDFGLARR 143

                  ..
gi 1370461664 359 LP 360
Cdd:cd14010   144 EG 145
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
307-356 1.18e-04

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: 43.96  E-value: 1.18e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1370461664 307 LSLAQGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDLGLA 356
Cdd:cd07839   106 FQLLKGLAFCHSHN---------VLHRDLKPQNLLINKNGELKLADFGLA 146
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
247-358 1.20e-04

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: 43.87  E-value: 1.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 247 LYELPGLQHDHIVRFI---TASRGGPGRLLSgplLVLElHPKGSLCHYLTQyTSDWGSSLR----MALSLAQGLAFLHEE 319
Cdd:cd07862    55 LRHLETFEHPNVVRLFdvcTVSRTDRETKLT---LVFE-HVDQDLTTYLDK-VPEPGVPTEtikdMMFQLLRGLDFLHSH 129
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1370461664 320 RwqngqykpgIAHRDLSSQNVLIREDGSCAIGDLGLALV 358
Cdd:cd07862   130 R---------VVHRDLKPQNILVTSSGQIKLADFGLARI 159
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
287-385 1.22e-04

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: 43.85  E-value: 1.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 287 SLCHYL--TQYTSDWGSSLRMALSLAQGLAFLHEErwqngqykpGIAHRDLSSQNVLIREDGSCAIGDLGLALVlpgltq 364
Cdd:cd14150    81 SLYRHLhvTETRFDTMQLIDVARQTAQGMDYLHAK---------NIIHRDLKSNNIFLHEGLTVKIGDFGLATV------ 145
                          90       100
                  ....*....|....*....|.
gi 1370461664 365 PPAWTPTQPqgpaaiMEDPDG 385
Cdd:cd14150   146 KTRWSGSQQ------VEQPSG 160
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
255-374 1.46e-04

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: 43.60  E-value: 1.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 255 HDHIVRFITASRGG---PGRLLSGP--LLVLELHPKGSLCHYLTQ---YTSDWGSslRMALSLAQGLAFLHeerwqngqy 326
Cdd:cd14171    58 HPNIVQIYDVYANSvqfPGESSPRArlLIVMELMEGGELFDRISQhrhFTEKQAA--QYTKQIALAVQHCH--------- 126
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1370461664 327 KPGIAHRDLSSQNVLIR---EDGSCAIGDLGLALVLPGLTQPPAWTP--TQPQ 374
Cdd:cd14171   127 SLNIAHRDLKPENLLLKdnsEDAPIKLCDFGFAKVDQGDLMTPQFTPyyVAPQ 179
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
225-356 1.62e-04

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: 43.40  E-value: 1.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 225 GKLVAIKAFP------PRSVAQFQAERALYELpgLQHDHIVRFITASRGgpgrllSGPL-LVLELHPKGSLCHYLTQYts 297
Cdd:cd14081    26 GQKVAIKIVNkeklskESVLMKVEREIAIMKL--IEHPNVLKLYDVYEN------KKYLyLVLEYVSGGELFDYLVKK-- 95
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370461664 298 dwGS-SLRMALSLAQ----GLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDLGLA 356
Cdd:cd14081    96 --GRlTEKEARKFFRqiisALDYCHSHS---------ICHRDLKPENLLLDEKNNIKIADFGMA 148
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
257-354 1.68e-04

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: 41.66  E-value: 1.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 257 HIVRFITASRggpgrlLSGPL-LVLELHPKGSLCHYLTQYTSDWGSSLRMALSLAQGLAFLHEERwqngqykpgIAHRDL 335
Cdd:cd13968    53 NIPKVLVTED------VDGPNiLLMELVKGGTLIAYTQEEELDEKDVESIMYQLAECMRLLHSFH---------LIHRDL 117
                          90
                  ....*....|....*....
gi 1370461664 336 SSQNVLIREDGSCAIGDLG 354
Cdd:cd13968   118 NNDNILLSEDGNVKLIDFG 136
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
208-356 1.70e-04

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: 43.01  E-value: 1.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 208 QVIREGGHAVVWAGQLQ--GKLVAIKAFPPRSvaqfQAERALYEL-------PGLQHDHIVRFITASRGgpgrllSGPLL 278
Cdd:cd14002     7 ELIGEGSFGKVYKGRRKytGQVVALKFIPKRG----KSEKELRNLrqeieilRKLNHPNIIEMLDSFET------KKEFV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 279 VLELHPKGSLchylTQYTSDWGSsL------RMALSLAQGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGD 352
Cdd:cd14002    77 VVTEYAQGEL----FQILEDDGT-LpeeevrSIAKQLVSALHYLHSNR---------IIHRDMKPQNILIGKGGVVKLCD 142

                  ....
gi 1370461664 353 LGLA 356
Cdd:cd14002   143 FGFA 146
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
312-356 1.73e-04

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: 43.42  E-value: 1.73e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1370461664 312 GLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDLGLA 356
Cdd:cd07838   119 GLDFLHSHR---------IVHRDLKPQNILVTSDGQVKLADFGLA 154
PK_GC_unk cd14045
Pseudokinase domain of the unknown subfamily of membrane Guanylate Cyclase receptors; The ...
221-357 2.11e-04

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: 42.92  E-value: 2.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 221 GQLQGKLVAIKAFPPRSVAQFQAERA-LYELPGLQHDHIVRFItasrggpGRLLSGP--LLVLELHPKGSLCHYL--TQY 295
Cdd:cd14045    26 GIYDGRTVAIKKIAKKSFTLSKRIRKeVKQVRELDHPNLCKFI-------GGCIEVPnvAIITEYCPKGSLNDVLlnEDI 98
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370461664 296 TSDWGSSLRMALSLAQGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDLGLAL 357
Cdd:cd14045    99 PLNWGFRFSFATDIARGMAYLHQHK---------IYHGRLKSSNCVIDDRWVCKIADYGLTT 151
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
253-356 2.25e-04

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: 42.80  E-value: 2.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 253 LQHDHIVRFITASRGGpgrllSGPLLVLELHPKGSLCHYLTQYTS-DWGSSLRMALSLAQGLAFLHEERwqngqykpgIA 331
Cdd:cd06630    60 LNHPNIVRMLGATQHK-----SHFNIFVEWMAGGSVASLLSKYGAfSENVIINYTLQILRGLAYLHDNQ---------II 125
                          90       100
                  ....*....|....*....|....*.
gi 1370461664 332 HRDLSSQNVLIREDGS-CAIGDLGLA 356
Cdd:cd06630   126 HRDLKGANLLVDSTGQrLRIADFGAA 151
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
212-356 2.53e-04

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: 43.06  E-value: 2.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 212 EGGHAVVWAG--QLQGKLVAIKA--FPPRSVAQFQAERALYELPGLQHDHIVRFITASRggPGRLLSgplLVLELHPKGs 287
Cdd:cd07872    16 EGTYATVFKGrsKLTENLVALKEirLEHEEGAPCTAIREVSLLKDLKHANIVTLHDIVH--TDKSLT---LVFEYLDKD- 89
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370461664 288 lchyLTQYTSDWGSSLRM------ALSLAQGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDLGLA 356
Cdd:cd07872    90 ----LKQYMDDCGNIMSMhnvkifLYQILRGLAYCHRRK---------VLHRDLKPQNLLINERGELKLADFGLA 151
PTKc_TAM cd05035
Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer ...
208-356 2.68e-04

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: 42.91  E-value: 2.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 208 QVIREGGHAVVWAGQL------QGKlVAIKAFPPRSVAQFQAERALYE---LPGLQHDHIVRFITAS-RGGPGRLLSGPL 277
Cdd:cd05035     5 KILGEGEFGSVMEAQLkqddgsQLK-VAVKTMKVDIHTYSEIEEFLSEaacMKDFDHPNVMRLIGVCfTASDLNKPPSPM 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 278 LVLELHPKGSLCHYLTQYTSDWGSS-------LRMALSLAQGLAFLHEERWqngqykpgiAHRDLSSQNVLIREDGSCAI 350
Cdd:cd05035    84 VILPFMKHGDLHSYLLYSRLGGLPEklplqtlLKFMVDIAKGMEYLSNRNF---------IHRDLAARNCMLDENMTVCV 154

                  ....*.
gi 1370461664 351 GDLGLA 356
Cdd:cd05035   155 ADFGLS 160
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
202-356 2.81e-04

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: 42.63  E-value: 2.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 202 ELCFSQQvIREGGHAVVWAGQLQGKL-VAIKAFPPRSVAQFQAERALYELPGLQHDHIVRFITASrggpgrLLSGPL-LV 279
Cdd:cd05112     5 ELTFVQE-IGSGQFGLVHLGYWLNKDkVAIKTIREGAMSEEDFIEEAEVMMKLSHPKLVQLYGVC------LEQAPIcLV 77
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370461664 280 LELHPKGSLCHYLTQYTSDWGSS--LRMALSLAQGLAFLHEErwqngqykpGIAHRDLSSQNVLIREDGSCAIGDLGLA 356
Cdd:cd05112    78 FEFMEHGCLSDYLRTQRGLFSAEtlLGMCLDVCEGMAYLEEA---------SVIHRDLAARNCLVGENQVVKVSDFGMT 147
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
250-356 3.40e-04

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 42.94  E-value: 3.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 250 LPGLQHDHIVRFITAsrggpgrLLSGPLLVLEL-HPKGSLCHYLTQYTS--DWGSSLRMALSLAQGLAFLHEERwqngqy 326
Cdd:PHA03209  111 LQNVNHPSVIRMKDT-------LVSGAITCMVLpHYSSDLYTYLTKRSRplPIDQALIIEKQILEGLRYLHAQR------ 177
                          90       100       110
                  ....*....|....*....|....*....|
gi 1370461664 327 kpgIAHRDLSSQNVLIREDGSCAIGDLGLA 356
Cdd:PHA03209  178 ---IIHRDVKTENIFINDVDQVCIGDLGAA 204
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
250-356 3.45e-04

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: 42.64  E-value: 3.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 250 LPGLQHDHIVRFITA-SRGGPgrllsgPLLVLELHPKGSL-----------CHYLTQYTSDWGSSL----------RMAL 307
Cdd:cd05045    57 LKQVNHPHVIKLYGAcSQDGP------LLLIVEYAKYGSLrsflresrkvgPSYLGSDGNRNSSYLdnpderaltmGDLI 130
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1370461664 308 SLA----QGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDLGLA 356
Cdd:cd05045   131 SFAwqisRGMQYLAEMK---------LVHRDLAARNVLVAEGRKMKISDFGLS 174
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
204-361 3.50e-04

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: 42.30  E-value: 3.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 204 CF-SQQVIREGGHAVVWAGQLQ--GKLVAIKafppRSVAQFQAE----RALYELPGL----QHDHIVRFITA--SRGgpg 270
Cdd:cd14050     2 CFtILSKLGEGSFGEVFKVRSRedGKLYAVK----RSRSRFRGEkdrkRKLEEVERHeklgEHPNCVRFIKAweEKG--- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 271 rllsgpllvlELHPKGSLCH-YLTQYTSDWGSSLRMA-----LSLAQGLAFLHEErwqngqykpGIAHRDLSSQNVLIRE 344
Cdd:cd14050    75 ----------ILYIQTELCDtSLQQYCEETHSLPESEvwnilLDLLKGLKHLHDH---------GLIHLDIKPANIFLSK 135
                         170
                  ....*....|....*..
gi 1370461664 345 DGSCAIGDLGLALVLPG 361
Cdd:cd14050   136 DGVCKLGDFGLVVELDK 152
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
309-356 3.93e-04

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: 42.27  E-value: 3.93e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1370461664 309 LAQGLAFLHEErWqngqykpgIAHRDLSSQNVLI----REDGSCAIGDLGLA 356
Cdd:cd07842   117 ILNGIHYLHSN-W--------VLHRDLKPANILVmgegPERGVVKIGDLGLA 159
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
208-359 3.95e-04

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: 42.03  E-value: 3.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 208 QVIREGGHAVVWAGQLQ--GKLVAIKAFPPRSVAQFQAERALYE---LPGLQHDHIVRFITASRggPGRLLSgplLVLEL 282
Cdd:cd08220     6 RVVGRGAYGTVYLCRRKddNKLVIIKQIPVEQMTKEERQAALNEvkvLSMLHHPNIIEYYESFL--EDKALM---IVMEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 283 HPKGSLCHYLTQYTSDWGSS---LRMALSLAQGLAFLHEERwqngqykpgIAHRDLSSQNVLI-REDGSCAIGDLGLALV 358
Cdd:cd08220    81 APGGTLFEYIQQRKGSLLSEeeiLHFFVQILLALHHVHSKQ---------ILHRDLKTQNILLnKKRTVVKIGDFGISKI 151

                  .
gi 1370461664 359 L 359
Cdd:cd08220   152 L 152
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
208-413 4.28e-04

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: 41.92  E-value: 4.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 208 QVIREGGHAVVWAGQLQGKL-VAIKA----FPPRSVAQFQAERALYElpglQHDH--IVRFI-TASRGGPgrllsgPLLV 279
Cdd:cd05085     2 ELLGKGNFGEVYKGTLKDKTpVAVKTckedLPQELKIKFLSEARILK----QYDHpnIVKLIgVCTQRQP------IYIV 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 280 LELHPKGSLCHYLTQYTSDWGSS--LRMALSLAQGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDLGLA- 356
Cdd:cd05085    72 MELVPGGDFLSFLRKKKDELKTKqlVKFSLDAAAGMAYLESKN---------CIHRDLAARNCLVGENNALKISDFGMSr 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 357 ------LVLPGLTQ-PPAWTP------------------------------------TQPQGP---------AAIMEDPD 384
Cdd:cd05085   143 qeddgvYSSSGLKQiPIKWTApealnygryssesdvwsfgillwetfslgvcpypgmTNQQAReqvekgyrmSAPQRCPE 222
                         250       260
                  ....*....|....*....|....*....
gi 1370461664 385 GLRELLEDCWDADPEARLTAECVQQRLAA 413
Cdd:cd05085   223 DIYKIMQRCWDYNPENRPKFSELQKELAA 251
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
225-354 4.43e-04

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: 41.93  E-value: 4.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 225 GKLVAIKAFP--------PRSVAQFQAERALyeLPGLQHDHIVRFITASRGGPGRLLSgplLVLELHPKGSLCHYLTQYT 296
Cdd:cd06653    27 GRELAVKQVPfdpdsqetSKEVNALECEIQL--LKNLRHDRIVQYYGCLRDPEEKKLS---IFVEYMPGGSVKDQLKAYG 101
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1370461664 297 S-DWGSSLRMALSLAQGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDLG 354
Cdd:cd06653   102 AlTENVTRRYTRQILQGVSYLHSNM---------IVHRDIKGANILRDSAGNVKLGDFG 151
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
307-356 5.29e-04

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 42.06  E-value: 5.29e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1370461664 307 LSLAQGLAFLHeerwqngqyKPGIAHRDLSSQNVLIREDGSCAIGDLGLA 356
Cdd:PTZ00024  126 LQILNGLNVLH---------KWYFMHRDLSPANIFINSKGICKIADFGLA 166
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
207-414 5.92e-04

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: 41.55  E-value: 5.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 207 QQVIREGGHAVVWAGQLQGKLVAIKAF---PPRSVA----QFQAERALYELpgLQHDHIVRFitasrggPGRLLSGP--L 277
Cdd:cd14147     8 EEVIGIGGFGKVYRGSWRGELVAVKAArqdPDEDISvtaeSVRQEARLFAM--LAHPNIIAL-------KAVCLEEPnlC 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 278 LVLELHPKGSLCHYLTQYTSDWGSSLRMALSLAQGLAFLHEErwqngQYKPGIaHRDLSSQNVLI--------REDGSCA 349
Cdd:cd14147    79 LVMEYAAGGPLSRALAGRRVPPHVLVNWAVQIARGMHYLHCE-----ALVPVI-HRDLKSNNILLlqpienddMEHKTLK 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 350 IGDLGLALVLPGLTQPPAWTPTQPQGPAAIMED----------------------------------------------- 382
Cdd:cd14147   153 ITDFGLAREWHKTTQMSAAGTYAWMAPEVIKAStfskgsdvwsfgvllwelltgevpyrgidclavaygvavnkltlpip 232
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1370461664 383 ---PDGLRELLEDCWDADPEARLTAECVQQRLAAL 414
Cdd:cd14147   233 stcPEPFAQLMADCWAQDPHRRPDFASILQQLEAL 267
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
225-405 5.96e-04

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: 41.57  E-value: 5.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 225 GKLVAIKAFP--------PRSVAQFQAERALyeLPGLQHDHIVRFITASRGgPGRLLsgplLVLELHPKGSLCHYLTQYt 296
Cdd:cd06625    25 GRELAVKQVEidpinteaSKEVKALECEIQL--LKNLQHERIVQYYGCLQD-EKSLS----IFMEYMPGGSVKDEIKAY- 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 297 sdwgSSLRMALS------LAQGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDLGLA-------------- 356
Cdd:cd06625    97 ----GALTENVTrkytrqILEGLAYLHSNM---------IVHRDIKGANILRDSNGNVKLGDFGASkrlqticsstgmks 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 357 -----------------------------LVLPGLTQPPAWT--------------PTQPQGPAAIMEDpdgLRELLEDC 393
Cdd:cd06625   164 vtgtpywmspevingegygrkadiwsvgcTVVEMLTTKPPWAefepmaaifkiatqPTNPQLPPHVSED---ARDFLSLI 240
                         250
                  ....*....|..
gi 1370461664 394 WDADPEARLTAE 405
Cdd:cd06625   241 FVRNKKQRPSAE 252
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
277-417 6.04e-04

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: 41.49  E-value: 6.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 277 LLVLELHPKGSLCHYLTQYTSDWGSSLR-MALSLAQGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDLGL 355
Cdd:cd14181    92 FLVFDLMRRGELFDYLTEKVTLSEKETRsIMRSLLEAVSYLHANN---------IVHRDLKPENILLDDQLHIKLSDFGF 162
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 356 ALVL-----------------------------PGLTQ------------------PPAWTPTQPQGPAAIMED------ 382
Cdd:cd14181   163 SCHLepgeklrelcgtpgylapeilkcsmdethPGYGKevdlwacgvilftllagsPPFWHRRQMLMLRMIMEGryqfss 242
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1370461664 383 ------PDGLRELLEDCWDADPEARLTAEcvqqrlAALAHP 417
Cdd:cd14181   243 pewddrSSTVKDLISRLLVVDPEIRLTAE------QALQHP 277
STKc_IRAK1 cd14159
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; ...
210-356 6.22e-04

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: 41.73  E-value: 6.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 210 IREGGHAVVWAGQLQGKLVAIKAFPPRSVAQFQAERALY-----ELPGLQHDHIVRFITAS-RGGPGRLLSGPLlvlelh 283
Cdd:cd14159     1 IGEGGFGCVYQAVMRNTEYAVKRLKEDSELDWSVVKNSFlteveKLSRFRHPNIVDLAGYSaQQGNYCLIYVYL------ 74
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370461664 284 PKGSLCHYLTQYTS----DWGSSLRMALSLAQGLAFLHeerwqngQYKPGIAHRDLSSQNVLIREDGSCAIGDLGLA 356
Cdd:cd14159    75 PNGSLEDRLHCQVScpclSWSQRLHVLLGTARAIQYLH-------SDSPSLIHGDVKSSNILLDAALNPKLGDFGLA 144
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
225-356 6.23e-04

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: 41.60  E-value: 6.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 225 GKLVAIKAFPPRSVAQFQ----AERALYELPGLQHDHIVRF--ITASRggpgrllSGPLLVLELHPKGSLCHYLTQYTS- 297
Cdd:cd14073    26 GREVAIKSIKKDKIEDEQdmvrIRREIEIMSSLNHPHIIRIyeVFENK-------DKIVIVMEYASGGELYDYISERRRl 98
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1370461664 298 DWGSSLRMALSLAQGLAFLHeerwqngqyKPGIAHRDLSSQNVLIREDGSCAIGDLGLA 356
Cdd:cd14073    99 PEREARRIFRQIVSAVHYCH---------KNGVVHRDLKLENILLDQNGNAKIADFGLS 148
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
278-396 6.97e-04

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: 41.52  E-value: 6.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 278 LVLELHPKGSLCHYLT---QYTSDWGSSlrMALSLAQGLAFLHEErwqngqykpGIAHRDLSSQNVLIRE--DGSCAI-- 350
Cdd:cd14183    81 LVMELVKGGDLFDAITstnKYTERDASG--MLYNLASAIKYLHSL---------NIVHRDIKPENLLVYEhqDGSKSLkl 149
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1370461664 351 GDLGLALVLPGLTQPPAWTPTQpQGPAAIMEDPDGLRellEDCWDA 396
Cdd:cd14183   150 GDFGLATVVDGPLYTVCGTPTY-VAPEIIAETGYGLK---VDIWAA 191
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
205-361 6.99e-04

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: 41.53  E-value: 6.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 205 FSQQ-VIREGGHAVVWAGQLQGKL---VAIKAFPPRSVAQFQA--ERALYELPGLQHDHIVRFITASRggpgrlLSGPL- 277
Cdd:cd14202     4 FSRKdLIGHGAFAVVFKGRHKEKHdleVAVKCINKKNLAKSQTllGKEIKILKELKHENIVALYDFQE------IANSVy 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 278 LVLELHPKGSLCHYLTQYTSDWGSSLRMALS-LAQGLAFLHEErwqngqykpGIAHRDLSSQNVLIREDGS--------- 347
Cdd:cd14202    78 LVMEYCNGGDLADYLHTMRTLSEDTIRLFLQqIAGAMKMLHSK---------GIIHRDLKPQNILLSYSGGrksnpnnir 148
                         170
                  ....*....|....
gi 1370461664 348 CAIGDLGLALVLPG 361
Cdd:cd14202   149 IKIADFGFARYLQN 162
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
243-359 7.20e-04

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: 41.27  E-value: 7.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 243 AERALYELPGLQHDHIVRFITASRGGPGRLLsgplLVLELHPKGSLCHYLTQYTS---------DWGSSLRMALSlaqgl 313
Cdd:cd08223    46 AEQEAKLLSKLKHPNIVSYKESFEGEDGFLY----IVMGFCEGGDLYTRLKEQKGvlleerqvvEWFVQIAMALQ----- 116
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1370461664 314 aFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDLGLALVL 359
Cdd:cd08223   117 -YMHERN---------ILHRDLKTQNIFLTKSNIIKVGDLGIARVL 152
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
225-354 7.43e-04

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: 41.18  E-value: 7.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 225 GKLVAIKA--FPPRS------VAQFQAERALyeLPGLQHDHIVRFITASRGGPGRLLSgplLVLELHPKGSLCHYLTQYT 296
Cdd:cd06652    27 GRELAVKQvqFDPESpetskeVNALECEIQL--LKNLLHERIVQYYGCLRDPQERTLS---IFMEYMPGGSIKDQLKSYG 101
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1370461664 297 S-DWGSSLRMALSLAQGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDLG 354
Cdd:cd06652   102 AlTENVTRKYTRQILEGVHYLHSNM---------IVHRDIKGANILRDSVGNVKLGDFG 151
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
207-359 7.80e-04

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: 41.11  E-value: 7.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 207 QQVIREGGHAVVWAGQLQ--GK---LVAIKAFPP----RSVAQFQAERALyeLPGLQHDHIVRFitasrGGPGRLLSGPL 277
Cdd:cd05063    10 QKVIGAGEFGEVFRGILKmpGRkevAVAIKTLKPgyteKQRQDFLSEASI--MGQFSHHNIIRL-----EGVVTKFKPAM 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 278 LVLELHPKGSLCHYLTQYTSDWGSS--LRMALSLAQGLAFLHEERWqngqykpgiAHRDLSSQNVLIREDGSCAIGDLGL 355
Cdd:cd05063    83 IITEYMENGALDKYLRDHDGEFSSYqlVGMLRGIAAGMKYLSDMNY---------VHRDLAARNILVNSNLECKVSDFGL 153

                  ....
gi 1370461664 356 ALVL 359
Cdd:cd05063   154 SRVL 157
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
278-355 7.81e-04

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: 41.07  E-value: 7.81e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370461664 278 LVLELHPKGSLCHYLTQYTSDWGSSLRMALSLAQGLAFLHEErwqngqykpGIAHRDLSSQNVLIREDGSCAIGDLGL 355
Cdd:cd06647    81 VVMEYLAGGSLTDVVTETCMDEGQIAAVCRECLQALEFLHSN---------QVIHRDIKSDNILLGMDGSVKLTDFGF 149
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
311-356 8.19e-04

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: 41.19  E-value: 8.19e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1370461664 311 QGLAFLHeerwQNGQykpgiAHRDLSSQNVLIREDGSCAIGDLGLA 356
Cdd:cd06610   113 KGLEYLH----SNGQ-----IHRDVKAGNILLGEDGSVKIADFGVS 149
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
309-380 8.22e-04

Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase signal-integrating kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK signal-integrating kinases (Mnks) are MAPK-activated protein kinases and is comprised by a group of four proteins, produced by alternative splicing from two genes (Mnk1 and Mnk2). The isoforms of Mnk1 (1a/1b) and Mnk2 (2a/2b) differ at their C-termini, with the a-form having a longer C-terminus containing a MAPK-binding region. All Mnks contain a catalytic kinase domain and a polybasic region at the N-terminus which binds importin and the eukaryotic initiation factor eIF4G. The best characterized Mnk substrate is eIF4G, whose phosphorylation may promote the export of certain mRNAs from the nucleus. Mnk also phosphorylate substrates that bind to AU-rich elements that regulate mRNA stability and translation. Mnks have also been implicated in tyrosine kinase receptor signaling, inflammation, and cell prolieration or survival. The Mnk subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270992 [Multi-domain]  Cd Length: 289  Bit Score: 41.25  E-value: 8.22e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370461664 309 LAQGLAFLHeerwqngqyKPGIAHRDLSSQNVLIREDGSCA---IGDLGLALVLPGLTQP--PAWTP--TQPQGPAAIM 380
Cdd:cd14090   109 IASALDFLH---------DKGIAHRDLKPENILCESMDKVSpvkICDFDLGSGIKLSSTSmtPVTTPelLTPVGSAEYM 178
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
299-356 8.51e-04

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: 41.33  E-value: 8.51e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1370461664 299 WGSSLRMALSLAqglaFLHEERwqngqykpGIAHRDLSSQNVLIREDGSCAIGDLGLA 356
Cdd:cd08528   116 WNIFVQMVLALR----YLHKEK--------QIVHRDLKPNNIMLGEDDKVTITDFGLA 161
PTKc_Aatyk1 cd05087
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 1; PTKs ...
277-356 9.11e-04

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: 41.13  E-value: 9.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 277 LLVLELHPKGSL------CHYLTQYTSDWGSSLRMALSLAQGLAFLHEERWqngqykpgiAHRDLSSQNVLIREDGSCAI 350
Cdd:cd05087    73 LLVMEFCPLGDLkgylrsCRAAESMAPDPLTLQRMACEVACGLLHLHRNNF---------VHSDLALRNCLLTADLTVKI 143

                  ....*.
gi 1370461664 351 GDLGLA 356
Cdd:cd05087   144 GDYGLS 149
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
225-369 9.66e-04

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: 41.20  E-value: 9.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 225 GKLVAIK---------AFPprsvaqFQAERALYELPGLQHDHIVRFITASRGGP---GRLLSGPLLVLEL--HPKGSLCH 290
Cdd:cd07865    37 GQIVALKkvlmenekeGFP------ITALREIKILQLLKHENVVNLIEICRTKAtpyNRYKGSIYLVFEFceHDLAGLLS 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 291 YlTQYTSDWGSSLRMALSLAQGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDLGLA--LVLPGLTQPPAW 368
Cdd:cd07865   111 N-KNVKFTLSEIKKVMKMLLNGLYYIHRNK---------ILHRDMKAANILITKDGVLKLADFGLAraFSLAKNSQPNRY 180

                  .
gi 1370461664 369 T 369
Cdd:cd07865   181 T 181
PTK_Ryk cd05043
Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase ...
206-356 9.82e-04

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: 40.90  E-value: 9.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 206 SQQVIREGGHAVVWAGQLQGKLVAIKAFPPRSVA----QFQAERALYE---LPGLQHDHIVRFITASRGGPGRllsgPLL 278
Cdd:cd05043    10 LSDLLQEGTFGRIFHGILRDEKGKEEEVLVKTVKdhasEIQVTMLLQEsslLYGLSHQNLLPILHVCIEDGEK----PMV 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 279 VLELHPKGSLCHYLTQ---YTSDWGSSLR------MALSLAQGLAFLHeerwqngqyKPGIAHRDLSSQNVLIREDGSCA 349
Cdd:cd05043    86 LYPYMNWGNLKLFLQQcrlSEANNPQALStqqlvhMALQIACGMSYLH---------RRGVIHKDIAARNCVIDDELQVK 156

                  ....*..
gi 1370461664 350 IGDLGLA 356
Cdd:cd05043   157 ITDNALS 163
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
188-358 9.95e-04

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: 41.17  E-value: 9.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 188 DSGRDWSVELQELpelcFSQQVIREGGHAVVWAGQLQGKlVAIKAFP-----PRSVAQFQAERALyeLPGLQHDHIVRFI 262
Cdd:cd14149     2 DSSYYWEIEASEV----MLSTRIGSGSFGTVYKGKWHGD-VAVKILKvvdptPEQFQAFRNEVAV--LRKTRHVNILLFM 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 263 tasrggpGRLLSGPLLVLELHPKGSLCHY---LTQYTSDWGSSLRMALSLAQGLAFLHEErwqngqykpGIAHRDLSSQN 339
Cdd:cd14149    75 -------GYMTKDNLAIVTQWCEGSSLYKhlhVQETKFQMFQLIDIARQTAQGMDYLHAK---------NIIHRDMKSNN 138
                         170
                  ....*....|....*....
gi 1370461664 340 VLIREDGSCAIGDLGLALV 358
Cdd:cd14149   139 IFLHEGLTVKIGDFGLATV 157
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
224-356 1.00e-03

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: 40.71  E-value: 1.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 224 QGKLVAIKAFPPRSVAQFQ----AERALYELPGLQHDHIVRFITASRGGpgrllSGPLLVLELHPKGSLCHYLTQytsdw 299
Cdd:cd14161    26 SGRLVAIKSIRKDRIKDEQdllhIRREIEIMSSLNHPHIISVYEVFENS-----SKIVIVMEYASRGDLYDYISE----- 95
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1370461664 300 gsslRMALSLAQGLAFLHE-ERWQNGQYKPGIAHRDLSSQNVLIREDGSCAIGDLGLA 356
Cdd:cd14161    96 ----RQRLSELEARHFFRQiVSAVHYCHANGIVHRDLKLENILLDANGNIKIADFGLS 149
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
207-356 1.01e-03

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: 41.36  E-value: 1.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 207 QQVIREGGHAVVWAG--QLQGKLVAIKAFPPRSVAQFQAERALYE---LPGLQHDHIVRFITASRGGPGRLLSGPLLVLE 281
Cdd:cd07834     5 LKPIGSGAYGVVCSAydKRTGRKVAIKKISNVFDDLIDAKRILREikiLRHLKHENIIGLLDILRPPSPEEFNDVYIVTE 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 282 LhpkgslchyltqYTSDWGSSLRMALSLA---------Q---GLAFLHEErwqngqykpGIAHRDLSSQNVLIREDGSCA 349
Cdd:cd07834    85 L------------METDLHKVIKSPQPLTddhiqyflyQilrGLKYLHSA---------GVIHRDLKPSNILVNSNCDLK 143

                  ....*..
gi 1370461664 350 IGDLGLA 356
Cdd:cd07834   144 ICDFGLA 150
PTKc_EphR_B cd05065
Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze ...
207-379 1.04e-03

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: 41.01  E-value: 1.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 207 QQVIREGGHAVVWAGQLQ--GK---LVAIK----AFPPRSVAQFQAERALyeLPGLQHDHIVRF---ITASRggpgrlls 274
Cdd:cd05065     9 EEVIGAGEFGEVCRGRLKlpGKreiFVAIKtlksGYTEKQRRDFLSEASI--MGQFDHPNIIHLegvVTKSR-------- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 275 gPLLVL-ELHPKGSLCHYLTQYTSDWG--SSLRMALSLAQGLAFLHEERWqngqykpgiAHRDLSSQNVLIREDGSCAIG 351
Cdd:cd05065    79 -PVMIItEFMENGALDSFLRQNDGQFTviQLVGMLRGIAAGMKYLSEMNY---------VHRDLAARNILVNSNLVCKVS 148
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1370461664 352 DLGLALVLPGLTQPPAWT-------PTQPQGPAAI 379
Cdd:cd05065   149 DFGLSRFLEDDTSDPTYTsslggkiPIRWTAPEAI 183
PTKc_Mer cd14204
Catalytic Domain of the Protein Tyrosine Kinase, Mer; PTKs catalyze the transfer of the ...
208-356 1.16e-03

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: 40.69  E-value: 1.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 208 QVIREGGHAVVWAGQLQ-----GKLVAIKA-----FPPRSVAQFQAERALyeLPGLQHDHIVRFITASRGGPGRLLSGPL 277
Cdd:cd14204    13 KVLGEGEFGSVMEGELQqpdgtNHKVAVKTmkldnFSQREIEEFLSEAAC--MKDFNHPNVIRLLGVCLEVGSQRIPKPM 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 278 LVLELHPKGSLCHYLTQYTSDWGSS-------LRMALSLAQGLAFLHEERWqngqykpgiAHRDLSSQNVLIREDGSCAI 350
Cdd:cd14204    91 VILPFMKYGDLHSFLLRSRLGSGPQhvplqtlLKFMIDIALGMEYLSSRNF---------LHRDLAARNCMLRDDMTVCV 161

                  ....*.
gi 1370461664 351 GDLGLA 356
Cdd:cd14204   162 ADFGLS 167
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
228-356 1.17e-03

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: 40.53  E-value: 1.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 228 VAIKAFPPRSVAQFQAE----RALYELPGLQHDHIVRFITASRGGPGRLLsgplLVLELHPKGSLCHYLT-QYTSDWGSS 302
Cdd:cd14165    29 VAIKIIDKKKAPDDFVEkflpRELEILARLNHKSIIKTYEIFETSDGKVY----IVMELGVQGDLLEFIKlRGALPEDVA 104
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1370461664 303 LRMALSLAQGLAFLHEErwqngqykpGIAHRDLSSQNVLIREDGSCAIGDLGLA 356
Cdd:cd14165   105 RKMFHQLSSAIKYCHEL---------DIVHRDLKCENLLLDKDFNIKLTDFGFS 149
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
219-367 1.24e-03

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: 40.80  E-value: 1.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 219 WAGQLQGKLVAIKAFPPRSVAQFQAERALYElpGLQHDHIVRFItasrggpGRLLSGPLL--VLELHPKGSLCHYLTQYT 296
Cdd:cd14063    21 WHGDVAIKLLNIDYLNEEQLEAFKEEVAAYK--NTRHDNLVLFM-------GACMDPPHLaiVTSLCKGRTLYSLIHERK 91
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370461664 297 SDWGSS--LRMALSLAQGLAFLHeerwqngqyKPGIAHRDLSSQNVLIrEDGSCAIGDLGLaLVLPGLTQPPA 367
Cdd:cd14063    92 EKFDFNktVQIAQQICQGMGYLH---------AKGIIHKDLKSKNIFL-ENGRVVITDFGL-FSLSGLLQPGR 153
PTKc_TrkC cd05094
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze ...
227-356 1.48e-03

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: 40.38  E-value: 1.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 227 LVAIKAFPPRSVA---QFQAERALyeLPGLQHDHIVRFITASRGGpgrllsGPL-LVLELHPKGSLCHYLTQYTSD---- 298
Cdd:cd05094    37 LVAVKTLKDPTLAarkDFQREAEL--LTNLQHDHIVKFYGVCGDG------DPLiMVFEYMKHGDLNKFLRAHGPDamil 108
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370461664 299 -------------WGSSLRMALSLAQGLAFLHEERWqngqykpgiAHRDLSSQNVLIREDGSCAIGDLGLA 356
Cdd:cd05094   109 vdgqprqakgelgLSQMLHIATQIASGMVYLASQHF---------VHRDLATRNCLVGANLLVKIGDFGMS 170
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
180-356 1.48e-03

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: 40.77  E-value: 1.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 180 EPVPE------PRPDSGRDWSVELQELPELCFSQQVIREGgHAVVWAGQLQGKLVAIKAFP----PRSVAQFQAERALYE 249
Cdd:cd05101     6 AGVSEyelpedPKWEFPRDKLTLGKPLGEGCFGQVVMAEA-VGIDKDKPKEAVTVAVKMLKddatEKDLSDLVSEMEMMK 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 250 LPGlQHDHIVRFITASRGGpgrllsGPLLVL-ELHPKGSLCHYL-------TQYTSD----------WGSSLRMALSLAQ 311
Cdd:cd05101    85 MIG-KHKNIINLLGACTQD------GPLYVIvEYASKGNLREYLrarrppgMEYSYDinrvpeeqmtFKDLVSCTYQLAR 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1370461664 312 GLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDLGLA 356
Cdd:cd05101   158 GMEYLASQK---------CIHRDLAARNVLVTENNVMKIADFGLA 193
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
201-356 1.49e-03

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: 40.33  E-value: 1.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 201 PELCFS-QQVIREGGHAVVWAG-QLQ-GKLVAIKAFPPRSVAQfQAERALYELPGLQHDHIVRFItasrgGPGRLLSGPL 277
Cdd:cd06612     1 PEEVFDiLEKLGEGSYGSVYKAiHKEtGQVVAIKVVPVEEDLQ-EIIKEISILKQCDSPYIVKYY-----GSYFKNTDLW 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 278 LVLELHPKGSLCHyLTQYTSDWGSSLRMALSLAQ---GLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDLG 354
Cdd:cd06612    75 IVMEYCGAGSVSD-IMKITNKTLTEEEIAAILYQtlkGLEYLHSNK---------KIHRDIKAGNILLNEEGQAKLADFG 144

                  ..
gi 1370461664 355 LA 356
Cdd:cd06612   145 VS 146
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
278-355 1.51e-03

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: 40.48  E-value: 1.51e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370461664 278 LVLELHPKGSLCHYLTQYTSDWGSSLRMALSLAQGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDLGL 355
Cdd:cd06654    94 VVMEYLAGGSLTDVVTETCMDEGQIAAVCRECLQALEFLHSNQ---------VIHRDIKSDNILLGMDGSVKLTDFGF 162
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
207-359 1.59e-03

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: 40.38  E-value: 1.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 207 QQVIREGGHAVVWAGQLQGKL---VAIKAFPPRSVAQFQA--ERALYELPGLQHDHIVRFITASRggpgrLLSGPLLVLE 281
Cdd:cd14201    11 KDLVGHGAFAVVFKGRHRKKTdweVAIKSINKKNLSKSQIllGKEIKILKELQHENIVALYDVQE-----MPNSVFLVME 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 282 LHPKGSLCHYLTQYTSDWGSSLRMAL-SLAQGLAFLHEErwqngqykpGIAHRDLSSQNVLI----REDGSCA-----IG 351
Cdd:cd14201    86 YCNGGDLADYLQAKGTLSEDTIRVFLqQIAAAMRILHSK---------GIIHRDLKPQNILLsyasRKKSSVSgirikIA 156

                  ....*...
gi 1370461664 352 DLGLALVL 359
Cdd:cd14201   157 DFGFARYL 164
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
182-356 1.63e-03

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: 40.38  E-value: 1.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 182 VPE-PRPDSGRDWSVELQELPELCFSQQVIREgghAVVWAGQLQGKL--VAIKAFPP----RSVAQFQAERALYELPGlQ 254
Cdd:cd05098     2 LPEdPRWELPRDRLVLGKPLGEGCFGQVVLAE---AIGLDKDKPNRVtkVAVKMLKSdateKDLSDLISEMEMMKMIG-K 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 255 HDHIVRFITASRGgpgrllSGPLLVL-ELHPKGSLCHYLTQ---------YTSDWGSSLRM--------ALSLAQGLAFL 316
Cdd:cd05098    78 HKNIINLLGACTQ------DGPLYVIvEYASKGNLREYLQArrppgmeycYNPSHNPEEQLsskdlvscAYQVARGMEYL 151
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1370461664 317 HEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDLGLA 356
Cdd:cd05098   152 ASKK---------CIHRDLAARNVLVTEDNVMKIADFGLA 182
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
242-355 1.80e-03

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: 40.17  E-value: 1.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 242 QAERALYELPGLQHDHIVRF----------ITASRGGPGRLLSGPLLV-LELHPKGSLCHYLTQ---YTSDWGSSLRMAL 307
Cdd:cd14047    45 KAEREVKALAKLDHPNIVRYngcwdgfdydPETSSSNSSRSKTKCLFIqMEFCEKGTLESWIEKrngEKLDKVLALEIFE 124
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1370461664 308 SLAQGLAFLHEErwqngqykpGIAHRDLSSQNVLIREDGSCAIGDLGL 355
Cdd:cd14047   125 QITKGVEYIHSK---------KLIHRDLKPSNIFLVDTGKVKIGDFGL 163
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
250-356 1.90e-03

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: 39.86  E-value: 1.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 250 LPGLQHDHIVR-----------FItasrggpgrllsgpllVLELHPKGSLCHYLTQYTSDWGS-SLRMALSLAQGLAFLH 317
Cdd:cd14080    56 LRKLRHPNIIQvysifergskvFI----------------FMEYAEHGDLLEYIQKRGALSESqARIWFRQLALAVQYLH 119
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1370461664 318 EErwqngqykpGIAHRDLSSQNVLIREDGSCAIGDLGLA 356
Cdd:cd14080   120 SL---------DIAHRDLKCENILLDSNNNVKLSDFGFA 149
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
311-359 1.93e-03

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: 40.25  E-value: 1.93e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1370461664 311 QGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDLGLALVL 359
Cdd:cd05608   116 SGLEHLHQRR---------IIYRDLKPENVLLDDDGNVRISDLGLAVEL 155
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
254-356 1.98e-03

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: 40.16  E-value: 1.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 254 QHDHIVRFITASRggpgrlLSGPLLVL-ELHPKGSLCHYLTQYTSDWGSS---LRMALSLAQGLAFLHEErwqngqykpG 329
Cdd:cd05055    97 NHENIVNLLGACT------IGGPILVItEYCCYGDLLNFLRRKRESFLTLedlLSFSYQVAKGMAFLASK---------N 161
                          90       100
                  ....*....|....*....|....*..
gi 1370461664 330 IAHRDLSSQNVLIREDGSCAIGDLGLA 356
Cdd:cd05055   162 CIHRDLAARNVLLTHGKIVKICDFGLA 188
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
277-360 2.20e-03

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: 39.90  E-value: 2.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 277 LLVLELHPKGSLCHYLT-QYTSDWGSSLRMALSLAQGLAFLHeerwqngqyKPGIAHRDLSSQNVLIREDGSCAIGDLGL 355
Cdd:cd14182    86 FLVFDLMKKGELFDYLTeKVTLSEKETRKIMRALLEVICALH---------KLNIVHRDLKPENILLDDDMNIKLTDFGF 156

                  ....*
gi 1370461664 356 ALVLP 360
Cdd:cd14182   157 SCQLD 161
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
306-360 2.23e-03

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: 40.03  E-value: 2.23e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1370461664 306 ALSLAQGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDLGLALVLP 360
Cdd:cd05605   108 AAEITCGLEHLHSER---------IVYRDLKPENILLDDHGHVRISDLGLAVEIP 153
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
312-360 2.27e-03

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: 39.95  E-value: 2.27e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1370461664 312 GLAFLHEErwqngqykpGIAHRDLSSQNVLIREDGSCAIGDLGLALVLP 360
Cdd:cd05632   116 GLEDLHRE---------NTVYRDLKPENILLDDYGHIRISDLGLAVKIP 155
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
210-356 2.33e-03

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: 39.90  E-value: 2.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 210 IREGGHAVVWAGQ--LQGKLVAIK---------AFPPRSVAQFQAeralyeLPGLQHDHIVrfiTASRGGPGRLLSGPLL 278
Cdd:cd07843    13 IEEGTYGVVYRARdkKTGEIVALKklkmekekeGFPITSLREINI------LLKLQHPNIV---TVKEVVVGSNLDKIYM 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 279 VLEL--HP-KGSLCHYLTQYTSdwgSSLR-MALSLAQGLAFLHEeRWqngqykpgIAHRDLSSQNVLIREDGSCAIGDLG 354
Cdd:cd07843    84 VMEYveHDlKSLMETMKQPFLQ---SEVKcLMLQLLSGVAHLHD-NW--------ILHRDLKTSNLLLNNRGILKICDFG 151

                  ..
gi 1370461664 355 LA 356
Cdd:cd07843   152 LA 153
PTKc_Aatyk cd05042
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinases; PTKs ...
277-356 2.60e-03

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: 39.49  E-value: 2.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 277 LLVLELHPKGSLCHYL------TQYTSDWGSSLRMALSLAQGLAFLHEERWqngqykpgiAHRDLSSQNVLIREDGSCAI 350
Cdd:cd05042    71 LLVMEFCDLGDLKAYLrserehERGDSDTRTLQRMACEVAAGLAHLHKLNF---------VHSDLALRNCLLTSDLTVKI 141

                  ....*.
gi 1370461664 351 GDLGLA 356
Cdd:cd05042   142 GDYGLA 147
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
278-355 2.61e-03

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: 39.70  E-value: 2.61e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370461664 278 LVLELHPKGSLCHYLTQYTSDWGSSLRMALSLAQGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDLGL 355
Cdd:cd06656    93 VVMEYLAGGSLTDVVTETCMDEGQIAAVCRECLQALDFLHSNQ---------VIHRDIKSDNILLGMDGSVKLTDFGF 161
PTKc_DDR cd05051
Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze ...
253-355 2.73e-03

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: 39.63  E-value: 2.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 253 LQHDHIVRFITASRGGPgrllsgPL-LVLELHPKGSLCHYLTQY-------------TSDWGSSLRMALSLAQGLAFLHE 318
Cdd:cd05051    76 LKDPNIVRLLGVCTRDE------PLcMIVEYMENGDLNQFLQKHeaetqgasatnskTLSYGTLLYMATQIASGMKYLES 149
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1370461664 319 ERWqngqykpgiAHRDLSSQNVLIREDGSCAIGDLGL 355
Cdd:cd05051   150 LNF---------VHRDLATRNCLVGPNYTIKIADFGM 177
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
309-361 2.77e-03

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: 39.55  E-value: 2.77e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1370461664 309 LAQGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDLGLALVLPG 361
Cdd:cd05578   109 IVLALDYLHSKN---------IIHRDIKPDNILLDEQGHVHITDFNIATKLTD 152
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
208-356 2.85e-03

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: 39.38  E-value: 2.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 208 QVIREGGHAVVWAGQ--LQGKLVAIKAF----PPRSVAQFQAERA-LYELPGLQHDHIVRFItasrggpGRLLSGPLL-- 278
Cdd:cd06917     7 ELVGRGSYGAVYRGYhvKTGRVVALKVLnldtDDDDVSDIQKEVAlLSQLKLGQPKNIIKYY-------GSYLKGPSLwi 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370461664 279 VLELHPKGSLCHYL-TQYTSDWGSSLRMALSLaQGLAFLHeerwqngqyKPGIAHRDLSSQNVLIREDGSCAIGDLGLA 356
Cdd:cd06917    80 IMDYCEGGSIRTLMrAGPIAERYIAVIMREVL-VALKFIH---------KDGIIHRDIKAANILVTNTGNVKLCDFGVA 148
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
250-364 3.36e-03

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: 39.45  E-value: 3.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 250 LPGLQHDHIVRFItasrggpGRLLSGP----LLVLELHPKGSLCHYLTQYTSDwGSSL------RMALSLAQGLAFLHEE 319
Cdd:cd08217    53 LRELKHPNIVRYY-------DRIVDRAnttlYIVMEYCEGGDLAQLIKKCKKE-NQYIpeefiwKIFTQLLLALYECHNR 124
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1370461664 320 RWQNGQykpgIAHRDLSSQNVLIREDGSCAIGDLGLALVLPGLTQ 364
Cdd:cd08217   125 SVGGGK----ILHRDLKPANIFLDSDNNVKLGDFGLARVLSHDSS 165
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
208-355 3.36e-03

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: 39.21  E-value: 3.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 208 QVIREGGHAVVWAGQLQ--GKLVAIKAFPPRSVAQfqaERALYELPGL----QHDHIVRFITA-----SRGGPGRLLsgp 276
Cdd:cd06608    12 EVIGEGTYGKVYKARHKktGQLAAIKIMDIIEDEE---EEIKLEINILrkfsNHPNIATFYGAfikkdPPGGDDQLW--- 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 277 lLVLELHPKGSLCHyLTQYTSDWGSSLRMAL------SLAQGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAI 350
Cdd:cd06608    86 -LVMEYCGGGSVTD-LVKGLRKKGKRLKEEWiayilrETLRGLAYLHENK---------VIHRDIKGQNILLTEEAEVKL 154

                  ....*
gi 1370461664 351 GDLGL 355
Cdd:cd06608   155 VDFGV 159
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
228-356 3.79e-03

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: 39.19  E-value: 3.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 228 VAIKAFPPRSVAQFQAERALYE---LPGLQHDHIVR---------FItasrggpgrllsgpLLVLELHPKGSLCHYLTQY 295
Cdd:cd14121    24 VAVKCVSKSSLNKASTENLLTEielLKKLKHPHIVElkdfqwdeeHI--------------YLIMEYCSGGDLSRFIRSR 89
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370461664 296 TSDWGSSLRMALS-LAQGLAFLHEErwqngqykpGIAHRDLSSQNVLI--REDGSCAIGDLGLA 356
Cdd:cd14121    90 RTLPESTVRRFLQqLASALQFLREH---------NISHMDLKPQNLLLssRYNPVLKLADFGFA 144
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
209-356 3.87e-03

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: 39.26  E-value: 3.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 209 VIREGGHAVVW-AGQLQ-GKLVAIKA---FPPRSVA--QFQAERALYELPGL----QHDHIVRFItasrggpgRLLSGP- 276
Cdd:cd13993     7 PIGEGAYGVVYlAVDLRtGRKYAIKClykSGPNSKDgnDFQKLPQLREIDLHrrvsRHPNIITLH--------DVFETEv 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 277 --LLVLELHPKGSLCHYLT---QYTSDWGSSLRMALSLAQGLAFLHEErwqngqykpGIAHRDLSSQNVLIRED-GSCAI 350
Cdd:cd13993    79 aiYIVLEYCPNGDLFEAITenrIYVGKTELIKNVFLQLIDAVKHCHSL---------GIYHRDIKPENILLSQDeGTVKL 149

                  ....*.
gi 1370461664 351 GDLGLA 356
Cdd:cd13993   150 CDFGLA 155
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
329-361 4.10e-03

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: 39.12  E-value: 4.10e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1370461664 329 GIAHRDLSSQNVLIREDGSCAIGDLGLALVLPG 361
Cdd:cd05607   124 KIVYRDMKPENVLLDDNGNCRLSDLGLAVEVKE 156
PTKc_Aatyk3 cd14206
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 3; PTKs ...
277-356 4.19e-03

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: 39.16  E-value: 4.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 277 LLVLELHPKGSLCHYLTQY-----------TSDWGSSLRMALSLAQGLAFLHEERWqngqykpgiAHRDLSSQNVLIRED 345
Cdd:cd14206    73 LLIMEFCQLGDLKRYLRAQrkadgmtpdlpTRDLRTLQRMAYEITLGLLHLHKNNY---------IHSDLALRNCLLTSD 143
                          90
                  ....*....|.
gi 1370461664 346 GSCAIGDLGLA 356
Cdd:cd14206   144 LTVRIGDYGLS 154
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
210-355 4.21e-03

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: 39.12  E-value: 4.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 210 IREGGHAVVWAGQ--LQGKLVAIKAFPPRS------VAQFQAERALyeLPGLQHDHIVRF---ITASRggpgrllsgPL- 277
Cdd:cd05579     1 ISRGAYGRVYLAKkkSTGDLYAIKVIKKRDmirknqVDSVLAERNI--LSQAQNPFVVKLyysFQGKK---------NLy 69
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370461664 278 LVLELHPKGSLCHYLTQYTSDWGSSLRMALS-LAQGLAFLHEErwqngqykpGIAHRDLSSQNVLIREDGSCAIGDLGL 355
Cdd:cd05579    70 LVMEYLPGGDLYSLLENVGALDEDVARIYIAeIVLALEYLHSH---------GIIHRDLKPDNILIDANGHLKLTDFGL 139
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
208-356 4.22e-03

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: 38.76  E-value: 4.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 208 QVIREGGHAVVWAGQLQG--KLVAIKA----FPPRSVAQFQAERALyeLPGLQHDHIVRFI-TASRGGPgrllsgPLLVL 280
Cdd:cd05084     2 ERIGRGNFGEVFSGRLRAdnTPVAVKScretLPPDLKAKFLQEARI--LKQYSHPNIVRLIgVCTQKQP------IYIVM 73
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370461664 281 ELHPKGSLCHYLTQYTSDWGSS--LRMALSLAQGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDLGLA 356
Cdd:cd05084    74 ELVQGGDFLTFLRTEGPRLKVKelIRMVENAAAGMEYLESKH---------CIHRDLAARNCLVTEKNVLKISDFGMS 142
PTKc_Musk cd05050
Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the ...
227-356 4.49e-03

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: 39.04  E-value: 4.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 227 LVAIKAFPPRSVAQ----FQAERALyeLPGLQHDHIVRFITASRGGPgrllsgPL-LVLELHPKGSLCHYLTQYTSDWGS 301
Cdd:cd05050    37 MVAVKMLKEEASADmqadFQREAAL--MAEFDHPNIVKLLGVCAVGK------PMcLLFEYMAYGDLNEFLRHRSPRAQC 108
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370461664 302 S-----------------------LRMALSLAQGLAFLHEERWqngqykpgiAHRDLSSQNVLIREDGSCAIGDLGLA 356
Cdd:cd05050   109 SlshstssarkcglnplplscteqLCIAKQVAAGMAYLSERKF---------VHRDLATRNCLVGENMVVKIADFGLS 177
PK_KSR2 cd14153
Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to ...
219-355 4.80e-03

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: 38.84  E-value: 4.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 219 WAGQLQGKLVAIKAFPPRSVAQFQAERALYElpGLQHDHIVRFItasrggpGRLLSGPLLVLelhpKGSLCHYLTQYTS- 297
Cdd:cd14153    21 WHGEVAIRLIDIERDNEEQLKAFKREVMAYR--QTRHENVVLFM-------GACMSPPHLAI----ITSLCKGRTLYSVv 87
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370461664 298 -------DWGSSLRMALSLAQGLAFLHEErwqngqykpGIAHRDLSSQNVLIrEDGSCAIGDLGL 355
Cdd:cd14153    88 rdakvvlDVNKTRQIAQEIVKGMGYLHAK---------GILHKDLKSKNVFY-DNGKVVITDFGL 142
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
207-356 4.82e-03

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: 38.82  E-value: 4.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 207 QQVIREGGHAVVWAG--QLQGKLVAIKAfpprsVAQFQA-ERALYE-LP-------GLQHDHIVRFI----TASRggpgr 271
Cdd:cd14162     5 GKTLGHGSYAVVKKAysTKHKCKVAIKI-----VSKKKApEDYLQKfLPreievikGLKHPNLICFYeaieTTSR----- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 272 llsgPLLVLELHPKGSLCHYLTQYTSdwGSSLRMALSLAQ---GLAFLHEErwqngqykpGIAHRDLSSQNVLIREDGSC 348
Cdd:cd14162    75 ----VYIIMELAENGDLLDYIRKNGA--LPEPQARRWFRQlvaGVEYCHSK---------GVVHRDLKCENLLLDKNNNL 139

                  ....*...
gi 1370461664 349 AIGDLGLA 356
Cdd:cd14162   140 KITDFGFA 147
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
225-358 4.86e-03

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: 38.61  E-value: 4.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 225 GKLVAIKAFPPRSVAQFQA-----ERALYELPGLQHDHIVRFITasrggpgrLLSGP---LLVLELHPKGSLCHYLtqyt 296
Cdd:cd14098    25 GKMRAIKQIVKRKVAGNDKnlqlfQREINILKSLEHPGIVRLID--------WYEDDqhiYLVMEYVEGGDLMDFI---- 92
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370461664 297 SDWGS-----SLRMALSLAQGLAFLHeerwqngqyKPGIAHRDLSSQNVLIREDGS--CAIGDLGLALV 358
Cdd:cd14098    93 MAWGAipeqhARELTKQILEAMAYTH---------SMGITHRDLKPENILITQDDPviVKISDFGLAKV 152
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
226-364 4.97e-03

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: 38.84  E-value: 4.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 226 KLVAIKAFPPRSVAQ-FQAERALYELP---GLQHDHIVRFITASRGGpgrllSGPLLVLELHPKGSLCHYLTQYTSDWGS 301
Cdd:cd14188    27 KVYAAKIIPHSRVSKpHQREKIDKEIElhrILHHKHVVQFYHYFEDK-----ENIYILLEYCSRRSMAHILKARKVLTEP 101
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370461664 302 SLRMAL-SLAQGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDLGLALVLPGLTQ 364
Cdd:cd14188   102 EVRYYLrQIVSGLKYLHEQE---------ILHRDLKLGNFFINENMELKVGDFGLAARLEPLEH 156
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
309-356 4.97e-03

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: 38.67  E-value: 4.97e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1370461664 309 LAQGLAFLHeerwqngqyKPGIAHRDLSSQNVLIREDGSCAIGDLGLA 356
Cdd:cd07830   108 ILQGLAHIH---------KHGFFHRDLKPENLLVSGPEVVKIADFGLA 146
PTKc_TrkB cd05093
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze ...
227-356 5.16e-03

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: 38.87  E-value: 5.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 227 LVAIKAFPPRS---VAQFQAERALyeLPGLQHDHIVRFITASrggpgrLLSGPL-LVLELHPKGSLCHYLTQYTSD---- 298
Cdd:cd05093    37 LVAVKTLKDASdnaRKDFHREAEL--LTNLQHEHIVKFYGVC------VEGDPLiMVFEYMKHGDLNKFLRAHGPDavlm 108
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370461664 299 ----------WGSSLRMALSLAQGLAFLHEERWqngqykpgiAHRDLSSQNVLIREDGSCAIGDLGLA 356
Cdd:cd05093   109 aegnrpaeltQSQMLHIAQQIAAGMVYLASQHF---------VHRDLATRNCLVGENLLVKIGDFGMS 167
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
207-354 5.21e-03

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: 38.82  E-value: 5.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 207 QQVIREGGHAVVWAGQL--QGKLVAIKAF--PPR-SVAQFQAERALYELpgLQHDHIVRFIT---ASRGGPGRLLsgpLL 278
Cdd:cd13986     5 QRLLGEGGFSFVYLVEDlsTGRLYALKKIlcHSKeDVKEAMREIENYRL--FNHPNILRLLDsqiVKEAGGKKEV---YL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 279 VLELHPKGSLCHYLTQyTSDWGSS------LRMALSLAQGLAFLHEERwqngqyKPGIAHRDLSSQNVLIREDGSCAIGD 352
Cdd:cd13986    80 LLPYYKRGSLQDEIER-RLVKGTFfpedriLHIFLGICRGLKAMHEPE------LVPYAHRDIKPGNVLLSEDDEPILMD 152

                  ..
gi 1370461664 353 LG 354
Cdd:cd13986   153 LG 154
PK_GC-A_B cd14042
Pseudokinase domain of the membrane Guanylate Cyclase receptors, GC-A and GC-B; The ...
224-356 6.48e-03

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: 38.35  E-value: 6.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 224 QGKLVAIKAFPPRSVAQFQAER-ALYELPGLQHDHIVRFITASrGGPGRLlsgpLLVLELHPKGSLCHYLT--QYTSDW- 299
Cdd:cd14042    29 KGNLVAIKKVNKKRIDLTREVLkELKHMRDLQHDNLTRFIGAC-VDPPNI----CILTEYCPKGSLQDILEneDIKLDWm 103
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 300 -GSSLRMalSLAQGLAFLHeerwqNGQYKpgiAHRDLSSQNVLIreDGS--CAIGDLGLA 356
Cdd:cd14042   104 fRYSLIH--DIVKGMHYLH-----DSEIK---SHGNLKSSNCVV--DSRfvLKITDFGLH 151
STKc_RIP2 cd14026
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze ...
278-356 6.63e-03

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: 38.36  E-value: 6.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 278 LVLELHPKGSL---CHYLTQYTS-DWGSSLRMALSLAQGLAFLHeerwqngQYKPGIAHRDLSSQNVLIREDGSCAIGDL 353
Cdd:cd14026    74 IVTEYMTNGSLnelLHEKDIYPDvAWPLRLRILYEIALGVNYLH-------NMSPPLLHHDLKTQNILLDGEFHVKIADF 146

                  ...
gi 1370461664 354 GLA 356
Cdd:cd14026   147 GLS 149
PTK_CCK4 cd05046
Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also ...
226-382 7.00e-03

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: 38.21  E-value: 7.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 226 KLVAIKAFPPRSVAQFQAE--RALYELPGLQHDHIVRFItasrgGPGRLLSGPLLVLELHPKGSLCHYL--TQYTSDWGS 301
Cdd:cd05046    36 TLVLVKALQKTKDENLQSEfrRELDMFRKLSHKNVVRLL-----GLCREAEPHYMILEYTDLGDLKQFLraTKSKDEKLK 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 302 S--------LRMALSLAQGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGdlglalvLPGLTQPP------- 366
Cdd:cd05046   111 PpplstkqkVALCTQIALGMDHLSNAR---------FVHRDLAARNCLVSSQREVKVS-------LLSLSKDVynseyyk 174
                         170
                  ....*....|....*....
gi 1370461664 367 ---AWTPTQPQGPAAIMED 382
Cdd:cd05046   175 lrnALIPLRWLAPEAVQED 193
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
312-370 7.16e-03

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: 38.33  E-value: 7.16e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1370461664 312 GLAFLHEErwqngqykpGIAHRDLSSQNVLIREDGSCAIGDLGLALVLPGLTQPPAWTP 370
Cdd:cd05580   113 ALEYLHSL---------DIVYRDLKPENLLLDSDGHIKITDFGFAKRVKDRTYTLCGTP 162
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
225-356 7.16e-03

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: 38.15  E-value: 7.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 225 GKLVAIKAFPPRSVAQF----QAERALYELPGLQHDHIVRF--ITASRggpgrllSGPLLVLELHPKGSLCHYL-TQYTS 297
Cdd:cd14663    25 GESVAIKIIDKEQVAREgmveQIKREIAIMKLLRHPNIVELheVMATK-------TKIFFVMELVTGGELFSKIaKNGRL 97
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1370461664 298 DWGSSLRMALSLAQGLAFLHeerwqngqyKPGIAHRDLSSQNVLIREDGSCAIGDLGLA 356
Cdd:cd14663    98 KEDKARKYFQQLIDAVDYCH---------SRGVFHRDLKPENLLLDEDGNLKISDFGLS 147
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
225-356 7.63e-03

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: 38.02  E-value: 7.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461664 225 GKLVAIKAFPPRSVAQFQAERALYELPGLQHDHIVRFITASRGGPG-----RLLSGPLLVLELHPKGSLCH-----YLTQ 294
Cdd:cd14006    18 GREFAAKFIPKRDKKKEAVLREISILNQLQHPRIIQLHEAYESPTElvlilELCSGGELLDRLAERGSLSEeevrtYMRQ 97
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370461664 295 ytsdwgsslrmalsLAQGLAFLHEERwqngqykpgIAHRDLSSQNVLI--REDGSCAIGDLGLA 356
Cdd:cd14006    98 --------------LLEGLQYLHNHH---------ILHLDLKPENILLadRPSPQIKIIDFGLA 138
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
330-359 7.65e-03

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


Pssm-ID: 270858 [Multi-domain]  Cd Length: 256  Bit Score: 38.25  E-value: 7.65e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1370461664 330 IAHRDLSSQNVLIREDGSCAIGDLGLALVL 359
Cdd:cd08218   122 ILHRDIKSQNIFLTKDGIIKLGDFGIARVL 151
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
311-356 8.56e-03

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: 37.99  E-value: 8.56e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1370461664 311 QGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDLGLA 356
Cdd:cd06609   109 LGLEYLHSEG---------KIHRDIKAANILLSEEGDVKLADFGVS 145
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
305-378 9.49e-03

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: 38.06  E-value: 9.49e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370461664 305 MALSLAQGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDLGLALVLPGltqppawTPTQPQGPAA 378
Cdd:cd07866   120 YMLQLLEGINYLHENH---------ILHRDIKAANILIDNQGILKIADFGLARPYDG-------PPPNPKGGGG 177
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH