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Conserved domains on  [gi|108936965|ref|NP_033742|]
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serine/threonine-protein kinase receptor R3 isoform a precursor [Mus musculus]

Protein Classification

TGFB receptor family serine/threonine-protein kinase (domain architecture ID 10553646)

TGFB (transforming growth factor-beta) receptor family serine/threonine-protein kinase contains an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain that catalyzes the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
STKc_ACVR1_ALK1 cd14142
Catalytic domain of the Serine/Threonine Kinases, Activin Type I Receptor and Activin ...
195-492 0e+00

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: 640.64  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108936965 195 RTVARQVALVECVGKGRYGEVWRGSWHGESVAVKIFSSRDEQSWFRETEIYNTVLLRHDNILGFIASDMTSRNSSTQLWL 274
Cdd:cd14142    1 RTVARQITLVECIGKGRYGEVWRGQWQGESVAVKIFSSRDEKSWFRETEIYNTVLLRHENILGFIASDMTSRNSCTQLWL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108936965 275 ITHYHEHGSLYDFLQRQTLEPQLALRLAVSAACGLAHLHVEIFGTQGKPAIAHRDLKSRNVLVKSNLQCCIADLGLAVMH 354
Cdd:cd14142   81 ITHYHENGSLYDYLQRTTLDHQEMLRLALSAASGLVHLHTEIFGTQGKPAIAHRDLKSKNILVKSNGQCCIADLGLAVTH 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108936965 355 SQSSDYLDIGNNPRVGTKRYMAPEVLDEHIRTDCFESYKWTDIWAFGLVLWEIARRTIINGIVEDYRPPFYDMVPNDPSF 434
Cdd:cd14142  161 SQETNQLDVGNNPRVGTKRYMAPEVLDETINTDCFESYKRVDIYAFGLVLWEVARRCVSGGIVEEYKPPFYDVVPSDPSF 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 108936965 435 EDMKKVVCVDQQTPTIPNRLAADPVLSGLAQMMRECWYPNPSARLTALRIKKTLQKLS 492
Cdd:cd14142  241 EDMRKVVCVDQQRPNIPNRWSSDPTLTAMAKLMKECWYQNPSARLTALRIKKTLLKIL 298
TGF_beta_GS pfam08515
Transforming growth factor beta type I GS-motif; This motif is found in the transforming ...
172-199 1.61e-12

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


:

Pssm-ID: 400699  Cd Length: 28  Bit Score: 61.40  E-value: 1.61e-12
                          10        20
                  ....*....|....*....|....*...
gi 108936965  172 MLGDFLDSDCTTGSGSGLPFLVQRTVAR 199
Cdd:pfam08515   1 TLKDLIDESCTSGSGSGLPLLVQRTIAR 28
 
Name Accession Description Interval E-value
STKc_ACVR1_ALK1 cd14142
Catalytic domain of the Serine/Threonine Kinases, Activin Type I Receptor and Activin ...
195-492 0e+00

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: 640.64  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108936965 195 RTVARQVALVECVGKGRYGEVWRGSWHGESVAVKIFSSRDEQSWFRETEIYNTVLLRHDNILGFIASDMTSRNSSTQLWL 274
Cdd:cd14142    1 RTVARQITLVECIGKGRYGEVWRGQWQGESVAVKIFSSRDEKSWFRETEIYNTVLLRHENILGFIASDMTSRNSCTQLWL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108936965 275 ITHYHEHGSLYDFLQRQTLEPQLALRLAVSAACGLAHLHVEIFGTQGKPAIAHRDLKSRNVLVKSNLQCCIADLGLAVMH 354
Cdd:cd14142   81 ITHYHENGSLYDYLQRTTLDHQEMLRLALSAASGLVHLHTEIFGTQGKPAIAHRDLKSKNILVKSNGQCCIADLGLAVTH 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108936965 355 SQSSDYLDIGNNPRVGTKRYMAPEVLDEHIRTDCFESYKWTDIWAFGLVLWEIARRTIINGIVEDYRPPFYDMVPNDPSF 434
Cdd:cd14142  161 SQETNQLDVGNNPRVGTKRYMAPEVLDETINTDCFESYKRVDIYAFGLVLWEVARRCVSGGIVEEYKPPFYDVVPSDPSF 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 108936965 435 EDMKKVVCVDQQTPTIPNRLAADPVLSGLAQMMRECWYPNPSARLTALRIKKTLQKLS 492
Cdd:cd14142  241 EDMRKVVCVDQQRPNIPNRWSSDPTLTAMAKLMKECWYQNPSARLTALRIKKTLLKIL 298
Pkinase_Tyr pfam07714
Protein tyrosine kinase;
201-488 9.05e-41

Protein tyrosine kinase;


Pssm-ID: 400179 [Multi-domain]  Cd Length: 258  Bit Score: 147.26  E-value: 9.05e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108936965  201 VALVECVGKGRYGEVWRGSWHGES------VAVKI----FSSRDEQSWFRETEIYNTvlLRHDNILGFIASDMTSRNsst 270
Cdd:pfam07714   1 LTLGEKLGEGAFGEVYKGTLKGEGentkikVAVKTlkegADEEEREDFLEEASIMKK--LDHPNIVKLLGVCTQGEP--- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108936965  271 qLWLITHYHEHGSLYDFLQRQT--LEPQLALRLAVSAACGLAHLHveifgtqGKPAIaHRDLKSRNVLVKSNLQCCIADL 348
Cdd:pfam07714  76 -LYIVTEYMPGGDLLDFLRKHKrkLTLPDLLSMALQIAKGMEYLE-------SKNFV-HRDLAARNCLVSENLVVKISDF 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108936965  349 GLAVMHSQSSDYLdignnPRVGTK---RYMAPEVLDEHIrtdcFESYkwTDIWAFGLVLWEIarrtIINGivedyRPPFY 425
Cdd:pfam07714 147 GLSRDIYDDDYYR-----KRGGGKlpiKWMAPESLKDGK----FTSK--SDVWSFGVLLWEI----FTLG-----EQPYP 206
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 108936965  426 DMVPndpsfEDMKKVVCVDQQTPTIPNRLAAdpvlsgLAQMMRECWYPNPSARLTALRIKKTL 488
Cdd:pfam07714 207 GMSN-----EEVLEYLEDGYRLPQPENCPDE------LYDLMKQCWAYDPEDRPTFSELVEDL 258
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
203-486 2.50e-39

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 143.05  E-value: 2.50e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108936965   203 LVECVGKGRYGEVWRGSWH--GESVAVKI----FSSRDEQSWFRETEIYNTvlLRHDNILGFIASDMTSRNsstqLWLIT 276
Cdd:smart00220   3 ILEKLGEGSFGKVYLARDKktGKLVAIKVikkkKIKKDRERILREIKILKK--LKHPNIVRLYDVFEDEDK----LYLVM 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108936965   277 HYHEHGSLYDFLQRQ-TLEPQLALRLAVSAACGLAHLHveifgTQGkpaIAHRDLKSRNVLVKSNLQCCIADLGLAVMHS 355
Cdd:smart00220  77 EYCEGGDLFDLLKKRgRLSEDEARFYLRQILSALEYLH-----SKG---IVHRDLKPENILLDEDGHVKLADFGLARQLD 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108936965   356 QSSDYldignNPRVGTKRYMAPEVLDEHirtdcfesyKWT---DIWAFGLVLWEIARRtiingivedyRPPFYDmvpnDP 432
Cdd:smart00220 149 PGEKL-----TTFVGTPEYMAPEVLLGK---------GYGkavDIWSLGVILYELLTG----------KPPFPG----DD 200
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 108936965   433 SFEDMKKVVCvdqqTPTIPNRLAADPVLSGLAQMMRECWYPNPSARLTALRIKK 486
Cdd:smart00220 201 QLLELFKKIG----KPKPPFPPPEWDISPEAKDLIRKLLVKDPEKRLTAEEALQ 250
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
203-502 3.12e-21

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 223589 [Multi-domain]  Cd Length: 384  Bit Score: 95.58  E-value: 3.12e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108936965 203 LVECVGKGRYGEVWRGsWHGESVAVKIFS------SRDEQSWFRETEIYNTvLLRHDNILGFIASdmtsRNSSTQLWLIT 276
Cdd:COG0515    4 ILRKLGEGSFGEVYLA-RDRKLVALKVLAkkleskSKEVERFLREIQILAS-LNHPPNIVKLYDF----FQDEGSLYLVM 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108936965 277 HYHEHGSLYDFL----QRQTLEPQLALRLAVSAACGLAHLHveifgTQGkpaIAHRDLKSRNVLVKSNL-QCCIADLGLA 351
Cdd:COG0515   78 EYVDGGSLEDLLkkigRKGPLSESEALFILAQILSALEYLH-----SKG---IIHRDIKPENILLDRDGrVVKLIDFGLA 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108936965 352 --VMHSQSSDYLDIGNNPRVGTKRYMAPEVLdehIRTDCFESYKWTDIWAFGLVLWEIARrtiingivedYRPPFYDMVP 429
Cdd:COG0515  150 klLPDPGSTSSIPALPSTSVGTPGYMAPEVL---LGLSLAYASSSSDIWSLGITLYELLT----------GLPPFEGEKN 216
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 108936965 430 NDPSFEDMKKV-VCVDQQTPTIPNRLAADPVLSGLAQMMRECWYPNPSARLTA-LRIKKTLQKLSHNPEKPKVIH 502
Cdd:COG0515  217 SSATSQTLKIIlELPTPSLASPLSPSNPELISKAASDLLKKLLAKDPKNRLSSsSDLSHDLLAHLKLKESDLSDL 291
TGF_beta_GS pfam08515
Transforming growth factor beta type I GS-motif; This motif is found in the transforming ...
172-199 1.61e-12

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


Pssm-ID: 400699  Cd Length: 28  Bit Score: 61.40  E-value: 1.61e-12
                          10        20
                  ....*....|....*....|....*...
gi 108936965  172 MLGDFLDSDCTTGSGSGLPFLVQRTVAR 199
Cdd:pfam08515   1 TLKDLIDESCTSGSGSGLPLLVQRTIAR 28
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
207-406 4.26e-12

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 67.54  E-value: 4.26e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108936965 207 VGKGRYGEVWRGSWH--GESVAVK-IFSSRDE---QSWFRETEIYNTVllRHDNILGfiASDMTSRNSSTQLWLitHYHE 280
Cdd:PLN00034  82 IGSGAGGTVYKVIHRptGRLYALKvIYGNHEDtvrRQICREIEILRDV--NHPNVVK--CHDMFDHNGEIQVLL--EFMD 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108936965 281 HGSLYDflQRQTLEPQLAlRLAVSAACGLAHLHveifgtqgKPAIAHRDLKSRNVLVKSNLQCCIADLGLAVMHSQSSDY 360
Cdd:PLN00034 156 GGSLEG--THIADEQFLA-DVARQILSGIAYLH--------RRHIVHRDIKPSNLLINSAKNVKIADFGVSRILAQTMDP 224
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 108936965 361 LdignNPRVGTKRYMAPEVLDEHIRTDCFESYKwTDIWAFGLVLWE 406
Cdd:PLN00034 225 C----NSSVGTIAYMSPERINTDLNHGAYDGYA-GDIWSLGVSILE 265
GS smart00467
GS motif; Aa approx. 30 amino acid motif that precedes the kinase domain in types I and II TGF ...
171-201 6.86e-10

GS motif; Aa approx. 30 amino acid motif that precedes the kinase domain in types I and II TGF beta receptors. Mutation of two or more of the serines or threonines in the TTSGSGSG of TGF-beta type I receptor impairs phosphorylation and signaling activity.


Pssm-ID: 197743  Cd Length: 30  Bit Score: 54.09  E-value: 6.86e-10
                           10        20        30
                   ....*....|....*....|....*....|.
gi 108936965   171 SMLGDFLDsDCTTGSGSGLPFLVQRTVARQV 201
Cdd:smart00467   1 KTLSDLLE-DTTSGSGSGLPLLVQRTVARQI 30
 
Name Accession Description Interval E-value
STKc_ACVR1_ALK1 cd14142
Catalytic domain of the Serine/Threonine Kinases, Activin Type I Receptor and Activin ...
195-492 0e+00

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: 640.64  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108936965 195 RTVARQVALVECVGKGRYGEVWRGSWHGESVAVKIFSSRDEQSWFRETEIYNTVLLRHDNILGFIASDMTSRNSSTQLWL 274
Cdd:cd14142    1 RTVARQITLVECIGKGRYGEVWRGQWQGESVAVKIFSSRDEKSWFRETEIYNTVLLRHENILGFIASDMTSRNSCTQLWL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108936965 275 ITHYHEHGSLYDFLQRQTLEPQLALRLAVSAACGLAHLHVEIFGTQGKPAIAHRDLKSRNVLVKSNLQCCIADLGLAVMH 354
Cdd:cd14142   81 ITHYHENGSLYDYLQRTTLDHQEMLRLALSAASGLVHLHTEIFGTQGKPAIAHRDLKSKNILVKSNGQCCIADLGLAVTH 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108936965 355 SQSSDYLDIGNNPRVGTKRYMAPEVLDEHIRTDCFESYKWTDIWAFGLVLWEIARRTIINGIVEDYRPPFYDMVPNDPSF 434
Cdd:cd14142  161 SQETNQLDVGNNPRVGTKRYMAPEVLDETINTDCFESYKRVDIYAFGLVLWEVARRCVSGGIVEEYKPPFYDVVPSDPSF 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 108936965 435 EDMKKVVCVDQQTPTIPNRLAADPVLSGLAQMMRECWYPNPSARLTALRIKKTLQKLS 492
Cdd:cd14142  241 EDMRKVVCVDQQRPNIPNRWSSDPTLTAMAKLMKECWYQNPSARLTALRIKKTLLKIL 298
STKc_TGFbR_I cd14056
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type ...
205-491 0e+00

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


Pssm-ID: 270958 [Multi-domain]  Cd Length: 287  Bit Score: 543.79  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108936965 205 ECVGKGRYGEVWRGSWHGESVAVKIFSSRDEQSWFRETEIYNTVLLRHDNILGFIASDMTSRNSSTQLWLITHYHEHGSL 284
Cdd:cd14056    1 KTIGKGRYGEVWLGKYRGEKVAVKIFSSRDEDSWFRETEIYQTVMLRHENILGFIAADIKSTGSWTQLWLITEYHEHGSL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108936965 285 YDFLQRQTLEPQLALRLAVSAACGLAHLHVEIFGTQGKPAIAHRDLKSRNVLVKSNLQCCIADLGLAVMHSQSSDYLDIG 364
Cdd:cd14056   81 YDYLQRNTLDTEEALRLAYSAASGLAHLHTEIVGTQGKPAIAHRDLKSKNILVKRDGTCCIADLGLAVRYDSDTNTIDIP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108936965 365 NNPRVGTKRYMAPEVLDEHIRTDCFESYKWTDIWAFGLVLWEIARRTIINGIVEDYRPPFYDMVPNDPSFEDMKKVVCVD 444
Cdd:cd14056  161 PNPRVGTKRYMAPEVLDDSINPKSFESFKMADIYSFGLVLWEIARRCEIGGIAEEYQLPYFGMVPSDPSFEEMRKVVCVE 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 108936965 445 QQTPTIPNRLAADPVLSGLAQMMRECWYPNPSARLTALRIKKTLQKL 491
Cdd:cd14056  241 KLRPPIPNRWKSDPVLRSMVKLMQECWSENPHARLTALRVKKTLAKL 287
STKc_TGFbR1_ACVR1b_ACVR1c cd14143
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta Type I ...
205-492 4.14e-174

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: 491.19  E-value: 4.14e-174
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108936965 205 ECVGKGRYGEVWRGSWHGESVAVKIFSSRDEQSWFRETEIYNTVLLRHDNILGFIASDMTSRNSSTQLWLITHYHEHGSL 284
Cdd:cd14143    1 ESIGKGRFGEVWRGRWRGEDVAVKIFSSREERSWFREAEIYQTVMLRHENILGFIAADNKDNGTWTQLWLVSDYHEHGSL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108936965 285 YDFLQRQTLEPQLALRLAVSAACGLAHLHVEIFGTQGKPAIAHRDLKSRNVLVKSNLQCCIADLGLAVMHSQSSDYLDIG 364
Cdd:cd14143   81 FDYLNRYTVTVEGMIKLALSIASGLAHLHMEIVGTQGKPAIAHRDLKSKNILVKKNGTCCIADLGLAVRHDSATDTIDIA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108936965 365 NNPRVGTKRYMAPEVLDEHIRTDCFESYKWTDIWAFGLVLWEIARRTIINGIVEDYRPPFYDMVPNDPSFEDMKKVVCVD 444
Cdd:cd14143  161 PNHRVGTKRYMAPEVLDDTINMKHFESFKRADIYALGLVFWEIARRCSIGGIHEDYQLPYYDLVPSDPSIEEMRKVVCEQ 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 108936965 445 QQTPTIPNRLAADPVLSGLAQMMRECWYPNPSARLTALRIKKTLQKLS 492
Cdd:cd14143  241 KLRPNIPNRWQSCEALRVMAKIMRECWYANGAARLTALRIKKTLSQLS 288
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
205-491 4.66e-169

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: 478.47  E-value: 4.66e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108936965 205 ECVGKGRYGEVWRGSWHGESVAVKIFSSRDEQSWFRETEIYNTVLLRHDNILGFIASDMTSRNSSTQLWLITHYHEHGSL 284
Cdd:cd13998    1 EVIGKGRFGEVWKASLKNEPVAVKIFSSRDKQSWFREKEIYRTPMLKHENILQFIAADERDTALRTELWLVTAFHPNGSL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108936965 285 YDFLQRQTLEPQLALRLAVSAACGLAHLHVEIFG-TQGKPAIAHRDLKSRNVLVKSNLQCCIADLGLAVMHSQSSDYLDI 363
Cdd:cd13998   81 *DYLSLHTIDWVSLCRLALSVARGLAHLHSEIPGcTQGKPAIAHRDLKSKNILVKNDGTCCIADFGLAVRLSPSTGEEDN 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108936965 364 GNNPRVGTKRYMAPEVLDEHIRTDCFESYKWTDIWAFGLVLWEIARRTIIN-GIVEDYRPPFYDMVPNDPSFEDMKKVVC 442
Cdd:cd13998  161 ANNGQVGTKRYMAPEVLEGAINLRDFESFKRVDIYAMGLVLWEMASRCTDLfGIVEEYKPPFYSEVPNHPSFEDMQEVVV 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 108936965 443 VDQQTPTIPNRLAADPVLSGLAQMMRECWYPNPSARLTALRIKKTLQKL 491
Cdd:cd13998  241 RDKQRPNIPNRWLSHPGLQSLAETIEECWDHDAEARLTAQCIEERLSEF 289
STKc_BMPR1 cd14144
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type I Receptor; ...
207-491 1.67e-168

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: 476.97  E-value: 1.67e-168
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108936965 207 VGKGRYGEVWRGSWHGESVAVKIFSSRDEQSWFRETEIYNTVLLRHDNILGFIASDMTSRNSSTQLWLITHYHEHGSLYD 286
Cdd:cd14144    3 VGKGRYGEVWKGKWRGEKVAVKIFFTTEEASWFRETEIYQTVLMRHENILGFIAADIKGTGSWTQLYLITDYHENGSLYD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108936965 287 FLQRQTLEPQLALRLAVSAACGLAHLHVEIFGTQGKPAIAHRDLKSRNVLVKSNLQCCIADLGLAVMHSQSSDYLDIGNN 366
Cdd:cd14144   83 FLRGNTLDTQSMLKLAYSAACGLAHLHTEIFGTQGKPAIAHRDIKSKNILVKKNGTCCIADLGLAVKFISETNEVDLPPN 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108936965 367 PRVGTKRYMAPEVLDEHIRTDCFESYKWTDIWAFGLVLWEIARRTIINGIVEDYRPPFYDMVPNDPSFEDMKKVVCVDQQ 446
Cdd:cd14144  163 TRVGTKRYMAPEVLDESLNRNHFDAYKMADMYSFGLVLWEIARRCISGGIVEEYQLPYYDAVPSDPSYEDMRRVVCVERR 242
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 108936965 447 TPTIPNRLAADPVLSGLAQMMRECWYPNPSARLTALRIKKTLQKL 491
Cdd:cd14144  243 RPSIPNRWSSDEVLRTMSKLMSECWAHNPAARLTALRVKKTLGKL 287
STKc_BMPR1a cd14220
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IA Receptor; ...
207-491 5.58e-144

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: 414.44  E-value: 5.58e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108936965 207 VGKGRYGEVWRGSWHGESVAVKIFSSRDEQSWFRETEIYNTVLLRHDNILGFIASDMTSRNSSTQLWLITHYHEHGSLYD 286
Cdd:cd14220    3 IGKGRYGEVWMGKWRGEKVAVKVFFTTEEASWFRETEIYQTVLMRHENILGFIAADIKGTGSWTQLYLITDYHENGSLYD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108936965 287 FLQRQTLEPQLALRLAVSAACGLAHLHVEIFGTQGKPAIAHRDLKSRNVLVKSNLQCCIADLGLAVMHSQSSDYLDIGNN 366
Cdd:cd14220   83 FLKCTTLDTRALLKLAYSAACGLCHLHTEIYGTQGKPAIAHRDLKSKNILIKKNGTCCIADLGLAVKFNSDTNEVDVPLN 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108936965 367 PRVGTKRYMAPEVLDEHIRTDCFESYKWTDIWAFGLVLWEIARRTIINGIVEDYRPPFYDMVPNDPSFEDMKKVVCVDQQ 446
Cdd:cd14220  163 TRVGTKRYMAPEVLDESLNKNHFQAYIMADIYSFGLIIWEMARRCVTGGIVEEYQLPYYDMVPSDPSYEDMREVVCVKRL 242
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 108936965 447 TPTIPNRLAADPVLSGLAQMMRECWYPNPSARLTALRIKKTLQKL 491
Cdd:cd14220  243 RPTVSNRWNSDECLRAVLKLMSECWAHNPASRLTALRIKKTLAKM 287
STKc_BMPR1b cd14219
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IB; STKs ...
195-496 1.95e-137

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: 398.65  E-value: 1.95e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108936965 195 RTVARQVALVECVGKGRYGEVWRGSWHGESVAVKIFSSRDEQSWFRETEIYNTVLLRHDNILGFIASDMTSRNSSTQLWL 274
Cdd:cd14219    1 RTIAKQIQMVKQIGKGRYGEVWMGKWRGEKVAVKVFFTTEEASWFRETEIYQTVLMRHENILGFIAADIKGTGSWTQLYL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108936965 275 ITHYHEHGSLYDFLQRQTLEPQLALRLAVSAACGLAHLHVEIFGTQGKPAIAHRDLKSRNVLVKSNLQCCIADLGLAVMH 354
Cdd:cd14219   81 ITDYHENGSLYDYLKSTTLDTKAMLKLAYSSVSGLCHLHTEIFSTQGKPAIAHRDLKSKNILVKKNGTCCIADLGLAVKF 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108936965 355 SQSSDYLDIGNNPRVGTKRYMAPEVLDEHIRTDCFESYKWTDIWAFGLVLWEIARRTIINGIVEDYRPPFYDMVPNDPSF 434
Cdd:cd14219  161 ISDTNEVDIPPNTRVGTKRYMPPEVLDESLNRNHFQSYIMADMYSFGLILWEVARRCVSGGIVEEYQLPYHDLVPSDPSY 240
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 108936965 435 EDMKKVVCVDQQTPTIPNRLAADPVLSGLAQMMRECWYPNPSARLTALRIKKTLQKLSHNPE 496
Cdd:cd14219  241 EDMREIVCIKRLRPSFPNRWSSDECLRQMGKLMTECWAHNPASRLTALRVKKTLAKMSESQD 302
STKc_ACVR2 cd14053
Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the ...
209-494 6.57e-98

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: 296.93  E-value: 6.57e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108936965 209 KGRYGEVWRGSWHGESVAVKIFSSRDEQSWFRETEIYNTVLLRHDNILGFIASDMTSRNSSTQLWLITHYHEHGSLYDFL 288
Cdd:cd14053    5 RGRFGAVWKAQYLNRLVAVKIFPLQEKQSWLTEREIYSLPGMKHENILQFIGAEKHGESLEAEYWLITEFHERGSLCDYL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108936965 289 QRQTLEPQLALRLAVSAACGLAHLHVEIFGTQG--KPAIAHRDLKSRNVLVKSNLQCCIADLGLAVMHSQSSDYLDigNN 366
Cdd:cd14053   85 KGNVISWNELCKIAESMARGLAYLHEDIPATNGghKPSIAHRDFKSKNVLLKSDLTACIADFGLALKFEPGKSCGD--TH 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108936965 367 PRVGTKRYMAPEVLDEHI--RTDCFesyKWTDIWAFGLVLWEIARRTIINGI-VEDYRPPFYDMVPNDPSFEDMKKVVCV 443
Cdd:cd14053  163 GQVGTRRYMAPEVLEGAInfTRDAF---LRIDMYAMGLVLWELLSRCSVHDGpVDEYQLPFEEEVGQHPTLEDMQECVVH 239
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 108936965 444 DQQTPTIPNRLAADPVLSGLAQMMRECWYPNPSARLTALRIKKTLQKLSHN 494
Cdd:cd14053  240 KKLRPQIRDEWRKHPGLAQLCETIEECWDHDAEARLSAGCVEERLSQLSRS 290
STKc_TGFbR2_like cd14055
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II ...
207-481 2.27e-91

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: 280.42  E-value: 2.27e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108936965 207 VGKGRYGEVWRGSW------HGESVAVKIFSSRDEQSWFRETEIYNTVLLRHDNILGFIASDMTSRNSSTQLWLITHYHE 280
Cdd:cd14055    3 VGKGRFAEVWKAKLkqnasgQYETVAVKIFPYEEYASWKNEKDIFTDASLKHENILQFLTAEERGVGLDRQYWLITAYHE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108936965 281 HGSLYDFLQRQTLEPQLALRLAVSAACGLAHLHVEiFGTQGKP--AIAHRDLKSRNVLVKSNLQCCIADLGLAVMHSQSS 358
Cdd:cd14055   83 NGSLQDYLTRHILSWEDLCKMAGSLARGLAHLHSD-RTPCGRPkiPIAHRDLKSSNILVKNDGTCVLADFGLALRLDPSL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108936965 359 DYLDIGNNPRVGTKRYMAPEVLDEHIRTDCFESYKWTDIWAFGLVLWEIARRTIINGIVEDYRPPFYDMVPNDPSFEDMK 438
Cdd:cd14055  162 SVDELANSGQVGTARYMAPEALESRVNLEDLESFKQIDVYSMALVLWEMASRCEASGEVKPYELPFGSKVRERPCVESMK 241
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 108936965 439 KVVCVDQQTPTIPNRLAADPVLSGLAQMMRECWYPNPSARLTA 481
Cdd:cd14055  242 DLVLRDRGRPEIPDSWLTHQGMCVLCDTITECWDHDPEARLTA 284
STKc_BMPR2_AMHR2 cd14054
Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and ...
205-491 1.99e-77

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: 244.58  E-value: 1.99e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108936965 205 ECVGKGRYGEVWRGSWHGESVAVKIFSSRDEQSWFRETEIYNTVLLRHDNILGFIASD--MTSRNSSTQLwLITHYHEHG 282
Cdd:cd14054    1 QLIGQGRYGTVWKGSLDERPVAVKVFPARHRQNFQNEKDIYELPLMEHSNILRFIGADerPTADGRMEYL-LVLEYAPKG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108936965 283 SLYDFLQRQTLEPQLALRLAVSAACGLAHLHVEI-FGTQGKPAIAHRDLKSRNVLVKSNLQCCIADLGLAVMHSQSSDYL 361
Cdd:cd14054   80 SLCSYLRENTLDWMSSCRMALSLTRGLAYLHTDLrRGDQYKPAIAHRDLNSRNVLVKADGSCVICDFGLAMVLRGSSLVR 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108936965 362 ---DIGNNP---RVGTKRYMAPEVLDEHIR-TDCFESYKWTDIWAFGLVLWEIARRT---IINGIVEDYRPPFYDMVPND 431
Cdd:cd14054  160 grpGAAENAsisEVGTLRYMAPEVLEGAVNlRDCESALKQVDVYALGLVLWEIAMRCsdlYPGESVPPYQMPYEAELGNH 239
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 108936965 432 PSFEDMKKVVCVDQQTPTIPN---RLAADPvlSGLAQMMRECWYPNPSARLTALRIKKTLQKL 491
Cdd:cd14054  240 PTFEDMQLLVSREKARPKFPDawkENSLAV--RSLKETIEDCWDQDAEARLTALCVEERLAEL 300
STKc_ACVR2a cd14141
Catalytic domain of the Serine/Threonine Kinase, Activin Type IIA Receptor; STKs catalyze the ...
205-481 3.37e-71

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: 228.39  E-value: 3.37e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108936965 205 ECVGKGRYGEVWRGSWHGESVAVKIFSSRDEQSWFRETEIYNTVLLRHDNILGFIASDMTSRNSSTQLWLITHYHEHGSL 284
Cdd:cd14141    1 EIKARGRFGCVWKAQLLNEYVAVKIFPIQDKLSWQNEYEIYSLPGMKHENILQFIGAEKRGTNLDVDLWLITAFHEKGSL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108936965 285 YDFLQRQTLEPQLALRLAVSAACGLAHLHVEIFGTQG--KPAIAHRDLKSRNVLVKSNLQCCIADLGLAVMHSQSSDYLD 362
Cdd:cd14141   81 TDYLKANVVSWNELCHIAQTMARGLAYLHEDIPGLKDghKPAIAHRDIKSKNVLLKNNLTACIADFGLALKFEAGKSAGD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108936965 363 igNNPRVGTKRYMAPEVLDEHI--RTDCFESykwTDIWAFGLVLWEIARR-TIINGIVEDYRPPFYDMVPNDPSFEDMKK 439
Cdd:cd14141  161 --THGQVGTRRYMAPEVLEGAInfQRDAFLR---IDMYAMGLVLWELASRcTASDGPVDEYMLPFEEEVGQHPSLEDMQE 235
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 108936965 440 VVCVDQQTPTIPNRLAADPVLSGLAQMMRECWYPNPSARLTA 481
Cdd:cd14141  236 VVVHKKKRPVLRECWQKHAGMAMLCETIEECWDHDAEARLSA 277
STKc_ACVR2b cd14140
Catalytic domain of the Serine/Threonine Kinase, Activin Type IIB Receptor; STKs catalyze the ...
205-481 1.78e-70

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: 226.45  E-value: 1.78e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108936965 205 ECVGKGRYGEVWRGSWHGESVAVKIFSSRDEQSWFRETEIYNTVLLRHDNILGFIASDMTSRNSSTQLWLITHYHEHGSL 284
Cdd:cd14140    1 EIKARGRFGCVWKAQLMNEYVAVKIFPIQDKQSWQSEREIFSTPGMKHENLLQFIAAEKRGSNLEMELWLITAFHDKGSL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108936965 285 YDFLQRQTLEPQLALRLAVSAACGLAHLHVEIFGTQG---KPAIAHRDLKSRNVLVKSNLQCCIADLGLAVMHSQSSDYL 361
Cdd:cd14140   81 TDYLKGNIVSWNELCHIAETMARGLSYLHEDVPRCKGeghKPAIAHRDFKSKNVLLKNDLTAVLADFGLAVRFEPGKPPG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108936965 362 DigNNPRVGTKRYMAPEVLDEHIRTDcFESYKWTDIWAFGLVLWEIARR-TIINGIVEDYRPPFYDMVPNDPSFEDMKKV 440
Cdd:cd14140  161 D--THGQVGTRRYMAPEVLEGAINFQ-RDSFLRIDMYAMGLVLWELVSRcKAADGPVDEYMLPFEEEIGQHPSLEDLQEV 237
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 108936965 441 VCVDQQTPTIPNRLAADPVLSGLAQMMRECWYPNPSARLTA 481
Cdd:cd14140  238 VVHKKMRPVFKDHWLKHPGLAQLCVTIEECWDHDAEARLSA 278
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
207-478 2.87e-55

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: 185.05  E-value: 2.87e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108936965 207 VGKGRYGEVWRGSWHGESVAVKIFSSRDEQSWF-----RETEIYntVLLRHDNILGFIASDMTSRNsstqLWLITHYHEH 281
Cdd:cd13999    1 IGSGSFGEVYKGKWRGTDVAIKKLKVEDDNDELlkefrREVSIL--SKLRHPNIVQFIGACLSPPP----LCIVTEYMPG 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108936965 282 GSLYDFLQRQ--TLEPQLALRLAVSAACGLAHLHveifgtqgKPAIAHRDLKSRNVLVKSNLQCCIADLGLavmhSQSSD 359
Cdd:cd13999   75 GSLYDLLHKKkiPLSWSLRLKIALDIARGMNYLH--------SPPIIHRDLKSLNILLDENFTVKIADFGL----SRIKN 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108936965 360 YLDIGNNPRVGTKRYMAPEVldehIRTDCFeSYKwTDIWAFGLVLWEIARRtiingivedyRPPFYDMVPNDPSFEdmkk 439
Cdd:cd13999  143 STTEKMTGVVGTPRWMAPEV----LRGEPY-TEK-ADVYSFGIVLWELLTG----------EVPFKELSPIQIAAA---- 202
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 108936965 440 vVCVDQQTPTIPNRLaaDPVLSGLaqmMRECWYPNPSAR 478
Cdd:cd13999  203 -VVQKGLRPPIPPDC--PPELSKL---IKRCWNEDPEKR 235
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
205-489 1.36e-41

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: 149.61  E-value: 1.36e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108936965 205 ECVGKGRYGEVWRGSWHGES-----VAVKI---FSSRDEQSWF-RETEIYNTvlLRHDNILGFIASDMTSRNsstqLWLI 275
Cdd:cd00192    1 KKLGEGAFGEVYKGKLKGGDgktvdVAVKTlkeDASESERKDFlKEARVMKK--LGHPNVVRLLGVCTEEEP----LYLV 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108936965 276 THYHEHGSLYDFLQ----------RQTLEPQLALRLAVSAACGLAHLHveifgtqgKPAIAHRDLKSRNVLVKSNLQCCI 345
Cdd:cd00192   75 MEYMEGGDLLDFLRksrpvfpspePSTLSLKDLLSFAIQIAKGMEYLA--------SKKFVHRDLAARNCLVGEDLVVKI 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108936965 346 ADLGLavmhsqsSDYLDIGNNPRVGTK-----RYMAPEVLDEHIrtdcFeSYKwTDIWAFGLVLWEIarrtIINGivedy 420
Cdd:cd00192  147 SDFGL-------SRDIYDDDYYRKKTGgklpiRWMAPESLKDGI----F-TSK-SDVWSFGVLLWEI----FTLG----- 204
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108936965 421 RPPFYDMvpndpSFEDMKKVVCVDqqtptipNRLAA-DPVLSGLAQMMRECWYPNPSARLTALRIKKTLQ 489
Cdd:cd00192  205 ATPYPGL-----SNEEVLEYLRKG-------YRLPKpENCPDELYELMLSCWQLDPEDRPTFSELVERLE 262
Pkinase_Tyr pfam07714
Protein tyrosine kinase;
201-488 9.05e-41

Protein tyrosine kinase;


Pssm-ID: 400179 [Multi-domain]  Cd Length: 258  Bit Score: 147.26  E-value: 9.05e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108936965  201 VALVECVGKGRYGEVWRGSWHGES------VAVKI----FSSRDEQSWFRETEIYNTvlLRHDNILGFIASDMTSRNsst 270
Cdd:pfam07714   1 LTLGEKLGEGAFGEVYKGTLKGEGentkikVAVKTlkegADEEEREDFLEEASIMKK--LDHPNIVKLLGVCTQGEP--- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108936965  271 qLWLITHYHEHGSLYDFLQRQT--LEPQLALRLAVSAACGLAHLHveifgtqGKPAIaHRDLKSRNVLVKSNLQCCIADL 348
Cdd:pfam07714  76 -LYIVTEYMPGGDLLDFLRKHKrkLTLPDLLSMALQIAKGMEYLE-------SKNFV-HRDLAARNCLVSENLVVKISDF 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108936965  349 GLAVMHSQSSDYLdignnPRVGTK---RYMAPEVLDEHIrtdcFESYkwTDIWAFGLVLWEIarrtIINGivedyRPPFY 425
Cdd:pfam07714 147 GLSRDIYDDDYYR-----KRGGGKlpiKWMAPESLKDGK----FTSK--SDVWSFGVLLWEI----FTLG-----EQPYP 206
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 108936965  426 DMVPndpsfEDMKKVVCVDQQTPTIPNRLAAdpvlsgLAQMMRECWYPNPSARLTALRIKKTL 488
Cdd:pfam07714 207 GMSN-----EEVLEYLEDGYRLPQPENCPDE------LYDLMKQCWAYDPEDRPTFSELVEDL 258
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
203-486 2.50e-39

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 143.05  E-value: 2.50e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108936965   203 LVECVGKGRYGEVWRGSWH--GESVAVKI----FSSRDEQSWFRETEIYNTvlLRHDNILGFIASDMTSRNsstqLWLIT 276
Cdd:smart00220   3 ILEKLGEGSFGKVYLARDKktGKLVAIKVikkkKIKKDRERILREIKILKK--LKHPNIVRLYDVFEDEDK----LYLVM 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108936965   277 HYHEHGSLYDFLQRQ-TLEPQLALRLAVSAACGLAHLHveifgTQGkpaIAHRDLKSRNVLVKSNLQCCIADLGLAVMHS 355
Cdd:smart00220  77 EYCEGGDLFDLLKKRgRLSEDEARFYLRQILSALEYLH-----SKG---IVHRDLKPENILLDEDGHVKLADFGLARQLD 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108936965   356 QSSDYldignNPRVGTKRYMAPEVLDEHirtdcfesyKWT---DIWAFGLVLWEIARRtiingivedyRPPFYDmvpnDP 432
Cdd:smart00220 149 PGEKL-----TTFVGTPEYMAPEVLLGK---------GYGkavDIWSLGVILYELLTG----------KPPFPG----DD 200
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 108936965   433 SFEDMKKVVCvdqqTPTIPNRLAADPVLSGLAQMMRECWYPNPSARLTALRIKK 486
Cdd:smart00220 201 QLLELFKKIG----KPKPPFPPPEWDISPEAKDLIRKLLVKDPEKRLTAEEALQ 250
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
208-488 5.56e-39

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 142.28  E-value: 5.56e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108936965   208 GKGRYGEVWRGSW------HGESVAVKIF----SSRDEQSWFRETEIYNTvlLRHDNILGFIASDMTSRNsstqLWLITH 277
Cdd:smart00219   8 GEGAFGEVYKGKLkgkggkKKVEVAVKTLkedaSEQQIEEFLREARIMRK--LDHPNVVKLLGVCTEEEP----LYIVME 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108936965   278 YHEHGSLYDFLQ--RQTLEPQLALRLAVSAACGLAHLHveifgtqGKPAIaHRDLKSRNVLVKSNLQCCIADLGLAVMHS 355
Cdd:smart00219  82 YMEGGDLLSYLRknRPKLSLSDLLSFALQIARGMEYLE-------SKNFI-HRDLAARNCLVGENLVVKISDFGLSRDLY 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108936965   356 qSSDYLDIGnnprvGTK---RYMAPEVLDEHIrtdcFeSYKwTDIWAFGLVLWEIArrtiingivEDYRPPFYDMVPndp 432
Cdd:smart00219 154 -DDDYYRKR-----GGKlpiRWMAPESLKEGK----F-TSK-SDVWSFGVLLWEIF---------TLGEQPYPGMSN--- 209
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 108936965   433 sfEDMKKVVcVDQQTPTIPNRLAADpvlsgLAQMMRECWYPNPSARLTALRIKKTL 488
Cdd:smart00219 210 --EEVLEYL-KNGYRLPQPPNCPPE-----LYDLMLQCWAEDPEDRPTFSELVEIL 257
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
208-407 1.70e-38

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: 139.71  E-value: 1.70e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108936965 208 GKGRYGEVWRGSW--HGESVAVKIF--SSRDEQSWFRETEIYNTVLLRHDNILGFIASDMTSRNsstqLWLITHYHEHGS 283
Cdd:cd00180    2 GKGSFGKVYKARDkeTGKKVAVKVIpkEKLKKLLEELLREIEILKKLNHPNIVKLYDVFETENF----LYLVMEYCEGGS 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108936965 284 LYDFLQRQ--TLEPQLALRLAVSAACGLAHLHVEifgtqgkpAIAHRDLKSRNVLVKSNLQCCIADLGLAVMHSQSSDYL 361
Cdd:cd00180   78 LKDLLKENkgPLSEEEALSILRQLLSALEYLHSN--------GIIHRDLKPENILLDSDGTVKLADFGLAKDLDSDDSLL 149
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 108936965 362 DIGNNPrvGTKRYMAPEVLDEHIRTdcfesyKWTDIWAFGLVLWEI 407
Cdd:cd00180  150 KTTGGT--TPPYYAPPELLGGRYYG------PKVDIWSLGVILYEL 187
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
208-488 2.82e-38

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: 140.38  E-value: 2.82e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108936965   208 GKGRYGEVWRGSW------HGESVAVKIF----SSRDEQSWFRETEIYNTvlLRHDNI---LGFIASDMtsrnsstQLWL 274
Cdd:smart00221   8 GEGAFGEVYKGTLkgkgdgKEVEVAVKTLkedaSEQQIEEFLREARIMRK--LDHPNIvklLGVCTEEE-------PLMI 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108936965   275 ITHYHEHGSLYDFLQ---RQTLEPQLALRLAVSAACGLAHLHveifgtqGKPAIaHRDLKSRNVLVKSNLQCCIADLGLA 351
Cdd:smart00221  79 VMEYMPGGDLLDYLRknrPKELSLSDLLSFALQIARGMEYLE-------SKNFI-HRDLAARNCLVGENLVVKISDFGLS 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108936965   352 VMHSqSSDYLDIGnnprvGTK---RYMAPEVLDEHIrtdcFeSYKwTDIWAFGLVLWEiarrtiingIVEDYRPPFYDMV 428
Cdd:smart00221 151 RDLY-DDDYYKVK--