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Conserved domains on  [gi|6678323|ref|NP_033396|]
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TGF-beta receptor type-1 isoform 1 precursor [Mus musculus]

Protein Classification

Activin_recp and STKc_TGFbR1_ACVR1b_ACVR1c domain-containing protein (domain architecture ID 10471083)

protein containing domains Activin_recp, TGF_beta_GS, and STKc_TGFbR1_ACVR1b_ACVR1c

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
STKc_TGFbR1_ACVR1b_ACVR1c cd14143
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta Type I ...
209-496 0e+00

Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta Type I Receptor and Activin Type IB/IC Receptors; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TGFbR1, also called Activin receptor-Like Kinase 5 (ALK5), functions as a receptor for TGFbeta and phoshorylates SMAD2/3. TGFbeta proteins are cytokines that regulate cell growth, differentiation, and survival, and are critical in the development and progression of many human cancers. Mutations in TGFbR1 (and TGFbR2) can cause aortic aneurysm disorders such as Loeys-Dietz and Marfan syndromes. ACVR1b (also called ALK4) and ACVR1c (also called ALK7) act as receptors for activin A and B, respectively. TGFbR1, ACVR1b, and ACVR1c belong to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like TGFbR1, ACVR1b, and ACVR1c, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The TGFbR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


:

Pssm-ID: 271045  Cd Length: 288  Bit Score: 662.60  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678323  209 ESIGKGRFGEVWRGKWRGEEVAVKIFSSREERSWFREAEIYQTVMLRHENILGFIAADNKDNGTWTQLWLVSDYHEHGSL 288
Cdd:cd14143   1 ESIGKGRFGEVWRGRWRGEDVAVKIFSSREERSWFREAEIYQTVMLRHENILGFIAADNKDNGTWTQLWLVSDYHEHGSL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678323  289 FDYLNRYTVTVEGMIKLALSTASGLAHLHMEIVGTQGKPAIAHRDLKSKNILVKKNGTCCIADLGLAVRHDSATDTIDIA 368
Cdd:cd14143  81 FDYLNRYTVTVEGMIKLALSIASGLAHLHMEIVGTQGKPAIAHRDLKSKNILVKKNGTCCIADLGLAVRHDSATDTIDIA 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678323  369 PNHRVGTKRYMAPEVLDDSINMKHFESFKRADIYAMGLVFWEIARRCSIGGIHEDYQLPYYDLVPSDPSVEEMRKVVCEQ 448
Cdd:cd14143 161 PNHRVGTKRYMAPEVLDDTINMKHFESFKRADIYALGLVFWEIARRCSIGGIHEDYQLPYYDLVPSDPSIEEMRKVVCEQ 240
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 6678323  449 KLRPNIPNRWQSCEALRVMAKIMRECWYANGAARLTALRIKKTLSQLS 496
Cdd:cd14143 241 KLRPNIPNRWQSCEALRVMAKIMRECWYANGAARLTALRIKKTLSQLS 288
Activin_recp pfam01064
Activin types I and II receptor domain; This Pfam entry consists of both TGF-beta receptor ...
30-106 6.47e-25

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


:

Pssm-ID: 307282  Cd Length: 79  Bit Score: 99.15  E-value: 6.47e-25
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6678323     30 LQCFCHLCTKDNFTCETDGLCFVSVTETTD-KVIHNSMCIAEIDLIPRDRPFVCAPSSKTGAVTTTYCCN-QDHCNKIE 106
Cdd:pfam01064   1 LKCYCEGEEIENETCETDGSCFTSVEENEDgKEIVSKGCISEEDLGPLNSPFECKLSNTPPQGGRIECCCeGDYCNKNL 79
TGF_beta_GS pfam08515
Transforming growth factor beta type I GS-motif; This motif is found in the transforming ...
176-203 2.70e-13

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: 312125  Cd Length: 28  Bit Score: 65.58  E-value: 2.70e-13
                          10        20
                  ....*....|....*....|....*...
gi 6678323    176 TLKDLIYDMTTSGSGSGLPLLVQRTIAR 203
Cdd:pfam08515   1 TLKDLIEESCTSGSGSGLPLLVQRTIAR 28
 
Name Accession Description Interval E-value
STKc_TGFbR1_ACVR1b_ACVR1c cd14143
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta Type I ...
209-496 0e+00

Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta Type I Receptor and Activin Type IB/IC Receptors; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TGFbR1, also called Activin receptor-Like Kinase 5 (ALK5), functions as a receptor for TGFbeta and phoshorylates SMAD2/3. TGFbeta proteins are cytokines that regulate cell growth, differentiation, and survival, and are critical in the development and progression of many human cancers. Mutations in TGFbR1 (and TGFbR2) can cause aortic aneurysm disorders such as Loeys-Dietz and Marfan syndromes. ACVR1b (also called ALK4) and ACVR1c (also called ALK7) act as receptors for activin A and B, respectively. TGFbR1, ACVR1b, and ACVR1c belong to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like TGFbR1, ACVR1b, and ACVR1c, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The TGFbR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271045  Cd Length: 288  Bit Score: 662.60  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678323  209 ESIGKGRFGEVWRGKWRGEEVAVKIFSSREERSWFREAEIYQTVMLRHENILGFIAADNKDNGTWTQLWLVSDYHEHGSL 288
Cdd:cd14143   1 ESIGKGRFGEVWRGRWRGEDVAVKIFSSREERSWFREAEIYQTVMLRHENILGFIAADNKDNGTWTQLWLVSDYHEHGSL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678323  289 FDYLNRYTVTVEGMIKLALSTASGLAHLHMEIVGTQGKPAIAHRDLKSKNILVKKNGTCCIADLGLAVRHDSATDTIDIA 368
Cdd:cd14143  81 FDYLNRYTVTVEGMIKLALSIASGLAHLHMEIVGTQGKPAIAHRDLKSKNILVKKNGTCCIADLGLAVRHDSATDTIDIA 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678323  369 PNHRVGTKRYMAPEVLDDSINMKHFESFKRADIYAMGLVFWEIARRCSIGGIHEDYQLPYYDLVPSDPSVEEMRKVVCEQ 448
Cdd:cd14143 161 PNHRVGTKRYMAPEVLDDTINMKHFESFKRADIYALGLVFWEIARRCSIGGIHEDYQLPYYDLVPSDPSIEEMRKVVCEQ 240
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 6678323  449 KLRPNIPNRWQSCEALRVMAKIMRECWYANGAARLTALRIKKTLSQLS 496
Cdd:cd14143 241 KLRPNIPNRWQSCEALRVMAKIMRECWYANGAARLTALRIKKTLSQLS 288
Pkinase_Tyr pfam07714
Protein tyrosine kinase;
205-492 8.86e-40

Protein tyrosine kinase;


Pssm-ID: 311583  Cd Length: 258  Bit Score: 146.11  E-value: 8.86e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678323    205 IVLQESIGKGRFGEVWRGKWRGE------EVAVKI----FSSREERSWFREAEIyqtvM--LRHENILGFIAADNKDNgt 272
Cdd:pfam07714   1 LTLGEKLGEGAFGEVYKGTLKGDgegtkiKVAVKTlkegADEEEREDFLEEASI----MkkLSHPNIVRLLGVCTQGE-- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678323    273 wtQLWLVSDYHEHGSLFDYL--NRYTVTVEGMIKLALSTASGLAHLH-MEIVgtqgkpaiaHRDLKSKNILVKKNGTCCI 349
Cdd:pfam07714  75 --PLYIVTEYMPGGDLLDFLrkHKGKLTLPDLLQMALQIAKGMEYLEsKNFV---------HRDLAARNCLVTENLVVKI 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678323    350 ADLGLAvrhdsatDTIDIAPNHRVGTK-----RYMAPEVLDDSINmkhfeSFKrADIYAMGLVFWEIarrCSIGGIhedy 424
Cdd:pfam07714 144 SDFGLS-------RDIYDDDYYRKRGGgklpiKWMAPESLKDGKF-----TSK-SDVWSFGVLLWEI---FTLGEQ---- 203
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678323    425 qlPYYDLvpsdpSVEEMRKVVcEQKLRPNIPnrwQSC--EalrvMAKIMRECWYANGAARLTALRIKKTL 492
Cdd:pfam07714 204 --PYPGM-----SNEEVLEFL-EDGYRLPQP---ENCpdE----LYDLMTQCWAYDPEDRPTFSELVEDL 258
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
205-492 2.65e-39

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


Pssm-ID: 197581  Cd Length: 257  Bit Score: 144.60  E-value: 2.65e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678323     205 IVLQESIGKGRFGEVWRGKWRG------EEVAVKIF----SSREERSWFREAEIYQtvMLRHENILGFIAADNKDNgtwt 274
Cdd:smart00219   1 LTLGKKLGEGAFGEVYKGKLKGkggkkkVEVAVKTLkedaSEQQIEEFLREARIMR--KLDHPNVVKLLGVCTEEE---- 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678323     275 QLWLVSDYHEHGSLFDYL--NRYTVTVEGMIKLALSTASGLAHLHmeivgtqGKPAIaHRDLKSKNILVKKNGTCCIADL 352
Cdd:smart00219  75 PLYIVMEYMEGGDLLSYLrkNRPKLSLSDLLSFALQIARGMEYLE-------SKNFI-HRDLAARNCLVGENLVVKISDF 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678323     353 GLAVRHDSaTDTIDIApnhrvGTK---RYMAPEVLDDSInmkhFeSFKrADIYAMGLVFWEIARRCsiggihedyQLPYY 429
Cdd:smart00219 147 GLSRDLYD-DDYYRKR-----GGKlpiRWMAPESLKEGK----F-TSK-SDVWSFGVLLWEIFTLG---------EQPYP 205
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6678323     430 DLvpsdpSVEEMRKVVcEQKLRPNIPnrwQSCEAlrVMAKIMRECWYANGAARLTALRIKKTL 492
Cdd:smart00219 206 GM-----SNEEVLEYL-KNGYRLPQP---PNCPP--ELYDLMLQCWAEDPEDRPTFSELVEIL 257
Activin_recp pfam01064
Activin types I and II receptor domain; This Pfam entry consists of both TGF-beta receptor ...
30-106 6.47e-25

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


Pssm-ID: 307282  Cd Length: 79  Bit Score: 99.15  E-value: 6.47e-25
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6678323     30 LQCFCHLCTKDNFTCETDGLCFVSVTETTD-KVIHNSMCIAEIDLIPRDRPFVCAPSSKTGAVTTTYCCN-QDHCNKIE 106
Cdd:pfam01064   1 LKCYCEGEEIENETCETDGSCFTSVEENEDgKEIVSKGCISEEDLGPLNSPFECKLSNTPPQGGRIECCCeGDYCNKNL 79
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
207-465 8.95e-24

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 223589  Cd Length: 384  Bit Score: 102.90  E-value: 8.95e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678323  207 LQESIGKGRFGEVWRGKwRGEEVAVKIFS------SREERSWFREAEIYQTVmLRHENILGFIAADNKDNgtwtQLWLVS 280
Cdd:COG0515   4 ILRKLGEGSFGEVYLAR-DRKLVALKVLAkkleskSKEVERFLREIQILASL-NHPPNIVKLYDFFQDEG----SLYLVM 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678323  281 DYHEHGSLFDYLN----RYTVTVEGMIKLALSTASGLAHLHmeivgTQGkpaIAHRDLKSKNILVKKNGT-CCIADLGLA 355
Cdd:COG0515  78 EYVDGGSLEDLLKkigrKGPLSESEALFILAQILSALEYLH-----SKG---IIHRDIKPENILLDRDGRvVKLIDFGLA 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678323  356 --VRHDSATDTIDIAPNHRVGTKRYMAPEVLddsINMKHFESFKRADIYAMGLVFWEIARRcsiggihedyqLPYYDLVP 433
Cdd:COG0515 150 klLPDPGSTSSIPALPSTSVGTPGYMAPEVL---LGLSLAYASSSSDIWSLGITLYELLTG-----------LPPFEGEK 215
                       250       260       270
                ....*....|....*....|....*....|..
gi 6678323  434 SDPSVEEMRKVVCEQKLRPNIPNRWQSCEALR 465
Cdd:COG0515 216 NSSATSQTLKIILELPTPSLASPLSPSNPELI 247
TGF_beta_GS pfam08515
Transforming growth factor beta type I GS-motif; This motif is found in the transforming ...
176-203 2.70e-13

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: 312125  Cd Length: 28  Bit Score: 65.58  E-value: 2.70e-13
                          10        20
                  ....*....|....*....|....*...
gi 6678323    176 TLKDLIYDMTTSGSGSGLPLLVQRTIAR 203
Cdd:pfam08515   1 TLKDLIEESCTSGSGSGLPLLVQRTIAR 28
GS smart00467
GS motif; Aa approx. 30 amino acid motif that precedes the kinase domain in types I and II TGF ...
175-205 1.17e-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: 57.94  E-value: 1.17e-10
                           10        20        30
                   ....*....|....*....|....*....|.
gi 6678323     175 TTLKDLIYDmTTSGSGSGLPLLVQRTIARTI 205
Cdd:smart00467   1 KTLSDLLED-TTSGSGSGLPLLVQRTVARQI 30
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
211-410 4.12e-09

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036  Cd Length: 353  Bit Score: 57.91  E-value: 4.12e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678323   211 IGKGRFGEVWRGKWR--GEEVAVK-IFSSREE---RSWFREAEIYQTVmlRHENILGfiAADNKDNGTWTQLWLvsDYHE 284
Cdd:PLN00034  82 IGSGAGGTVYKVIHRptGRLYALKvIYGNHEDtvrRQICREIEILRDV--NHPNVVK--CHDMFDHNGEIQVLL--EFMD 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678323   285 HGSLfdyLNRYTVTVEGMIKLALSTASGLAHLHmeivgtqgKPAIAHRDLKSKNILVKKNGTCCIADLGLAvrhDSATDT 364
Cdd:PLN00034 156 GGSL---EGTHIADEQFLADVARQILSGIAYLH--------RRHIVHRDIKPSNLLINSAKNVKIADFGVS---RILAQT 221
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 6678323   365 IDiaP-NHRVGTKRYMAPEVLDDSINMKHFESFKrADIYAMGLVFWE 410
Cdd:PLN00034 222 MD--PcNSSVGTIAYMSPERINTDLNHGAYDGYA-GDIWSLGVSILE 265
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
226-410 8.18e-05

TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, in multiple species of Burkholderia, in Acidovorax avenae subsp. citrulli AAC00-1 and Delftia acidovorans SPH-1, and in multiple copies in Sorangium cellulosum, in genomic neighborhoods that include a cyclodehydratase/docking scaffold fusion protein (TIGR03882) and a member of the thiazole/oxazole modified metabolite (TOMM) precursor family TIGR03795. It has a kinase domain in the N-terminal 300 amino acids, followed by a cyclase homology domain, followed by regions without named domain definitions. It is a probable bacteriocin-like metabolite biosynthesis protein. [Cellular processes, Toxin production and resistance]


Pssm-ID: 274846  Cd Length: 1266  Bit Score: 45.22  E-value: 8.18e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678323     226 GEEVAVKIF---SSREERSWFR-EAEIYQTVMLRHENILGFIAADNKDNGtwtQLWLVSDYHEHGSLFDYL-NRYTVTVE 300
Cdd:TIGR03903    3 GHEVAIKLLrtdAPEEEHQRARfRRETALCARLYHPNIVALLDSGEAPPG---LLFAVFEYVPGRTLREVLaADGALPAG 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678323     301 GMIKLALSTASGLAHLHmeivgTQGkpaIAHRDLKSKNILVKKNG-TCC--IADLGLAV----RHDSATDTIDIApNHRV 373
Cdd:TIGR03903   80 ETGRLMLQVLDALACAH-----NQG---IVHRDLKPQNIMVSQTGvRPHakVLDFGIGTllpgVRDADVATLTRT-TEVL 150
                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 6678323     374 GTKRYMAPEVLDDSinmkhfESFKRADIYAMGLVFWE 410
Cdd:TIGR03903  151 GTPTYCAPEQLRGE------PVTPNSDLYAWGLIFLE 181
 
Name Accession Description Interval E-value
STKc_TGFbR1_ACVR1b_ACVR1c cd14143
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta Type I ...
209-496 0e+00

Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta Type I Receptor and Activin Type IB/IC Receptors; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TGFbR1, also called Activin receptor-Like Kinase 5 (ALK5), functions as a receptor for TGFbeta and phoshorylates SMAD2/3. TGFbeta proteins are cytokines that regulate cell growth, differentiation, and survival, and are critical in the development and progression of many human cancers. Mutations in TGFbR1 (and TGFbR2) can cause aortic aneurysm disorders such as Loeys-Dietz and Marfan syndromes. ACVR1b (also called ALK4) and ACVR1c (also called ALK7) act as receptors for activin A and B, respectively. TGFbR1, ACVR1b, and ACVR1c belong to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like TGFbR1, ACVR1b, and ACVR1c, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The TGFbR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271045  Cd Length: 288  Bit Score: 662.60  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678323  209 ESIGKGRFGEVWRGKWRGEEVAVKIFSSREERSWFREAEIYQTVMLRHENILGFIAADNKDNGTWTQLWLVSDYHEHGSL 288
Cdd:cd14143   1 ESIGKGRFGEVWRGRWRGEDVAVKIFSSREERSWFREAEIYQTVMLRHENILGFIAADNKDNGTWTQLWLVSDYHEHGSL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678323  289 FDYLNRYTVTVEGMIKLALSTASGLAHLHMEIVGTQGKPAIAHRDLKSKNILVKKNGTCCIADLGLAVRHDSATDTIDIA 368
Cdd:cd14143  81 FDYLNRYTVTVEGMIKLALSIASGLAHLHMEIVGTQGKPAIAHRDLKSKNILVKKNGTCCIADLGLAVRHDSATDTIDIA 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678323  369 PNHRVGTKRYMAPEVLDDSINMKHFESFKRADIYAMGLVFWEIARRCSIGGIHEDYQLPYYDLVPSDPSVEEMRKVVCEQ 448
Cdd:cd14143 161 PNHRVGTKRYMAPEVLDDTINMKHFESFKRADIYALGLVFWEIARRCSIGGIHEDYQLPYYDLVPSDPSIEEMRKVVCEQ 240
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 6678323  449 KLRPNIPNRWQSCEALRVMAKIMRECWYANGAARLTALRIKKTLSQLS 496
Cdd:cd14143 241 KLRPNIPNRWQSCEALRVMAKIMRECWYANGAARLTALRIKKTLSQLS 288
STKc_TGFbR_I cd14056
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type ...
209-495 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  Cd Length: 287  Bit Score: 586.93  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678323  209 ESIGKGRFGEVWRGKWRGEEVAVKIFSSREERSWFREAEIYQTVMLRHENILGFIAADNKDNGTWTQLWLVSDYHEHGSL 288
Cdd:cd14056   1 KTIGKGRYGEVWLGKYRGEKVAVKIFSSRDEDSWFRETEIYQTVMLRHENILGFIAADIKSTGSWTQLWLITEYHEHGSL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678323  289 FDYLNRYTVTVEGMIKLALSTASGLAHLHMEIVGTQGKPAIAHRDLKSKNILVKKNGTCCIADLGLAVRHDSATDTIDIA 368
Cdd:cd14056  81 YDYLQRNTLDTEEALRLAYSAASGLAHLHTEIVGTQGKPAIAHRDLKSKNILVKRDGTCCIADLGLAVRYDSDTNTIDIP 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678323  369 PNHRVGTKRYMAPEVLDDSINMKHFESFKRADIYAMGLVFWEIARRCSIGGIHEDYQLPYYDLVPSDPSVEEMRKVVCEQ 448
Cdd:cd14056 161 PNPRVGTKRYMAPEVLDDSINPKSFESFKMADIYSFGLVLWEIARRCEIGGIAEEYQLPYFGMVPSDPSFEEMRKVVCVE 240
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 6678323  449 KLRPNIPNRWQSCEALRVMAKIMRECWYANGAARLTALRIKKTLSQL 495
Cdd:cd14056 241 KLRPPIPNRWKSDPVLRSMVKLMQECWSENPHARLTALRVKKTLAKL 287
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
209-495 0e+00

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  Cd Length: 289  Bit Score: 546.27  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678323  209 ESIGKGRFGEVWRGKWRGEEVAVKIFSSREERSWFREAEIYQTVMLRHENILGFIAADNKDNGTWTQLWLVSDYHEHGSL 288
Cdd:cd13998   1 EVIGKGRFGEVWKASLKNEPVAVKIFSSRDKQSWFREKEIYRTPMLKHENILQFIAADERDTALRTELWLVTAFHPNGSL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678323  289 FDYLNRYTVTVEGMIKLALSTASGLAHLHMEIVG-TQGKPAIAHRDLKSKNILVKKNGTCCIADLGLAVRHDSATDTIDI 367
Cdd:cd13998  81 *DYLSLHTIDWVSLCRLALSVARGLAHLHSEIPGcTQGKPAIAHRDLKSKNILVKNDGTCCIADFGLAVRLSPSTGEEDN 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678323  368 APNHRVGTKRYMAPEVLDDSINMKHFESFKRADIYAMGLVFWEIARRCSI-GGIHEDYQLPYYDLVPSDPSVEEMRKVVC 446
Cdd:cd13998 161 ANNGQVGTKRYMAPEVLEGAINLRDFESFKRVDIYAMGLVLWEMASRCTDlFGIVEEYKPPFYSEVPNHPSFEDMQEVVV 240
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 6678323  447 EQKLRPNIPNRWQSCEALRVMAKIMRECWYANGAARLTALRIKKTLSQL 495
Cdd:cd13998 241 RDKQRPNIPNRWLSHPGLQSLAETIEECWDHDAEARLTAQCIEERLSEF 289
STKc_ACVR1_ALK1 cd14142
Catalytic domain of the Serine/Threonine Kinases, Activin Type I Receptor and Activin ...
199-496 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  Cd Length: 298  Bit Score: 524.70  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678323  199 RTIARTIVLQESIGKGRFGEVWRGKWRGEEVAVKIFSSREERSWFREAEIYQTVMLRHENILGFIAADNKDNGTWTQLWL 278
Cdd:cd14142   1 RTVARQITLVECIGKGRYGEVWRGQWQGESVAVKIFSSRDEKSWFRETEIYNTVLLRHENILGFIASDMTSRNSCTQLWL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678323  279 VSDYHEHGSLFDYLNRYTVTVEGMIKLALSTASGLAHLHMEIVGTQGKPAIAHRDLKSKNILVKKNGTCCIADLGLAVRH 358
Cdd:cd14142  81 ITHYHENGSLYDYLQRTTLDHQEMLRLALSAASGLVHLHTEIFGTQGKPAIAHRDLKSKNILVKSNGQCCIADLGLAVTH 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678323  359 DSATDTIDIAPNHRVGTKRYMAPEVLDDSINMKHFESFKRADIYAMGLVFWEIARRCSIGGIHEDYQLPYYDLVPSDPSV 438
Cdd:cd14142 161 SQETNQLDVGNNPRVGTKRYMAPEVLDETINTDCFESYKRVDIYAFGLVLWEVARRCVSGGIVEEYKPPFYDVVPSDPSF 240
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 6678323  439 EEMRKVVCEQKLRPNIPNRWQSCEALRVMAKIMRECWYANGAARLTALRIKKTLSQLS 496
Cdd:cd14142 241 EDMRKVVCVDQQRPNIPNRWSSDPTLTAMAKLMKECWYQNPSARLTALRIKKTLLKIL 298
STKc_BMPR1 cd14144
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type I Receptor; ...
210-495 1.50e-179

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  Cd Length: 287  Bit Score: 509.71  E-value: 1.50e-179
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678323  210 SIGKGRFGEVWRGKWRGEEVAVKIFSSREERSWFREAEIYQTVMLRHENILGFIAADNKDNGTWTQLWLVSDYHEHGSLF 289
Cdd:cd14144   2 SVGKGRYGEVWKGKWRGEKVAVKIFFTTEEASWFRETEIYQTVLMRHENILGFIAADIKGTGSWTQLYLITDYHENGSLY 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678323  290 DYLNRYTVTVEGMIKLALSTASGLAHLHMEIVGTQGKPAIAHRDLKSKNILVKKNGTCCIADLGLAVRHDSATDTIDIAP 369
Cdd:cd14144  82 DFLRGNTLDTQSMLKLAYSAACGLAHLHTEIFGTQGKPAIAHRDIKSKNILVKKNGTCCIADLGLAVKFISETNEVDLPP 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678323  370 NHRVGTKRYMAPEVLDDSINMKHFESFKRADIYAMGLVFWEIARRCSIGGIHEDYQLPYYDLVPSDPSVEEMRKVVCEQK 449
Cdd:cd14144 162 NTRVGTKRYMAPEVLDESLNRNHFDAYKMADMYSFGLVLWEIARRCISGGIVEEYQLPYYDAVPSDPSYEDMRRVVCVER 241
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 6678323  450 LRPNIPNRWQSCEALRVMAKIMRECWYANGAARLTALRIKKTLSQL 495
Cdd:cd14144 242 RRPSIPNRWSSDEVLRTMSKLMSECWAHNPAARLTALRVKKTLGKL 287
STKc_BMPR1b cd14219
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IB; STKs ...
199-503 4.29e-156

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  Cd Length: 305  Bit Score: 450.66  E-value: 4.29e-156
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678323  199 RTIARTIVLQESIGKGRFGEVWRGKWRGEEVAVKIFSSREERSWFREAEIYQTVMLRHENILGFIAADNKDNGTWTQLWL 278
Cdd:cd14219   1 RTIAKQIQMVKQIGKGRYGEVWMGKWRGEKVAVKVFFTTEEASWFRETEIYQTVLMRHENILGFIAADIKGTGSWTQLYL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678323  279 VSDYHEHGSLFDYLNRYTVTVEGMIKLALSTASGLAHLHMEIVGTQGKPAIAHRDLKSKNILVKKNGTCCIADLGLAVRH 358
Cdd:cd14219  81 ITDYHENGSLYDYLKSTTLDTKAMLKLAYSSVSGLCHLHTEIFSTQGKPAIAHRDLKSKNILVKKNGTCCIADLGLAVKF 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678323  359 DSATDTIDIAPNHRVGTKRYMAPEVLDDSINMKHFESFKRADIYAMGLVFWEIARRCSIGGIHEDYQLPYYDLVPSDPSV 438
Cdd:cd14219 161 ISDTNEVDIPPNTRVGTKRYMPPEVLDESLNRNHFQSYIMADMYSFGLILWEVARRCVSGGIVEEYQLPYHDLVPSDPSY 240
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6678323  439 EEMRKVVCEQKLRPNIPNRWQSCEALRVMAKIMRECWYANGAARLTALRIKKTLSQLSQQEGIKM 503
Cdd:cd14219 241 EDMREIVCIKRLRPSFPNRWSSDECLRQMGKLMTECWAHNPASRLTALRVKKTLAKMSESQDIKL 305
STKc_BMPR1a cd14220
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IA Receptor; ...
211-495 1.47e-154

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  Cd Length: 287  Bit Score: 446.02  E-value: 1.47e-154
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678323  211 IGKGRFGEVWRGKWRGEEVAVKIFSSREERSWFREAEIYQTVMLRHENILGFIAADNKDNGTWTQLWLVSDYHEHGSLFD 290
Cdd:cd14220   3 IGKGRYGEVWMGKWRGEKVAVKVFFTTEEASWFRETEIYQTVLMRHENILGFIAADIKGTGSWTQLYLITDYHENGSLYD 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678323  291 YLNRYTVTVEGMIKLALSTASGLAHLHMEIVGTQGKPAIAHRDLKSKNILVKKNGTCCIADLGLAVRHDSATDTIDIAPN 370
Cdd:cd14220  83 FLKCTTLDTRALLKLAYSAACGLCHLHTEIYGTQGKPAIAHRDLKSKNILIKKNGTCCIADLGLAVKFNSDTNEVDVPLN 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678323  371 HRVGTKRYMAPEVLDDSINMKHFESFKRADIYAMGLVFWEIARRCSIGGIHEDYQLPYYDLVPSDPSVEEMRKVVCEQKL 450
Cdd:cd14220 163 TRVGTKRYMAPEVLDESLNKNHFQAYIMADIYSFGLIIWEMARRCVTGGIVEEYQLPYYDMVPSDPSYEDMREVVCVKRL 242
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 6678323  451 RPNIPNRWQSCEALRVMAKIMRECWYANGAARLTALRIKKTLSQL 495
Cdd:cd14220 243 RPTVSNRWNSDECLRAVLKLMSECWAHNPASRLTALRIKKTLAKM 287
STKc_ACVR2 cd14053
Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the ...
209-497 2.66e-115

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  Cd Length: 290  Bit Score: 345.85  E-value: 2.66e-115
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678323  209 ESIGKGRFGEVWRGKWRGEEVAVKIFSSREERSWFREAEIYQTVMLRHENILGFIAADNKDNGTWTQLWLVSDYHEHGSL 288
Cdd:cd14053   1 EIKARGRFGAVWKAQYLNRLVAVKIFPLQEKQSWLTEREIYSLPGMKHENILQFIGAEKHGESLEAEYWLITEFHERGSL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678323  289 FDYLNRYTVTVEGMIKLALSTASGLAHLHMEIVGTQG--KPAIAHRDLKSKNILVKKNGTCCIADLGLAVRHDSATDTID 366
Cdd:cd14053  81 CDYLKGNVISWNELCKIAESMARGLAYLHEDIPATNGghKPSIAHRDFKSKNVLLKSDLTACIADFGLALKFEPGKSCGD 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678323  367 iapNH-RVGTKRYMAPEVLDDSINMKHfESFKRADIYAMGLVFWEIARRCSIGGIH-EDYQLPYYDLVPSDPSVEEMRKV 444
Cdd:cd14053 161 ---THgQVGTRRYMAPEVLEGAINFTR-DAFLRIDMYAMGLVLWELLSRCSVHDGPvDEYQLPFEEEVGQHPTLEDMQEC 236
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 6678323  445 VCEQKLRPNIPNRWQSCEALRVMAKIMRECWYANGAARLTALRIKKTLSQLSQ 497
Cdd:cd14053 237 VVHKKLRPQIRDEWRKHPGLAQLCETIEECWDHDAEARLSAGCVEERLSQLSR 289
STKc_TGFbR2_like cd14055
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II ...
209-485 8.40e-110

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  Cd Length: 295  Bit Score: 331.65  E-value: 8.40e-110
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678323  209 ESIGKGRFGEVWRGKWRG------EEVAVKIFSSREERSWFREAEIYQTVMLRHENILGFIAADNKDNGTWTQLWLVSDY 282
Cdd:cd14055   1 KLVGKGRFAEVWKAKLKQnasgqyETVAVKIFPYEEYASWKNEKDIFTDASLKHENILQFLTAEERGVGLDRQYWLITAY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678323  283 HEHGSLFDYLNRYTVTVEGMIKLALSTASGLAHLHMEIVGtQGKP--AIAHRDLKSKNILVKKNGTCCIADLGLAVRHDS 360
Cdd:cd14055  81 HENGSLQDYLTRHILSWEDLCKMAGSLARGLAHLHSDRTP-CGRPkiPIAHRDLKSSNILVKNDGTCVLADFGLALRLDP 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678323  361 ATDTIDIAPNHRVGTKRYMAPEVLDDSINMKHFESFKRADIYAMGLVFWEIARRCSIGGIHEDYQLPYYDLVPSDPSVEE 440
Cdd:cd14055 160 SLSVDELANSGQVGTARYMAPEALESRVNLEDLESFKQIDVYSMALVLWEMASRCEASGEVKPYELPFGSKVRERPCVES 239
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 6678323  441 MRKVVCEQKLRPNIPNRWQSCEALRVMAKIMRECWYANGAARLTA 485
Cdd:cd14055 240 MKDLVLRDRGRPEIPDSWLTHQGMCVLCDTITECWDHDPEARLTA 284
STKc_BMPR2_AMHR2 cd14054
Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and ...
209-495 2.64e-96

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  Cd Length: 300  Bit Score: 296.97  E-value: 2.64e-96
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678323  209 ESIGKGRFGEVWRGKWRGEEVAVKIFSSREERSWFREAEIYQTVMLRHENILGFIAADNKDNGT-WTQLWLVSDYHEHGS 287
Cdd:cd14054   1 QLIGQGRYGTVWKGSLDERPVAVKVFPARHRQNFQNEKDIYELPLMEHSNILRFIGADERPTADgRMEYLLVLEYAPKGS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678323  288 LFDYLNRYTVTVEGMIKLALSTASGLAHLHMEI-VGTQGKPAIAHRDLKSKNILVKKNGTCCIADLGLAVR--------- 357
Cdd:cd14054  81 LCSYLRENTLDWMSSCRMALSLTRGLAYLHTDLrRGDQYKPAIAHRDLNSRNVLVKADGSCVICDFGLAMVlrgsslvrg 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678323  358 HDSATDTIDIApnhRVGTKRYMAPEVLDDSINMKHFESF-KRADIYAMGLVFWEIARRCS---IGGIHEDYQLPYYDLVP 433
Cdd:cd14054 161 RPGAAENASIS---EVGTLRYMAPEVLEGAVNLRDCESAlKQVDVYALGLVLWEIAMRCSdlyPGESVPPYQMPYEAELG 237
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6678323  434 SDPSVEEMRKVVCEQKLRPNIPNRW-QSCEALRVMAKIMRECWYANGAARLTALRIKKTLSQL 495
Cdd:cd14054 238 NHPTFEDMQLLVSREKARPKFPDAWkENSLAVRSLKETIEDCWDQDAEARLTALCVEERLAEL 300
STKc_ACVR2a cd14141
Catalytic domain of the Serine/Threonine Kinase, Activin Type IIA Receptor; STKs catalyze the ...
209-498 5.01e-81

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  Cd Length: 290  Bit Score: 257.28  E-value: 5.01e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678323  209 ESIGKGRFGEVWRGKWRGEEVAVKIFSSREERSWFREAEIYQTVMLRHENILGFIAADNKDNGTWTQLWLVSDYHEHGSL 288
Cdd:cd14141   1 EIKARGRFGCVWKAQLLNEYVAVKIFPIQDKLSWQNEYEIYSLPGMKHENILQFIGAEKRGTNLDVDLWLITAFHEKGSL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678323  289 FDYLNRYTVTVEGMIKLALSTASGLAHLHMEIVGTQG--KPAIAHRDLKSKNILVKKNGTCCIADLGLAVRHD---SATD 363
Cdd:cd14141  81 TDYLKANVVSWNELCHIAQTMARGLAYLHEDIPGLKDghKPAIAHRDIKSKNVLLKNNLTACIADFGLALKFEagkSAGD 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678323  364 TidiapNHRVGTKRYMAPEVLDDSINMKHfESFKRADIYAMGLVFWEIARRCSIG-GIHEDYQLPYYDLVPSDPSVEEMR 442
Cdd:cd14141 161 T-----HGQVGTRRYMAPEVLEGAINFQR-DAFLRIDMYAMGLVLWELASRCTASdGPVDEYMLPFEEEVGQHPSLEDMQ 234
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 6678323  443 KVVCEQKLRPNIPNRWQSCEALRVMAKIMRECWYANGAARLTALRIKKTLSQLSQQ 498
Cdd:cd14141 235 EVVVHKKKRPVLRECWQKHAGMAMLCETIEECWDHDAEARLSAGCVEERIIQMQRL 290
STKc_ACVR2b cd14140
Catalytic domain of the Serine/Threonine Kinase, Activin Type IIB Receptor; STKs catalyze the ...
209-497 1.99e-79

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  Cd Length: 291  Bit Score: 253.03  E-value: 1.99e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678323  209 ESIGKGRFGEVWRGKWRGEEVAVKIFSSREERSWFREAEIYQTVMLRHENILGFIAADNKDNGTWTQLWLVSDYHEHGSL 288
Cdd:cd14140   1 EIKARGRFGCVWKAQLMNEYVAVKIFPIQDKQSWQSEREIFSTPGMKHENLLQFIAAEKRGSNLEMELWLITAFHDKGSL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678323  289 FDYLNRYTVTVEGMIKLALSTASGLAHLHMEIVGTQG---KPAIAHRDLKSKNILVKKNGTCCIADLGLAVRHDSATDTI 365
Cdd:cd14140  81 TDYLKGNIVSWNELCHIAETMARGLSYLHEDVPRCKGeghKPAIAHRDFKSKNVLLKNDLTAVLADFGLAVRFEPGKPPG 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678323  366 DIapNHRVGTKRYMAPEVLDDSINMKHfESFKRADIYAMGLVFWEIARRC-SIGGIHEDYQLPYYDLVPSDPSVEEMRKV 444
Cdd:cd14140 161 DT--HGQVGTRRYMAPEVLEGAINFQR-DSFLRIDMYAMGLVLWELVSRCkAADGPVDEYMLPFEEEIGQHPSLEDLQEV 237
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 6678323  445 VCEQKLRPNIPNRWQSCEALRVMAKIMRECWYANGAARLTALRIKKTLSQLSQ 497
Cdd:cd14140 238 VVHKKMRPVFKDHWLKHPGLAQLCVTIEECWDHDAEARLSAGCVEERISQIRR 290
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
211-475 5.63e-57

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


Pssm-ID: 270901  Cd Length: 245  Bit Score: 192.37  E-value: 5.63e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678323  211 IGKGRFGEVWRGKWRGEEVAVKIFSSREERSWFREA---EIYQTVMLRHENILGFIAADNKDNgtwtQLWLVSDYHEHGS 287
Cdd:cd13999   1 IGSGSFGEVYKGKWRGTDVAIKKLKVEDDNDELLKEfrrEVSILSKLRHPNIVQFIGACLSPP----PLCIVTEYMPGGS 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678323  288 LFDYL--NRYTVTVEGMIKLALSTASGLAHLHmeivgtqgKPAIAHRDLKSKNILVKKNGTCCIADLGLAVRHDSATDTI 365
Cdd:cd13999  77 LYDLLhkKKIPLSWSLRLKIALDIARGMNYLH--------SPPIIHRDLKSLNILLDENFTVKIADFGLSRIKNSTTEKM 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678323  366 diapNHRVGTKRYMAPEVlddsINMKHFeSFKrADIYAMGLVFWEIARRcsiggihedyQLPYYDLVPsdpsvEEMRKVV 445
Cdd:cd13999 149 ----TGVVGTPRWMAPEV----LRGEPY-TEK-ADVYSFGIVLWELLTG----------EVPFKELSP-----IQIAAAV 203
                       250       260       270
                ....*....|....*....|....*....|
gi 6678323  446 CEQKLRPNIPNRWQScealrVMAKIMRECW 475
Cdd:cd13999 204 VQKGLRPPIPPDCPP-----ELSKLIKRCW 228
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
211-411 9.09e-42

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  Cd Length: 215  Bit Score: 150.50  E-value: 9.09e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678323  211 IGKGRFGEVWRGKWR--GEEVAVKIFS----SREERSWFREAEIYQtvMLRHENILGFIAADNKDNgtwtQLWLVSDYHE 284
Cdd:cd00180   1 LGKGSFGKVYKARDKetGKKVAVKVIPkeklKKLLEELLREIEILK--KLNHPNIVKLYDVFETEN----FLYLVMEYCE 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678323  285 HGSLFDYL--NRYTVTVEGMIKLALSTASGLAHLHMEivgtqgkpAIAHRDLKSKNILVKKNGTCCIADLGLAVRHDSAT 362
Cdd:cd00180  75 GGSLKDLLkeNKGPLSEEEALSILRQLLSALEYLHSN--------GIIHRDLKPENILLDSDGTVKLADFGLAKDLDSDD 146
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 6678323  363 DTIDIAPNHrvGTKRYMAPEVlddsinMKHFESFKRADIYAMGLVFWEI 411
Cdd:cd00180 147 SLLKTTGGT--TPPYYAPPEL------LGGRYYGPKVDIWSLGVILYEL 187
Pkinase_Tyr pfam07714
Protein tyrosine kinase;
205-492 8.86e-40

Protein tyrosine kinase;


Pssm-ID: 311583  Cd Length: 258  Bit Score: 146.11  E-value: 8.86e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678323    205 IVLQESIGKGRFGEVWRGKWRGE------EVAVKI----FSSREERSWFREAEIyqtvM--LRHENILGFIAADNKDNgt 272
Cdd:pfam07714   1 LTLGEKLGEGAFGEVYKGTLKGDgegtkiKVAVKTlkegADEEEREDFLEEASI----MkkLSHPNIVRLLGVCTQGE-- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678323    273 wtQLWLVSDYHEHGSLFDYL--NRYTVTVEGMIKLALSTASGLAHLH-MEIVgtqgkpaiaHRDLKSKNILVKKNGTCCI 349
Cdd:pfam07714  75 --PLYIVTEYMPGGDLLDFLrkHKGKLTLPDLLQMALQIAKGMEYLEsKNFV---------HRDLAARNCLVTENLVVKI 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678323    350 ADLGLAvrhdsatDTIDIAPNHRVGTK-----RYMAPEVLDDSINmkhfeSFKrADIYAMGLVFWEIarrCSIGGIhedy 424
Cdd:pfam07714 144 SDFGLS-------RDIYDDDYYRKRGGgklpiKWMAPESLKDGKF-----TSK-SDVWSFGVLLWEI---FTLGEQ---- 203
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678323    425 qlPYYDLvpsdpSVEEMRKVVcEQKLRPNIPnrwQSC--EalrvMAKIMRECWYANGAARLTALRIKKTL 492
Cdd:pfam07714 204 --PYPGM-----SNEEVLEFL-EDGYRLPQP---ENCpdE----LYDLMTQCWAYDPEDRPTFSELVEDL 258
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
205-492 2.65e-39

Tyrosine kinase,