NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|17136928|ref|NP_477000|]
View 

baboon, isoform A [Drosophila melanogaster]

Protein Classification

Activin_recp and STKc_TGFbR1_ACVR1b_ACVR1c domain-containing protein (domain architecture ID 10471091)

protein containing domains Activin_recp, GS, and STKc_TGFbR1_ACVR1b_ACVR1c

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
307-594 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: 612.91  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136928 307 HVIGKGRFGEVWRGRWRGENVAVKIFSSREECSWFREAEIYQTVMLRHENILGFIAADNKDNGTWTQLWLVTDYHENGSL 386
Cdd:cd14143   1 ESIGKGRFGEVWRGRWRGEDVAVKIFSSREERSWFREAEIYQTVMLRHENILGFIAADNKDNGTWTQLWLVSDYHEHGSL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136928 387 FDYLTTHPVDTNTMLNMSLSIATGLAHLHMDIVGTRGKPAIAHRDLKSKNILVKSNLSCAIGDLGLAVRHVEKNDSVDIP 466
Cdd:cd14143  81 FDYLNRYTVTVEGMIKLALSIASGLAHLHMEIVGTQGKPAIAHRDLKSKNILVKKNGTCCIADLGLAVRHDSATDTIDIA 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136928 467 STHRVGTKRYMAPEVLDESMNDQHFDSYKRADVYAFGLILWEIARRCNMGMIYDEYQLPYYDVVQPDPSIEEMKKVVCIE 546
Cdd:cd14143 161 PNHRVGTKRYMAPEVLDDTINMKHFESFKRADIYALGLVFWEIARRCSIGGIHEDYQLPYYDLVPSDPSIEEMRKVVCEQ 240
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 17136928 547 KCRPNIPNRWHASDVLHNMAKVMKECWYPNPVARLTALRIKKTLASIS 594
Cdd:cd14143 241 KLRPNIPNRWQSCEALRVMAKIMRECWYANGAARLTALRIKKTLSQLS 288
Activin_recp pfam01064
Activin types I and II receptor domain; This Pfam entry consists of both TGF-beta receptor ...
127-204 7.85e-27

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: 105.70  E-value: 7.85e-27
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17136928   127 IKCHCDTCKESNNICETDGFCFTSVEKNSDGSIIFSYSCMVVKYNMQRSKPFECLTSNERFDTYRIDCCKS-DFCNKNE 204
Cdd:pfam01064   1 LKCYCEGEEIENETCETDGSCFTSVEENEDGKEIVSKGCISEEDLGPLNSPFECKLSNTPPQGGRIECCCEgDYCNKNL 79
GS smart00467
GS motif; Aa approx. 30 amino acid motif that precedes the kinase domain in types I and II TGF ...
273-303 2.87e-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: 57.56  E-value: 2.87e-10
                           10        20        30
                   ....*....|....*....|....*....|.
gi 17136928    273 TTIHDIIEMTTSGSGSaGLPLLVQRSIARQV 303
Cdd:smart00467   1 KTLSDLLEDTTSGSGS-GLPLLVQRTVARQI 30
 
Name Accession Description Interval E-value
STKc_TGFbR1_ACVR1b_ACVR1c cd14143
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta Type I ...
307-594 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: 612.91  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136928 307 HVIGKGRFGEVWRGRWRGENVAVKIFSSREECSWFREAEIYQTVMLRHENILGFIAADNKDNGTWTQLWLVTDYHENGSL 386
Cdd:cd14143   1 ESIGKGRFGEVWRGRWRGEDVAVKIFSSREERSWFREAEIYQTVMLRHENILGFIAADNKDNGTWTQLWLVSDYHEHGSL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136928 387 FDYLTTHPVDTNTMLNMSLSIATGLAHLHMDIVGTRGKPAIAHRDLKSKNILVKSNLSCAIGDLGLAVRHVEKNDSVDIP 466
Cdd:cd14143  81 FDYLNRYTVTVEGMIKLALSIASGLAHLHMEIVGTQGKPAIAHRDLKSKNILVKKNGTCCIADLGLAVRHDSATDTIDIA 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136928 467 STHRVGTKRYMAPEVLDESMNDQHFDSYKRADVYAFGLILWEIARRCNMGMIYDEYQLPYYDVVQPDPSIEEMKKVVCIE 546
Cdd:cd14143 161 PNHRVGTKRYMAPEVLDDTINMKHFESFKRADIYALGLVFWEIARRCSIGGIHEDYQLPYYDLVPSDPSIEEMRKVVCEQ 240
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 17136928 547 KCRPNIPNRWHASDVLHNMAKVMKECWYPNPVARLTALRIKKTLASIS 594
Cdd:cd14143 241 KLRPNIPNRWQSCEALRVMAKIMRECWYANGAARLTALRIKKTLSQLS 288
Pkinase_Tyr pfam07714
Protein tyrosine kinase;
303-590 3.02e-45

Protein tyrosine kinase;


Pssm-ID: 311583  Cd Length: 258  Bit Score: 162.67  E-value: 3.02e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136928   303 VQLCHVIGKGRFGEVWRGRWRGEN------VAVKI----FSSREECSWFREAEIyqtvM--LRHENILGFIAADNKDNgt 370
Cdd:pfam07714   1 LTLGEKLGEGAFGEVYKGTLKGDGegtkikVAVKTlkegADEEEREDFLEEASI----MkkLSHPNIVRLLGVCTQGE-- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136928   371 wtQLWLVTDYHENGSLFDYLTTH--PVDTNTMLNMSLSIATGLAHLH-MDIVgtrgkpaiaHRDLKSKNILVKSNLSCAI 447
Cdd:pfam07714  75 --PLYIVTEYMPGGDLLDFLRKHkgKLTLPDLLQMALQIAKGMEYLEsKNFV---------HRDLAARNCLVTENLVVKI 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136928   448 GDLGLAvRHVEKNDSvdipSTHRVGTK---RYMAPEVLdesmNDQHFDSYkrADVYAFGLILWEIarrCNMGMIydeyql 524
Cdd:pfam07714 144 SDFGLS-RDIYDDDY----YRKRGGGKlpiKWMAPESL----KDGKFTSK--SDVWSFGVLLWEI---FTLGEQ------ 203
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17136928   525 PYYDVvqpdpSIEEMKKVVcIEKCRPNIPNRWHASdvlhnMAKVMKECWYPNPVARLTALRIKKTL 590
Cdd:pfam07714 204 PYPGM-----SNEEVLEFL-EDGYRLPQPENCPDE-----LYDLMTQCWAYDPEDRPTFSELVEDL 258
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
303-590 9.60e-42

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


Pssm-ID: 197581  Cd Length: 257  Bit Score: 152.30  E-value: 9.60e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136928    303 VQLCHVIGKGRFGEVWRGRWRG------ENVAVKifSSREECS------WFREAEIYQtvMLRHENILGFIAADNKDNgt 370
Cdd:smart00219   1 LTLGKKLGEGAFGEVYKGKLKGkggkkkVEVAVK--TLKEDASeqqieeFLREARIMR--KLDHPNVVKLLGVCTEEE-- 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136928    371 wtQLWLVTDYHENGSLFDYL--TTHPVDTNTMLNMSLSIATGLAHLHmdivgtrGKPAIaHRDLKSKNILVKSNLSCAIG 448
Cdd:smart00219  75 --PLYIVMEYMEGGDLLSYLrkNRPKLSLSDLLSFALQIARGMEYLE-------SKNFI-HRDLAARNCLVGENLVVKIS 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136928    449 DLGLAvRHVEKNDSVDipSTHRVGTKRYMAPEVLDESMndqhFDSYkrADVYAFGLILWEIARRCnmgmiydeyQLPYYD 528
Cdd:smart00219 145 DFGLS-RDLYDDDYYR--KRGGKLPIRWMAPESLKEGK----FTSK--SDVWSFGVLLWEIFTLG---------EQPYPG 206
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17136928    529 VvqpdpSIEEMKKVVcIEKCRPNIPNrwHASDvlhNMAKVMKECWYPNPVARLTALRIKKTL 590
Cdd:smart00219 207 M-----SNEEVLEYL-KNGYRLPQPP--NCPP---ELYDLMLQCWAEDPEDRPTFSELVEIL 257
Activin_recp pfam01064
Activin types I and II receptor domain; This Pfam entry consists of both TGF-beta receptor ...
127-204 7.85e-27

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: 105.70  E-value: 7.85e-27
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17136928   127 IKCHCDTCKESNNICETDGFCFTSVEKNSDGSIIFSYSCMVVKYNMQRSKPFECLTSNERFDTYRIDCCKS-DFCNKNE 204
Cdd:pfam01064   1 LKCYCEGEEIENETCETDGSCFTSVEENEDGKEIVSKGCISEEDLGPLNSPFECKLSNTPPQGGRIECCCEgDYCNKNL 79
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
304-511 7.37e-21

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 223589  Cd Length: 384  Bit Score: 94.81  E-value: 7.37e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136928 304 QLCHVIGKGRFGEVWRGRwRGENVAVKIFS------SREECSWFREAEIYQTVmLRHENILGFIAADNKDNgtwtQLWLV 377
Cdd:COG0515   3 RILRKLGEGSFGEVYLAR-DRKLVALKVLAkkleskSKEVERFLREIQILASL-NHPPNIVKLYDFFQDEG----SLYLV 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136928 378 TDYHENGSLFDYL----TTHPVDTNTMLNMSLSIATGLAHLHmdivgTRGkpaIAHRDLKSKNILVKSNLS-CAIGDLGL 452
Cdd:COG0515  77 MEYVDGGSLEDLLkkigRKGPLSESEALFILAQILSALEYLH-----SKG---IIHRDIKPENILLDRDGRvVKLIDFGL 148
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17136928 453 A--VRHVEKNDSVDIPSTHRVGTKRYMAPEVLdESMNDQHFDSykRADVYAFGLILWEIAR 511
Cdd:COG0515 149 AklLPDPGSTSSIPALPSTSVGTPGYMAPEVL-LGLSLAYASS--SSDIWSLGITLYELLT 206
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
282-508 3.79e-13

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036  Cd Length: 353  Bit Score: 71.01  E-value: 3.79e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136928  282 TTSGSGSAGLPLLVQRSIARQVQLCHV-----IGKGRFGEVWRGRWR--GENVAVK-IFSSREEC---SWFREAEIYQTV 350
Cdd:PLN00034  50 PSSSSSSSSSSSASGSAPSAAKSLSELervnrIGSGAGGTVYKVIHRptGRLYALKvIYGNHEDTvrrQICREIEILRDV 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136928  351 mlRHENILGfiAADNKDNGTWTQLWLvtDYHENGSLFDyltTHPVDTNTMLNMSLSIATGLAHLHmdivgtrgKPAIAHR 430
Cdd:PLN00034 130 --NHPNVVK--CHDMFDHNGEIQVLL--EFMDGGSLEG---THIADEQFLADVARQILSGIAYLH--------RRHIVHR 192
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17136928  431 DLKSKNILVKSNLSCAIGDLGLAvRHVekNDSVDiPSTHRVGTKRYMAPEVLDESMNDQHFDSYKrADVYAFGLILWE 508
Cdd:PLN00034 193 DIKPSNLLINSAKNVKIADFGVS-RIL--AQTMD-PCNSSVGTIAYMSPERINTDLNHGAYDGYA-GDIWSLGVSILE 265
GS smart00467
GS motif; Aa approx. 30 amino acid motif that precedes the kinase domain in types I and II TGF ...
273-303 2.87e-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: 57.56  E-value: 2.87e-10
                           10        20        30
                   ....*....|....*....|....*....|.
gi 17136928    273 TTIHDIIEMTTSGSGSaGLPLLVQRSIARQV 303
Cdd:smart00467   1 KTLSDLLEDTTSGSGS-GLPLLVQRTVARQI 30
TGF_beta_GS pfam08515
Transforming growth factor beta type I GS-motif; This motif is found in the transforming ...
274-301 1.10e-08

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: 52.87  E-value: 1.10e-08
                          10        20
                  ....*....|....*....|....*....
gi 17136928   274 TIHDIIEMT-TSGSGSaGLPLLVQRSIAR 301
Cdd:pfam08515   1 TLKDLIEEScTSGSGS-GLPLLVQRTIAR 28
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
341-508 1.18e-04

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: 1.18e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136928    341 FReAEIYQTVMLRHENILGFIAADNKDNGtwtQLWLVTDYHENGSLFDYLTTH----PVDTNTMLnmsLSIATGLAHLHm 416
Cdd:TIGR03903   25 FR-RETALCARLYHPNIVALLDSGEAPPG---LLFAVFEYVPGRTLREVLAADgalpAGETGRLM---LQVLDALACAH- 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136928    417 divgTRGkpaIAHRDLKSKNILVKSN--------LSCAIGDLGLAVRHVeknDSVDIPSTHRV-GTKRYMAPEVL-DESM 486
Cdd:TIGR03903   97 ----NQG---IVHRDLKPQNIMVSQTgvrphakvLDFGIGTLLPGVRDA---DVATLTRTTEVlGTPTYCAPEQLrGEPV 166
                          170       180
                   ....*....|....*....|..
gi 17136928    487 NDQhfdsykrADVYAFGLILWE 508
Cdd:TIGR03903  167 TPN-------SDLYAWGLIFLE 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 ...
307-594 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: 612.91  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136928 307 HVIGKGRFGEVWRGRWRGENVAVKIFSSREECSWFREAEIYQTVMLRHENILGFIAADNKDNGTWTQLWLVTDYHENGSL 386
Cdd:cd14143   1 ESIGKGRFGEVWRGRWRGEDVAVKIFSSREERSWFREAEIYQTVMLRHENILGFIAADNKDNGTWTQLWLVSDYHEHGSL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136928 387 FDYLTTHPVDTNTMLNMSLSIATGLAHLHMDIVGTRGKPAIAHRDLKSKNILVKSNLSCAIGDLGLAVRHVEKNDSVDIP 466
Cdd:cd14143  81 FDYLNRYTVTVEGMIKLALSIASGLAHLHMEIVGTQGKPAIAHRDLKSKNILVKKNGTCCIADLGLAVRHDSATDTIDIA 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136928 467 STHRVGTKRYMAPEVLDESMNDQHFDSYKRADVYAFGLILWEIARRCNMGMIYDEYQLPYYDVVQPDPSIEEMKKVVCIE 546
Cdd:cd14143 161 PNHRVGTKRYMAPEVLDDTINMKHFESFKRADIYALGLVFWEIARRCSIGGIHEDYQLPYYDLVPSDPSIEEMRKVVCEQ 240
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 17136928 547 KCRPNIPNRWHASDVLHNMAKVMKECWYPNPVARLTALRIKKTLASIS 594
Cdd:cd14143 241 KLRPNIPNRWQSCEALRVMAKIMRECWYANGAARLTALRIKKTLSQLS 288
STKc_TGFbR_I cd14056
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type ...
307-593 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: 537.24  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136928 307 HVIGKGRFGEVWRGRWRGENVAVKIFSSREECSWFREAEIYQTVMLRHENILGFIAADNKDNGTWTQLWLVTDYHENGSL 386
Cdd:cd14056   1 KTIGKGRYGEVWLGKYRGEKVAVKIFSSRDEDSWFRETEIYQTVMLRHENILGFIAADIKSTGSWTQLWLITEYHEHGSL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136928 387 FDYLTTHPVDTNTMLNMSLSIATGLAHLHMDIVGTRGKPAIAHRDLKSKNILVKSNLSCAIGDLGLAVRHVEKNDSVDIP 466
Cdd:cd14056  81 YDYLQRNTLDTEEALRLAYSAASGLAHLHTEIVGTQGKPAIAHRDLKSKNILVKRDGTCCIADLGLAVRYDSDTNTIDIP 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136928 467 STHRVGTKRYMAPEVLDESMNDQHFDSYKRADVYAFGLILWEIARRCNMGMIYDEYQLPYYDVVQPDPSIEEMKKVVCIE 546
Cdd:cd14056 161 PNPRVGTKRYMAPEVLDDSINPKSFESFKMADIYSFGLVLWEIARRCEIGGIAEEYQLPYFGMVPSDPSFEEMRKVVCVE 240
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 17136928 547 KCRPNIPNRWHASDVLHNMAKVMKECWYPNPVARLTALRIKKTLASI 593
Cdd:cd14056 241 KLRPPIPNRWKSDPVLRSMVKLMQECWSENPHARLTALRVKKTLAKL 287
STKc_ACVR1_ALK1 cd14142
Catalytic domain of the Serine/Threonine Kinases, Activin Type I Receptor and Activin ...
297-594 2.76e-178

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: 510.44  E-value: 2.76e-178
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136928 297 RSIARQVQLCHVIGKGRFGEVWRGRWRGENVAVKIFSSREECSWFREAEIYQTVMLRHENILGFIAADNKDNGTWTQLWL 376
Cdd:cd14142   1 RTVARQITLVECIGKGRYGEVWRGQWQGESVAVKIFSSRDEKSWFRETEIYNTVLLRHENILGFIASDMTSRNSCTQLWL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136928 377 VTDYHENGSLFDYLTTHPVDTNTMLNMSLSIATGLAHLHMDIVGTRGKPAIAHRDLKSKNILVKSNLSCAIGDLGLAVRH 456
Cdd:cd14142  81 ITHYHENGSLYDYLQRTTLDHQEMLRLALSAASGLVHLHTEIFGTQGKPAIAHRDLKSKNILVKSNGQCCIADLGLAVTH 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136928 457 VEKNDSVDIPSTHRVGTKRYMAPEVLDESMNDQHFDSYKRADVYAFGLILWEIARRCNMGMIYDEYQLPYYDVVQPDPSI 536
Cdd:cd14142 161 SQETNQLDVGNNPRVGTKRYMAPEVLDETINTDCFESYKRVDIYAFGLVLWEVARRCVSGGIVEEYKPPFYDVVPSDPSF 240
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 17136928 537 EEMKKVVCIEKCRPNIPNRWHASDVLHNMAKVMKECWYPNPVARLTALRIKKTLASIS 594
Cdd:cd14142 241 EDMRKVVCVDQQRPNIPNRWSSDPTLTAMAKLMKECWYQNPSARLTALRIKKTLLKIL 298
STKc_BMPR1 cd14144
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type I Receptor; ...
307-593 2.99e-171

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: 492.38  E-value: 2.99e-171
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136928 307 HVIGKGRFGEVWRGRWRGENVAVKIFSSREECSWFREAEIYQTVMLRHENILGFIAADNKDNGTWTQLWLVTDYHENGSL 386
Cdd:cd14144   1 RSVGKGRYGEVWKGKWRGEKVAVKIFFTTEEASWFRETEIYQTVLMRHENILGFIAADIKGTGSWTQLYLITDYHENGSL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136928 387 FDYLTTHPVDTNTMLNMSLSIATGLAHLHMDIVGTRGKPAIAHRDLKSKNILVKSNLSCAIGDLGLAVRHVEKNDSVDIP 466
Cdd:cd14144  81 YDFLRGNTLDTQSMLKLAYSAACGLAHLHTEIFGTQGKPAIAHRDIKSKNILVKKNGTCCIADLGLAVKFISETNEVDLP 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136928 467 STHRVGTKRYMAPEVLDESMNDQHFDSYKRADVYAFGLILWEIARRCNMGMIYDEYQLPYYDVVQPDPSIEEMKKVVCIE 546
Cdd:cd14144 161 PNTRVGTKRYMAPEVLDESLNRNHFDAYKMADMYSFGLVLWEIARRCISGGIVEEYQLPYYDAVPSDPSYEDMRRVVCVE 240
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 17136928 547 KCRPNIPNRWHASDVLHNMAKVMKECWYPNPVARLTALRIKKTLASI 593
Cdd:cd14144 241 RRRPSIPNRWSSDEVLRTMSKLMSECWAHNPAARLTALRVKKTLGKL 287
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
308-593 3.46e-164

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: 474.23  E-value: 3.46e-164
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136928 308 VIGKGRFGEVWRGRWRGENVAVKIFSSREECSWFREAEIYQTVMLRHENILGFIAADNKDNGTWTQLWLVTDYHENGSLF 387
Cdd:cd13998   2 VIGKGRFGEVWKASLKNEPVAVKIFSSRDKQSWFREKEIYRTPMLKHENILQFIAADERDTALRTELWLVTAFHPNGSL* 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136928 388 DYLTTHPVDTNTMLNMSLSIATGLAHLHMDIVG-TRGKPAIAHRDLKSKNILVKSNLSCAIGDLGLAVRHVEKNDSVDIP 466
Cdd:cd13998  82 DYLSLHTIDWVSLCRLALSVARGLAHLHSEIPGcTQGKPAIAHRDLKSKNILVKNDGTCCIADFGLAVRLSPSTGEEDNA 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136928 467 STHRVGTKRYMAPEVLDESMNDQHFDSYKRADVYAFGLILWEIARRCNMGM-IYDEYQLPYYDVVQPDPSIEEMKKVVCI 545
Cdd:cd13998 162 NNGQVGTKRYMAPEVLEGAINLRDFESFKRVDIYAMGLVLWEMASRCTDLFgIVEEYKPPFYSEVPNHPSFEDMQEVVVR 241
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 17136928 546 EKCRPNIPNRWHASDVLHNMAKVMKECWYPNPVARLTALRIKKTLASI 593
Cdd:cd13998 242 DKQRPNIPNRWLSHPGLQSLAETIEECWDHDAEARLTAQCIEERLSEF 289
STKc_BMPR1b cd14219
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IB; STKs ...
297-600 6.75e-146

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: 428.31  E-value: 6.75e-146
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136928 297 RSIARQVQLCHVIGKGRFGEVWRGRWRGENVAVKIFSSREECSWFREAEIYQTVMLRHENILGFIAADNKDNGTWTQLWL 376
Cdd:cd14219   1 RTIAKQIQMVKQIGKGRYGEVWMGKWRGEKVAVKVFFTTEEASWFRETEIYQTVLMRHENILGFIAADIKGTGSWTQLYL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136928 377 VTDYHENGSLFDYLTTHPVDTNTMLNMSLSIATGLAHLHMDIVGTRGKPAIAHRDLKSKNILVKSNLSCAIGDLGLAVRH 456
Cdd:cd14219  81 ITDYHENGSLYDYLKSTTLDTKAMLKLAYSSVSGLCHLHTEIFSTQGKPAIAHRDLKSKNILVKKNGTCCIADLGLAVKF 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136928 457 VEKNDSVDIPSTHRVGTKRYMAPEVLDESMNDQHFDSYKRADVYAFGLILWEIARRCNMGMIYDEYQLPYYDVVQPDPSI 536
Cdd:cd14219 161 ISDTNEVDIPPNTRVGTKRYMPPEVLDESLNRNHFQSYIMADMYSFGLILWEVARRCVSGGIVEEYQLPYHDLVPSDPSY 240
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17136928 537 EEMKKVVCIEKCRPNIPNRWHASDVLHNMAKVMKECWYPNPVARLTALRIKKTLASISVEDKVK 600
Cdd:cd14219 241 EDMREIVCIKRLRPSFPNRWSSDECLRQMGKLMTECWAHNPASRLTALRVKKTLAKMSESQDIK 304
STKc_BMPR1a cd14220
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IA Receptor; ...
309-593 1.11e-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  Cd Length: 287  Bit Score: 424.45  E-value: 1.11e-144
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136928 309 IGKGRFGEVWRGRWRGENVAVKIFSSREECSWFREAEIYQTVMLRHENILGFIAADNKDNGTWTQLWLVTDYHENGSLFD 388
Cdd:cd14220   3 IGKGRYGEVWMGKWRGEKVAVKVFFTTEEASWFRETEIYQTVLMRHENILGFIAADIKGTGSWTQLYLITDYHENGSLYD 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136928 389 YLTTHPVDTNTMLNMSLSIATGLAHLHMDIVGTRGKPAIAHRDLKSKNILVKSNLSCAIGDLGLAVRHVEKNDSVDIPST 468
Cdd:cd14220  83 FLKCTTLDTRALLKLAYSAACGLCHLHTEIYGTQGKPAIAHRDLKSKNILIKKNGTCCIADLGLAVKFNSDTNEVDVPLN 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136928 469 HRVGTKRYMAPEVLDESMNDQHFDSYKRADVYAFGLILWEIARRCNMGMIYDEYQLPYYDVVQPDPSIEEMKKVVCIEKC 548
Cdd:cd14220 163 TRVGTKRYMAPEVLDESLNKNHFQAYIMADIYSFGLIIWEMARRCVTGGIVEEYQLPYYDMVPSDPSYEDMREVVCVKRL 242
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 17136928 549 RPNIPNRWHASDVLHNMAKVMKECWYPNPVARLTALRIKKTLASI 593
Cdd:cd14220 243 RPTVSNRWNSDECLRAVLKLMSECWAHNPASRLTALRIKKTLAKM 287
STKc_ACVR2 cd14053
Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the ...
308-583 8.58e-107

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: 326.98  E-value: 8.58e-107
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136928 308 VIGKGRFGEVWRGRWRGENVAVKIFSSREECSWFREAEIYQTVMLRHENILGFIAADNKDNGTWTQLWLVTDYHENGSLF 387
Cdd:cd14053   2 IKARGRFGAVWKAQYLNRLVAVKIFPLQEKQSWLTEREIYSLPGMKHENILQFIGAEKHGESLEAEYWLITEFHERGSLC 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136928 388 DYLTTHPVDTNTMLNMSLSIATGLAHLHMDIVGTRG--KPAIAHRDLKSKNILVKSNLSCAIGDLGLAVRHvekNDSVDI 465
Cdd:cd14053  82 DYLKGNVISWNELCKIAESMARGLAYLHEDIPATNGghKPSIAHRDFKSKNVLLKSDLTACIADFGLALKF---EPGKSC 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136928 466 PSTH-RVGTKRYMAPEVLDESMNDQHfDSYKRADVYAFGLILWEIARRCNMGMI-YDEYQLPYYDVVQPDPSIEEMKKVV 543
Cdd:cd14053 159 GDTHgQVGTRRYMAPEVLEGAINFTR-DAFLRIDMYAMGLVLWELLSRCSVHDGpVDEYQLPFEEEVGQHPTLEDMQECV 237
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 17136928 544 CIEKCRPNIPNRWHASDVLHNMAKVMKECWYPNPVARLTA 583
Cdd:cd14053 238 VHKKLRPQIRDEWRKHPGLAQLCETIEECWDHDAEARLSA 277
STKc_TGFbR2_like cd14055
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II ...
308-583 7.10e-99

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: 306.61  E-value: 7.10e-99
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136928 308 VIGKGRFGEVWRGRWRGEN------VAVKIFSSREECSWFREAEIYQTVMLRHENILGFIAADNKDNGTWTQLWLVTDYH 381
Cdd:cd14055   2 LVGKGRFAEVWKAKLKQNAsgqyetVAVKIFPYEEYASWKNEKDIFTDASLKHENILQFLTAEERGVGLDRQYWLITAYH 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136928 382 ENGSLFDYLTTHPVDTNTMLNMSLSIATGLAHLHMDIVGT-RGKPAIAHRDLKSKNILVKSNLSCAIGDLGLAVRHVEKN 460
Cdd:cd14055  82 ENGSLQDYLTRHILSWEDLCKMAGSLARGLAHLHSDRTPCgRPKIPIAHRDLKSSNILVKNDGTCVLADFGLALRLDPSL 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136928 461 DSVDIPSTHRVGTKRYMAPEVLDESMNDQHFDSYKRADVYAFGLILWEIARRCNMGMIYDEYQLPYYDVVQPDPSIEEMK 540
Cdd:cd14055 162 SVDELANSGQVGTARYMAPEALESRVNLEDLESFKQIDVYSMALVLWEMASRCEASGEVKPYELPFGSKVRERPCVESMK 241
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 17136928 541 KVVCIEKCRPNIPNRWHASDVLHNMAKVMKECWYPNPVARLTA 583
Cdd:cd14055 242 DLVLRDRGRPEIPDSWLTHQGMCVLCDTITECWDHDPEARLTA 284
STKc_BMPR2_AMHR2 cd14054
Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and ...
308-593 3.70e-88

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: 278.86  E-value: 3.70e-88
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136928 308 VIGKGRFGEVWRGRWRGENVAVKIFSSREECSWFREAEIYQTVMLRHENILGFIAADNKDNGT-WTQLWLVTDYHENGSL 386
Cdd:cd14054   2 LIGQGRYGTVWKGSLDERPVAVKVFPARHRQNFQNEKDIYELPLMEHSNILRFIGADERPTADgRMEYLLVLEYAPKGSL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136928 387 FDYLTTHPVDTNTMLNMSLSIATGLAHLHMDI-VGTRGKPAIAHRDLKSKNILVKSNLSCAIGDLGLAVR-------HVE 458
Cdd:cd14054  82 CSYLRENTLDWMSSCRMALSLTRGLAYLHTDLrRGDQYKPAIAHRDLNSRNVLVKADGSCVICDFGLAMVlrgsslvRGR 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136928 459 KNDSvDIPSTHRVGTKRYMAPEVLDESMNDQHFDSY-KRADVYAFGLILWEIARRCN---MGMIYDEYQLPYYDVVQPDP 534
Cdd:cd14054 162 PGAA-ENASISEVGTLRYMAPEVLEGAVNLRDCESAlKQVDVYALGLVLWEIAMRCSdlyPGESVPPYQMPYEAELGNHP 240
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17136928 535 SIEEMKKVVCIEKCRPNIPNRWhasDVLHNMAKVMKE----CWYPNPVARLTALRIKKTLASI 593
Cdd:cd14054 241 TFEDMQLLVSREKARPKFPDAW---KENSLAVRSLKEtiedCWDQDAEARLTALCVEERLAEL 300
STKc_ACVR2b cd14140
Catalytic domain of the Serine/Threonine Kinase, Activin Type IIB Receptor; STKs catalyze the ...
308-593 6.79e-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: 254.57  E-value: 6.79e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136928 308 VIGKGRFGEVWRGRWRGENVAVKIFSSREECSWFREAEIYQTVMLRHENILGFIAADNKDNGTWTQLWLVTDYHENGSLF 387
Cdd:cd14140   2 IKARGRFGCVWKAQLMNEYVAVKIFPIQDKQSWQSEREIFSTPGMKHENLLQFIAAEKRGSNLEMELWLITAFHDKGSLT 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136928 388 DYLTTHPVDTNTMLNMSLSIATGLAHLHMDIVGTRG---KPAIAHRDLKSKNILVKSNLSCAIGDLGLAVRHVEKNDSVD 464
Cdd:cd14140  82 DYLKGNIVSWNELCHIAETMARGLSYLHEDVPRCKGeghKPAIAHRDFKSKNVLLKNDLTAVLADFGLAVRFEPGKPPGD 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136928 465 ipsTH-RVGTKRYMAPEVLDESMNDQHfDSYKRADVYAFGLILWEIARRCNM--GMIyDEYQLPYYDVVQPDPSIEEMKK 541
Cdd:cd14140 162 ---THgQVGTRRYMAPEVLEGAINFQR-DSFLRIDMYAMGLVLWELVSRCKAadGPV-DEYMLPFEEEIGQHPSLEDLQE 236
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 17136928 542 VVCIEKCRPNIPNRWHASDVLHNMAKVMKECWYPNPVARLTALRIKKTLASI 593
Cdd:cd14140 237 VVVHKKMRPVFKDHWLKHPGLAQLCVTIEECWDHDAEARLSAGCVEERISQI 288
STKc_ACVR2a cd14141
Catalytic domain of the Serine/Threonine Kinase, Activin Type IIA Receptor; STKs catalyze the ...
308-583 1.01e-76

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: 248.80  E-value: 1.01e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136928 308 VIGKGRFGEVWRGRWRGENVAVKIFSSREECSWFREAEIYQTVMLRHENILGFIAADNKDNGTWTQLWLVTDYHENGSLF 387
Cdd:cd14141   2 IKARGRFGCVWKAQLLNEYVAVKIFPIQDKLSWQNEYEIYSLPGMKHENILQFIGAEKRGTNLDVDLWLITAFHEKGSLT 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136928 388 DYLTTHPVDTNTMLNMSLSIATGLAHLHMDIVGTRG--KPAIAHRDLKSKNILVKSNLSCAIGDLGLAVRHVEKNDSVDi 465
Cdd:cd14141  82 DYLKANVVSWNELCHIAQTMARGLAYLHEDIPGLKDghKPAIAHRDIKSKNVLLKNNLTACIADFGLALKFEAGKSAGD- 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136928 466 psTH-RVGTKRYMAPEVLDESMNDQHfDSYKRADVYAFGLILWEIARRCNM--GMIyDEYQLPYYDVVQPDPSIEEMKKV 542
Cdd:cd14141 161 --THgQVGTRRYMAPEVLEGAINFQR-DAFLRIDMYAMGLVLWELASRCTAsdGPV-DEYMLPFEEEVGQHPSLEDMQEV 236
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 17136928 543 VCIEKCRPNIPNRWHASDVLHNMAKVMKECWYPNPVARLTA 583
Cdd:cd14141 237 VVHKKKRPVLRECWQKHAGMAMLCETIEECWDHDAEARLSA 277
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
309-580 3.64e-63

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: 211.24  E-value: 3.64e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136928 309 IGKGRFGEVWRGRWRGENVAVKIFSSREECSWFREA---EIYQTVMLRHENILGFIAADNKDNgtwtQLWLVTDYHENGS 385
Cdd:cd13999   1 IGSGSFGEVYKGKWRGTDVAIKKLKVEDDNDELLKEfrrEVSILSKLRHPNIVQFIGACLSPP----PLCIVTEYMPGGS 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136928 386 LFDYLTT--HPVDTNTMLNMSLSIATGLAHLHmdivgtrgKPAIAHRDLKSKNILVKSNLSCAIGDLGLAVRHVEKNDSv 463
Cdd:cd13999  77 LYDLLHKkkIPLSWSLRLKIALDIARGMNYLH--------SPPIIHRDLKSLNILLDENFTVKIADFGLSRIKNSTTEK- 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136928 464 dipSTHRVGTKRYMAPEVLDESMNDQHfdsykrADVYAFGLILWEIARRcnmgmiydeyQLPYYDVvqpdpSIEEMKKVV 543
Cdd:cd13999 148 ---MTGVVGTPRWMAPEVLRGEPYTEK------ADVYSFGIVLWELLTG----------EVPFKEL-----SPIQIAAAV 203
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 17136928 544 CIEKCRPNIPNRWHasdvlHNMAKVMKECWYPNPVAR 580
Cdd:cd13999 204 VQKGLRPPIPPDCP-----PELSKLIKRCWNEDPEKR 235
Pkinase_Tyr pfam07714
Protein tyrosine kinase;
303-590 3.02e-45

Protein tyrosine kinase;


Pssm-ID: 311583  Cd Length: 258  Bit Score: 162.67  E-value: 3.02e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136928   303 VQLCHVIGKGRFGEVWRGRWRGEN------VAVKI----FSSREECSWFREAEIyqtvM--LRHENILGFIAADNKDNgt 370
Cdd:pfam07714   1 LTLGEKLGEGAFGEVYKGTLKGDGegtkikVAVKTlkegADEEEREDFLEEASI----MkkLSHPNIVRLLGVCTQGE-- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136928   371 wtQLWLVTDYHENGSLFDYLTTH--PVDTNTMLNMSLSIATGLAHLH-MDIVgtrgkpaiaHRDLKSKNILVKSNLSCAI 447
Cdd:pfam07714  75 --PLYIVTEYMPGGDLLDFLRKHkgKLTLPDLLQMALQIAKGMEYLEsKNFV---------HRDLAARNCLVTENLVVKI 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136928   448 GDLGLAvRHVEKNDSvdipSTHRVGTK---RYMAPEVLdesmNDQHFDSYkrADVYAFGLILWEIarrCNMGMIydeyql 524
Cdd:pfam07714 144 SDFGLS-RDIYDDDY----YRKRGGGKlpiKWMAPESL----KDGKFTSK--SDVWSFGVLLWEI---FTLGEQ------ 203
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17136928   525 PYYDVvqpdpSIEEMKKVVcIEKCRPNIP