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Conserved domains on  [gi|1770965938|ref|NP_001362533|]
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vitamin K-dependent protein C isoform 6 precursor [Homo sapiens]

Protein Classification

coagulation factor( domain architecture ID 10637862)

coagulation factor is a vitamin K-dependent protein S1 family serine peptidase, similar to human coagulation factor X that converts prothrombin to thrombin in the presence of factor Va, calcium and phospholipid during blood clotting

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 234-469 4.73e-92

Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad residues.


:

Pssm-ID: 238113 [Multi-domain]  Cd Length: 232  Bit Score: 279.16  E-value: 4.73e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770965938 234 IDGKMTRRGDSPWQVVLLDSKKKLACGAVLIHPSWVLTAAHCMDES--KKLLVRLGEYDLRRWEKWELDLDIKEVFVHPN 311
Cdd:cd00190     2 VGGSEAKIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCVYSSapSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHPN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770965938 312 YSKSTTDNDIALLHLAQPATLSQTIVPICLPDSGlaerELNQAGQETLVTGWGYHSSREkeakrNRTFVLNFIKIPVVPH 391
Cdd:cd00190    82 YNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSG----YNLPAGTTCTVSGWGRTSEGG-----PLPDVLQEVNVPIVSN 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770965938 392 NECSEVMS--NMVSENMLCAGILGDRQDACEGDSGGPMVASFHGTWFLVGLVSWGEGCGLLHNYGVYTKVSRYLDWIHGH 469
Cdd:cd00190   153 AECKRAYSygGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
GLA smart00069
Domain containing Gla (gamma-carboxyglutamate) residues; A hyaluronan-binding domain found in ...
 45-108 5.50e-26

Domain containing Gla (gamma-carboxyglutamate) residues; A hyaluronan-binding domain found in proteins associated with the extracellular matrix, cell adhesion and cell migration.


:

Pssm-ID: 214503  Cd Length: 65  Bit Score: 100.08  E-value: 5.50e-26
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1770965938   45 DSVFSSSERAHQVLRIRKRANSF-LEELRHSSLERECIEEICDFEEAKEIFQNVDDTLAFWSKHV 108
Cdd:smart00069   1 GSVFLSRQEANKVLRRQRRANAFlLEELRPGNLERECQEEICSLEEAREVFEDNEGTDEFYRRYY 65
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 161-196 1.69e-11

Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is found to be the target for a potent inhibitor of coagulation, TAK-442.


:

Pssm-ID: 464251 [Multi-domain]  Cd Length: 36  Bit Score: 58.79  E-value: 1.69e-11
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1770965938 161 CSLDNGGCTHYCLEEVGWRRCSCAPGYKLGDDLLQC 196
Cdd:pfam14670   1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 122-153 6.20e-08

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


:

Pssm-ID: 238011  Cd Length: 38  Bit Score: 48.40  E-value: 6.20e-08
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1770965938 122 CAS--LCCGHGTCIDGIGSFSCDCRSGWEGRFCQ 153
Cdd:cd00054     5 CASgnPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 234-469 4.73e-92

Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad residues.


Pssm-ID: 238113 [Multi-domain]  Cd Length: 232  Bit Score: 279.16  E-value: 4.73e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770965938 234 IDGKMTRRGDSPWQVVLLDSKKKLACGAVLIHPSWVLTAAHCMDES--KKLLVRLGEYDLRRWEKWELDLDIKEVFVHPN 311
Cdd:cd00190     2 VGGSEAKIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCVYSSapSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHPN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770965938 312 YSKSTTDNDIALLHLAQPATLSQTIVPICLPDSGlaerELNQAGQETLVTGWGYHSSREkeakrNRTFVLNFIKIPVVPH 391
Cdd:cd00190    82 YNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSG----YNLPAGTTCTVSGWGRTSEGG-----PLPDVLQEVNVPIVSN 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770965938 392 NECSEVMS--NMVSENMLCAGILGDRQDACEGDSGGPMVASFHGTWFLVGLVSWGEGCGLLHNYGVYTKVSRYLDWIHGH 469
Cdd:cd00190   153 AECKRAYSygGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 232-466 2.09e-86

Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. A few, however, are active as single chain molecules, and others are inactive due to substitutions of the catalytic triad residues.


Pssm-ID: 214473  Cd Length: 229  Bit Score: 264.54  E-value: 2.09e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770965938  232 RLIDGKMTRRGDSPWQVVLLDSKKKLACGAVLIHPSWVLTAAHCMDES--KKLLVRLGEYDLRRWEKWELdLDIKEVFVH 309
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGRHFCGGSLISPRWVLTAAHCVRGSdpSNIRVRLGSHDLSSGEEGQV-IKVSKVIIH 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770965938  310 PNYSKSTTDNDIALLHLAQPATLSQTIVPICLPDSGlaerELNQAGQETLVTGWGyhssREKEAKRNRTFVLNFIKIPVV 389
Cdd:smart00020  80 PNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSN----YNVPAGTTCTVSGWG----RTSEGAGSLPDTLQEVNVPIV 151

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1770965938  390 PHNECSEVMSNM--VSENMLCAGILGDRQDACEGDSGGPMVASfHGTWFLVGLVSWGEGCGLLHNYGVYTKVSRYLDWI 466
Cdd:smart00020 152 SNATCRRAYSGGgaITDNMLCAGGLEGGKDACQGDSGGPLVCN-DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
234-466 1.85e-81

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 251.59  E-value: 1.85e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770965938 234 IDGKMTRRGDSPWQVVLLDSKKKLACGAVLIHPSWVLTAAHCMDESKKLLVRLGEYDLRRWEKWELDLDIKEVFVHPNYS 313
Cdd:pfam00089   2 VGGDEAQPGSFPWQVSLQLSSGKHFCGGSLISENWVLTAAHCVSGASDVKVVLGAHNIVLREGGEQKFDVEKIIVHPNYN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770965938 314 KSTTDNDIALLHLAQPATLSQTIVPICLPDSGlaerELNQAGQETLVTGWGYHSSrekeakRNRTFVLNFIKIPVVPHNE 393
Cdd:pfam00089  82 PDTLDNDIALLKLESPVTLGDTVRPICLPDAS----SDLPVGTTCTVSGWGNTKT------LGPSDTLQEVTVPVVSRET 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1770965938 394 CSEVMSNMVSENMLCAGilGDRQDACEGDSGGPMVASFHgtwFLVGLVSWGEGCGLLHNYGVYTKVSRYLDWI 466
Cdd:pfam00089 152 CRSAYGGTVTDTMICAG--AGGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 225-471 5.47e-63

Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 205.27  E-value: 5.47e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770965938 225 QEDQVDPRLIDGKMTRRGDSPWQVVLLDSKKKLA--CGAVLIHPSWVLTAAHCMDES--KKLLVRLGEYDLRRWEKWELD 300
Cdd:COG5640    23 PAADAAPAIVGGTPATVGEYPWMVALQSSNGPSGqfCGGTLIAPRWVLTAAHCVDGDgpSDLRVVIGSTDLSTSGGTVVK 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770965938 301 ldIKEVFVHPNYSKSTTDNDIALLHLAQPATLSQtivPICLPDSGLAERelnqAGQETLVTGWGyhSSREKEAKRNRTfv 380
Cdd:COG5640   103 --VARIVVHPDYDPATPGNDIALLKLATPVPGVA---PAPLATSADAAA----PGTPATVAGWG--RTSEGPGSQSGT-- 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770965938 381 LNFIKIPVVPHNECSeVMSNMVSENMLCAGILGDRQDACEGDSGGPMVASFHGTWFLVGLVSWGEGCGLLHNYGVYTKVS 460
Cdd:COG5640   170 LRKADVPVVSDATCA-AYGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVS 248

                         250
                  ....*....|.
gi 1770965938 461 RYLDWIHGHIR 471
Cdd:COG5640   249 AYRDWIKSTAG 259
GLA smart00069
Domain containing Gla (gamma-carboxyglutamate) residues; A hyaluronan-binding domain found in ...
 45-108 5.50e-26

Domain containing Gla (gamma-carboxyglutamate) residues; A hyaluronan-binding domain found in proteins associated with the extracellular matrix, cell adhesion and cell migration.


Pssm-ID: 214503  Cd Length: 65  Bit Score: 100.08  E-value: 5.50e-26
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1770965938   45 DSVFSSSERAHQVLRIRKRANSF-LEELRHSSLERECIEEICDFEEAKEIFQNVDDTLAFWSKHV 108
Cdd:smart00069   1 GSVFLSRQEANKVLRRQRRANAFlLEELRPGNLERECQEEICSLEEAREVFEDNEGTDEFYRRYY 65
Gla pfam00594
Vitamin K-dependent carboxylation/gamma-carboxyglutamic (GLA) domain; This domain is ...
 68-108 1.65e-18

Vitamin K-dependent carboxylation/gamma-carboxyglutamic (GLA) domain; This domain is responsible for the high-affinity binding of calcium ions. This domain contains post-translational modifications of many glutamate residues by Vitamin K-dependent carboxylation to form gamma-carboxyglutamate (Gla).


Pssm-ID: 459861  Cd Length: 41  Bit Score: 78.73  E-value: 1.65e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1770965938  68 LEELRHSSLERECIEEICDFEEAKEIFQNVDDTLAFWSKHV 108
Cdd:pfam00594   1 LEELKPGNLERECYEEICSYEEAREIFEDDEKTMEFWKKYT 41
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 161-196 1.69e-11

Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is found to be the target for a potent inhibitor of coagulation, TAK-442.


Pssm-ID: 464251 [Multi-domain]  Cd Length: 36  Bit Score: 58.79  E-value: 1.69e-11
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1770965938 161 CSLDNGGCTHYCLEEVGWRRCSCAPGYKLGDDLLQC 196
Cdd:pfam14670   1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 122-153 6.20e-08

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 48.40  E-value: 6.20e-08
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1770965938 122 CAS--LCCGHGTCIDGIGSFSCDCRSGWEGRFCQ 153
Cdd:cd00054     5 CASgnPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
EGF_CA smart00179
Calcium-binding EGF-like domain;
122-153 1.00e-05

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 42.23  E-value: 1.00e-05
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1770965938  122 CAS--LCCGHGTCIDGIGSFSCDCRSGWE-GRFCQ 153
Cdd:smart00179   5 CASgnPCQNGGTCVNTVGSYRCECPPGYTdGRNCE 39
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 126-151 4.37e-03

EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very similar, but has 8 instead of 6 conserved cysteines. Includes some cytokine receptors. The EGF domain misses the N-terminus regions of the Ca2+ binding EGF domains (this is the main reason of discrepancy between swiss-prot domain start/end and Pfam). The family is hard to model due to many similar but different sub-types of EGF domains. Pfam certainly misses a number of EGF domains.


Pssm-ID: 394967  Cd Length: 31  Bit Score: 34.67  E-value: 4.37e-03
                          10        20
                  ....*....|....*....|....*.
gi 1770965938 126 CCGHGTCIDGIGSFSCDCRSGWEGRF 151
Cdd:pfam00008   6 CSNGGTCVDTPGGYTCICPEGYTGKR 31
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 234-469 4.73e-92

Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad residues.


Pssm-ID: 238113 [Multi-domain]  Cd Length: 232  Bit Score: 279.16  E-value: 4.73e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770965938 234 IDGKMTRRGDSPWQVVLLDSKKKLACGAVLIHPSWVLTAAHCMDES--KKLLVRLGEYDLRRWEKWELDLDIKEVFVHPN 311
Cdd:cd00190     2 VGGSEAKIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCVYSSapSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHPN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770965938 312 YSKSTTDNDIALLHLAQPATLSQTIVPICLPDSGlaerELNQAGQETLVTGWGYHSSREkeakrNRTFVLNFIKIPVVPH 391
Cdd:cd00190    82 YNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSG----YNLPAGTTCTVSGWGRTSEGG-----PLPDVLQEVNVPIVSN 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770965938 392 NECSEVMS--NMVSENMLCAGILGDRQDACEGDSGGPMVASFHGTWFLVGLVSWGEGCGLLHNYGVYTKVSRYLDWIHGH 469
Cdd:cd00190   153 AECKRAYSygGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 232-466 2.09e-86

Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. A few, however, are active as single chain molecules, and others are inactive due to substitutions of the catalytic triad residues.


Pssm-ID: 214473  Cd Length: 229  Bit Score: 264.54  E-value: 2.09e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770965938  232 RLIDGKMTRRGDSPWQVVLLDSKKKLACGAVLIHPSWVLTAAHCMDES--KKLLVRLGEYDLRRWEKWELdLDIKEVFVH 309
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGRHFCGGSLISPRWVLTAAHCVRGSdpSNIRVRLGSHDLSSGEEGQV-IKVSKVIIH 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770965938  310 PNYSKSTTDNDIALLHLAQPATLSQTIVPICLPDSGlaerELNQAGQETLVTGWGyhssREKEAKRNRTFVLNFIKIPVV 389
Cdd:smart00020  80 PNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSN----YNVPAGTTCTVSGWG----RTSEGAGSLPDTLQEVNVPIV 151

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1770965938  390 PHNECSEVMSNM--VSENMLCAGILGDRQDACEGDSGGPMVASfHGTWFLVGLVSWGEGCGLLHNYGVYTKVSRYLDWI 466
Cdd:smart00020 152 SNATCRRAYSGGgaITDNMLCAGGLEGGKDACQGDSGGPLVCN-DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
234-466 1.85e-81

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 251.59  E-value: 1.85e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770965938 234 IDGKMTRRGDSPWQVVLLDSKKKLACGAVLIHPSWVLTAAHCMDESKKLLVRLGEYDLRRWEKWELDLDIKEVFVHPNYS 313
Cdd:pfam00089   2 VGGDEAQPGSFPWQVSLQLSSGKHFCGGSLISENWVLTAAHCVSGASDVKVVLGAHNIVLREGGEQKFDVEKIIVHPNYN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770965938 314 KSTTDNDIALLHLAQPATLSQTIVPICLPDSGlaerELNQAGQETLVTGWGYHSSrekeakRNRTFVLNFIKIPVVPHNE 393
Cdd:pfam00089  82 PDTLDNDIALLKLESPVTLGDTVRPICLPDAS----SDLPVGTTCTVSGWGNTKT------LGPSDTLQEVTVPVVSRET 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1770965938 394 CSEVMSNMVSENMLCAGilGDRQDACEGDSGGPMVASFHgtwFLVGLVSWGEGCGLLHNYGVYTKVSRYLDWI 466
Cdd:pfam00089 152 CRSAYGGTVTDTMICAG--AGGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 225-471 5.47e-63

Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 205.27  E-value: 5.47e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770965938 225 QEDQVDPRLIDGKMTRRGDSPWQVVLLDSKKKLA--CGAVLIHPSWVLTAAHCMDES--KKLLVRLGEYDLRRWEKWELD 300
Cdd:COG5640    23 PAADAAPAIVGGTPATVGEYPWMVALQSSNGPSGqfCGGTLIAPRWVLTAAHCVDGDgpSDLRVVIGSTDLSTSGGTVVK 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770965938 301 ldIKEVFVHPNYSKSTTDNDIALLHLAQPATLSQtivPICLPDSGLAERelnqAGQETLVTGWGyhSSREKEAKRNRTfv 380
Cdd:COG5640   103 --VARIVVHPDYDPATPGNDIALLKLATPVPGVA---PAPLATSADAAA----PGTPATVAGWG--RTSEGPGSQSGT-- 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770965938 381 LNFIKIPVVPHNECSeVMSNMVSENMLCAGILGDRQDACEGDSGGPMVASFHGTWFLVGLVSWGEGCGLLHNYGVYTKVS 460
Cdd:COG5640   170 LRKADVPVVSDATCA-AYGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVS 248

                         250
                  ....*....|.
gi 1770965938 461 RYLDWIHGHIR 471
Cdd:COG5640   249 AYRDWIKSTAG 259
GLA smart00069
Domain containing Gla (gamma-carboxyglutamate) residues; A hyaluronan-binding domain found in ...
 45-108 5.50e-26

Domain containing Gla (gamma-carboxyglutamate) residues; A hyaluronan-binding domain found in proteins associated with the extracellular matrix, cell adhesion and cell migration.


Pssm-ID: 214503  Cd Length: 65  Bit Score: 100.08  E-value: 5.50e-26
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1770965938   45 DSVFSSSERAHQVLRIRKRANSF-LEELRHSSLERECIEEICDFEEAKEIFQNVDDTLAFWSKHV 108
Cdd:smart00069   1 GSVFLSRQEANKVLRRQRRANAFlLEELRPGNLERECQEEICSLEEAREVFEDNEGTDEFYRRYY 65
Gla pfam00594
Vitamin K-dependent carboxylation/gamma-carboxyglutamic (GLA) domain; This domain is ...
 68-108 1.65e-18

Vitamin K-dependent carboxylation/gamma-carboxyglutamic (GLA) domain; This domain is responsible for the high-affinity binding of calcium ions. This domain contains post-translational modifications of many glutamate residues by Vitamin K-dependent carboxylation to form gamma-carboxyglutamate (Gla).


Pssm-ID: 459861  Cd Length: 41  Bit Score: 78.73  E-value: 1.65e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1770965938  68 LEELRHSSLERECIEEICDFEEAKEIFQNVDDTLAFWSKHV 108
Cdd:pfam00594   1 LEELKPGNLERECYEEICSYEEAREIFEDDEKTMEFWKKYT 41
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
 259-456 4.61e-15

V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 73.56  E-value: 4.61e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770965938 259 CGAVLIHPSWVLTAAHCMDESK------KLLVRLGeYDLRRWEKWEldldIKEVFVHPNYSKSTTDN-DIALLHLAQPAT 331
Cdd:COG3591    14 CTGTLIGPNLVLTAGHCVYDGAgggwatNIVFVPG-YNGGPYGTAT----ATRFRVPPGWVASGDAGyDYALLRLDEPLG 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770965938 332 LSQTIVPICLPDSGLAERELNQAgqetlvtgwGYHSSREKEAKRNRTfvlnfikipvvphNECSEVMSNMVSenMLCagi 411
Cdd:COG3591    89 DTTGWLGLAFNDAPLAGEPVTII---------GYPGDRPKDLSLDCS-------------GRVTGVQGNRLS--YDC--- 141

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1770965938 412 lgdrqDACEGDSGGPMVASFHGTWFLVGLVSWGEGCGllHNYGVY 456
Cdd:COG3591   142 -----DTTGGSSGSPVLDDSDGGGRVVGVHSAGGADR--ANTGVR 179
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 161-196 1.69e-11

Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is found to be the target for a potent inhibitor of coagulation, TAK-442.


Pssm-ID: 464251 [Multi-domain]  Cd Length: 36  Bit Score: 58.79  E-value: 1.69e-11
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1770965938 161 CSLDNGGCTHYCLEEVGWRRCSCAPGYKLGDDLLQC 196
Cdd:pfam14670   1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 122-153 6.20e-08

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 48.40  E-value: 6.20e-08
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1770965938 122 CAS--LCCGHGTCIDGIGSFSCDCRSGWEGRFCQ 153
Cdd:cd00054     5 CASgnPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
EGF_CA smart00179
Calcium-binding EGF-like domain;
122-153 1.00e-05

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 42.23  E-value: 1.00e-05
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1770965938  122 CAS--LCCGHGTCIDGIGSFSCDCRSGWE-GRFCQ 153
Cdd:smart00179   5 CASgnPCQNGGTCVNTVGSYRCECPPGYTdGRNCE 39
EGF cd00053
Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large ...
 121-153 2.73e-04

Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large number of proteins, mostly animal; the list of proteins currently known to contain one or more copies of an EGF-like pattern is large and varied; the functional significance of EGF-like domains in what appear to be unrelated proteins is not yet clear; a common feature is that these repeats are found in the extracellular domain of membrane-bound proteins or in proteins known to be secreted (exception: prostaglandin G/H synthase); the domain includes six cysteine residues which have been shown to be involved in disulfide bonds; the main structure is a two-stranded beta-sheet followed by a loop to a C-terminal short two-stranded sheet; Subdomains between the conserved cysteines vary in length; the region between the 5th and 6th cysteine contains two conserved glycines of which at least one is present in most EGF-like domains; a subset of these bind calcium.


Pssm-ID: 238010  Cd Length: 36  Bit Score: 38.23  E-value: 2.73e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1770965938 121 PCA--SLCCGHGTCIDGIGSFSCDCRSGWEG-RFCQ 153
Cdd:cd00053     1 ECAasNPCSNGGTCVNTPGSYRCVCPPGYTGdRSCE 36
EGF smart00181
Epidermal growth factor-like domain;
121-153 4.17e-04

Epidermal growth factor-like domain;


Pssm-ID: 214544  Cd Length: 35  Bit Score: 37.88  E-value: 4.17e-04
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1770965938  121 PCASLC-CGHGTCIDGIGSFSCDCRSGWEG-RFCQ 153
Cdd:smart00181   1 ECASGGpCSNGTCINTPGSYTCSCPPGYTGdKRCE 35
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 126-151 4.37e-03

EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very similar, but has 8 instead of 6 conserved cysteines. Includes some cytokine receptors. The EGF domain misses the N-terminus regions of the Ca2+ binding EGF domains (this is the main reason of discrepancy between swiss-prot domain start/end and Pfam). The family is hard to model due to many similar but different sub-types of EGF domains. Pfam certainly misses a number of EGF domains.


Pssm-ID: 394967  Cd Length: 31  Bit Score: 34.67  E-value: 4.37e-03
                          10        20
                  ....*....|....*....|....*.
gi 1770965938 126 CCGHGTCIDGIGSFSCDCRSGWEGRF 151
Cdd:pfam00008   6 CSNGGTCVDTPGGYTCICPEGYTGKR 31
hEGF pfam12661
Human growth factor-like EGF; hEGF, or human growth factor-like EGF, domains have six ...
 126-147 5.28e-03

Human growth factor-like EGF; hEGF, or human growth factor-like EGF, domains have six conserved residues disulfide-bonded into the characteriztic 'ababcc' pattern. They are involved in growth and proliferation of cells, in proteins of the Notch/Delta pathway, neurogulin and selectins. hEGFs are also found in mosaic proteins with four-disulfide laminin EGFs such as aggrecan and perlecan. The core fold of the EGF domain consists of two small beta-hairpins packed against each other. Two major structural variants have been identified based on the structural context of the C-terminal Cys residue of disulfide 'c' in the C-terminal hairpin: hEGFs and cEGFs. In hEGFs the C-terminal thiol resides in the beta-turn, resulting in shorter loop-lengths between the Cys residues of disulfide 'c', typically C[8-9]XC. These shorter loop-lengths are also typical of the four-disulfide EGF domains, laminin ad integrin. Tandem hEGF domains have six linking residues between terminal cysteines of adjacent domains. hEGF domains may or may not bind calcium in the linker region. hEGF domains with the consensus motif CXD4X[F,Y]XCXC are hydroxylated exclusively in the Asp residue.


Pssm-ID: 463660  Cd Length: 22  Bit Score: 34.23  E-value: 5.28e-03
                          10        20
                  ....*....|....*....|..
gi 1770965938 126 CCGHGTCIDGIGSFSCDCRSGW 147
Cdd:pfam12661   1 CQNGGTCVDGVNGYKCQCPPGY 22
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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