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Conserved domains on  [gi|182257999|gb|ACB87203|]
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factor VII [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 ...
 213-449 1.16e-90

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: 275.31  E-value: 1.16e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182257999 213 IVGGKVCPKGECPWQVLLLVN-GAQLCGGTLINTIWVVSAAHCFDKiKNWRNLIAVLGEHDLSEHDGDEQSRRVAQVIIP 291
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYS-SAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVH 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182257999 292 STYVPGTTNHDIALLRLHQPVVLTDHVVPLCLPErtfSERTLAFVRFSLVSGWGQLLDRGATALELMVLNVPRLMTQDCL 371
Cdd:cd00190   80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPS---SGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECK 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 182257999 372 QQSRKvgdSPNITEYMFCAGYSDGSKDSCKGDSGGPHATHYRGTWYLTGIVSWGQGCATVGHFGVYTRVSQYIEWLQK 449
Cdd:cd00190  157 RAYSY---GGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQK 231
GLA smart00069
Domain containing Gla (gamma-carboxyglutamate) residues; A hyaluronan-binding domain found in ...
 42-104 2.47e-28

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: 106.63  E-value: 2.47e-28
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 182257999    42 HRVFVTQEEAHGVLHRRRRANAF-LEELRPGSLERECKEEQCSFEEAREIFKDAERTKLFWISY 104
Cdd:smart00069   1 GSVFLSRQEANKVLRRQRRANAFlLEELRPGNLERECQEEICSLEEAREVFEDNEGTDEFYRRY 64
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 151-187 4.34e-09

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: 51.86  E-value: 4.34e-09
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 182257999  151 CVNENGGCEQYCSDhTGTKRSCRCHEGYSLLADGVSC 187
Cdd:pfam14670   1 CSVNNGGCSHLCLN-TPGGYTCSCPEGYELQDDGRTC 36
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 106-142 4.39e-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: 48.79  E-value: 4.39e-08
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 182257999 106 DGDQCAS-SPCQNGGSCKDQLQSYICFCLPAFEGRNCE 142
Cdd:cd00054    1 DIDECASgNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 213-449 1.16e-90

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: 275.31  E-value: 1.16e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182257999 213 IVGGKVCPKGECPWQVLLLVN-GAQLCGGTLINTIWVVSAAHCFDKiKNWRNLIAVLGEHDLSEHDGDEQSRRVAQVIIP 291
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYS-SAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVH 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182257999 292 STYVPGTTNHDIALLRLHQPVVLTDHVVPLCLPErtfSERTLAFVRFSLVSGWGQLLDRGATALELMVLNVPRLMTQDCL 371
Cdd:cd00190   80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPS---SGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECK 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 182257999 372 QQSRKvgdSPNITEYMFCAGYSDGSKDSCKGDSGGPHATHYRGTWYLTGIVSWGQGCATVGHFGVYTRVSQYIEWLQK 449
Cdd:cd00190  157 RAYSY---GGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQK 231
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 212-446 1.97e-84

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: 259.15  E-value: 1.97e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182257999   212 RIVGGKVCPKGECPWQVLLLVNG-AQLCGGTLINTIWVVSAAHCFDKiKNWRNLIAVLGEHDLSEhDGDEQSRRVAQVII 290
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVRG-SDPSNIRVRLGSHDLSS-GEEGQVIKVSKVII 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182257999   291 PSTYVPGTTNHDIALLRLHQPVVLTDHVVPLCLPErtfSERTLAFVRFSLVSGWGQL-LDRGATALELMVLNVPRLMTQD 369
Cdd:smart00020  79 HPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPS---SNYNVPAGTTCTVSGWGRTsEGAGSLPDTLQEVNVPIVSNAT 155

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 182257999   370 ClqqSRKVGDSPNITEYMFCAGYSDGSKDSCKGDSGGPHATHyRGTWYLTGIVSWGQGCATVGHFGVYTRVSQYIEW 446
Cdd:smart00020 156 C---RRAYSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVCN-DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDW 228
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 206-455 1.26e-58

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 193.71  E-value: 1.26e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182257999 206 ASKPQGRIVGGKVCPKGECPWQVLLLVNG---AQLCGGTLINTIWVVSAAHCFDKIKNwRNLIAVLGEHDLSEHDGdeQS 282
Cdd:COG5640   24 AADAAPAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDGP-SDLRVVIGSTDLSTSGG--TV 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182257999 283 RRVAQVIIPSTYVPGTTNHDIALLRLHQPVvltDHVVPLCLPERTFSERTLAFVRfslVSGWGQLL-DRGATALELMVLN 361
Cdd:COG5640  101 VKVARIVVHPDYDPATPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPAT---VAGWGRTSeGPGSQSGTLRKAD 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182257999 362 VPRLMTQDCLQQSRkvgdspNITEYMFCAGYSDGSKDSCKGDSGGPHATHYRGTWYLTGIVSWGQG-CATvGHFGVYTRV 440
Cdd:COG5640  175 VPVVSDATCAAYGG------FDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGpCAA-GYPGVYTRV 247

                        250
                 ....*....|....*
gi 182257999 441 SQYIEWLQKLMRSEP 455
Cdd:COG5640  248 SAYRDWIKSTAGGLG 262
Trypsin pfam00089
Trypsin;
213-447 1.62e-58

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 191.89  E-value: 1.62e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182257999  213 IVGGKVCPKGECPWQVLLLV-NGAQLCGGTLINTIWVVSAAHCFDKIKNWRnliAVLGEHDLSEHDGDEQSRRVAQVIIP 291
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLsSGKHFCGGSLISENWVLTAAHCVSGASDVK---VVLGAHNIVLREGGEQKFDVEKIIVH 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182257999  292 STYVPGTTNHDIALLRLHQPVVLTDHVVPLCLPE--RTFSERTLAFvrfslVSGWGQLLDRGaTALELMVLNVPRLMTQD 369
Cdd:pfam00089  78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDasSDLPVGTTCT-----VSGWGNTKTLG-PSDTLQEVTVPVVSRET 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 182257999  370 CLQQSRkvgdsPNITEYMFCAGYsdGSKDSCKGDSGGPHATHYRgtwYLTGIVSWGQGCATVGHFGVYTRVSQYIEWL 447
Cdd:pfam00089 152 CRSAYG-----GTVTDTMICAGA--GGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
GLA smart00069
Domain containing Gla (gamma-carboxyglutamate) residues; A hyaluronan-binding domain found in ...
 42-104 2.47e-28

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: 106.63  E-value: 2.47e-28
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 182257999    42 HRVFVTQEEAHGVLHRRRRANAF-LEELRPGSLERECKEEQCSFEEAREIFKDAERTKLFWISY 104
Cdd:smart00069   1 GSVFLSRQEANKVLRRQRRANAFlLEELRPGNLERECQEEICSLEEAREVFEDNEGTDEFYRRY 64
Gla pfam00594
Vitamin K-dependent carboxylation/gamma-carboxyglutamic (GLA) domain; This domain is ...
 65-105 1.89e-22

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: 89.51  E-value: 1.89e-22
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 182257999   65 LEELRPGSLERECKEEQCSFEEAREIFKDAERTKLFWISYS 105
Cdd:pfam00594   1 LEELKPGNLERECYEEICSYEEAREIFEDDEKTMEFWKKYT 41
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 151-187 4.34e-09

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: 51.86  E-value: 4.34e-09
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 182257999  151 CVNENGGCEQYCSDhTGTKRSCRCHEGYSLLADGVSC 187
Cdd:pfam14670   1 CSVNNGGCSHLCLN-TPGGYTCSCPEGYELQDDGRTC 36
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 106-142 4.39e-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: 48.79  E-value: 4.39e-08
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 182257999 106 DGDQCAS-SPCQNGGSCKDQLQSYICFCLPAFEGRNCE 142
Cdd:cd00054    1 DIDECASgNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
EGF_CA smart00179
Calcium-binding EGF-like domain;
106-142 9.77e-06

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 42.23  E-value: 9.77e-06
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 182257999   106 DGDQCAS-SPCQNGGSCKDQLQSYICFCLPAFE-GRNCE 142
Cdd:smart00179   1 DIDECASgNPCQNGGTCVNTVGSYRCECPPGYTdGRNCE 39
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 110-140 5.91e-04

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: 36.98  E-value: 5.91e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 182257999  110 CASSPCQNGGSCKDQLQSYICFCLPAFEGRN 140
Cdd:pfam00008   1 CAPNPCSNGGTCVDTPGGYTCICPEGYTGKR 31
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 213-449 1.16e-90

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: 275.31  E-value: 1.16e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182257999 213 IVGGKVCPKGECPWQVLLLVN-GAQLCGGTLINTIWVVSAAHCFDKiKNWRNLIAVLGEHDLSEHDGDEQSRRVAQVIIP 291
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYS-SAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVH 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182257999 292 STYVPGTTNHDIALLRLHQPVVLTDHVVPLCLPErtfSERTLAFVRFSLVSGWGQLLDRGATALELMVLNVPRLMTQDCL 371
Cdd:cd00190   80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPS---SGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECK 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 182257999 372 QQSRKvgdSPNITEYMFCAGYSDGSKDSCKGDSGGPHATHYRGTWYLTGIVSWGQGCATVGHFGVYTRVSQYIEWLQK 449
Cdd:cd00190  157 RAYSY---GGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQK 231
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 212-446 1.97e-84

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: 259.15  E-value: 1.97e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182257999   212 RIVGGKVCPKGECPWQVLLLVNG-AQLCGGTLINTIWVVSAAHCFDKiKNWRNLIAVLGEHDLSEhDGDEQSRRVAQVII 290
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVRG-SDPSNIRVRLGSHDLSS-GEEGQVIKVSKVII 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182257999   291 PSTYVPGTTNHDIALLRLHQPVVLTDHVVPLCLPErtfSERTLAFVRFSLVSGWGQL-LDRGATALELMVLNVPRLMTQD 369
Cdd:smart00020  79 HPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPS---SNYNVPAGTTCTVSGWGRTsEGAGSLPDTLQEVNVPIVSNAT 155

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 182257999   370 ClqqSRKVGDSPNITEYMFCAGYSDGSKDSCKGDSGGPHATHyRGTWYLTGIVSWGQGCATVGHFGVYTRVSQYIEW 446
Cdd:smart00020 156 C---RRAYSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVCN-DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDW 228
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 206-455 1.26e-58

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 193.71  E-value: 1.26e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182257999 206 ASKPQGRIVGGKVCPKGECPWQVLLLVNG---AQLCGGTLINTIWVVSAAHCFDKIKNwRNLIAVLGEHDLSEHDGdeQS 282
Cdd:COG5640   24 AADAAPAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDGP-SDLRVVIGSTDLSTSGG--TV 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182257999 283 RRVAQVIIPSTYVPGTTNHDIALLRLHQPVvltDHVVPLCLPERTFSERTLAFVRfslVSGWGQLL-DRGATALELMVLN 361
Cdd:COG5640  101 VKVARIVVHPDYDPATPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPAT---VAGWGRTSeGPGSQSGTLRKAD 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182257999 362 VPRLMTQDCLQQSRkvgdspNITEYMFCAGYSDGSKDSCKGDSGGPHATHYRGTWYLTGIVSWGQG-CATvGHFGVYTRV 440
Cdd:COG5640  175 VPVVSDATCAAYGG------FDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGpCAA-GYPGVYTRV 247

                        250
                 ....*....|....*
gi 182257999 441 SQYIEWLQKLMRSEP 455
Cdd:COG5640  248 SAYRDWIKSTAGGLG 262
Trypsin pfam00089
Trypsin;
213-447 1.62e-58

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 191.89  E-value: 1.62e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182257999  213 IVGGKVCPKGECPWQVLLLV-NGAQLCGGTLINTIWVVSAAHCFDKIKNWRnliAVLGEHDLSEHDGDEQSRRVAQVIIP 291
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLsSGKHFCGGSLISENWVLTAAHCVSGASDVK---VVLGAHNIVLREGGEQKFDVEKIIVH 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182257999  292 STYVPGTTNHDIALLRLHQPVVLTDHVVPLCLPE--RTFSERTLAFvrfslVSGWGQLLDRGaTALELMVLNVPRLMTQD 369
Cdd:pfam00089  78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDasSDLPVGTTCT-----VSGWGNTKTLG-PSDTLQEVTVPVVSRET 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 182257999  370 CLQQSRkvgdsPNITEYMFCAGYsdGSKDSCKGDSGGPHATHYRgtwYLTGIVSWGQGCATVGHFGVYTRVSQYIEWL 447
Cdd:pfam00089 152 CRSAYG-----GTVTDTMICAGA--GGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
GLA smart00069
Domain containing Gla (gamma-carboxyglutamate) residues; A hyaluronan-binding domain found in ...
 42-104 2.47e-28

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: 106.63  E-value: 2.47e-28
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 182257999    42 HRVFVTQEEAHGVLHRRRRANAF-LEELRPGSLERECKEEQCSFEEAREIFKDAERTKLFWISY 104
Cdd:smart00069   1 GSVFLSRQEANKVLRRQRRANAFlLEELRPGNLERECQEEICSLEEAREVFEDNEGTDEFYRRY 64
Gla pfam00594
Vitamin K-dependent carboxylation/gamma-carboxyglutamic (GLA) domain; This domain is ...
 65-105 1.89e-22

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: 89.51  E-value: 1.89e-22
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 182257999   65 LEELRPGSLERECKEEQCSFEEAREIFKDAERTKLFWISYS 105
Cdd:pfam00594   1 LEELKPGNLERECYEEICSYEEAREIFEDDEKTMEFWKKYT 41
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
 229-453 6.39e-10

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 58.53  E-value: 6.39e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182257999 229 LLLVNGAQLCGGTLINTIWVVSAAHCF---DKIKNWRNLIAVLGehdlsEHDGDEQSRRVAQVIIPSTYVP-GTTNHDIA 304
Cdd:COG3591    5 LETDGGGGVCTGTLIGPNLVLTAGHCVydgAGGGWATNIVFVPG-----YNGGPYGTATATRFRVPPGWVAsGDAGYDYA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182257999 305 LLRLHQPVVLTDHVVPLCLPERTFSERTLAfvrfslVSGWGQllDRGATAlelmvlnvprlmtqdCLQQSRKVGDSPNIT 384
Cdd:COG3591   80 LLRLDEPLGDTTGWLGLAFNDAPLAGEPVT------IIGYPG--DRPKDL---------------SLDCSGRVTGVQGNR 136

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 182257999 385 EYMFCagysdgskDSCKGDSGGPHATHYRGTWYLTGIVSWGQgcATVGHFGVYTRvSQYIEWLQKLMRS 453
Cdd:COG3591  137 LSYDC--------DTTGGSSGSPVLDDSDGGGRVVGVHSAGG--ADRANTGVRLT-SAIVAALRAWASA 194
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 151-187 4.34e-09

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: 51.86  E-value: 4.34e-09
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 182257999  151 CVNENGGCEQYCSDhTGTKRSCRCHEGYSLLADGVSC 187
Cdd:pfam14670   1 CSVNNGGCSHLCLN-TPGGYTCSCPEGYELQDDGRTC 36
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 106-142 4.39e-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: 48.79  E-value: 4.39e-08
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 182257999 106 DGDQCAS-SPCQNGGSCKDQLQSYICFCLPAFEGRNCE 142
Cdd:cd00054    1 DIDECASgNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
EGF_CA smart00179
Calcium-binding EGF-like domain;
106-142 9.77e-06

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 42.23  E-value: 9.77e-06
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 182257999   106 DGDQCAS-SPCQNGGSCKDQLQSYICFCLPAFE-GRNCE 142
Cdd:smart00179   1 DIDECASgNPCQNGGTCVNTVGSYRCECPPGYTdGRNCE 39
DUF1986 pfam09342
Domain of unknown function (DUF1986); This domain is found in serine proteases and is ...
 224-325 2.85e-05

Domain of unknown function (DUF1986); This domain is found in serine proteases and is predicted to contain disulphide bonds.


Pssm-ID: 286432  Cd Length: 116  Bit Score: 43.31  E-value: 2.85e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182257999  224 CPWQVLLLVNGAQLCGGTLINTIWVVSAAHCFDKIKNWRNLIAVL---GEHDLSEHDGDEQSRRVAQViipsTYVPGTtn 300
Cdd:pfam09342   1 WPWIAKVYLDGNMICSGVLIDASWVIVSGSCLRDTNLRHQYISVVlggAKTLKSIEGPYEQIVRVDCR----HDIPES-- 74

                          90       100
                  ....*....|....*....|....*
gi 182257999  301 hDIALLRLHQPVVLTDHVVPLCLPE 325
Cdd:pfam09342  75 -EISLLHLASPASFSNHVLPTFVPE 98
EGF cd00053
Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large ...
 111-142 3.76e-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: 37.84  E-value: 3.76e-04
                         10        20        30
                 ....*....|....*....|....*....|...
gi 182257999 111 ASSPCQNGGSCKDQLQSYICFCLPAFEG-RNCE 142
Cdd:cd00053    4 ASNPCSNGGTCVNTPGSYRCVCPPGYTGdRSCE 36
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 110-140 5.91e-04

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: 36.98  E-value: 5.91e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 182257999  110 CASSPCQNGGSCKDQLQSYICFCLPAFEGRN 140
Cdd:pfam00008   1 CAPNPCSNGGTCVDTPGGYTCICPEGYTGKR 31
 
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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