NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|10518503|ref|NP_062562|]
View 

coagulation factor VII isoform b 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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 191-427 5.31e-91

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: 5.31e-91
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10518503 191 IVGGKVCPKGECPWQVLLLVN-GAQLCGGTLINTIWVVSAAHCFDKiKNWRNLIAVLGEHDLSEHDGDEQSRRVAQVIIP 269
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYS-SAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVH 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10518503 270 STYVPGTTNHDIALLRLHQPVVLTDHVVPLCLPErtfSERTLAFVRFSLVSGWGQLLDRGATALELMVLNVPRLMTQDCL 349
Cdd:cd00190  80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPS---SGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECK 156

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 10518503 350 QQSRKvgdSPNITEYMFCAGYSDGSKDSCKGDSGGPHATHYRGTWYLTGIVSWGQGCATVGHFGVYTRVSQYIEWLQK 427
Cdd:cd00190 157 RAYSY---GGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQK 231
GLA smart00069
Domain containing Gla (gamma-carboxyglutamate) residues; A hyaluronan-binding domain found in ...
 21-82 9.65e-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: 104.70  E-value: 9.65e-28
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 10518503     21 AVFVTQEEAHGVLHRRRRANAF-LEELRPGSLERECKEEQCSFEEAREIFKDAERTKLFWISY 82
Cdd:smart00069   2 SVFLSRQEANKVLRRQRRANAFlLEELRPGNLERECQEEICSLEEAREVFEDNEGTDEFYRRY 64
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 129-165 5.77e-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: 51.47  E-value: 5.77e-09
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 10518503   129 CVNENGGCEQYCSDhTGTKRSCRCHEGYSLLADGVSC 165
Cdd:pfam14670   1 CSVNNGGCSHLCLN-TPGGYTCSCPEGYELQDDGRTC 36
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 84-120 5.83e-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: 5.83e-08
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 10518503  84 DGDQCAS-SPCQNGGSCKDQLQSYICFCLPAFEGRNCE 120
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 ...
 191-427 5.31e-91

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: 5.31e-91
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10518503 191 IVGGKVCPKGECPWQVLLLVN-GAQLCGGTLINTIWVVSAAHCFDKiKNWRNLIAVLGEHDLSEHDGDEQSRRVAQVIIP 269
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYS-SAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVH 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10518503 270 STYVPGTTNHDIALLRLHQPVVLTDHVVPLCLPErtfSERTLAFVRFSLVSGWGQLLDRGATALELMVLNVPRLMTQDCL 349
Cdd:cd00190  80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPS---SGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECK 156

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 10518503 350 QQSRKvgdSPNITEYMFCAGYSDGSKDSCKGDSGGPHATHYRGTWYLTGIVSWGQGCATVGHFGVYTRVSQYIEWLQK 427
Cdd:cd00190 157 RAYSY---GGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQK 231
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 190-424 9.12e-85

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: 9.12e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10518503    190 RIVGGKVCPKGECPWQVLLLVNG-AQLCGGTLINTIWVVSAAHCFDKiKNWRNLIAVLGEHDLSEhDGDEQSRRVAQVII 268
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVRG-SDPSNIRVRLGSHDLSS-GEEGQVIKVSKVII 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10518503    269 PSTYVPGTTNHDIALLRLHQPVVLTDHVVPLCLPErtfSERTLAFVRFSLVSGWGQL-LDRGATALELMVLNVPRLMTQD 347
Cdd:smart00020  79 HPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPS---SNYNVPAGTTCTVSGWGRTsEGAGSLPDTLQEVNVPIVSNAT 155

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 10518503    348 ClqqSRKVGDSPNITEYMFCAGYSDGSKDSCKGDSGGPHATHyRGTWYLTGIVSWGQGCATVGHFGVYTRVSQYIEW 424
Cdd:smart00020 156 C---RRAYSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVCN-DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDW 228
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 184-433 2.19e-59

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 194.87  E-value: 2.19e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10518503 184 ASKPQGRIVGGKVCPKGECPWQVLLLVNG---AQLCGGTLINTIWVVSAAHCFDKIKNwRNLIAVLGEHDLSEHDGdeQS 260
Cdd:COG5640  24 AADAAPAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDGP-SDLRVVIGSTDLSTSGG--TV 100

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10518503 261 RRVAQVIIPSTYVPGTTNHDIALLRLHQPVvltDHVVPLCLPERTFSERTLAFVRfslVSGWGQLL-DRGATALELMVLN 339
Cdd:COG5640 101 VKVARIVVHPDYDPATPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPAT---VAGWGRTSeGPGSQSGTLRKAD 174

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10518503 340 VPRLMTQDCLQQSRkvgdspNITEYMFCAGYSDGSKDSCKGDSGGPHATHYRGTWYLTGIVSWGQG-CATvGHFGVYTRV 418
Cdd:COG5640 175 VPVVSDATCAAYGG------FDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGpCAA-GYPGVYTRV 247

                       250
                ....*....|....*
gi 10518503 419 SQYIEWLQKLMRSEP 433
Cdd:COG5640 248 SAYRDWIKSTAGGLG 262
Trypsin pfam00089
Trypsin;
191-425 5.45e-59

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 192.66  E-value: 5.45e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10518503   191 IVGGKVCPKGECPWQVLLLV-NGAQLCGGTLINTIWVVSAAHCFDKIKNWRnliAVLGEHDLSEHDGDEQSRRVAQVIIP 269
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLsSGKHFCGGSLISENWVLTAAHCVSGASDVK---VVLGAHNIVLREGGEQKFDVEKIIVH 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10518503   270 STYVPGTTNHDIALLRLHQPVVLTDHVVPLCLPE--RTFSERTLAFvrfslVSGWGQLLDRGaTALELMVLNVPRLMTQD 347
Cdd:pfam00089  78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDasSDLPVGTTCT-----VSGWGNTKTLG-PSDTLQEVTVPVVSRET 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 10518503   348 CLQQSRkvgdsPNITEYMFCAGYsdGSKDSCKGDSGGPHATHYRgtwYLTGIVSWGQGCATVGHFGVYTRVSQYIEWL 425
Cdd:pfam00089 152 CRSAYG-----GTVTDTMICAGA--GGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
GLA smart00069
Domain containing Gla (gamma-carboxyglutamate) residues; A hyaluronan-binding domain found in ...
 21-82 9.65e-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: 104.70  E-value: 9.65e-28
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 10518503     21 AVFVTQEEAHGVLHRRRRANAF-LEELRPGSLERECKEEQCSFEEAREIFKDAERTKLFWISY 82
Cdd:smart00069   2 SVFLSRQEANKVLRRQRRANAFlLEELRPGNLERECQEEICSLEEAREVFEDNEGTDEFYRRY 64
Gla pfam00594
Vitamin K-dependent carboxylation/gamma-carboxyglutamic (GLA) domain; This domain is ...
 43-83 2.82e-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: 89.13  E-value: 2.82e-22
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 10518503    43 LEELRPGSLERECKEEQCSFEEAREIFKDAERTKLFWISYS 83
Cdd:pfam00594   1 LEELKPGNLERECYEEICSYEEAREIFEDDEKTMEFWKKYT 41
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 129-165 5.77e-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: 51.47  E-value: 5.77e-09
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 10518503   129 CVNENGGCEQYCSDhTGTKRSCRCHEGYSLLADGVSC 165
Cdd:pfam14670   1 CSVNNGGCSHLCLN-TPGGYTCSCPEGYELQDDGRTC 36
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 84-120 5.83e-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: 5.83e-08
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 10518503  84 DGDQCAS-SPCQNGGSCKDQLQSYICFCLPAFEGRNCE 120
Cdd:cd00054   1 DIDECASgNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
EGF_CA smart00179
Calcium-binding EGF-like domain;
84-120 1.29e-05

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 41.85  E-value: 1.29e-05
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 10518503     84 DGDQCAS-SPCQNGGSCKDQLQSYICFCLPAFE-GRNCE 120
Cdd:smart00179   1 DIDECASgNPCQNGGTCVNTVGSYRCECPPGYTdGRNCE 39
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 88-118 6.73e-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: 6.73e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 10518503    88 CASSPCQNGGSCKDQLQSYICFCLPAFEGRN 118
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 ...
 191-427 5.31e-91

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: 5.31e-91
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10518503 191 IVGGKVCPKGECPWQVLLLVN-GAQLCGGTLINTIWVVSAAHCFDKiKNWRNLIAVLGEHDLSEHDGDEQSRRVAQVIIP 269
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYS-SAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVH 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10518503 270 STYVPGTTNHDIALLRLHQPVVLTDHVVPLCLPErtfSERTLAFVRFSLVSGWGQLLDRGATALELMVLNVPRLMTQDCL 349
Cdd:cd00190  80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPS---SGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECK 156

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 10518503 350 QQSRKvgdSPNITEYMFCAGYSDGSKDSCKGDSGGPHATHYRGTWYLTGIVSWGQGCATVGHFGVYTRVSQYIEWLQK 427
Cdd:cd00190 157 RAYSY---GGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQK 231
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 190-424 9.12e-85

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: 9.12e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10518503    190 RIVGGKVCPKGECPWQVLLLVNG-AQLCGGTLINTIWVVSAAHCFDKiKNWRNLIAVLGEHDLSEhDGDEQSRRVAQVII 268
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVRG-SDPSNIRVRLGSHDLSS-GEEGQVIKVSKVII 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10518503    269 PSTYVPGTTNHDIALLRLHQPVVLTDHVVPLCLPErtfSERTLAFVRFSLVSGWGQL-LDRGATALELMVLNVPRLMTQD 347
Cdd:smart00020  79 HPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPS---SNYNVPAGTTCTVSGWGRTsEGAGSLPDTLQEVNVPIVSNAT 155

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 10518503    348 ClqqSRKVGDSPNITEYMFCAGYSDGSKDSCKGDSGGPHATHyRGTWYLTGIVSWGQGCATVGHFGVYTRVSQYIEW 424
Cdd:smart00020 156 C---RRAYSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVCN-DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDW 228
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 184-433 2.19e-59

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 194.87  E-value: 2.19e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10518503 184 ASKPQGRIVGGKVCPKGECPWQVLLLVNG---AQLCGGTLINTIWVVSAAHCFDKIKNwRNLIAVLGEHDLSEHDGdeQS 260
Cdd:COG5640  24 AADAAPAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDGP-SDLRVVIGSTDLSTSGG--TV 100

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10518503 261 RRVAQVIIPSTYVPGTTNHDIALLRLHQPVvltDHVVPLCLPERTFSERTLAFVRfslVSGWGQLL-DRGATALELMVLN 339
Cdd:COG5640 101 VKVARIVVHPDYDPATPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPAT---VAGWGRTSeGPGSQSGTLRKAD 174

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10518503 340 VPRLMTQDCLQQSRkvgdspNITEYMFCAGYSDGSKDSCKGDSGGPHATHYRGTWYLTGIVSWGQG-CATvGHFGVYTRV 418
Cdd:COG5640 175 VPVVSDATCAAYGG------FDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGpCAA-GYPGVYTRV 247

                       250
                ....*....|....*
gi 10518503 419 SQYIEWLQKLMRSEP 433
Cdd:COG5640 248 SAYRDWIKSTAGGLG 262
Trypsin pfam00089
Trypsin;
191-425 5.45e-59

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 192.66  E-value: 5.45e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10518503   191 IVGGKVCPKGECPWQVLLLV-NGAQLCGGTLINTIWVVSAAHCFDKIKNWRnliAVLGEHDLSEHDGDEQSRRVAQVIIP 269
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLsSGKHFCGGSLISENWVLTAAHCVSGASDVK---VVLGAHNIVLREGGEQKFDVEKIIVH 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10518503   270 STYVPGTTNHDIALLRLHQPVVLTDHVVPLCLPE--RTFSERTLAFvrfslVSGWGQLLDRGaTALELMVLNVPRLMTQD 347
Cdd:pfam00089  78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDasSDLPVGTTCT-----VSGWGNTKTLG-PSDTLQEVTVPVVSRET 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 10518503   348 CLQQSRkvgdsPNITEYMFCAGYsdGSKDSCKGDSGGPHATHYRgtwYLTGIVSWGQGCATVGHFGVYTRVSQYIEWL 425
Cdd:pfam00089 152 CRSAYG-----GTVTDTMICAGA--GGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
GLA smart00069
Domain containing Gla (gamma-carboxyglutamate) residues; A hyaluronan-binding domain found in ...
 21-82 9.65e-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: 104.70  E-value: 9.65e-28
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 10518503     21 AVFVTQEEAHGVLHRRRRANAF-LEELRPGSLERECKEEQCSFEEAREIFKDAERTKLFWISY 82
Cdd:smart00069   2 SVFLSRQEANKVLRRQRRANAFlLEELRPGNLERECQEEICSLEEAREVFEDNEGTDEFYRRY 64
Gla pfam00594
Vitamin K-dependent carboxylation/gamma-carboxyglutamic (GLA) domain; This domain is ...
 43-83 2.82e-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: 89.13  E-value: 2.82e-22
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 10518503    43 LEELRPGSLERECKEEQCSFEEAREIFKDAERTKLFWISYS 83
Cdd:pfam00594   1 LEELKPGNLERECYEEICSYEEAREIFEDDEKTMEFWKKYT 41
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
 207-431 3.87e-10

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 58.92  E-value: 3.87e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10518503 207 LLLVNGAQLCGGTLINTIWVVSAAHCF---DKIKNWRNLIAVLGehdlsEHDGDEQSRRVAQVIIPSTYVP-GTTNHDIA 282
Cdd:COG3591   5 LETDGGGGVCTGTLIGPNLVLTAGHCVydgAGGGWATNIVFVPG-----YNGGPYGTATATRFRVPPGWVAsGDAGYDYA 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10518503 283 LLRLHQPVVLTDHVVPLCLPERTFSERTLAfvrfslVSGWGQllDRGATAlelmvlnvprlmtqdCLQQSRKVGDSPNIT 362
Cdd:COG3591  80 LLRLDEPLGDTTGWLGLAFNDAPLAGEPVT------IIGYPG--DRPKDL---------------SLDCSGRVTGVQGNR 136

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 10518503 363 EYMFCagysdgskDSCKGDSGGPHATHYRGTWYLTGIVSWGQgcATVGHFGVYTRvSQYIEWLQKLMRS 431
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 ...
 129-165 5.77e-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: 51.47  E-value: 5.77e-09
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 10518503   129 CVNENGGCEQYCSDhTGTKRSCRCHEGYSLLADGVSC 165
Cdd:pfam14670   1 CSVNNGGCSHLCLN-TPGGYTCSCPEGYELQDDGRTC 36
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 84-120 5.83e-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: 5.83e-08
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 10518503  84 DGDQCAS-SPCQNGGSCKDQLQSYICFCLPAFEGRNCE 120
Cdd:cd00054   1 DIDECASgNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
EGF_CA smart00179
Calcium-binding EGF-like domain;
84-120 1.29e-05

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 41.85  E-value: 1.29e-05
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 10518503     84 DGDQCAS-SPCQNGGSCKDQLQSYICFCLPAFE-GRNCE 120
Cdd:smart00179   1 DIDECASgNPCQNGGTCVNTVGSYRCECPPGYTdGRNCE 39
DUF1986 pfam09342
Domain of unknown function (DUF1986); This domain is found in serine proteases and is ...
 202-303 2.86e-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: 2.86e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10518503   202 CPWQVLLLVNGAQLCGGTLINTIWVVSAAHCFDKIKNWRNLIAVL---GEHDLSEHDGDEQSRRVAQViipsTYVPGTtn 278
Cdd:pfam09342   1 WPWIAKVYLDGNMICSGVLIDASWVIVSGSCLRDTNLRHQYISVVlggAKTLKSIEGPYEQIVRVDCR----HDIPES-- 74

                          90       100
                  ....*....|....*....|....*
gi 10518503   279 hDIALLRLHQPVVLTDHVVPLCLPE 303
Cdd:pfam09342  75 -EISLLHLASPASFSNHVLPTFVPE 98
EGF cd00053
Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large ...
 89-120 4.76e-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: 37.46  E-value: 4.76e-04
                        10        20        30
                ....*....|....*....|....*....|...
gi 10518503  89 ASSPCQNGGSCKDQLQSYICFCLPAFEG-RNCE 120
Cdd:cd00053   4 ASNPCSNGGTCVNTPGSYRCVCPPGYTGdRSCE 36
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 88-118 6.73e-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: 6.73e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 10518503    88 CASSPCQNGGSCKDQLQSYICFCLPAFEGRN 118
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH