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Conserved domains on  [gi|6981412|ref|NP_036935|]
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vitamin K-dependent protein C precursor [Rattus norvegicus]

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 ...
 213-447 4.55e-89

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: 271.07  E-value: 4.55e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981412  213 IVNGTLTKQGDSPWQAILLDSKKKLACGGVLIHTSWVLTAAHCLESS--KKLTVRLGEYDLRRRDPWELDLDIKEVLVHP 290
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCVYSSapSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981412  291 NYTRSNSDNDIALLRLSQPATLSKTIVPICLPNSGlaqELSQAGQETVVTGWGYQSDKVkdgrrNRTFILTFIRIPLAAR 370
Cdd:cd00190  81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSG---YNLPAGTTCTVSGWGRTSEGG-----PLPDVLQEVNVPIVSN 152

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6981412  371 NDCMQVM--NNVVSENMLCAGIIGDTRDACDGDSGGPMVVFFRGTWFLVGLVSWGEGCGHLNNYGVYTKVGSYLKWIHS 447
Cdd:cd00190 153 AECKRAYsyGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQK 231
GLA smart00069
Domain containing Gla (gamma-carboxyglutamate) residues; A hyaluronan-binding domain found in ...
 26-86 5.35e-24

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: 94.68  E-value: 5.35e-24
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6981412      26 VFSSSEGAHQVL-RVRRANSF-LEEVRAGSLERECMEEICDFEEAQEIFQNVEDTLAFWIKYF 86
Cdd:smart00069   3 VFLSRQEANKVLrRQRRANAFlLEELRPGNLERECQEEICSLEEAREVFEDNEGTDEFYRRYY 65
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 139-174 3.46e-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: 3.46e-09
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 6981412    139 CRVKNGGCYHYCLEETRGRRCRCAPGYELADDHMHC 174
Cdd:pfam14670   1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 87-131 5.60e-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: 5.60e-08
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 6981412   87 DGDQCSTPpldhqcdSPCCGHGTCIDGLGGFSCSCDKGWEGRFCQ 131
Cdd:cd00054   1 DIDECASG-------NPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 213-447 4.55e-89

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: 271.07  E-value: 4.55e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981412  213 IVNGTLTKQGDSPWQAILLDSKKKLACGGVLIHTSWVLTAAHCLESS--KKLTVRLGEYDLRRRDPWELDLDIKEVLVHP 290
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCVYSSapSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981412  291 NYTRSNSDNDIALLRLSQPATLSKTIVPICLPNSGlaqELSQAGQETVVTGWGYQSDKVkdgrrNRTFILTFIRIPLAAR 370
Cdd:cd00190  81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSG---YNLPAGTTCTVSGWGRTSEGG-----PLPDVLQEVNVPIVSN 152

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6981412  371 NDCMQVM--NNVVSENMLCAGIIGDTRDACDGDSGGPMVVFFRGTWFLVGLVSWGEGCGHLNNYGVYTKVGSYLKWIHS 447
Cdd:cd00190 153 AECKRAYsyGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQK 231
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 212-445 2.65e-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: 258.76  E-value: 2.65e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981412     212 RIVNGTLTKQGDSPWQAILLDSKKKLACGGVLIHTSWVLTAAHCLESS--KKLTVRLGEYDLRRRDPWELdLDIKEVLVH 289
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGRHFCGGSLISPRWVLTAAHCVRGSdpSNIRVRLGSHDLSSGEEGQV-IKVSKVIIH 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981412     290 PNYTRSNSDNDIALLRLSQPATLSKTIVPICLPNSGlaqELSQAGQETVVTGWGYqsdkVKDGRRNRTFILTFIRIPLAA 369
Cdd:smart00020  80 PNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSN---YNVPAGTTCTVSGWGR----TSEGAGSLPDTLQEVNVPIVS 152

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6981412     370 RNDCMQVM--NNVVSENMLCAGIIGDTRDACDGDSGGPMVVfFRGTWFLVGLVSWGEGCGHLNNYGVYTKVGSYLKWI 445
Cdd:smart00020 153 NATCRRAYsgGGAITDNMLCAGGLEGGKDACQGDSGGPLVC-NDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
213-445 2.21e-75

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 235.41  E-value: 2.21e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981412    213 IVNGTLTKQGDSPWQAILLDSKKKLACGGVLIHTSWVLTAAHCLESSKKLTVRLGEYDLRRRDPWELDLDIKEVLVHPNY 292
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGKHFCGGSLISENWVLTAAHCVSGASDVKVVLGAHNIVLREGGEQKFDVEKIIVHPNY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981412    293 TRSNSDNDIALLRLSQPATLSKTIVPICLPNSGlaqELSQAGQETVVTGWGYQsdkvkdGRRNRTFILTFIRIPLAARND 372
Cdd:pfam00089  81 NPDTLDNDIALLKLESPVTLGDTVRPICLPDAS---SDLPVGTTCTVSGWGNT------KTLGPSDTLQEVTVPVVSRET 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6981412    373 CMQVMNNVVSENMLCAGIIGdtRDACDGDSGGPMVvffRGTWFLVGLVSWGEGCGHLNNYGVYTKVGSYLKWI 445
Cdd:pfam00089 152 CRSAYGGTVTDTMICAGAGG--KDACQGDSGGPLV---CSDGELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 210-451 6.10e-67

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 215.28  E-value: 6.10e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981412  210 GPRIVNGTLTKQGDSPWQAILLDSKKKLA--CGGVLIHTSWVLTAAHCLE--SSKKLTVRLGEYDLRRRDPWELDldIKE 285
Cdd:COG5640  28 APAIVGGTPATVGEYPWMVALQSSNGPSGqfCGGTLIAPRWVLTAAHCVDgdGPSDLRVVIGSTDLSTSGGTVVK--VAR 105

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981412  286 VLVHPNYTRSNSDNDIALLRLSQPATLSKtivPICLPNSGLAqelSQAGQETVVTGWGYQSDKvkDGRRNRTfiLTFIRI 365
Cdd:COG5640 106 IVVHPDYDPATPGNDIALLKLATPVPGVA---PAPLATSADA---AAPGTPATVAGWGRTSEG--PGSQSGT--LRKADV 175

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981412  366 PLAARNDCmQVMNNVVSENMLCAGIIGDTRDACDGDSGGPMVVFFRGTWFLVGLVSWGEGCGHLNNYGVYTKVGSYLKWI 445
Cdd:COG5640 176 PVVSDATC-AAYGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWI 254


                ....*.
gi 6981412  446 HSYIGE 451
Cdd:COG5640 255 KSTAGG 260
GLA smart00069
Domain containing Gla (gamma-carboxyglutamate) residues; A hyaluronan-binding domain found in ...
 26-86 5.35e-24

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: 94.68  E-value: 5.35e-24
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6981412      26 VFSSSEGAHQVL-RVRRANSF-LEEVRAGSLERECMEEICDFEEAQEIFQNVEDTLAFWIKYF 86
Cdd:smart00069   3 VFLSRQEANKVLrRQRRANAFlLEELRPGNLERECQEEICSLEEAREVFEDNEGTDEFYRRYY 65
Gla pfam00594
Vitamin K-dependent carboxylation/gamma-carboxyglutamic (GLA) domain; This domain is ...
 46-85 2.02e-21

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: 86.82  E-value: 2.02e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 6981412     46 LEEVRAGSLERECMEEICDFEEAQEIFQNVEDTLAFWIKY 85
Cdd:pfam00594   1 LEELKPGNLERECYEEICSYEEAREIFEDDEKTMEFWKKY 40
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 139-174 3.46e-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: 3.46e-09
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 6981412    139 CRVKNGGCYHYCLEETRGRRCRCAPGYELADDHMHC 174
Cdd:pfam14670   1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 87-131 5.60e-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: 5.60e-08
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 6981412   87 DGDQCSTPpldhqcdSPCCGHGTCIDGLGGFSCSCDKGWEGRFCQ 131
Cdd:cd00054   1 DIDECASG-------NPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
EGF_CA smart00179
Calcium-binding EGF-like domain;
87-131 8.02e-06

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 42.62  E-value: 8.02e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 6981412      87 DGDQCSTPpldhqcdSPCCGHGTCIDGLGGFSCSCDKGWE-GRFCQ 131
Cdd:smart00179   1 DIDECASG-------NPCQNGGTCVNTVGSYRCECPPGYTdGRNCE 39
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 100-129 2.46e-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: 38.13  E-value: 2.46e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 6981412    100 CDS-PCCGHGTCIDGLGGFSCSCDKGWEGRF 129
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 ...
 213-447 4.55e-89

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: 271.07  E-value: 4.55e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981412  213 IVNGTLTKQGDSPWQAILLDSKKKLACGGVLIHTSWVLTAAHCLESS--KKLTVRLGEYDLRRRDPWELDLDIKEVLVHP 290
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCVYSSapSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981412  291 NYTRSNSDNDIALLRLSQPATLSKTIVPICLPNSGlaqELSQAGQETVVTGWGYQSDKVkdgrrNRTFILTFIRIPLAAR 370
Cdd:cd00190  81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSG---YNLPAGTTCTVSGWGRTSEGG-----PLPDVLQEVNVPIVSN 152

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6981412  371 NDCMQVM--NNVVSENMLCAGIIGDTRDACDGDSGGPMVVFFRGTWFLVGLVSWGEGCGHLNNYGVYTKVGSYLKWIHS 447
Cdd:cd00190 153 AECKRAYsyGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQK 231
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 212-445 2.65e-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: 258.76  E-value: 2.65e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981412     212 RIVNGTLTKQGDSPWQAILLDSKKKLACGGVLIHTSWVLTAAHCLESS--KKLTVRLGEYDLRRRDPWELdLDIKEVLVH 289
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGRHFCGGSLISPRWVLTAAHCVRGSdpSNIRVRLGSHDLSSGEEGQV-IKVSKVIIH 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981412     290 PNYTRSNSDNDIALLRLSQPATLSKTIVPICLPNSGlaqELSQAGQETVVTGWGYqsdkVKDGRRNRTFILTFIRIPLAA 369
Cdd:smart00020  80 PNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSN---YNVPAGTTCTVSGWGR----TSEGAGSLPDTLQEVNVPIVS 152

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6981412     370 RNDCMQVM--NNVVSENMLCAGIIGDTRDACDGDSGGPMVVfFRGTWFLVGLVSWGEGCGHLNNYGVYTKVGSYLKWI 445
Cdd:smart00020 153 NATCRRAYsgGGAITDNMLCAGGLEGGKDACQGDSGGPLVC-NDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
213-445 2.21e-75

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 235.41  E-value: 2.21e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981412    213 IVNGTLTKQGDSPWQAILLDSKKKLACGGVLIHTSWVLTAAHCLESSKKLTVRLGEYDLRRRDPWELDLDIKEVLVHPNY 292
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGKHFCGGSLISENWVLTAAHCVSGASDVKVVLGAHNIVLREGGEQKFDVEKIIVHPNY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981412    293 TRSNSDNDIALLRLSQPATLSKTIVPICLPNSGlaqELSQAGQETVVTGWGYQsdkvkdGRRNRTFILTFIRIPLAARND 372
Cdd:pfam00089  81 NPDTLDNDIALLKLESPVTLGDTVRPICLPDAS---SDLPVGTTCTVSGWGNT------KTLGPSDTLQEVTVPVVSRET 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6981412    373 CMQVMNNVVSENMLCAGIIGdtRDACDGDSGGPMVvffRGTWFLVGLVSWGEGCGHLNNYGVYTKVGSYLKWI 445
Cdd:pfam00089 152 CRSAYGGTVTDTMICAGAGG--KDACQGDSGGPLV---CSDGELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 210-451 6.10e-67

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 215.28  E-value: 6.10e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981412  210 GPRIVNGTLTKQGDSPWQAILLDSKKKLA--CGGVLIHTSWVLTAAHCLE--SSKKLTVRLGEYDLRRRDPWELDldIKE 285
Cdd:COG5640  28 APAIVGGTPATVGEYPWMVALQSSNGPSGqfCGGTLIAPRWVLTAAHCVDgdGPSDLRVVIGSTDLSTSGGTVVK--VAR 105

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981412  286 VLVHPNYTRSNSDNDIALLRLSQPATLSKtivPICLPNSGLAqelSQAGQETVVTGWGYQSDKvkDGRRNRTfiLTFIRI 365
Cdd:COG5640 106 IVVHPDYDPATPGNDIALLKLATPVPGVA---PAPLATSADA---AAPGTPATVAGWGRTSEG--PGSQSGT--LRKADV 175

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981412  366 PLAARNDCmQVMNNVVSENMLCAGIIGDTRDACDGDSGGPMVVFFRGTWFLVGLVSWGEGCGHLNNYGVYTKVGSYLKWI 445
Cdd:COG5640 176 PVVSDATC-AAYGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWI 254


                ....*.
gi 6981412  446 HSYIGE 451
Cdd:COG5640 255 KSTAGG 260
GLA smart00069
Domain containing Gla (gamma-carboxyglutamate) residues; A hyaluronan-binding domain found in ...
 26-86 5.35e-24

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: 94.68  E-value: 5.35e-24
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6981412      26 VFSSSEGAHQVL-RVRRANSF-LEEVRAGSLERECMEEICDFEEAQEIFQNVEDTLAFWIKYF 86
Cdd:smart00069   3 VFLSRQEANKVLrRQRRANAFlLEELRPGNLERECQEEICSLEEAREVFEDNEGTDEFYRRYY 65
Gla pfam00594
Vitamin K-dependent carboxylation/gamma-carboxyglutamic (GLA) domain; This domain is ...
 46-85 2.02e-21

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: 86.82  E-value: 2.02e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 6981412     46 LEEVRAGSLERECMEEICDFEEAQEIFQNVEDTLAFWIKY 85
Cdd:pfam00594   1 LEELKPGNLERECYEEICSYEEAREIFEDDEKTMEFWKKY 40
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
 239-435 1.74e-15

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 74.71  E-value: 1.74e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981412  239 CGGVLIHTSWVLTAAHCLESSK------KLTVRLGeydlRRRDPWElDLDIKEVLVHPNYTRS-NSDNDIALLRLSQPAT 311
Cdd:COG3591  14 CTGTLIGPNLVLTAGHCVYDGAgggwatNIVFVPG----YNGGPYG-TATATRFRVPPGWVASgDAGYDYALLRLDEPLG 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981412  312 LSKTIVPIclpnsgLAQELSQAGQETVVTGwgYQSDKVKDgrrnrtfiltfiripLAARNDCmqvmnNVVSENmlcAGII 391
Cdd:COG3591  89 DTTGWLGL------AFNDAPLAGEPVTIIG--YPGDRPKD---------------LSLDCSG-----RVTGVQ---GNRL 137

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 6981412  392 GDTRDACDGDSGGPMVVFFRGTWFLVGLVSWGEgcGHLNNYGVY 435
Cdd:COG3591 138 SYDCDTTGGSSGSPVLDDSDGGGRVVGVHSAGG--ADRANTGVR 179
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 139-174 3.46e-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: 3.46e-09
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 6981412    139 CRVKNGGCYHYCLEETRGRRCRCAPGYELADDHMHC 174
Cdd:pfam14670   1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 87-131 5.60e-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: 5.60e-08
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 6981412   87 DGDQCSTPpldhqcdSPCCGHGTCIDGLGGFSCSCDKGWEGRFCQ 131
Cdd:cd00054   1 DIDECASG-------NPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
EGF_CA smart00179
Calcium-binding EGF-like domain;
87-131 8.02e-06

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 42.62  E-value: 8.02e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 6981412      87 DGDQCSTPpldhqcdSPCCGHGTCIDGLGGFSCSCDKGWE-GRFCQ 131
Cdd:smart00179   1 DIDECASG-------NPCQNGGTCVNTVGSYRCECPPGYTdGRNCE 39
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 100-129 2.46e-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: 38.13  E-value: 2.46e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 6981412    100 CDS-PCCGHGTCIDGLGGFSCSCDKGWEGRF 129
Cdd:pfam00008   1 CAPnPCSNGGTCVDTPGGYTCICPEGYTGKR 31
EGF cd00053
Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large ...
 102-131 4.27e-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: 4.27e-04
                        10        20        30
                ....*....|....*....|....*....|.
gi 6981412  102 SPCCGHGTCIDGLGGFSCSCDKGWEG-RFCQ 131
Cdd:cd00053   6 NPCSNGGTCVNTPGSYRCVCPPGYTGdRSCE 36
EGF smart00181
Epidermal growth factor-like domain;
105-131 1.14e-03

Epidermal growth factor-like domain;


Pssm-ID: 214544  Cd Length: 35  Bit Score: 36.34  E-value: 1.14e-03
                           10        20
                   ....*....|....*....|....*...
gi 6981412     105 CGHGTCIDGLGGFSCSCDKGWEG-RFCQ 131
Cdd:smart00181   8 CSNGTCINTPGSYTCSCPPGYTGdKRCE 35
Trypsin_2 pfam13365
Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.
 241-311 8.91e-03

Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.


Pssm-ID: 433149 [Multi-domain]  Cd Length: 142  Bit Score: 36.63  E-value: 8.91e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6981412    241 GVLI-HTSWVLTAAHCLESSKKLTVRLGEYDLRRRDPWELDLdikevlvhpnyTRSNSDNDIALLRLSQPAT 311
Cdd:pfam13365   3 GFVVsSDGLVLTNAHVVDDAEEAAVELVSVVLADGREYPATV-----------VARDPDLDLALLRVSGDGR 63
 
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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