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Conserved domains on  [gi|332814313|ref|XP_515775|]
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vitamin K-dependent protein C isoform X7 [Pan troglodytes]

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 ...
 213-448 1.93e-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: 279.55  E-value: 1.93e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332814313 213 IDGKMTRRGDSPWQVVLLDSKKKLACGAVLIHPSWVLTAAHCMDES--KKLLVRLGEYDLRRWEKWELDLDIKEVFVHPN 290
Cdd:cd00190    2 VGGSEAKIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCVYSSapSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHPN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332814313 291 YSKSTTDNDIALLHLAQPATLSQTIVPICLPDSGlaerELNQAGQETLVTGWGYHSSREkeakrNRTFVLNFIKIPVVPH 370
Cdd:cd00190   82 YNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSG----YNLPAGTTCTVSGWGRTSEGG-----PLPDVLQEVNVPIVSN 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332814313 371 NECSEVMS--NMVSENMLCAGILGDRQDACEGDSGGPMVASFHGTWFLVGLVSWGEGCGLLHNYGVYTKVSRYLDWIHGH 448
Cdd:cd00190  153 AECKRAYSygGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
GLA smart00069
Domain containing Gla (gamma-carboxyglutamate) residues; A hyaluronan-binding domain found in ...
 24-87 4.70e-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: 4.70e-26
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 332814313    24 DSVFSSSERAHQVLRIRKRANSF-LEELRHSSLERECIEEICDFEEAKEIFQNVDDTLAFWSKHV 87
Cdd:smart00069   1 GSVFLSRQEANKVLRRQRRANAFlLEELRPGNLERECQEEICSLEEAREVFEDNEGTDEFYRRYY 65
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 140-175 1.13e-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: 59.18  E-value: 1.13e-11
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 332814313  140 CSLDNGGCTHYCLEEVGWRRCSCAPGYKLGDDLLQC 175
Cdd:pfam14670   1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 101-132 4.65e-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: 4.65e-08
                         10        20        30
                 ....*....|....*....|....*....|....
gi 332814313 101 CAS--LCCGHGTCIDGIGSFSCDCRSGWEGRFCQ 132
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 ...
 213-448 1.93e-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: 279.55  E-value: 1.93e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332814313 213 IDGKMTRRGDSPWQVVLLDSKKKLACGAVLIHPSWVLTAAHCMDES--KKLLVRLGEYDLRRWEKWELDLDIKEVFVHPN 290
Cdd:cd00190    2 VGGSEAKIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCVYSSapSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHPN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332814313 291 YSKSTTDNDIALLHLAQPATLSQTIVPICLPDSGlaerELNQAGQETLVTGWGYHSSREkeakrNRTFVLNFIKIPVVPH 370
Cdd:cd00190   82 YNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSG----YNLPAGTTCTVSGWGRTSEGG-----PLPDVLQEVNVPIVSN 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332814313 371 NECSEVMS--NMVSENMLCAGILGDRQDACEGDSGGPMVASFHGTWFLVGLVSWGEGCGLLHNYGVYTKVSRYLDWIHGH 448
Cdd:cd00190  153 AECKRAYSygGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 211-445 6.86e-87

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: 265.31  E-value: 6.86e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332814313   211 RLIDGKMTRRGDSPWQVVLLDSKKKLACGAVLIHPSWVLTAAHCMDES--KKLLVRLGEYDLRRWEKWELdLDIKEVFVH 288
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGRHFCGGSLISPRWVLTAAHCVRGSdpSNIRVRLGSHDLSSGEEGQV-IKVSKVIIH 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332814313   289 PNYSKSTTDNDIALLHLAQPATLSQTIVPICLPDSGlaerELNQAGQETLVTGWGyhssREKEAKRNRTFVLNFIKIPVV 368
Cdd:smart00020  80 PNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSN----YNVPAGTTCTVSGWG----RTSEGAGSLPDTLQEVNVPIV 151

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 332814313   369 PHNECSEVMSNM--VSENMLCAGILGDRQDACEGDSGGPMVASfHGTWFLVGLVSWGEGCGLLHNYGVYTKVSRYLDWI 445
Cdd:smart00020 152 SNATCRRAYSGGgaITDNMLCAGGLEGGKDACQGDSGGPLVCN-DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
213-445 5.67e-82

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 252.36  E-value: 5.67e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332814313  213 IDGKMTRRGDSPWQVVLLDSKKKLACGAVLIHPSWVLTAAHCMDESKKLLVRLGEYDLRRWEKWELDLDIKEVFVHPNYS 292
Cdd:pfam00089   2 VGGDEAQPGSFPWQVSLQLSSGKHFCGGSLISENWVLTAAHCVSGASDVKVVLGAHNIVLREGGEQKFDVEKIIVHPNYN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332814313  293 KSTTDNDIALLHLAQPATLSQTIVPICLPDSGlaerELNQAGQETLVTGWGYHSSrekeakRNRTFVLNFIKIPVVPHNE 372
Cdd:pfam00089  82 PDTLDNDIALLKLESPVTLGDTVRPICLPDAS----SDLPVGTTCTVSGWGNTKT------LGPSDTLQEVTVPVVSRET 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 332814313  373 CSEVMSNMVSENMLCAGilGDRQDACEGDSGGPMVASFHgtwFLVGLVSWGEGCGLLHNYGVYTKVSRYLDWI 445
Cdd:pfam00089 152 CRSAYGGTVTDTMICAG--AGGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 204-450 2.11e-63

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 206.04  E-value: 2.11e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332814313 204 QEDQVDPRLIDGKMTRRGDSPWQVVLLDSKKKLA--CGAVLIHPSWVLTAAHCMDES--KKLLVRLGEYDLRRWEKWELD 279
Cdd:COG5640   23 PAADAAPAIVGGTPATVGEYPWMVALQSSNGPSGqfCGGTLIAPRWVLTAAHCVDGDgpSDLRVVIGSTDLSTSGGTVVK 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332814313 280 ldIKEVFVHPNYSKSTTDNDIALLHLAQPATLSQtivPICLPDSGLAERelnqAGQETLVTGWGyhSSREKEAKRNRTfv 359
Cdd:COG5640  103 --VARIVVHPDYDPATPGNDIALLKLATPVPGVA---PAPLATSADAAA----PGTPATVAGWG--RTSEGPGSQSGT-- 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332814313 360 LNFIKIPVVPHNECSeVMSNMVSENMLCAGILGDRQDACEGDSGGPMVASFHGTWFLVGLVSWGEGCGLLHNYGVYTKVS 439
Cdd:COG5640  170 LRKADVPVVSDATCA-AYGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVS 248

                        250
                 ....*....|.
gi 332814313 440 RYLDWIHGHIR 450
Cdd:COG5640  249 AYRDWIKSTAG 259
GLA smart00069
Domain containing Gla (gamma-carboxyglutamate) residues; A hyaluronan-binding domain found in ...
 24-87 4.70e-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: 4.70e-26
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 332814313    24 DSVFSSSERAHQVLRIRKRANSF-LEELRHSSLERECIEEICDFEEAKEIFQNVDDTLAFWSKHV 87
Cdd:smart00069   1 GSVFLSRQEANKVLRRQRRANAFlLEELRPGNLERECQEEICSLEEAREVFEDNEGTDEFYRRYY 65
Gla pfam00594
Vitamin K-dependent carboxylation/gamma-carboxyglutamic (GLA) domain; This domain is ...
 47-87 2.18e-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: 78.34  E-value: 2.18e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 332814313   47 LEELRHSSLERECIEEICDFEEAKEIFQNVDDTLAFWSKHV 87
Cdd:pfam00594   1 LEELKPGNLERECYEEICSYEEAREIFEDDEKTMEFWKKYT 41
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 140-175 1.13e-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: 59.18  E-value: 1.13e-11
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 332814313  140 CSLDNGGCTHYCLEEVGWRRCSCAPGYKLGDDLLQC 175
Cdd:pfam14670   1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 101-132 4.65e-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: 4.65e-08
                         10        20        30
                 ....*....|....*....|....*....|....
gi 332814313 101 CAS--LCCGHGTCIDGIGSFSCDCRSGWEGRFCQ 132
Cdd:cd00054    5 CASgnPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
EGF_CA smart00179
Calcium-binding EGF-like domain;
101-132 8.42e-06

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 42.62  E-value: 8.42e-06
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 332814313   101 CAS--LCCGHGTCIDGIGSFSCDCRSGWE-GRFCQ 132
Cdd:smart00179   5 CASgnPCQNGGTCVNTVGSYRCECPPGYTdGRNCE 39
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 101-130 3.40e-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: 35.05  E-value: 3.40e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 332814313  101 CASL-CCGHGTCIDGIGSFSCDCRSGWEGRF 130
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 ...
 213-448 1.93e-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: 279.55  E-value: 1.93e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332814313 213 IDGKMTRRGDSPWQVVLLDSKKKLACGAVLIHPSWVLTAAHCMDES--KKLLVRLGEYDLRRWEKWELDLDIKEVFVHPN 290
Cdd:cd00190    2 VGGSEAKIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCVYSSapSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHPN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332814313 291 YSKSTTDNDIALLHLAQPATLSQTIVPICLPDSGlaerELNQAGQETLVTGWGYHSSREkeakrNRTFVLNFIKIPVVPH 370
Cdd:cd00190   82 YNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSG----YNLPAGTTCTVSGWGRTSEGG-----PLPDVLQEVNVPIVSN 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332814313 371 NECSEVMS--NMVSENMLCAGILGDRQDACEGDSGGPMVASFHGTWFLVGLVSWGEGCGLLHNYGVYTKVSRYLDWIHGH 448
Cdd:cd00190  153 AECKRAYSygGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 211-445 6.86e-87

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: 265.31  E-value: 6.86e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332814313   211 RLIDGKMTRRGDSPWQVVLLDSKKKLACGAVLIHPSWVLTAAHCMDES--KKLLVRLGEYDLRRWEKWELdLDIKEVFVH 288
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGRHFCGGSLISPRWVLTAAHCVRGSdpSNIRVRLGSHDLSSGEEGQV-IKVSKVIIH 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332814313   289 PNYSKSTTDNDIALLHLAQPATLSQTIVPICLPDSGlaerELNQAGQETLVTGWGyhssREKEAKRNRTFVLNFIKIPVV 368
Cdd:smart00020  80 PNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSN----YNVPAGTTCTVSGWG----RTSEGAGSLPDTLQEVNVPIV 151

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 332814313   369 PHNECSEVMSNM--VSENMLCAGILGDRQDACEGDSGGPMVASfHGTWFLVGLVSWGEGCGLLHNYGVYTKVSRYLDWI 445
Cdd:smart00020 152 SNATCRRAYSGGgaITDNMLCAGGLEGGKDACQGDSGGPLVCN-DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
213-445 5.67e-82

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 252.36  E-value: 5.67e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332814313  213 IDGKMTRRGDSPWQVVLLDSKKKLACGAVLIHPSWVLTAAHCMDESKKLLVRLGEYDLRRWEKWELDLDIKEVFVHPNYS 292
Cdd:pfam00089   2 VGGDEAQPGSFPWQVSLQLSSGKHFCGGSLISENWVLTAAHCVSGASDVKVVLGAHNIVLREGGEQKFDVEKIIVHPNYN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332814313  293 KSTTDNDIALLHLAQPATLSQTIVPICLPDSGlaerELNQAGQETLVTGWGYHSSrekeakRNRTFVLNFIKIPVVPHNE 372
Cdd:pfam00089  82 PDTLDNDIALLKLESPVTLGDTVRPICLPDAS----SDLPVGTTCTVSGWGNTKT------LGPSDTLQEVTVPVVSRET 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 332814313  373 CSEVMSNMVSENMLCAGilGDRQDACEGDSGGPMVASFHgtwFLVGLVSWGEGCGLLHNYGVYTKVSRYLDWI 445
Cdd:pfam00089 152 CRSAYGGTVTDTMICAG--AGGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 204-450 2.11e-63

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 206.04  E-value: 2.11e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332814313 204 QEDQVDPRLIDGKMTRRGDSPWQVVLLDSKKKLA--CGAVLIHPSWVLTAAHCMDES--KKLLVRLGEYDLRRWEKWELD 279
Cdd:COG5640   23 PAADAAPAIVGGTPATVGEYPWMVALQSSNGPSGqfCGGTLIAPRWVLTAAHCVDGDgpSDLRVVIGSTDLSTSGGTVVK 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332814313 280 ldIKEVFVHPNYSKSTTDNDIALLHLAQPATLSQtivPICLPDSGLAERelnqAGQETLVTGWGyhSSREKEAKRNRTfv 359
Cdd:COG5640  103 --VARIVVHPDYDPATPGNDIALLKLATPVPGVA---PAPLATSADAAA----PGTPATVAGWG--RTSEGPGSQSGT-- 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332814313 360 LNFIKIPVVPHNECSeVMSNMVSENMLCAGILGDRQDACEGDSGGPMVASFHGTWFLVGLVSWGEGCGLLHNYGVYTKVS 439
Cdd:COG5640  170 LRKADVPVVSDATCA-AYGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVS 248

                        250
                 ....*....|.
gi 332814313 440 RYLDWIHGHIR 450
Cdd:COG5640  249 AYRDWIKSTAG 259
GLA smart00069
Domain containing Gla (gamma-carboxyglutamate) residues; A hyaluronan-binding domain found in ...
 24-87 4.70e-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: 4.70e-26
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 332814313    24 DSVFSSSERAHQVLRIRKRANSF-LEELRHSSLERECIEEICDFEEAKEIFQNVDDTLAFWSKHV 87
Cdd:smart00069   1 GSVFLSRQEANKVLRRQRRANAFlLEELRPGNLERECQEEICSLEEAREVFEDNEGTDEFYRRYY 65
Gla pfam00594
Vitamin K-dependent carboxylation/gamma-carboxyglutamic (GLA) domain; This domain is ...
 47-87 2.18e-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: 78.34  E-value: 2.18e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 332814313   47 LEELRHSSLERECIEEICDFEEAKEIFQNVDDTLAFWSKHV 87
Cdd:pfam00594   1 LEELKPGNLERECYEEICSYEEAREIFEDDEKTMEFWKKYT 41
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
 238-435 2.64e-15

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 74.33  E-value: 2.64e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332814313 238 CGAVLIHPSWVLTAAHCMDESK------KLLVRLGeYDLRRWEKWEldldIKEVFVHPNYSKSTTDN-DIALLHLAQPAT 310
Cdd:COG3591   14 CTGTLIGPNLVLTAGHCVYDGAgggwatNIVFVPG-YNGGPYGTAT----ATRFRVPPGWVASGDAGyDYALLRLDEPLG 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332814313 311 LSQTIVPICLPDSGLAERELNQAgqetlvtgwGYHSSREKEAKRNRTfvlnfikipvvphNECSEVMSNMVSenMLCagi 390
Cdd:COG3591   89 DTTGWLGLAFNDAPLAGEPVTII---------GYPGDRPKDLSLDCS-------------GRVTGVQGNRLS--YDC--- 141

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 332814313 391 lgdrqDACEGDSGGPMVASFHGTWFLVGLVSWGEGCGllHNYGVY 435
Cdd:COG3591  142 -----DTTGGSSGSPVLDDSDGGGRVVGVHSAGGADR--ANTGVR 179
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 140-175 1.13e-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: 59.18  E-value: 1.13e-11
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 332814313  140 CSLDNGGCTHYCLEEVGWRRCSCAPGYKLGDDLLQC 175
Cdd:pfam14670   1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 101-132 4.65e-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: 4.65e-08
                         10        20        30
                 ....*....|....*....|....*....|....
gi 332814313 101 CAS--LCCGHGTCIDGIGSFSCDCRSGWEGRFCQ 132
Cdd:cd00054    5 CASgnPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
EGF_CA smart00179
Calcium-binding EGF-like domain;
101-132 8.42e-06

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 42.62  E-value: 8.42e-06
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 332814313   101 CAS--LCCGHGTCIDGIGSFSCDCRSGWE-GRFCQ 132
Cdd:smart00179   5 CASgnPCQNGGTCVNTVGSYRCECPPGYTdGRNCE 39
EGF cd00053
Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large ...
 100-132 1.89e-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: 38.61  E-value: 1.89e-04
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 332814313 100 PCA--SLCCGHGTCIDGIGSFSCDCRSGWEG-RFCQ 132
Cdd:cd00053    1 ECAasNPCSNGGTCVNTPGSYRCVCPPGYTGdRSCE 36
EGF smart00181
Epidermal growth factor-like domain;
100-132 3.06e-04

Epidermal growth factor-like domain;


Pssm-ID: 214544  Cd Length: 35  Bit Score: 37.88  E-value: 3.06e-04
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 332814313   100 PCASLC-CGHGTCIDGIGSFSCDCRSGWEG-RFCQ 132
Cdd:smart00181   1 ECASGGpCSNGTCINTPGSYTCSCPPGYTGdKRCE 35
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 101-130 3.40e-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: 35.05  E-value: 3.40e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 332814313  101 CASL-CCGHGTCIDGIGSFSCDCRSGWEGRF 130
Cdd:pfam00008   1 CAPNpCSNGGTCVDTPGGYTCICPEGYTGKR 31
hEGF pfam12661
Human growth factor-like EGF; hEGF, or human growth factor-like EGF, domains have six ...
 105-126 4.28e-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: 34.62  E-value: 4.28e-03
                          10        20
                  ....*....|....*....|..
gi 332814313  105 CCGHGTCIDGIGSFSCDCRSGW 126
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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