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Conserved domains on  [gi|2462575313|ref|XP_054199006|]
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vitamin K-dependent protein C isoform X3 [Homo sapiens]

Protein Classification

serine protease( domain architecture ID 10076129)

serine protease such as human cathepsin G with trypsin- and chymotrypsin-like specificity; also displays antibacterial activity against Gram-negative and Gram-positive bacteria independent of its protease activity

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 ...
24-259 2.81e-97

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: 284.94  E-value: 2.81e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575313  24 IDGKMTRRGDSPWQVVLLDSKKKLACGAVLIHPSWVLTAAHCMDES--KKLLVRLGEYDLRRWEKWELDLDIKEVFVHPN 101
Cdd:cd00190     2 VGGSEAKIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCVYSSapSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHPN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575313 102 YSKSTTDNDIALLHLAQPATLSQTIVPICLPDSGlaerELNQAGQETLVTGWGYHSSREkeakrNRTFVLNFIKIPVVPH 181
Cdd:cd00190    82 YNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSG----YNLPAGTTCTVSGWGRTSEGG-----PLPDVLQEVNVPIVSN 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575313 182 NECSEVMS--NMVSENMLCAGILGDRQDACEGDSGGPMVASFHGTWFLVGLVSWGEGCGLLHNYGVYTKVSRYLDWIHGH 259
Cdd:cd00190   153 AECKRAYSygGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
24-259 2.81e-97

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: 284.94  E-value: 2.81e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575313  24 IDGKMTRRGDSPWQVVLLDSKKKLACGAVLIHPSWVLTAAHCMDES--KKLLVRLGEYDLRRWEKWELDLDIKEVFVHPN 101
Cdd:cd00190     2 VGGSEAKIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCVYSSapSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHPN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575313 102 YSKSTTDNDIALLHLAQPATLSQTIVPICLPDSGlaerELNQAGQETLVTGWGYHSSREkeakrNRTFVLNFIKIPVVPH 181
Cdd:cd00190    82 YNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSG----YNLPAGTTCTVSGWGRTSEGG-----PLPDVLQEVNVPIVSN 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575313 182 NECSEVMS--NMVSENMLCAGILGDRQDACEGDSGGPMVASFHGTWFLVGLVSWGEGCGLLHNYGVYTKVSRYLDWIHGH 259
Cdd:cd00190   153 AECKRAYSygGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
22-256 1.04e-91

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: 270.70  E-value: 1.04e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575313   22 RLIDGKMTRRGDSPWQVVLLDSKKKLACGAVLIHPSWVLTAAHCMDES--KKLLVRLGEYDLRRWEKWELdLDIKEVFVH 99
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGRHFCGGSLISPRWVLTAAHCVRGSdpSNIRVRLGSHDLSSGEEGQV-IKVSKVIIH 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575313  100 PNYSKSTTDNDIALLHLAQPATLSQTIVPICLPDSGlaerELNQAGQETLVTGWGyhssREKEAKRNRTFVLNFIKIPVV 179
Cdd:smart00020  80 PNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSN----YNVPAGTTCTVSGWG----RTSEGAGSLPDTLQEVNVPIV 151
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462575313  180 PHNECSEVMSNM--VSENMLCAGILGDRQDACEGDSGGPMVASfHGTWFLVGLVSWGEGCGLLHNYGVYTKVSRYLDWI 256
Cdd:smart00020 152 SNATCRRAYSGGgaITDNMLCAGGLEGGKDACQGDSGGPLVCN-DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
24-256 8.93e-86

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 255.06  E-value: 8.93e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575313  24 IDGKMTRRGDSPWQVVLLDSKKKLACGAVLIHPSWVLTAAHCMDESKKLLVRLGEYDLRRWEKWELDLDIKEVFVHPNYS 103
Cdd:pfam00089   2 VGGDEAQPGSFPWQVSLQLSSGKHFCGGSLISENWVLTAAHCVSGASDVKVVLGAHNIVLREGGEQKFDVEKIIVHPNYN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575313 104 KSTTDNDIALLHLAQPATLSQTIVPICLPDSGlaerELNQAGQETLVTGWGYHSSrekeakRNRTFVLNFIKIPVVPHNE 183
Cdd:pfam00089  82 PDTLDNDIALLKLESPVTLGDTVRPICLPDAS----SDLPVGTTCTVSGWGNTKT------LGPSDTLQEVTVPVVSRET 151
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462575313 184 CSEVMSNMVSENMLCAGilGDRQDACEGDSGGPMVASFHgtwFLVGLVSWGEGCGLLHNYGVYTKVSRYLDWI 256
Cdd:pfam00089 152 CRSAYGGTVTDTMICAG--AGGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
15-261 7.68e-66

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 206.04  E-value: 7.68e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575313  15 QEDQVDPRLIDGKMTRRGDSPWQVVLLDSKKKLA--CGAVLIHPSWVLTAAHCMDES--KKLLVRLGEYDLRRWEKWELD 90
Cdd:COG5640    23 PAADAAPAIVGGTPATVGEYPWMVALQSSNGPSGqfCGGTLIAPRWVLTAAHCVDGDgpSDLRVVIGSTDLSTSGGTVVK 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575313  91 ldIKEVFVHPNYSKSTTDNDIALLHLAQPATLSQtivPICLPDSGLAERelnqAGQETLVTGWGyhSSREKEAKRNRTfv 170
Cdd:COG5640   103 --VARIVVHPDYDPATPGNDIALLKLATPVPGVA---PAPLATSADAAA----PGTPATVAGWG--RTSEGPGSQSGT-- 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575313 171 LNFIKIPVVPHNECSeVMSNMVSENMLCAGILGDRQDACEGDSGGPMVASFHGTWFLVGLVSWGEGCGLLHNYGVYTKVS 250
Cdd:COG5640   170 LRKADVPVVSDATCA-AYGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVS 248
                         250
                  ....*....|.
gi 2462575313 251 RYLDWIHGHIR 261
Cdd:COG5640   249 AYRDWIKSTAG 259
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
24-259 2.81e-97

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: 284.94  E-value: 2.81e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575313  24 IDGKMTRRGDSPWQVVLLDSKKKLACGAVLIHPSWVLTAAHCMDES--KKLLVRLGEYDLRRWEKWELDLDIKEVFVHPN 101
Cdd:cd00190     2 VGGSEAKIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCVYSSapSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHPN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575313 102 YSKSTTDNDIALLHLAQPATLSQTIVPICLPDSGlaerELNQAGQETLVTGWGYHSSREkeakrNRTFVLNFIKIPVVPH 181
Cdd:cd00190    82 YNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSG----YNLPAGTTCTVSGWGRTSEGG-----PLPDVLQEVNVPIVSN 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575313 182 NECSEVMS--NMVSENMLCAGILGDRQDACEGDSGGPMVASFHGTWFLVGLVSWGEGCGLLHNYGVYTKVSRYLDWIHGH 259
Cdd:cd00190   153 AECKRAYSygGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
22-256 1.04e-91

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: 270.70  E-value: 1.04e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575313   22 RLIDGKMTRRGDSPWQVVLLDSKKKLACGAVLIHPSWVLTAAHCMDES--KKLLVRLGEYDLRRWEKWELdLDIKEVFVH 99
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGRHFCGGSLISPRWVLTAAHCVRGSdpSNIRVRLGSHDLSSGEEGQV-IKVSKVIIH 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575313  100 PNYSKSTTDNDIALLHLAQPATLSQTIVPICLPDSGlaerELNQAGQETLVTGWGyhssREKEAKRNRTFVLNFIKIPVV 179
Cdd:smart00020  80 PNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSN----YNVPAGTTCTVSGWG----RTSEGAGSLPDTLQEVNVPIV 151
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462575313  180 PHNECSEVMSNM--VSENMLCAGILGDRQDACEGDSGGPMVASfHGTWFLVGLVSWGEGCGLLHNYGVYTKVSRYLDWI 256
Cdd:smart00020 152 SNATCRRAYSGGgaITDNMLCAGGLEGGKDACQGDSGGPLVCN-DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
24-256 8.93e-86

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 255.06  E-value: 8.93e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575313  24 IDGKMTRRGDSPWQVVLLDSKKKLACGAVLIHPSWVLTAAHCMDESKKLLVRLGEYDLRRWEKWELDLDIKEVFVHPNYS 103
Cdd:pfam00089   2 VGGDEAQPGSFPWQVSLQLSSGKHFCGGSLISENWVLTAAHCVSGASDVKVVLGAHNIVLREGGEQKFDVEKIIVHPNYN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575313 104 KSTTDNDIALLHLAQPATLSQTIVPICLPDSGlaerELNQAGQETLVTGWGYHSSrekeakRNRTFVLNFIKIPVVPHNE 183
Cdd:pfam00089  82 PDTLDNDIALLKLESPVTLGDTVRPICLPDAS----SDLPVGTTCTVSGWGNTKT------LGPSDTLQEVTVPVVSRET 151
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462575313 184 CSEVMSNMVSENMLCAGilGDRQDACEGDSGGPMVASFHgtwFLVGLVSWGEGCGLLHNYGVYTKVSRYLDWI 256
Cdd:pfam00089 152 CRSAYGGTVTDTMICAG--AGGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
15-261 7.68e-66

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 206.04  E-value: 7.68e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575313  15 QEDQVDPRLIDGKMTRRGDSPWQVVLLDSKKKLA--CGAVLIHPSWVLTAAHCMDES--KKLLVRLGEYDLRRWEKWELD 90
Cdd:COG5640    23 PAADAAPAIVGGTPATVGEYPWMVALQSSNGPSGqfCGGTLIAPRWVLTAAHCVDGDgpSDLRVVIGSTDLSTSGGTVVK 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575313  91 ldIKEVFVHPNYSKSTTDNDIALLHLAQPATLSQtivPICLPDSGLAERelnqAGQETLVTGWGyhSSREKEAKRNRTfv 170
Cdd:COG5640   103 --VARIVVHPDYDPATPGNDIALLKLATPVPGVA---PAPLATSADAAA----PGTPATVAGWG--RTSEGPGSQSGT-- 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575313 171 LNFIKIPVVPHNECSeVMSNMVSENMLCAGILGDRQDACEGDSGGPMVASFHGTWFLVGLVSWGEGCGLLHNYGVYTKVS 250
Cdd:COG5640   170 LRKADVPVVSDATCA-AYGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVS 248
                         250
                  ....*....|.
gi 2462575313 251 RYLDWIHGHIR 261
Cdd:COG5640   249 AYRDWIKSTAG 259
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
49-246 4.86e-16

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 74.33  E-value: 4.86e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575313  49 CGAVLIHPSWVLTAAHCMDESK------KLLVRLGeYDLRRWEKWEldldIKEVFVHPNYSKSTTDN-DIALLHLAQPAT 121
Cdd:COG3591    14 CTGTLIGPNLVLTAGHCVYDGAgggwatNIVFVPG-YNGGPYGTAT----ATRFRVPPGWVASGDAGyDYALLRLDEPLG 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575313 122 LSQTIVPICLPDSGLAERELNQAgqetlvtgwGYHSSREKEAKRNRTfvlnfikipvvphNECSEVMSNMVSenMLCagi 201
Cdd:COG3591    89 DTTGWLGLAFNDAPLAGEPVTII---------GYPGDRPKDLSLDCS-------------GRVTGVQGNRLS--YDC--- 141
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2462575313 202 lgdrqDACEGDSGGPMVASFHGTWFLVGLVSWGEGCGllHNYGVY 246
Cdd:COG3591   142 -----DTTGGSSGSPVLDDSDGGGRVVGVHSAGGADR--ANTGVR 179
 
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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