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Conserved domains on  [gi|2066300483|ref|NP_001382430|]
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serine protease 41 isoform 3 precursor [Homo sapiens]

Protein Classification

serine protease( domain architecture ID 10076129)

trypsin-like serine protease such as human plasminogen, the precursor of the widely distributed protease plasmin, or granzyme B, a human enzyme necessary for target cell lysis in cell-mediated immune responses

CATH:  2.40.10.10
EC:  3.4.21.-
PubMed:  18259688

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 ...
42-282 1.03e-90

Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad residues.


:

Pssm-ID: 238113 [Multi-domain]  Cd Length: 232  Bit Score: 269.53  E-value: 1.03e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066300483  42 VAGGVESARGRWPWQASLRLRR-RHRCGGSLLSRRWVLSAAHCFQKhYYPSEWTVQLGEltsrptpWNLRAYSS---RYK 117
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTGgRHFCGGSLISPRWVLTAAHCVYS-SAPSNYTVRLGS-------HDLSSNEGggqVIK 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066300483 118 VQDIIVNPDA-LGVLRNDIALLRLASSVTYNAYIQPICIESSTFNFVHRPDCWVTGWGLISPSGtplPPPYNLREAQVTI 196
Cdd:cd00190    73 VKKVIVHPNYnPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGG---PLPDVLQEVNVPI 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066300483 197 LNNTRCNYLFeqpSSRSMIWDSMFCAGAEDGSVDTCKGDSGGPLVCDKDGLWYQVGIVSWGMDCGQPNRPGVYTNISVYF 276
Cdd:cd00190   150 VSNAECKRAY---SYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYL 226

                  ....*.
gi 2066300483 277 HWIRRV 282
Cdd:cd00190   227 DWIQKT 232
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
42-282 1.03e-90

Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad residues.


Pssm-ID: 238113 [Multi-domain]  Cd Length: 232  Bit Score: 269.53  E-value: 1.03e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066300483  42 VAGGVESARGRWPWQASLRLRR-RHRCGGSLLSRRWVLSAAHCFQKhYYPSEWTVQLGEltsrptpWNLRAYSS---RYK 117
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTGgRHFCGGSLISPRWVLTAAHCVYS-SAPSNYTVRLGS-------HDLSSNEGggqVIK 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066300483 118 VQDIIVNPDA-LGVLRNDIALLRLASSVTYNAYIQPICIESSTFNFVHRPDCWVTGWGLISPSGtplPPPYNLREAQVTI 196
Cdd:cd00190    73 VKKVIVHPNYnPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGG---PLPDVLQEVNVPI 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066300483 197 LNNTRCNYLFeqpSSRSMIWDSMFCAGAEDGSVDTCKGDSGGPLVCDKDGLWYQVGIVSWGMDCGQPNRPGVYTNISVYF 276
Cdd:cd00190   150 VSNAECKRAY---SYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYL 226

                  ....*.
gi 2066300483 277 HWIRRV 282
Cdd:cd00190   227 DWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
42-279 8.89e-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: 259.53  E-value: 8.89e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066300483   42 VAGGVESARGRWPWQASLRLRR-RHRCGGSLLSRRWVLSAAHCFQKhYYPSEWTVQLGEltsrpTPWNLRAYSSRYKVQD 120
Cdd:smart00020   2 IVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVRG-SDPSNIRVRLGS-----HDLSSGEEGQVIKVSK 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066300483  121 IIVNPDA-LGVLRNDIALLRLASSVTYNAYIQPICIESSTFNFVHRPDCWVTGWGLISPSGTPLPPpyNLREAQVTILNN 199
Cdd:smart00020  76 VIIHPNYnPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPD--TLQEVNVPIVSN 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066300483  200 TRCNYLFeqpSSRSMIWDSMFCAGAEDGSVDTCKGDSGGPLVCdKDGLWYQVGIVSWGMDCGQPNRPGVYTNISVYFHWI 279
Cdd:smart00020 154 ATCRRAY---SGGGAITDNMLCAGGLEGGKDACQGDSGGPLVC-NDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
44-279 3.10e-62

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 196.51  E-value: 3.10e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066300483  44 GGVESARGRWPWQASLRLRR-RHRCGGSLLSRRWVLSAAHCFqkhYYPSEWTVQLGELTSRPTpwnlRAYSSRYKVQDII 122
Cdd:pfam00089   3 GGDEAQPGSFPWQVSLQLSSgKHFCGGSLISENWVLTAAHCV---SGASDVKVVLGAHNIVLR----EGGEQKFDVEKII 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066300483 123 VNPDALGV-LRNDIALLRLASSVTYNAYIQPICIESSTFNFVHRPDCWVTGWGLISPSGtplpPPYNLREAQVTILNNTR 201
Cdd:pfam00089  76 VHPNYNPDtLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLG----PSDTLQEVTVPVVSRET 151
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2066300483 202 CNylfeqPSSRSMIWDSMFCAGAedGSVDTCKGDSGGPLVCDKDglwYQVGIVSWGMDCGQPNRPGVYTNISVYFHWI 279
Cdd:pfam00089 152 CR-----SAYGGTVTDTMICAGA--GGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
32-283 5.65e-61

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 194.87  E-value: 5.65e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066300483  32 ACGHREIHALVAGGVESARGRWPWQASLRLR---RRHRCGGSLLSRRWVLSAAHCFQKhYYPSEWTVQLGELTSRPTPwn 108
Cdd:COG5640    21 AAPAADAAPAIVGGTPATVGEYPWMVALQSSngpSGQFCGGTLIAPRWVLTAAHCVDG-DGPSDLRVVIGSTDLSTSG-- 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066300483 109 lraySSRYKVQDIIVNPD-ALGVLRNDIALLRLASSVTYNAYIQpicIESSTFNFVHRPDCWVTGWGLISPSGTPLPPpy 187
Cdd:COG5640    98 ----GTVVKVARIVVHPDyDPATPGNDIALLKLATPVPGVAPAP---LATSADAAAPGTPATVAGWGRTSEGPGSQSG-- 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066300483 188 NLREAQVTILNNTRCNylfeqpSSRSMIWDSMFCAGAEDGSVDTCKGDSGGPLVCDKDGLWYQVGIVSWGMDCGQPNRPG 267
Cdd:COG5640   169 TLRKADVPVVSDATCA------AYGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPG 242
                         250
                  ....*....|....*.
gi 2066300483 268 VYTNISVYFHWIRRVM 283
Cdd:COG5640   243 VYTRVSAYRDWIKSTA 258
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
42-282 1.03e-90

Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad residues.


Pssm-ID: 238113 [Multi-domain]  Cd Length: 232  Bit Score: 269.53  E-value: 1.03e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066300483  42 VAGGVESARGRWPWQASLRLRR-RHRCGGSLLSRRWVLSAAHCFQKhYYPSEWTVQLGEltsrptpWNLRAYSS---RYK 117
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTGgRHFCGGSLISPRWVLTAAHCVYS-SAPSNYTVRLGS-------HDLSSNEGggqVIK 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066300483 118 VQDIIVNPDA-LGVLRNDIALLRLASSVTYNAYIQPICIESSTFNFVHRPDCWVTGWGLISPSGtplPPPYNLREAQVTI 196
Cdd:cd00190    73 VKKVIVHPNYnPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGG---PLPDVLQEVNVPI 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066300483 197 LNNTRCNYLFeqpSSRSMIWDSMFCAGAEDGSVDTCKGDSGGPLVCDKDGLWYQVGIVSWGMDCGQPNRPGVYTNISVYF 276
Cdd:cd00190   150 VSNAECKRAY---SYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYL 226

                  ....*.
gi 2066300483 277 HWIRRV 282
Cdd:cd00190   227 DWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
42-279 8.89e-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: 259.53  E-value: 8.89e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066300483   42 VAGGVESARGRWPWQASLRLRR-RHRCGGSLLSRRWVLSAAHCFQKhYYPSEWTVQLGEltsrpTPWNLRAYSSRYKVQD 120
Cdd:smart00020   2 IVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVRG-SDPSNIRVRLGS-----HDLSSGEEGQVIKVSK 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066300483  121 IIVNPDA-LGVLRNDIALLRLASSVTYNAYIQPICIESSTFNFVHRPDCWVTGWGLISPSGTPLPPpyNLREAQVTILNN 199
Cdd:smart00020  76 VIIHPNYnPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPD--TLQEVNVPIVSN 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066300483  200 TRCNYLFeqpSSRSMIWDSMFCAGAEDGSVDTCKGDSGGPLVCdKDGLWYQVGIVSWGMDCGQPNRPGVYTNISVYFHWI 279
Cdd:smart00020 154 ATCRRAY---SGGGAITDNMLCAGGLEGGKDACQGDSGGPLVC-NDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
44-279 3.10e-62

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 196.51  E-value: 3.10e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066300483  44 GGVESARGRWPWQASLRLRR-RHRCGGSLLSRRWVLSAAHCFqkhYYPSEWTVQLGELTSRPTpwnlRAYSSRYKVQDII 122
Cdd:pfam00089   3 GGDEAQPGSFPWQVSLQLSSgKHFCGGSLISENWVLTAAHCV---SGASDVKVVLGAHNIVLR----EGGEQKFDVEKII 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066300483 123 VNPDALGV-LRNDIALLRLASSVTYNAYIQPICIESSTFNFVHRPDCWVTGWGLISPSGtplpPPYNLREAQVTILNNTR 201
Cdd:pfam00089  76 VHPNYNPDtLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLG----PSDTLQEVTVPVVSRET 151
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2066300483 202 CNylfeqPSSRSMIWDSMFCAGAedGSVDTCKGDSGGPLVCDKDglwYQVGIVSWGMDCGQPNRPGVYTNISVYFHWI 279
Cdd:pfam00089 152 CR-----SAYGGTVTDTMICAGA--GGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
32-283 5.65e-61

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 194.87  E-value: 5.65e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066300483  32 ACGHREIHALVAGGVESARGRWPWQASLRLR---RRHRCGGSLLSRRWVLSAAHCFQKhYYPSEWTVQLGELTSRPTPwn 108
Cdd:COG5640    21 AAPAADAAPAIVGGTPATVGEYPWMVALQSSngpSGQFCGGTLIAPRWVLTAAHCVDG-DGPSDLRVVIGSTDLSTSG-- 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066300483 109 lraySSRYKVQDIIVNPD-ALGVLRNDIALLRLASSVTYNAYIQpicIESSTFNFVHRPDCWVTGWGLISPSGTPLPPpy 187
Cdd:COG5640    98 ----GTVVKVARIVVHPDyDPATPGNDIALLKLATPVPGVAPAP---LATSADAAAPGTPATVAGWGRTSEGPGSQSG-- 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066300483 188 NLREAQVTILNNTRCNylfeqpSSRSMIWDSMFCAGAEDGSVDTCKGDSGGPLVCDKDGLWYQVGIVSWGMDCGQPNRPG 267
Cdd:COG5640   169 TLRKADVPVVSDATCA------AYGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPG 242
                         250
                  ....*....|....*.
gi 2066300483 268 VYTNISVYFHWIRRVM 283
Cdd:COG5640   243 VYTRVSAYRDWIKSTA 258
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
64-257 1.98e-08

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 53.14  E-value: 1.98e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066300483  64 RHRCGGSLLSRRWVLSAAHCF---QKHYYPSEWTVQLGeltsrptpWNLRAYSSrYKVQDIIVNPD--ALGVLRNDIALL 138
Cdd:COG3591    11 GGVCTGTLIGPNLVLTAGHCVydgAGGGWATNIVFVPG--------YNGGPYGT-ATATRFRVPPGwvASGDAGYDYALL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066300483 139 RLASSVTYnayiqpiciesstfnfvhrpdcwVTGWGLISPSGTPLpppynlREAQVTILNntrcnylfeQPSSRSMIwDS 218
Cdd:COG3591    82 RLDEPLGD-----------------------TTGWLGLAFNDAPL------AGEPVTIIG---------YPGDRPKD-LS 122
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2066300483 219 MFCAG---AEDGSV-----DTCKGDSGGPLVCDKDGLWYQVGIVSWG 257
Cdd:COG3591   123 LDCSGrvtGVQGNRlsydcDTTGGSSGSPVLDDSDGGGRVVGVHSAG 169
 
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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