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Conserved domains on  [gi|2066300950|ref|NP_001382429|]
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serine protease 41 isoform 1 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 ...
71-311 1.21e-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: 270.30  E-value: 1.21e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066300950  71 VAGGVESARGRWPWQASLRLRR-RHRCGGSLLSRRWVLSAAHCFQKhYYPSEWTVQLGEltsrptpWNLRAYSS---RYK 146
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTGgRHFCGGSLISPRWVLTAAHCVYS-SAPSNYTVRLGS-------HDLSSNEGggqVIK 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066300950 147 VQDIIVNPDA-LGVLRNDIALLRLASSVTYNAYIQPICIESSTFNFVHRPDCWVTGWGLISPSGtplPPPYNLREAQVTI 225
Cdd:cd00190    73 VKKVIVHPNYnPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGG---PLPDVLQEVNVPI 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066300950 226 LNNTRCNYLFeqpSSRSMIWDSMFCAGAEDGSVDTCKGDSGGPLVCDKDGLWYQVGIVSWGMDCGQPNRPGVYTNISVYF 305
Cdd:cd00190   150 VSNAECKRAY---SYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYL 226

                  ....*.
gi 2066300950 306 HWIRRV 311
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 ...
71-311 1.21e-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: 270.30  E-value: 1.21e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066300950  71 VAGGVESARGRWPWQASLRLRR-RHRCGGSLLSRRWVLSAAHCFQKhYYPSEWTVQLGEltsrptpWNLRAYSS---RYK 146
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTGgRHFCGGSLISPRWVLTAAHCVYS-SAPSNYTVRLGS-------HDLSSNEGggqVIK 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066300950 147 VQDIIVNPDA-LGVLRNDIALLRLASSVTYNAYIQPICIESSTFNFVHRPDCWVTGWGLISPSGtplPPPYNLREAQVTI 225
Cdd:cd00190    73 VKKVIVHPNYnPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGG---PLPDVLQEVNVPI 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066300950 226 LNNTRCNYLFeqpSSRSMIWDSMFCAGAEDGSVDTCKGDSGGPLVCDKDGLWYQVGIVSWGMDCGQPNRPGVYTNISVYF 305
Cdd:cd00190   150 VSNAECKRAY---SYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYL 226

                  ....*.
gi 2066300950 306 HWIRRV 311
Cdd:cd00190   227 DWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
71-308 1.09e-86

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: 260.30  E-value: 1.09e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066300950   71 VAGGVESARGRWPWQASLRLRR-RHRCGGSLLSRRWVLSAAHCFQKhYYPSEWTVQLGEltsrpTPWNLRAYSSRYKVQD 149
Cdd:smart00020   2 IVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVRG-SDPSNIRVRLGS-----HDLSSGEEGQVIKVSK 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066300950  150 IIVNPDA-LGVLRNDIALLRLASSVTYNAYIQPICIESSTFNFVHRPDCWVTGWGLISPSGTPLPPpyNLREAQVTILNN 228
Cdd:smart00020  76 VIIHPNYnPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPD--TLQEVNVPIVSN 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066300950  229 TRCNYLFeqpSSRSMIWDSMFCAGAEDGSVDTCKGDSGGPLVCdKDGLWYQVGIVSWGMDCGQPNRPGVYTNISVYFHWI 308
Cdd:smart00020 154 ATCRRAY---SGGGAITDNMLCAGGLEGGKDACQGDSGGPLVC-NDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
73-308 3.79e-62

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 197.28  E-value: 3.79e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066300950  73 GGVESARGRWPWQASLRLRR-RHRCGGSLLSRRWVLSAAHCFqkhYYPSEWTVQLGELTSRPTpwnlRAYSSRYKVQDII 151
Cdd:pfam00089   3 GGDEAQPGSFPWQVSLQLSSgKHFCGGSLISENWVLTAAHCV---SGASDVKVVLGAHNIVLR----EGGEQKFDVEKII 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066300950 152 VNPDALGV-LRNDIALLRLASSVTYNAYIQPICIESSTFNFVHRPDCWVTGWGLISPSGtplpPPYNLREAQVTILNNTR 230
Cdd:pfam00089  76 VHPNYNPDtLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLG----PSDTLQEVTVPVVSRET 151
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2066300950 231 CNylfeqPSSRSMIWDSMFCAGAedGSVDTCKGDSGGPLVCDKDglwYQVGIVSWGMDCGQPNRPGVYTNISVYFHWI 308
Cdd:pfam00089 152 CR-----SAYGGTVTDTMICAGA--GGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
61-312 1.32e-60

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 194.87  E-value: 1.32e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066300950  61 ACGHREIHALVAGGVESARGRWPWQASLRLR---RRHRCGGSLLSRRWVLSAAHCFQKhYYPSEWTVQLGELTSRPTPwn 137
Cdd:COG5640    21 AAPAADAAPAIVGGTPATVGEYPWMVALQSSngpSGQFCGGTLIAPRWVLTAAHCVDG-DGPSDLRVVIGSTDLSTSG-- 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066300950 138 lraySSRYKVQDIIVNPD-ALGVLRNDIALLRLASSVTYNAYIQpicIESSTFNFVHRPDCWVTGWGLISPSGTPLPPpy 216
Cdd:COG5640    98 ----GTVVKVARIVVHPDyDPATPGNDIALLKLATPVPGVAPAP---LATSADAAAPGTPATVAGWGRTSEGPGSQSG-- 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066300950 217 NLREAQVTILNNTRCNylfeqpSSRSMIWDSMFCAGAEDGSVDTCKGDSGGPLVCDKDGLWYQVGIVSWGMDCGQPNRPG 296
Cdd:COG5640   169 TLRKADVPVVSDATCA------AYGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPG 242
                         250
                  ....*....|....*.
gi 2066300950 297 VYTNISVYFHWIRRVM 312
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 ...
71-311 1.21e-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: 270.30  E-value: 1.21e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066300950  71 VAGGVESARGRWPWQASLRLRR-RHRCGGSLLSRRWVLSAAHCFQKhYYPSEWTVQLGEltsrptpWNLRAYSS---RYK 146
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTGgRHFCGGSLISPRWVLTAAHCVYS-SAPSNYTVRLGS-------HDLSSNEGggqVIK 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066300950 147 VQDIIVNPDA-LGVLRNDIALLRLASSVTYNAYIQPICIESSTFNFVHRPDCWVTGWGLISPSGtplPPPYNLREAQVTI 225
Cdd:cd00190    73 VKKVIVHPNYnPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGG---PLPDVLQEVNVPI 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066300950 226 LNNTRCNYLFeqpSSRSMIWDSMFCAGAEDGSVDTCKGDSGGPLVCDKDGLWYQVGIVSWGMDCGQPNRPGVYTNISVYF 305
Cdd:cd00190   150 VSNAECKRAY---SYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYL 226

                  ....*.
gi 2066300950 306 HWIRRV 311
Cdd:cd00190   227 DWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
71-308 1.09e-86

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: 260.30  E-value: 1.09e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066300950   71 VAGGVESARGRWPWQASLRLRR-RHRCGGSLLSRRWVLSAAHCFQKhYYPSEWTVQLGEltsrpTPWNLRAYSSRYKVQD 149
Cdd:smart00020   2 IVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVRG-SDPSNIRVRLGS-----HDLSSGEEGQVIKVSK 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066300950  150 IIVNPDA-LGVLRNDIALLRLASSVTYNAYIQPICIESSTFNFVHRPDCWVTGWGLISPSGTPLPPpyNLREAQVTILNN 228
Cdd:smart00020  76 VIIHPNYnPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPD--TLQEVNVPIVSN 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066300950  229 TRCNYLFeqpSSRSMIWDSMFCAGAEDGSVDTCKGDSGGPLVCdKDGLWYQVGIVSWGMDCGQPNRPGVYTNISVYFHWI 308
Cdd:smart00020 154 ATCRRAY---SGGGAITDNMLCAGGLEGGKDACQGDSGGPLVC-NDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
73-308 3.79e-62

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 197.28  E-value: 3.79e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066300950  73 GGVESARGRWPWQASLRLRR-RHRCGGSLLSRRWVLSAAHCFqkhYYPSEWTVQLGELTSRPTpwnlRAYSSRYKVQDII 151
Cdd:pfam00089   3 GGDEAQPGSFPWQVSLQLSSgKHFCGGSLISENWVLTAAHCV---SGASDVKVVLGAHNIVLR----EGGEQKFDVEKII 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066300950 152 VNPDALGV-LRNDIALLRLASSVTYNAYIQPICIESSTFNFVHRPDCWVTGWGLISPSGtplpPPYNLREAQVTILNNTR 230
Cdd:pfam00089  76 VHPNYNPDtLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLG----PSDTLQEVTVPVVSRET 151
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2066300950 231 CNylfeqPSSRSMIWDSMFCAGAedGSVDTCKGDSGGPLVCDKDglwYQVGIVSWGMDCGQPNRPGVYTNISVYFHWI 308
Cdd:pfam00089 152 CR-----SAYGGTVTDTMICAGA--GGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
61-312 1.32e-60

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 194.87  E-value: 1.32e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066300950  61 ACGHREIHALVAGGVESARGRWPWQASLRLR---RRHRCGGSLLSRRWVLSAAHCFQKhYYPSEWTVQLGELTSRPTPwn 137
Cdd:COG5640    21 AAPAADAAPAIVGGTPATVGEYPWMVALQSSngpSGQFCGGTLIAPRWVLTAAHCVDG-DGPSDLRVVIGSTDLSTSG-- 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066300950 138 lraySSRYKVQDIIVNPD-ALGVLRNDIALLRLASSVTYNAYIQpicIESSTFNFVHRPDCWVTGWGLISPSGTPLPPpy 216
Cdd:COG5640    98 ----GTVVKVARIVVHPDyDPATPGNDIALLKLATPVPGVAPAP---LATSADAAAPGTPATVAGWGRTSEGPGSQSG-- 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066300950 217 NLREAQVTILNNTRCNylfeqpSSRSMIWDSMFCAGAEDGSVDTCKGDSGGPLVCDKDGLWYQVGIVSWGMDCGQPNRPG 296
Cdd:COG5640   169 TLRKADVPVVSDATCA------AYGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPG 242
                         250
                  ....*....|....*.
gi 2066300950 297 VYTNISVYFHWIRRVM 312
Cdd:COG5640   243 VYTRVSAYRDWIKSTA 258
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
93-286 2.08e-08

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 53.53  E-value: 2.08e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066300950  93 RHRCGGSLLSRRWVLSAAHCF---QKHYYPSEWTVQLGeltsrptpWNLRAYSSrYKVQDIIVNPD--ALGVLRNDIALL 167
Cdd:COG3591    11 GGVCTGTLIGPNLVLTAGHCVydgAGGGWATNIVFVPG--------YNGGPYGT-ATATRFRVPPGwvASGDAGYDYALL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066300950 168 RLASSVTYnayiqpiciesstfnfvhrpdcwVTGWGLISPSGTPLpppynlREAQVTILNntrcnylfeQPSSRSMIwDS 247
Cdd:COG3591    82 RLDEPLGD-----------------------TTGWLGLAFNDAPL------AGEPVTIIG---------YPGDRPKD-LS 122
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2066300950 248 MFCAG---AEDGSV-----DTCKGDSGGPLVCDKDGLWYQVGIVSWG 286
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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