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Conserved domains on  [gi|568906110|ref|XP_006495919|]
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serine protease 40 isoform X1 [Mus musculus]

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 ...
69-260 4.49e-58

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: 185.17  E-value: 4.49e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906110  69 IYGGQIAGAERWPWQASLRLY-GRHICGAVLIDKNWVLSAAHCFqRSQEPSDYHVMLGYTDLNSPTRYSRTMSVQKVIVH 147
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCV-YSSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVH 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906110 148 KDYNRFhTQGSDIVLLQLRSSVEYSSHILPACVPEENIKIPKEKACWASGWGYLREDVriPLPNELYEAELIIMSNDQCK 227
Cdd:cd00190   80 PNYNPS-TYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGG--PLPDVLQEVNVPIVSNAECK 156
                        170       180       190
                 ....*....|....*....|....*....|...
gi 568906110 228 GFFPPPvpgsgrsYYIYDDMVCAADYDMSKSIC 260
Cdd:cd00190  157 RAYSYG-------GTITDNMLCAGGLEGGKDAC 182
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
69-260 4.49e-58

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: 185.17  E-value: 4.49e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906110  69 IYGGQIAGAERWPWQASLRLY-GRHICGAVLIDKNWVLSAAHCFqRSQEPSDYHVMLGYTDLNSPTRYSRTMSVQKVIVH 147
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCV-YSSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVH 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906110 148 KDYNRFhTQGSDIVLLQLRSSVEYSSHILPACVPEENIKIPKEKACWASGWGYLREDVriPLPNELYEAELIIMSNDQCK 227
Cdd:cd00190   80 PNYNPS-TYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGG--PLPDVLQEVNVPIVSNAECK 156
                        170       180       190
                 ....*....|....*....|....*....|...
gi 568906110 228 GFFPPPvpgsgrsYYIYDDMVCAADYDMSKSIC 260
Cdd:cd00190  157 RAYSYG-------GTITDNMLCAGGLEGGKDAC 182
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
68-260 1.81e-55

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: 178.64  E-value: 1.81e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906110    68 KIYGGQIAGAERWPWQASLRLYG-RHICGAVLIDKNWVLSAAHCFqRSQEPSDYHVMLGYTDLNSPTrYSRTMSVQKVIV 146
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCV-RGSDPSNIRVRLGSHDLSSGE-EGQVIKVSKVII 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906110   147 HKDYNRfHTQGSDIVLLQLRSSVEYSSHILPACVPEENIKIPKEKACWASGWGYLREDVRiPLPNELYEAELIIMSNDQC 226
Cdd:smart00020  79 HPNYNP-STYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAG-SLPDTLQEVNVPIVSNATC 156
                          170       180       190
                   ....*....|....*....|....*....|....
gi 568906110   227 KGFFPPPvpgsgrsYYIYDDMVCAADYDMSKSIC 260
Cdd:smart00020 157 RRAYSGG-------GAITDNMLCAGGLEGGKDAC 183
Trypsin pfam00089
Trypsin;
69-260 4.71e-39

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 136.03  E-value: 4.71e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906110   69 IYGGQIAGAERWPWQASLRLY-GRHICGAVLIDKNWVLSAAHCFQrsqEPSDYHVMLGYTDLNSPTRYSRTMSVQKVIVH 147
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSsGKHFCGGSLISENWVLTAAHCVS---GASDVKVVLGAHNIVLREGGEQKFDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906110  148 KDYNRFhTQGSDIVLLQLRSSVEYSSHILPACVPEENIKIPKEKACWASGWGYLREDVRiplPNELYEAELIIMSNDQCK 227
Cdd:pfam00089  78 PNYNPD-TLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP---SDTLQEVTVPVVSRETCR 153
                         170       180       190
                  ....*....|....*....|....*....|...
gi 568906110  228 GFFPPpvpgsgrsyYIYDDMVCAADYdmSKSIC 260
Cdd:pfam00089 154 SAYGG---------TVTDTMICAGAG--GKDAC 175
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
66-260 1.24e-35

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 128.23  E-value: 1.24e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906110  66 QGKIYGGQIAGAERWPWQASLRL---YGRHICGAVLIDKNWVLSAAHCFQRSQePSDYHVMLGYTDLNSPTRYSRTmsVQ 142
Cdd:COG5640   28 APAIVGGTPATVGEYPWMVALQSsngPSGQFCGGTLIAPRWVLTAAHCVDGDG-PSDLRVVIGSTDLSTSGGTVVK--VA 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906110 143 KVIVHKDYNRfHTQGSDIVLLQLRSSVEYSShilPACVPEENIKIPKEKACWASGWGYLREDVRiPLPNELYEAELIIMS 222
Cdd:COG5640  105 RIVVHPDYDP-ATPGNDIALLKLATPVPGVA---PAPLATSADAAAPGTPATVAGWGRTSEGPG-SQSGTLRKADVPVVS 179
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 568906110 223 NDQCKGFfpppvpgsgrSYYIYDDMVCAADYDMSKSIC 260
Cdd:COG5640  180 DATCAAY----------GGFDGGTMLCAGYPEGGKDAC 207
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
69-260 4.49e-58

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: 185.17  E-value: 4.49e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906110  69 IYGGQIAGAERWPWQASLRLY-GRHICGAVLIDKNWVLSAAHCFqRSQEPSDYHVMLGYTDLNSPTRYSRTMSVQKVIVH 147
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCV-YSSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVH 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906110 148 KDYNRFhTQGSDIVLLQLRSSVEYSSHILPACVPEENIKIPKEKACWASGWGYLREDVriPLPNELYEAELIIMSNDQCK 227
Cdd:cd00190   80 PNYNPS-TYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGG--PLPDVLQEVNVPIVSNAECK 156
                        170       180       190
                 ....*....|....*....|....*....|...
gi 568906110 228 GFFPPPvpgsgrsYYIYDDMVCAADYDMSKSIC 260
Cdd:cd00190  157 RAYSYG-------GTITDNMLCAGGLEGGKDAC 182
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
68-260 1.81e-55

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: 178.64  E-value: 1.81e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906110    68 KIYGGQIAGAERWPWQASLRLYG-RHICGAVLIDKNWVLSAAHCFqRSQEPSDYHVMLGYTDLNSPTrYSRTMSVQKVIV 146
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCV-RGSDPSNIRVRLGSHDLSSGE-EGQVIKVSKVII 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906110   147 HKDYNRfHTQGSDIVLLQLRSSVEYSSHILPACVPEENIKIPKEKACWASGWGYLREDVRiPLPNELYEAELIIMSNDQC 226
Cdd:smart00020  79 HPNYNP-STYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAG-SLPDTLQEVNVPIVSNATC 156
                          170       180       190
                   ....*....|....*....|....*....|....
gi 568906110   227 KGFFPPPvpgsgrsYYIYDDMVCAADYDMSKSIC 260
Cdd:smart00020 157 RRAYSGG-------GAITDNMLCAGGLEGGKDAC 183
Trypsin pfam00089
Trypsin;
69-260 4.71e-39

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 136.03  E-value: 4.71e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906110   69 IYGGQIAGAERWPWQASLRLY-GRHICGAVLIDKNWVLSAAHCFQrsqEPSDYHVMLGYTDLNSPTRYSRTMSVQKVIVH 147
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSsGKHFCGGSLISENWVLTAAHCVS---GASDVKVVLGAHNIVLREGGEQKFDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906110  148 KDYNRFhTQGSDIVLLQLRSSVEYSSHILPACVPEENIKIPKEKACWASGWGYLREDVRiplPNELYEAELIIMSNDQCK 227
Cdd:pfam00089  78 PNYNPD-TLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP---SDTLQEVTVPVVSRETCR 153
                         170       180       190
                  ....*....|....*....|....*....|...
gi 568906110  228 GFFPPpvpgsgrsyYIYDDMVCAADYdmSKSIC 260
Cdd:pfam00089 154 SAYGG---------TVTDTMICAGAG--GKDAC 175
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
66-260 1.24e-35

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 128.23  E-value: 1.24e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906110  66 QGKIYGGQIAGAERWPWQASLRL---YGRHICGAVLIDKNWVLSAAHCFQRSQePSDYHVMLGYTDLNSPTRYSRTmsVQ 142
Cdd:COG5640   28 APAIVGGTPATVGEYPWMVALQSsngPSGQFCGGTLIAPRWVLTAAHCVDGDG-PSDLRVVIGSTDLSTSGGTVVK--VA 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906110 143 KVIVHKDYNRfHTQGSDIVLLQLRSSVEYSShilPACVPEENIKIPKEKACWASGWGYLREDVRiPLPNELYEAELIIMS 222
Cdd:COG5640  105 RIVVHPDYDP-ATPGNDIALLKLATPVPGVA---PAPLATSADAAAPGTPATVAGWGRTSEGPG-SQSGTLRKADVPVVS 179
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 568906110 223 NDQCKGFfpppvpgsgrSYYIYDDMVCAADYDMSKSIC 260
Cdd:COG5640  180 DATCAAY----------GGFDGGTMLCAGYPEGGKDAC 207
DUF1986 pfam09342
Domain of unknown function (DUF1986); This domain is found in serine proteases and is ...
80-197 4.75e-09

Domain of unknown function (DUF1986); This domain is found in serine proteases and is predicted to contain disulphide bonds.


Pssm-ID: 286432  Cd Length: 116  Bit Score: 53.32  E-value: 4.75e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906110   80 WPWQASLRLYGRHICGAVLIDKNWVLSAAHCFQRSQEPSDY-HVMLG----YTDLNSPTRysrtmSVQKVIVHKDYNRfh 154
Cdd:pfam09342   1 WPWIAKVYLDGNMICSGVLIDASWVIVSGSCLRDTNLRHQYiSVVLGgaktLKSIEGPYE-----QIVRVDCRHDIPE-- 73
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 568906110  155 tqgSDIVLLQLRSSVEYSSHILPACVPEENIKIPKEKACWASG 197
Cdd:pfam09342  74 ---SEISLLHLASPASFSNHVLPTFVPETRNENEKDNECLAVG 113
 
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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