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Conserved domains on  [gi|2592807843|ref|WP_316248725|]
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trypsin-like peptidase domain-containing protein, partial [Staphylococcus pseudintermedius]

Protein Classification

trypsin-like serine peptidase( domain architecture ID 10007588)

trypsin-like serine protease catalyzes the cleavage of specific peptide bonds in protein substrates using an active site serine as the nucleophile

CATH:  2.40.10.10
EC:  3.4.21.-
PubMed:  7845208|7733651
SCOP:  3000114

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
113-300 7.87e-42

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


:

Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 143.28  E-value: 7.87e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2592807843 113 GYVASGVMVSKDTVLTAAHVVYDEGRKKIAERITVYSGlYGNIIRGSAKGIKTYVLKGYTSTLDSKYDLAAIKLDTNLGS 192
Cdd:COG3591    11 GGVCTGTLIGPNLVLTAGHCVYDGAGGGWATNIVFVPG-YNGGPYGTATATRFRVPPGWVASGDAGYDYALLRLDEPLGD 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2592807843 193 LTGSLGI--TSTIALGDKIATAGYPDDKtdrtnssdLKYYMWRSTGKIMNLDKYRVYYDADTSGGQSGSGVWDVKS--NK 268
Cdd:COG3591    90 TTGWLGLafNDAPLAGEPVTIIGYPGDR--------PKDLSLDCSGRVTGVQGNRLSYDCDTTGGSSGSPVLDDSDggGR 161
                         170       180       190
                  ....*....|....*....|....*....|...
gi 2592807843 269 LVAIHTNGG-KTFNFGTRITPQYLDYIKYWIGT 300
Cdd:COG3591   162 VVGVHSAGGaDRANTGVRLTSAIVAALRAWASA 194
 
Name Accession Description Interval E-value
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
113-300 7.87e-42

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 143.28  E-value: 7.87e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2592807843 113 GYVASGVMVSKDTVLTAAHVVYDEGRKKIAERITVYSGlYGNIIRGSAKGIKTYVLKGYTSTLDSKYDLAAIKLDTNLGS 192
Cdd:COG3591    11 GGVCTGTLIGPNLVLTAGHCVYDGAGGGWATNIVFVPG-YNGGPYGTATATRFRVPPGWVASGDAGYDYALLRLDEPLGD 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2592807843 193 LTGSLGI--TSTIALGDKIATAGYPDDKtdrtnssdLKYYMWRSTGKIMNLDKYRVYYDADTSGGQSGSGVWDVKS--NK 268
Cdd:COG3591    90 TTGWLGLafNDAPLAGEPVTIIGYPGDR--------PKDLSLDCSGRVTGVQGNRLSYDCDTTGGSSGSPVLDDSDggGR 161
                         170       180       190
                  ....*....|....*....|....*....|...
gi 2592807843 269 LVAIHTNGG-KTFNFGTRITPQYLDYIKYWIGT 300
Cdd:COG3591   162 VVGVHSAGGaDRANTGVRLTSAIVAALRAWASA 194
Trypsin_2 pfam13365
Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.
116-272 8.12e-12

Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.


Pssm-ID: 433149 [Multi-domain]  Cd Length: 142  Bit Score: 61.67  E-value: 8.12e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2592807843 116 ASGVMVSKD-TVLTAAHVVydegrkKIAERITVYsglYGNIIRGSAKGIKTYVLKgytstLDSKYDLAAIKLDTNLGSLT 194
Cdd:pfam13365   1 GTGFVVSSDgLVLTNAHVV------DDAEEAAVE---LVSVVLADGREYPATVVA-----RDPDLDLALLRVSGDGRGLP 66
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2592807843 195 G-SLGITSTIALGDKIATAGYPDDKTDRTNSSDlkYYMWRSTGKIMNLDKYRVYYDADTSGGQSGSGVWDVKsNKLVAI 272
Cdd:pfam13365  67 PlPLGDSEPLVGGERVYAVGYPLGGEKLSLSEG--IVSGVDEGRDGGDDGRVIQTDAALSPGSSGGPVFDAD-GRVVGI 142
 
Name Accession Description Interval E-value
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
113-300 7.87e-42

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 143.28  E-value: 7.87e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2592807843 113 GYVASGVMVSKDTVLTAAHVVYDEGRKKIAERITVYSGlYGNIIRGSAKGIKTYVLKGYTSTLDSKYDLAAIKLDTNLGS 192
Cdd:COG3591    11 GGVCTGTLIGPNLVLTAGHCVYDGAGGGWATNIVFVPG-YNGGPYGTATATRFRVPPGWVASGDAGYDYALLRLDEPLGD 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2592807843 193 LTGSLGI--TSTIALGDKIATAGYPDDKtdrtnssdLKYYMWRSTGKIMNLDKYRVYYDADTSGGQSGSGVWDVKS--NK 268
Cdd:COG3591    90 TTGWLGLafNDAPLAGEPVTIIGYPGDR--------PKDLSLDCSGRVTGVQGNRLSYDCDTTGGSSGSPVLDDSDggGR 161
                         170       180       190
                  ....*....|....*....|....*....|...
gi 2592807843 269 LVAIHTNGG-KTFNFGTRITPQYLDYIKYWIGT 300
Cdd:COG3591   162 VVGVHSAGGaDRANTGVRLTSAIVAALRAWASA 194
Trypsin_2 pfam13365
Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.
116-272 8.12e-12

Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.


Pssm-ID: 433149 [Multi-domain]  Cd Length: 142  Bit Score: 61.67  E-value: 8.12e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2592807843 116 ASGVMVSKD-TVLTAAHVVydegrkKIAERITVYsglYGNIIRGSAKGIKTYVLKgytstLDSKYDLAAIKLDTNLGSLT 194
Cdd:pfam13365   1 GTGFVVSSDgLVLTNAHVV------DDAEEAAVE---LVSVVLADGREYPATVVA-----RDPDLDLALLRVSGDGRGLP 66
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2592807843 195 G-SLGITSTIALGDKIATAGYPDDKTDRTNSSDlkYYMWRSTGKIMNLDKYRVYYDADTSGGQSGSGVWDVKsNKLVAI 272
Cdd:pfam13365  67 PlPLGDSEPLVGGERVYAVGYPLGGEKLSLSEG--IVSGVDEGRDGGDDGRVIQTDAALSPGSSGGPVFDAD-GRVVGI 142
Trypsin pfam00089
Trypsin;
113-298 1.43e-05

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 45.13  E-value: 1.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2592807843 113 GYVASGVMVSKDTVLTAAHVVYDEGRKKIAERITVYSGLYGNIIRGSAKGIktYVLKGYTS-TLDskYDLAAIKLDT--N 189
Cdd:pfam00089  24 KHFCGGSLISENWVLTAAHCVSGASDVKVVLGAHNIVLREGGEQKFDVEKI--IVHPNYNPdTLD--NDIALLKLESpvT 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2592807843 190 LGSLTGSLGITST---IALGDKIATAGYPDDKTDRTNSSDLKYYMW-RSTGKIMNLDKYRV--------YYDADTSGGQS 257
Cdd:pfam00089 100 LGDTVRPICLPDAssdLPVGTTCTVSGWGNTKTLGPSDTLQEVTVPvVSRETCRSAYGGTVtdtmicagAGGKDACQGDS 179
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2592807843 258 GSGVWdVKSNKLVAIHT-----NGGKTFNFGTRITpqyldYIKYWI 298
Cdd:pfam00089 180 GGPLV-CSDGELIGIVSwgygcASGNYPGVYTPVS-----SYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
107-190 1.29e-04

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 42.71  E-value: 1.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2592807843 107 SEGNYEGYVASGVMVSKDTVLTAAHVVYDEGrkkiAERITVYsglYGNIIRGSAKGIKTYVLK-----GYTSTLDSkYDL 181
Cdd:COG5640    50 SSNGPSGQFCGGTLIAPRWVLTAAHCVDGDG----PSDLRVV---IGSTDLSTSGGTVVKVARivvhpDYDPATPG-NDI 121

                  ....*....
gi 2592807843 182 AAIKLDTNL 190
Cdd:COG5640   122 ALLKLATPV 130
 
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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