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Conserved domains on  [gi|692318265|ref|WP_032129071|]
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MULTISPECIES: zinc-dependent metalloprotease [Stenotrophomonas]

Protein Classification

zinc-dependent metalloprotease( domain architecture ID 10616143)

zinc-dependent metalloprotease similar to Xanthomonas campestris peptidyl-Asp metalloendopeptidase that specifically cleaves on the N-terminal side of aspartyl, glutamyl and cysteic acid residues

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
195-383 4.53e-29

Metallo-peptidase family M12;


:

Pssm-ID: 372673  Cd Length: 191  Bit Score: 112.13  E-value: 4.53e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318265  195 TPATIRVLVVATNAAVTAYGGN-MQSLVQLAVAE-SNQGYVNSNvgITLQLAGYETTSYTES--------GNFTTDLTRF 264
Cdd:pfam13688   1 STRTVALLVAADCSYVAAFGGDaAQANIINMVNTaSNVYERDFN--ISLGLVNLTISDSTCPytppacstGDSSDRLSEF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318265  265 RNTSDGymdsihtsRNNTAADVGVLLIN-NTSYCGLASGIGSTASTAFAAVYWDC---------ATGYYSFAHEIGHLQS 334
Cdd:pfam13688  79 QDFSAW--------RGTQNDDLAYLFLMtNCSGGGLAWLGQLCNSGSAGSVSTRVsgnnvvvstATEWQVFAHEIGHNFG 150
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 692318265  335 ARHDIASDPStspYAYGHGYRYepSSGSRWRTIMAYDCSagcPRLNYWS 383
Cdd:pfam13688 151 AVHDCDSSTS---SQCCPPSNS--TCPAGGRYIMNPSSS---PNSTDFS 191
 
Name Accession Description Interval E-value
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
195-383 4.53e-29

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 112.13  E-value: 4.53e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318265  195 TPATIRVLVVATNAAVTAYGGN-MQSLVQLAVAE-SNQGYVNSNvgITLQLAGYETTSYTES--------GNFTTDLTRF 264
Cdd:pfam13688   1 STRTVALLVAADCSYVAAFGGDaAQANIINMVNTaSNVYERDFN--ISLGLVNLTISDSTCPytppacstGDSSDRLSEF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318265  265 RNTSDGymdsihtsRNNTAADVGVLLIN-NTSYCGLASGIGSTASTAFAAVYWDC---------ATGYYSFAHEIGHLQS 334
Cdd:pfam13688  79 QDFSAW--------RGTQNDDLAYLFLMtNCSGGGLAWLGQLCNSGSAGSVSTRVsgnnvvvstATEWQVFAHEIGHNFG 150
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 692318265  335 ARHDIASDPStspYAYGHGYRYepSSGSRWRTIMAYDCSagcPRLNYWS 383
Cdd:pfam13688 151 AVHDCDSSTS---SQCCPPSNS--TCPAGGRYIMNPSSS---PNSTDFS 191
 
Name Accession Description Interval E-value
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
195-383 4.53e-29

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 112.13  E-value: 4.53e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318265  195 TPATIRVLVVATNAAVTAYGGN-MQSLVQLAVAE-SNQGYVNSNvgITLQLAGYETTSYTES--------GNFTTDLTRF 264
Cdd:pfam13688   1 STRTVALLVAADCSYVAAFGGDaAQANIINMVNTaSNVYERDFN--ISLGLVNLTISDSTCPytppacstGDSSDRLSEF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318265  265 RNTSDGymdsihtsRNNTAADVGVLLIN-NTSYCGLASGIGSTASTAFAAVYWDC---------ATGYYSFAHEIGHLQS 334
Cdd:pfam13688  79 QDFSAW--------RGTQNDDLAYLFLMtNCSGGGLAWLGQLCNSGSAGSVSTRVsgnnvvvstATEWQVFAHEIGHNFG 150
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 692318265  335 ARHDIASDPStspYAYGHGYRYepSSGSRWRTIMAYDCSagcPRLNYWS 383
Cdd:pfam13688 151 AVHDCDSSTS---SQCCPPSNS--TCPAGGRYIMNPSSS---PNSTDFS 191
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
221-338 1.26e-19

Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the characteriztic binding motif HExxGHxxGxxH of Reprolysin-like peptidases of family M12B.


Pssm-ID: 463926 [Multi-domain]  Cd Length: 122  Bit Score: 83.96  E-value: 1.26e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318265  221 VQLAVAESNQGYvNSNVGITLQLAGYETTSYTESGNFTTDltrFRNTSDGYMDSIHTSRNNTAADVGVLLINNTSY--CG 298
Cdd:pfam13582   3 IVSLVNRANTIY-ERDLGIRLQLAAIIITTSADTPYTSSD---ALEILDELQEVNDTRIGQYGYDLGHLFTGRDGGggGG 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 692318265  299 LASGIGSTASTAFAAVYWDC----ATGYYSFAHEIGHLQSARHD 338
Cdd:pfam13582  79 IAYVGGVCNSGSKFGVNSGSgpvgDTGADTFAHEIGHNFGLNHT 122
Reprolysin_4 pfam13583
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
195-400 9.99e-07

Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the characteriztic binding motif HExxGHxxGxxH of Reprolysin-like peptidases of family M12B.


Pssm-ID: 404471  Cd Length: 203  Bit Score: 49.15  E-value: 9.99e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318265  195 TPATIRVLVvATNAAVTAYGGNMQSL---VQLAVAESNQGYvNSNVGITLQLAGYETTSYTESgnfTTDLTRFRNTSDGY 271
Cdd:pfam13583   1 TRRVYRVAV-ATDCTYSASFGSVDELranINATVTTANEVY-GRDFNVSLALISDRDVIYTDS---STDSFNADCSGGDL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318265  272 MDSI----HTSRNNTAADVGVLLI---NNTSYCGLA---SGIGSTASTAFAAVYWDCATGYYSFAHEIGHLQSARHDIAS 341
Cdd:pfam13583  76 GNWRlatlTSWRDSLNYDLAYLTLmtgPSGQNVGVAwvgALCSSARQNAKASGVARSRDEWDIFAHEIGHTFGAVHDCSS 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318265  342 DpstspyAYGHGYRYEPSSGSrwrTIMAYdcsAGCPRLNYWSNPNINY-NGIPMGNASTA 400
Cdd:pfam13583 156 Q------GEGLSSSTEDGSGQ---TIMSY---ASTASQTAFSPCTIRNiNGNPCSQANYG 203
 
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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