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Conserved domains on  [gi|148851513|gb|EDL65660|]
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hypothetical protein BSG1_12336 [Bacillus sp. SG-1]

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;
120-274 1.39e-40

Metallo-peptidase family M12;


:

Pssm-ID: 372673  Cd Length: 191  Bit Score: 139.48  E-value: 1.39e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148851513  120 ADRTVTVLVAVDEEYRAANP--DWQTLTQNIVEKADDAFMRDHGIDFKIQAFAEWSSQ---------GNDAVEILQDL-- 186
Cdd:pfam13688   1 STRTVALLVAADCSYVAAFGgdAAQANIINMVNTASNVYERDFNISLGLVNLTISDSTcpytppacsTGDSSDRLSEFqd 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148851513  187 ERDWNGRGYDFVAGFTKDANFNSGGIAYVYSSDPSGSAISVNLD-------QGAQNTSYAAQHEFSHNYGLGHDPQGS-- 257
Cdd:pfam13688  81 FSAWRGTQNDDLAYLFLMTNCSGGGLAWLGQLCNSGSAGSVSTRvsgnnvvVSTATEWQVFAHEIGHNFGAVHDCDSSts 160
                         170       180       190
                  ....*....|....*....|....*....|
gi 148851513  258 -------------GIKCIMNYDYSYQVDYW 274
Cdd:pfam13688 161 sqccppsnstcpaGGRYIMNPSSSPNSTDF 190
 
Name Accession Description Interval E-value
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
120-274 1.39e-40

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 139.48  E-value: 1.39e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148851513  120 ADRTVTVLVAVDEEYRAANP--DWQTLTQNIVEKADDAFMRDHGIDFKIQAFAEWSSQ---------GNDAVEILQDL-- 186
Cdd:pfam13688   1 STRTVALLVAADCSYVAAFGgdAAQANIINMVNTASNVYERDFNISLGLVNLTISDSTcpytppacsTGDSSDRLSEFqd 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148851513  187 ERDWNGRGYDFVAGFTKDANFNSGGIAYVYSSDPSGSAISVNLD-------QGAQNTSYAAQHEFSHNYGLGHDPQGS-- 257
Cdd:pfam13688  81 FSAWRGTQNDDLAYLFLMTNCSGGGLAWLGQLCNSGSAGSVSTRvsgnnvvVSTATEWQVFAHEIGHNFGAVHDCDSSts 160
                         170       180       190
                  ....*....|....*....|....*....|
gi 148851513  258 -------------GIKCIMNYDYSYQVDYW 274
Cdd:pfam13688 161 sqccppsnstcpaGGRYIMNPSSSPNSTDF 190
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
122-265 9.86e-05

Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ADAM family of metalloproteases contains proteolytic domains from snake venoms, proteases from the mammalian reproductive tract, and the tumor necrosis factor alpha convertase, TACE. ADAMs (A Disintegrin And Metalloprotease) are glycoproteins, which play roles in cell signaling, cell fusion, and cell-cell interactions.


Pssm-ID: 239795  Cd Length: 192  Bit Score: 42.41  E-value: 9.86e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148851513 122 RTVTVLVAVDEEYR-AANPDWQTLTQNIVEKAD--DAFMRDHGIDFKIQAFAE----WSSQ---GNDAVEILQDLERDW- 190
Cdd:cd04267    1 REIELVVVADHRMVsYFNSDENILQAYITELINiaNSIYRSTNLRLGIRISLEglqiLKGEqfaPPIDSDASNTLNSFSf 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148851513 191 ---NGRGYDFVAGFTKDANFNSGGI---AYVYSSDPSGSAISVNLDQG-AQNTSYAAQHEFSHNYGLGHD-------PQG 256
Cdd:cd04267   81 wraEGPIRHDNAVLLTAQDFIEGDIlglAYVGSMCNPYSSVGVVEDTGfTLLTALTMAHELGHNLGAEHDggdelafECD 160

                 ....*....
gi 148851513 257 SGIKCIMNY 265
Cdd:cd04267  161 GGGNYIMAP 169
 
Name Accession Description Interval E-value
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
120-274 1.39e-40

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 139.48  E-value: 1.39e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148851513  120 ADRTVTVLVAVDEEYRAANP--DWQTLTQNIVEKADDAFMRDHGIDFKIQAFAEWSSQ---------GNDAVEILQDL-- 186
Cdd:pfam13688   1 STRTVALLVAADCSYVAAFGgdAAQANIINMVNTASNVYERDFNISLGLVNLTISDSTcpytppacsTGDSSDRLSEFqd 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148851513  187 ERDWNGRGYDFVAGFTKDANFNSGGIAYVYSSDPSGSAISVNLD-------QGAQNTSYAAQHEFSHNYGLGHDPQGS-- 257
Cdd:pfam13688  81 FSAWRGTQNDDLAYLFLMTNCSGGGLAWLGQLCNSGSAGSVSTRvsgnnvvVSTATEWQVFAHEIGHNFGAVHDCDSSts 160
                         170       180       190
                  ....*....|....*....|....*....|
gi 148851513  258 -------------GIKCIMNYDYSYQVDYW 274
Cdd:pfam13688 161 sqccppsnstcpaGGRYIMNPSSSPNSTDF 190
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
146-253 5.38e-21

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: 85.88  E-value: 5.38e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148851513  146 QNIVEKADDAFMRDHGIDFKIQAFAEWSSQ-----GNDAVEILQDLERDW----NGRGYDFVAGFTKDANFNSGGIAYVY 216
Cdd:pfam13582   4 VSLVNRANTIYERDLGIRLQLAAIIITTSAdtpytSSDALEILDELQEVNdtriGQYGYDLGHLFTGRDGGGGGGIAYVG 83
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 148851513  217 SSDPSGSAISVNLDQGA--QNTSYAAQHEFSHNYGLGHD 253
Cdd:pfam13582  84 GVCNSGSKFGVNSGSGPvgDTGADTFAHEIGHNFGLNHT 122
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
122-265 9.86e-05

Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ADAM family of metalloproteases contains proteolytic domains from snake venoms, proteases from the mammalian reproductive tract, and the tumor necrosis factor alpha convertase, TACE. ADAMs (A Disintegrin And Metalloprotease) are glycoproteins, which play roles in cell signaling, cell fusion, and cell-cell interactions.


Pssm-ID: 239795  Cd Length: 192  Bit Score: 42.41  E-value: 9.86e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148851513 122 RTVTVLVAVDEEYR-AANPDWQTLTQNIVEKAD--DAFMRDHGIDFKIQAFAE----WSSQ---GNDAVEILQDLERDW- 190
Cdd:cd04267    1 REIELVVVADHRMVsYFNSDENILQAYITELINiaNSIYRSTNLRLGIRISLEglqiLKGEqfaPPIDSDASNTLNSFSf 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148851513 191 ---NGRGYDFVAGFTKDANFNSGGI---AYVYSSDPSGSAISVNLDQG-AQNTSYAAQHEFSHNYGLGHD-------PQG 256
Cdd:cd04267   81 wraEGPIRHDNAVLLTAQDFIEGDIlglAYVGSMCNPYSSVGVVEDTGfTLLTALTMAHELGHNLGAEHDggdelafECD 160

                 ....*....
gi 148851513 257 SGIKCIMNY 265
Cdd:cd04267  161 GGGNYIMAP 169
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
126-264 1.53e-03

Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom zinc endopeptidase. This subfamily contains other snake venom metalloproteinases, as well as membrane-anchored metalloproteases belonging to the ADAM family. ADAMs (A Disintegrin And Metalloprotease) are glycoproteins, which play roles in cell signaling, cell fusion, and cell-cell interactions.


Pssm-ID: 239797 [Multi-domain]  Cd Length: 194  Bit Score: 38.75  E-value: 1.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148851513 126 VLVAVDEEYRAANPDWQTLTQNIVEKAD--DAFMRDhgIDFKIQAFA-E-WS-----SQGNDAVEILQDL----ERDWNG 192
Cdd:cd04269    6 VVVVDNSLYKKYGSNLSKVRQRVIEIVNivDSIYRP--LNIRVVLVGlEiWTdkdkiSVSGDAGETLNRFldwkRSNLLP 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148851513 193 R-GYDFVAGFTKDaNFNSG--GIAYVYS--SDPSGSAISVNLDQGAQNTSYAAQHEFSHNYGLGHDPQG---SGIKCIMN 264
Cdd:cd04269   84 RkPHDNAQLLTGR-DFDGNtvGLAYVGGmcSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGGctcGRSTCIMA 162
Reprolysin_4 pfam13583
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
122-273 1.57e-03

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: 38.75  E-value: 1.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148851513  122 RTVTVLVAVDEEYRAANPDWQTLTQNI---VEKADDAFMRDHGIDFKI-------------QAFAEWSSQGNDAVEILQD 185
Cdd:pfam13583   3 RVYRVAVATDCTYSASFGSVDELRANInatVTTANEVYGRDFNVSLALisdrdviytdsstDSFNADCSGGDLGNWRLAT 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148851513  186 LERDWNGRGYDFVAGFTKD-ANFNSGGIAYVYssdpsgsAISVNLDQGAQNTSYAAQ--------HEFSHNYGLGHDPQG 256
Cdd:pfam13583  83 LTSWRDSLNYDLAYLTLMTgPSGQNVGVAWVG-------ALCSSARQNAKASGVARSrdewdifaHEIGHTFGAVHDCSS 155
                         170       180
                  ....*....|....*....|....*...
gi 148851513  257 SG-----------IKCIMNYDYSYQVDY 273
Cdd:pfam13583 156 QGeglssstedgsGQTIMSYASTASQTA 183
 
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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