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Conserved domains on  [gi|836726449|ref|WP_047858512|]
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zinc-dependent metalloprotease [Archangium gephyra]

Protein Classification

zinc-dependent metalloprotease( domain architecture ID 10574850)

zinc-dependent metalloprotease similar to Myxococcus xanthus protease B (prtB)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Peptidase_M57 pfam12388
Dual-action HEIGH metallo-peptidase; The catalytic triad for this family of proteases is ...
 49-253 1.16e-116

Dual-action HEIGH metallo-peptidase; The catalytic triad for this family of proteases is HE-H-H, which in many members is in the sequence motif HEIGH.


:

Pssm-ID: 432518  Cd Length: 212  Bit Score: 332.56  E-value: 1.16e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836726449   49 VYVGLDAHVTLEASREMLQTGKETAEQYRTTNLVAT--TVTKICVNPTSGFNSYTRLSQGLDLAIQNYNGLGLS--FTMA 124
Cdd:pfam12388   1 VYVGRDAVVTLEASREMLQTDSDTAEQYRTTNLVGTsvTVIKICVNPTSNFNSYSRLSTGLDLAIANYNRLGLRftFRLT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836726449  125 RGPTTGCS----ANITAQTMSGTGGSAGFPSGGKPYGTINIGTGLNSYSVDVNEHVITHELGHAIGFRHSDYYNRAISCG 200
Cdd:pfam12388  81 FGPNTGNSdmvtYDNTANTPSGTGGSAGFPSGGLPYGTIQIGTGLQSYSTDVNEHVITHELGHSIGFRHSDYYNRSISCG 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 836726449  201 SGGNEGASTVGAIHIPGTPTTATvGGSIMNSCFRSTETGEWTSSDKTALYYLY 253
Cdd:pfam12388 161 SGGNEGTAGVGAILIPGTPTTAT-GGSIMNSCFSSNETGEFTSSDITALTYLY 212
 
Name Accession Description Interval E-value
Peptidase_M57 pfam12388
Dual-action HEIGH metallo-peptidase; The catalytic triad for this family of proteases is ...
 49-253 1.16e-116

Dual-action HEIGH metallo-peptidase; The catalytic triad for this family of proteases is HE-H-H, which in many members is in the sequence motif HEIGH.


Pssm-ID: 432518  Cd Length: 212  Bit Score: 332.56  E-value: 1.16e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836726449   49 VYVGLDAHVTLEASREMLQTGKETAEQYRTTNLVAT--TVTKICVNPTSGFNSYTRLSQGLDLAIQNYNGLGLS--FTMA 124
Cdd:pfam12388   1 VYVGRDAVVTLEASREMLQTDSDTAEQYRTTNLVGTsvTVIKICVNPTSNFNSYSRLSTGLDLAIANYNRLGLRftFRLT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836726449  125 RGPTTGCS----ANITAQTMSGTGGSAGFPSGGKPYGTINIGTGLNSYSVDVNEHVITHELGHAIGFRHSDYYNRAISCG 200
Cdd:pfam12388  81 FGPNTGNSdmvtYDNTANTPSGTGGSAGFPSGGLPYGTIQIGTGLQSYSTDVNEHVITHELGHSIGFRHSDYYNRSISCG 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 836726449  201 SGGNEGASTVGAIHIPGTPTTATvGGSIMNSCFRSTETGEWTSSDKTALYYLY 253
Cdd:pfam12388 161 SGGNEGTAGVGAILIPGTPTTAT-GGSIMNSCFSSNETGEFTSSDITALTYLY 212
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 142-198 1.04e-05

Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix metalloproteinases (MMPs), serralysins, and the astacin_like family of proteases.


Pssm-ID: 239796 [Multi-domain]  Cd Length: 165  Bit Score: 44.41  E-value: 1.04e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 836726449 142 GTGGSAGFPSGGKPY-GTINIGTGLNSYSVDVNEHVITHELGHAIGFRHSDYYNRAIS 198
Cdd:cd04268   62 SYGPSQVDPLTGEILlARVYLYSSFVEYSGARLRNTAEHELGHALGLRHNFAASDRDD 119
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 141-194 6.33e-05

Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a subset of known subfamilies. Highest similarity occurs in the HExxH zinc-binding site/ active site.


Pssm-ID: 214576 [Multi-domain]  Cd Length: 139  Bit Score: 41.95  E-value: 6.33e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 836726449   141 SGTGGS-AGFPSGGkpyGTINIGTGlnsysvDVNEHVITHELGHAIGFRHSDYYN 194
Cdd:smart00235  60 SGCTLShAGRPGGD---QHLSLGNG------CINTGVAAHELGHALGLYHEQSRS 105
 
Name Accession Description Interval E-value
Peptidase_M57 pfam12388
Dual-action HEIGH metallo-peptidase; The catalytic triad for this family of proteases is ...
 49-253 1.16e-116

Dual-action HEIGH metallo-peptidase; The catalytic triad for this family of proteases is HE-H-H, which in many members is in the sequence motif HEIGH.


Pssm-ID: 432518  Cd Length: 212  Bit Score: 332.56  E-value: 1.16e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836726449   49 VYVGLDAHVTLEASREMLQTGKETAEQYRTTNLVAT--TVTKICVNPTSGFNSYTRLSQGLDLAIQNYNGLGLS--FTMA 124
Cdd:pfam12388   1 VYVGRDAVVTLEASREMLQTDSDTAEQYRTTNLVGTsvTVIKICVNPTSNFNSYSRLSTGLDLAIANYNRLGLRftFRLT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836726449  125 RGPTTGCS----ANITAQTMSGTGGSAGFPSGGKPYGTINIGTGLNSYSVDVNEHVITHELGHAIGFRHSDYYNRAISCG 200
Cdd:pfam12388  81 FGPNTGNSdmvtYDNTANTPSGTGGSAGFPSGGLPYGTIQIGTGLQSYSTDVNEHVITHELGHSIGFRHSDYYNRSISCG 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 836726449  201 SGGNEGASTVGAIHIPGTPTTATvGGSIMNSCFRSTETGEWTSSDKTALYYLY 253
Cdd:pfam12388 161 SGGNEGTAGVGAILIPGTPTTAT-GGSIMNSCFSSNETGEFTSSDITALTYLY 212
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 142-198 1.04e-05

Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix metalloproteinases (MMPs), serralysins, and the astacin_like family of proteases.


Pssm-ID: 239796 [Multi-domain]  Cd Length: 165  Bit Score: 44.41  E-value: 1.04e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 836726449 142 GTGGSAGFPSGGKPY-GTINIGTGLNSYSVDVNEHVITHELGHAIGFRHSDYYNRAIS 198
Cdd:cd04268   62 SYGPSQVDPLTGEILlARVYLYSSFVEYSGARLRNTAEHELGHALGLRHNFAASDRDD 119
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 141-194 6.33e-05

Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a subset of known subfamilies. Highest similarity occurs in the HExxH zinc-binding site/ active site.


Pssm-ID: 214576 [Multi-domain]  Cd Length: 139  Bit Score: 41.95  E-value: 6.33e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 836726449   141 SGTGGS-AGFPSGGkpyGTINIGTGlnsysvDVNEHVITHELGHAIGFRHSDYYN 194
Cdd:smart00235  60 SGCTLShAGRPGGD---QHLSLGNG------CINTGVAAHELGHALGLYHEQSRS 105
ZnMc_MMP_like_1 cd04279
Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ...
 88-190 3.44e-04

Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and fungal metalloproteinase domains similar to matrix metalloproteinases and astacin.


Pssm-ID: 239806 [Multi-domain]  Cd Length: 156  Bit Score: 40.13  E-value: 3.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836726449  88 KICVNPTSGFNS--YTRLSQGLDLAIQNYNGLGlSFTMARGPTTGCSANIT---AQTMSGTGGSAGFPSGGKPYGTINIG 162
Cdd:cd04279    5 RVYIDPTPAPPDsrAQSWLQAVKQAAAEWENVG-PLKFVYNPEEDNDADIViffDRPPPVGGAGGGLARAGFPLISDGNR 83

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 836726449 163 TGLNSYSVDVN----------EHVITHELGHAIGFRHS 190
Cdd:cd04279   84 KLFNRTDINLGpgqprgaenlQAIALHELGHALGLWHH 121
ZnMc_serralysin_like cd04277
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
 117-194 3.73e-04

Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases are important virulence factors in pathogenic bacteria. They may be secreted into the medium via a mechanism found in gram-negative bacteria, that does not require n-terminal signal sequences which are cleaved after the transmembrane translocation. A calcium-binding domain c-terminal to the metalloprotease domain, which contains multiple tandem repeats of a nine-residue motif including the pattern GGxGxD, and which forms a parallel beta roll may be involved in the translocation mechanism and/or substrate binding. Serralysin family members may have a broad spectrum of substrates each, including host immunoglobulins, complement proteins, cell matrix and cytoskeletal proteins, as well as antimicrobial peptides.


Pssm-ID: 239804 [Multi-domain]  Cd Length: 186  Bit Score: 40.09  E-value: 3.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836726449 117 LGLSFTMARGPTtgcSANIT----AQTMSGTGGSAGFP---SGGKPYGTINIGTGLNSYSVDVNEH---VITHELGHAIG 186
Cdd:cd04277   50 ADIDFVEVSDNS---GADIRfgnsSDPDGNTAGYAYYPgsgSGTAYGGDIWFNSSYDTNSDSPGSYgyqTIIHEIGHALG 126


                 ....*...
gi 836726449 187 FRHSDYYN 194
Cdd:cd04277  127 LEHPGDYN 134
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 158-213 1.03e-03

Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) are glycoproteins, which play roles in cell signaling, cell fusion, and cell-cell interactions. This particular subfamily represents domain architectures that combine ADAM-like metalloproteinases with thrombospondin type-1 repeats. ADAMTS (a disintegrin and metalloproteinase with thrombospondin motifs) proteinases are inhibited by TIMPs (tissue inhibitors of metalloproteinases), and they play roles in coagulation, angiogenesis, development and progression of arthritis. They hydrolyze the von Willebrand factor precursor and various components of the extracellular matrix.


Pssm-ID: 239801  Cd Length: 207  Bit Score: 39.14  E-value: 1.03e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 836726449 158 TINIGTGLNSysvdvnEHVITHELGHAIGFRHSDYYNraiSCGSGGNEG---ASTVGAI 213
Cdd:cd04273  131 SINEDTGLSS------AFTIAHELGHVLGMPHDGDGN---SCGPEGKDGhimSPTLGAN 180
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 136-253 2.00e-03

Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major branches, the astacin-like proteases and the adamalysin/reprolysin-like proteases. Both branches have wide phylogenetic distribution, and contain sub-families, which are involved in vertebrate development and disease.


Pssm-ID: 238124 [Multi-domain]  Cd Length: 167  Bit Score: 37.89  E-value: 2.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836726449 136 TAQTMS-GTGGSAGFPSGGKPY-GTINIGTglNSYSVDVNEHVITHELGHAIGFRHSDYYNraisCGSGGNEGASTvgai 213
Cdd:cd00203   59 TRQDFDgGTGGWAYLGRVCDSLrGVGVLQD--NQSGTKEGAQTIAHELGHALGFYHDHDRK----DRDDYPTIDDT---- 128

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 836726449 214 hipgTPTTATVGGSIMnSCFRSTETGE----WTSSDKTALYYLY 253
Cdd:cd00203  129 ----LNAEDDDYYSVM-SYTKGSFSDGqrkdFSQCDIDQINKLY 167
 
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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