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Conserved domains on  [gi|499819189|ref|WP_011499923|]
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matrixin family metalloprotease [Methanococcoides burtonii]

Protein Classification

ZnMc_MMP_like_1 domain-containing protein( domain architecture ID 10136682)

ZnMc_MMP_like_1 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ZnMc_MMP_like_1 cd04279
Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ...
 39-191 5.14e-42

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: 139.90  E-value: 5.14e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499819189  39 HSPITVYIDDVNTPP-HYSHTYRKAIVDATEYWETGGNGKLYYEPDFeiidSPDADIYVMWVETMEeVTGAEDGVAGYCR 117
Cdd:cd04279    1 KSPIRVYIDPTPAPPdSRAQSWLQAVKQAAAEWENVGPLKFVYNPEE----DNDADIVIFFDRPPP-VGGAGGGLARAGF 75

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499819189 118 PEIS---AGRFIRASIVLEVGdkrglswQQYGDANMEQIAIHELGHALGLDHSNDKK-DIMYPSYEQRDNVNPLLLEK 191
Cdd:cd04279   76 PLISdgnRKLFNRTDINLGPG-------QPRGAENLQAIALHELGHALGLWHHSDRPeDAMYPSQGQGPDGNPTLSAR 146
 
Name Accession Description Interval E-value
ZnMc_MMP_like_1 cd04279
Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ...
 39-191 5.14e-42

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: 139.90  E-value: 5.14e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499819189  39 HSPITVYIDDVNTPP-HYSHTYRKAIVDATEYWETGGNGKLYYEPDFeiidSPDADIYVMWVETMEeVTGAEDGVAGYCR 117
Cdd:cd04279    1 KSPIRVYIDPTPAPPdSRAQSWLQAVKQAAAEWENVGPLKFVYNPEE----DNDADIVIFFDRPPP-VGGAGGGLARAGF 75

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499819189 118 PEIS---AGRFIRASIVLEVGdkrglswQQYGDANMEQIAIHELGHALGLDHSNDKK-DIMYPSYEQRDNVNPLLLEK 191
Cdd:cd04279   76 PLISdgnRKLFNRTDINLGPG-------QPRGAENLQAIALHELGHALGLWHHSDRPeDAMYPSQGQGPDGNPTLSAR 146
COG5549 COG5549
Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones]; ...
 37-187 1.13e-13

Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444292 [Multi-domain]  Cd Length: 234  Bit Score: 67.79  E-value: 1.13e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499819189  37 WDHSPITVYID-DVNTPPHYSHTYRKAIVDATEYWEtggngklYYEPdFEIIDSPD-ADIYVMWVET-----MEEVTGAE 109
Cdd:COG5549   79 WSQFPVKVYIDrPPSAAQQRAQQWVAAVLQAIAEWN-------AYLP-LEVVENPEnADIIIVRSNPpltasPNPETGAR 150

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499819189 110 DGVAGYcRPEISaGRFIRASIVLEVGDkrglswqQYGDANMEQIAIHELGHALGL-DHSNDKKDIMYPSyeQRDNVNPL 187
Cdd:COG5549  151 SAETTY-EFYDT-GNILSHRFTILLSP-------NQTGKYLLATARHELGHALGIwGHSPSPTDAMYFS--QVRNPPPI 218
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 148-185 8.78e-12

Matrixin; The members of this family are enzymes that cleave peptides. These proteases require zinc for catalysis.


Pssm-ID: 425668 [Multi-domain]  Cd Length: 159  Bit Score: 61.09  E-value: 8.78e-12
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 499819189  148 ANMEQIAIHELGHALGLDHSNDKKDIMYPSYEQRDNVN 185
Cdd:pfam00413 106 INLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKK 143
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 152-182 4.72e-06

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: 44.65  E-value: 4.72e-06
                           10        20        30
                   ....*....|....*....|....*....|....
gi 499819189   152 QIAIHELGHALGLDHS---NDKKDIMYPSYEQRD 182
Cdd:smart00235  86 GVAAHELGHALGLYHEqsrSDRDNYMYINYTNID 119
 
Name Accession Description Interval E-value
ZnMc_MMP_like_1 cd04279
Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ...
 39-191 5.14e-42

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: 139.90  E-value: 5.14e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499819189  39 HSPITVYIDDVNTPP-HYSHTYRKAIVDATEYWETGGNGKLYYEPDFeiidSPDADIYVMWVETMEeVTGAEDGVAGYCR 117
Cdd:cd04279    1 KSPIRVYIDPTPAPPdSRAQSWLQAVKQAAAEWENVGPLKFVYNPEE----DNDADIVIFFDRPPP-VGGAGGGLARAGF 75

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499819189 118 PEIS---AGRFIRASIVLEVGdkrglswQQYGDANMEQIAIHELGHALGLDHSNDKK-DIMYPSYEQRDNVNPLLLEK 191
Cdd:cd04279   76 PLISdgnRKLFNRTDINLGPG-------QPRGAENLQAIALHELGHALGLWHHSDRPeDAMYPSQGQGPDGNPTLSAR 146
COG5549 COG5549
Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones]; ...
 37-187 1.13e-13

Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444292 [Multi-domain]  Cd Length: 234  Bit Score: 67.79  E-value: 1.13e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499819189  37 WDHSPITVYID-DVNTPPHYSHTYRKAIVDATEYWEtggngklYYEPdFEIIDSPD-ADIYVMWVET-----MEEVTGAE 109
Cdd:COG5549   79 WSQFPVKVYIDrPPSAAQQRAQQWVAAVLQAIAEWN-------AYLP-LEVVENPEnADIIIVRSNPpltasPNPETGAR 150

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499819189 110 DGVAGYcRPEISaGRFIRASIVLEVGDkrglswqQYGDANMEQIAIHELGHALGL-DHSNDKKDIMYPSyeQRDNVNPL 187
Cdd:COG5549  151 SAETTY-EFYDT-GNILSHRFTILLSP-------NQTGKYLLATARHELGHALGIwGHSPSPTDAMYFS--QVRNPPPI 218
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 148-185 8.78e-12

Matrixin; The members of this family are enzymes that cleave peptides. These proteases require zinc for catalysis.


Pssm-ID: 425668 [Multi-domain]  Cd Length: 159  Bit Score: 61.09  E-value: 8.78e-12
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 499819189  148 ANMEQIAIHELGHALGLDHSNDKKDIMYPSYEQRDNVN 185
Cdd:pfam00413 106 INLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKK 143
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 149-183 4.65e-11

Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are responsible for a great deal of pericellular proteolysis of extracellular matrix and cell surface molecules, playing crucial roles in morphogenesis, cell fate specification, cell migration, tissue repair, tumorigenesis, gain or loss of tissue-specific functions, and apoptosis. In many instances, they are anchored to cell membranes via trans-membrane domains, and their activity is controlled via TIMPs (tissue inhibitors of metalloproteinases).


Pssm-ID: 239805 [Multi-domain]  Cd Length: 157  Bit Score: 59.14  E-value: 4.65e-11
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 499819189 149 NMEQIAIHELGHALGLDHSNDKKDIMYPSYEQRDN 183
Cdd:cd04278  106 DLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVP 140
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 41-173 2.53e-08

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: 51.73  E-value: 2.53e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499819189  41 PITVYIDDvntppHYSHTYRKAIVDATEYWETGG-----NGKLYYEPDFEIIDSPDADIYVMWVETMEEVTGAEDGvagy 115
Cdd:cd04268    3 PITYYIDD-----SVPDKLRAAILDAIEAWNKAFaigfkNANDVDPADIRYSVIRWIPYNDGTWSYGPSQVDPLTG---- 73

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 499819189 116 crpEISAGRFIRASivlevgdkrglSWQQYGDANMEQIAIHELGHALGLDHSNDKKDI 173
Cdd:cd04268   74 ---EILLARVYLYS-----------SFVEYSGARLRNTAEHELGHALGLRHNFAASDR 117
ZnMc_MMP_like_2 cd04276
Zinc-dependent metalloprotease; MMP_like sub-family 2. A group of bacterial metalloproteinase ...
 33-182 7.66e-07

Zinc-dependent metalloprotease; MMP_like sub-family 2. A group of bacterial metalloproteinase domains similar to matrix metalloproteinases and astacin.


Pssm-ID: 239803  Cd Length: 197  Bit Score: 48.09  E-value: 7.66e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499819189  33 FDEPwdHSPITVYIDDvNTPphysHTYRKAIVDATEYWETGgngklyyepdFEIIDSPDADIyvmwVETMEEVTGAED-- 110
Cdd:cd04276    3 LSEP--KEPIVYYLDN-TFP----EKYRDAIREGVLYWNKA----------FEKAGFKNAII----VKVLPDDADPGDir 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499819189 111 -----------GVAGYCrPEIS---AGRFIRASIVLEVGDKR---GLSWQQYGDAnMEQIAIHELGHALGLDHsNDKKDI 173
Cdd:cd04276   62 ynvirwihspnGGWAYG-PSVVdprTGEILKADVILYSGFLRqdqLWYEDLLAAS-LRYLLAHEVGHTLGLRH-NFKASS 138


                 ....*....
gi 499819189 174 MYPSYEQRD 182
Cdd:cd04276  139 DGSNEELED 147
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 152-182 4.72e-06

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: 44.65  E-value: 4.72e-06
                           10        20        30
                   ....*....|....*....|....*....|....
gi 499819189   152 QIAIHELGHALGLDHS---NDKKDIMYPSYEQRD 182
Cdd:smart00235  86 GVAAHELGHALGLYHEqsrSDRDNYMYINYTNID 119
ZnMc_serralysin_like cd04277
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
 32-172 2.56e-05

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: 43.56  E-value: 2.56e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499819189  32 FFDEPWDHSPITVYIDDVNTPPHYSHTYRKAIVDATEYWETggngklYYEPDF-EIIDSPDADIYVMWVetmeevTGAED 110
Cdd:cd04277    8 FSNTGGPYSYGYGREEDTTNTAALSAAQQAAARDALEAWED------VADIDFvEVSDNSGADIRFGNS------SDPDG 75

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499819189 111 GVAGYCRPEISAGRFIRASivlEVGDKRGLSWQQYGDANME-QIAIHELGHALGLDHSNDKKD 172
Cdd:cd04277   76 NTAGYAYYPGSGSGTAYGG---DIWFNSSYDTNSDSPGSYGyQTIIHEIGHALGLEHPGDYNG 135
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
154-177 5.11e-05

Predicted Zn-dependent protease [General function prediction only];


Pssm-ID: 441517  Cd Length: 175  Bit Score: 42.25  E-value: 5.11e-05
                         10        20
                 ....*....|....*....|....
gi 499819189 154 AIHELGHALGLDHSNDKKDIMYPS 177
Cdd:COG1913  127 AVHELGHLFGLGHCPNPRCVMHFS 150
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 41-186 3.41e-04

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: 39.81  E-value: 3.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499819189  41 PITVYIDDVNTPPH---YSHTYRKAIVDATEYWETGGNGKLYYEPdfEIIDSPDADIYV-MWVETMEEVTGAEdgVAGYC 116
Cdd:cd00203    2 VIPYVVVADDRDVEeenLSAQIQSLILIAMQIWRDYLNIRFVLVG--VEIDKADIAILVtRQDFDGGTGGWAY--LGRVC 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499819189 117 RPEisagrfiRASIVLEVGdkrglswqQYGDANMEQIAIHELGHALGLDHSNDKKDI-MYPSYEQRDNVNP 186
Cdd:cd00203   78 DSL-------RGVGVLQDN--------QSGTKEGAQTIAHELGHALGFYHDHDRKDRdDYPTIDDTLNAED 133
Peptidase_M54 cd11375
Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 ...
 154-177 5.51e-04

Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 (archaemetzincin or archaelysin) is a zinc-dependent aminopeptidase that contains the consensus zinc-binding sequence HEXXHXXGXXH/D and a conserved Met residue at the active site, and is thus classified as a metzincin. Archaemetzincins, first identified in archaea, are also found in bacteria and eukaryotes, including two human members, archaemetzincin-1 and -2 (AMZ1 and AMZ2). AMZ1 is mainly found in the liver and heart while AMZ2 is primarily expressed in testis and heart; both have been reported to degrade synthetic substrates and peptides. The Peptidase M54 family contains an extended metzincin concensus sequence of HEXXHXXGX3CX4CXMX17CXXC such that a second zinc ion is bound to four cysteines, thus resembling a zinc finger. Phylogenetic analysis of this family reveals a complex evolutionary process involving a series of lateral gene transfer, gene loss and genetic duplication events.


Pssm-ID: 213029  Cd Length: 173  Bit Score: 39.59  E-value: 5.51e-04
                         10        20
                 ....*....|....*....|....
gi 499819189 154 AIHELGHALGLDHSNDKKDIMYPS 177
Cdd:cd11375  127 AVHELGHLFGLDHCPYYACVMNFS 150
 
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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