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Conserved domains on  [gi|1895765417|gb|QNI66967|]
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matrixin family protein [Synechococcus sp. BMK-MC-1]

Protein Classification

zinc metalloprotease; M10 family metallopeptidase domain-containing protein( domain architecture ID 10136682)

zinc metalloprotease may be a member of the astacin-like protease family or the adamalysin/reprolysin-like protease family; M10 family metallopeptidase domain-containing protein is a metalloendopeptidase similar to matrix metalloproteinases that may be endopeptidases that degrade various components of the extracellular matrix

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 ...
 43-199 3.99e-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: 3.99e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895765417  43 PSLPQWCVWVEPAAgmeADRWERRWLQGMDAALASWAKLLPIVRVEDP---QRAHVRVERRRPPLRQLPGGWRASNGRSL 119
Cdd:cd04279     1 KSPIRVYIDPTPAP---PDSRAQSWLQAVKQAAAEWENVGPLKFVYNPeedNDADIVIFFDRPPPVGGAGGGLARAGFPL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895765417 120 LQVlevtraGRTLLEPRVTVLVSPGL--RASSLRATALHELGHAFGLWGHSDNPADAMAPVQGSSPV--LEPSADDRLTL 195
Cdd:cd04279    78 ISD------GNRKLFNRTDINLGPGQprGAENLQAIALHELGHALGLWHHSDRPEDAMYPSQGQGPDgnPTLSARDVATL 151


                  ....
gi 1895765417 196 EWIR 199
Cdd:cd04279   152 KRLY 155
 
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 ...
 43-199 3.99e-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: 3.99e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895765417  43 PSLPQWCVWVEPAAgmeADRWERRWLQGMDAALASWAKLLPIVRVEDP---QRAHVRVERRRPPLRQLPGGWRASNGRSL 119
Cdd:cd04279     1 KSPIRVYIDPTPAP---PDSRAQSWLQAVKQAAAEWENVGPLKFVYNPeedNDADIVIFFDRPPPVGGAGGGLARAGFPL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895765417 120 LQVlevtraGRTLLEPRVTVLVSPGL--RASSLRATALHELGHAFGLWGHSDNPADAMAPVQGSSPV--LEPSADDRLTL 195
Cdd:cd04279    78 ISD------GNRKLFNRTDINLGPGQprGAENLQAIALHELGHALGLWHHSDRPEDAMYPSQGQGPDgnPTLSARDVATL 151


                  ....
gi 1895765417 196 EWIR 199
Cdd:cd04279   152 KRLY 155
COG5549 COG5549
Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones]; ...
 49-203 9.71e-35

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


Pssm-ID: 444292 [Multi-domain]  Cd Length: 234  Bit Score: 123.26  E-value: 9.71e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895765417  49 CVWVEPAAGMEADRwERRWLQGMDAALASWAKLLPIVRVEDPQRAHVRVERRRPPLRqlPGGWRASNGRSLLQVLEVTRA 128
Cdd:COG5549    85 KVYIDRPPSAAQQR-AQQWVAAVLQAIAEWNAYLPLEVVENPENADIIIVRSNPPLT--ASPNPETGARSAETTYEFYDT 161

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1895765417 129 GRTLLePRVTVLVSPGLRASSLRATALHELGHAFGLWGHSDNPADAMAPvQGSSPVLEPSADDRLTLEWIRRQPT 203
Cdd:COG5549   162 GNILS-HRFTILLSPNQTGKYLLATARHELGHALGIWGHSPSPTDAMYF-SQVRNPPPISPRDINTLKRIYQQPT 234
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 146-192 5.39e-06

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: 44.92  E-value: 5.39e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1895765417 146 RASSLRATALHELGHAFGLwGHSDNPADAMAPV--QGSSPVLEPSADDR 192
Cdd:pfam00413 104 HGINLFLVAAHEIGHALGL-GHSSDPGAIMYPTysPLDSKKFRLSQDDI 151
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 152-173 7.77e-03

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: 35.40  E-value: 7.77e-03
                           10        20
                   ....*....|....*....|..
gi 1895765417  152 ATALHELGHAFGLWgHSDNPAD 173
Cdd:smart00235  86 GVAAHELGHALGLY-HEQSRSD 106
 
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 ...
 43-199 3.99e-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: 3.99e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895765417  43 PSLPQWCVWVEPAAgmeADRWERRWLQGMDAALASWAKLLPIVRVEDP---QRAHVRVERRRPPLRQLPGGWRASNGRSL 119
Cdd:cd04279     1 KSPIRVYIDPTPAP---PDSRAQSWLQAVKQAAAEWENVGPLKFVYNPeedNDADIVIFFDRPPPVGGAGGGLARAGFPL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895765417 120 LQVlevtraGRTLLEPRVTVLVSPGL--RASSLRATALHELGHAFGLWGHSDNPADAMAPVQGSSPV--LEPSADDRLTL 195
Cdd:cd04279    78 ISD------GNRKLFNRTDINLGPGQprGAENLQAIALHELGHALGLWHHSDRPEDAMYPSQGQGPDgnPTLSARDVATL 151


                  ....
gi 1895765417 196 EWIR 199
Cdd:cd04279   152 KRLY 155
COG5549 COG5549
Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones]; ...
 49-203 9.71e-35

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


Pssm-ID: 444292 [Multi-domain]  Cd Length: 234  Bit Score: 123.26  E-value: 9.71e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895765417  49 CVWVEPAAGMEADRwERRWLQGMDAALASWAKLLPIVRVEDPQRAHVRVERRRPPLRqlPGGWRASNGRSLLQVLEVTRA 128
Cdd:COG5549    85 KVYIDRPPSAAQQR-AQQWVAAVLQAIAEWNAYLPLEVVENPENADIIIVRSNPPLT--ASPNPETGARSAETTYEFYDT 161

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1895765417 129 GRTLLePRVTVLVSPGLRASSLRATALHELGHAFGLWGHSDNPADAMAPvQGSSPVLEPSADDRLTLEWIRRQPT 203
Cdd:COG5549   162 GNILS-HRFTILLSPNQTGKYLLATARHELGHALGIWGHSPSPTDAMYF-SQVRNPPPISPRDINTLKRIYQQPT 234
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 146-193 9.12e-08

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: 49.90  E-value: 9.12e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1895765417 146 RASSLRATALHELGHAFGLwGHSDNPADAMAP-VQGSSPVLEPSADDRL 193
Cdd:cd04278   103 GGTDLFSVAAHEIGHALGL-GHSSDPDSIMYPyYQGPVPKFKLSQDDIR 150
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 146-192 5.39e-06

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: 44.92  E-value: 5.39e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1895765417 146 RASSLRATALHELGHAFGLwGHSDNPADAMAPV--QGSSPVLEPSADDR 192
Cdd:pfam00413 104 HGINLFLVAAHEIGHALGL-GHSSDPGAIMYPTysPLDSKKFRLSQDDI 151
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 65-187 5.70e-06

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: 44.82  E-value: 5.70e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895765417  65 RRWLQGMDAALASWAKLLPI---VRVEDPQRAHVRVERRRPPLRQLPGGW--RASNGRSLLQVlevtragrtlleprvTV 139
Cdd:cd00203    21 AQIQSLILIAMQIWRDYLNIrfvLVGVEIDKADIAILVTRQDFDGGTGGWayLGRVCDSLRGV---------------GV 85

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1895765417 140 LVSPGLRASSLRATALHELGHAFGLWGHSDNPADAMAPVQGSSPVLEP 187
Cdd:cd00203    86 LQDNQSGTKEGAQTIAHELGHALGFYHDHDRKDRDDYPTIDDTLNAED 133
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 61-207 1.42e-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: 43.64  E-value: 1.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895765417  61 DRWERRWLQGMDAalasWAKLLPI--VRVEDPQRAHVRVERRRPPLRQlPGGW----RASNGRSLlqvlEVTRAGRTLLE 134
Cdd:cd04268    14 DKLRAAILDAIEA----WNKAFAIgfKNANDVDPADIRYSVIRWIPYN-DGTWsygpSQVDPLTG----EILLARVYLYS 84

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1895765417 135 PRVtvlvspGLRASSLRATALHELGHAFGLWGHSDNPADAMAPVQGSSPVLEPS----ADDRLTLEWIRRQPTGFGQ 207
Cdd:cd04268    85 SFV------EYSGARLRNTAEHELGHALGLRHNFAASDRDDNVDLLAEKGDTSSvmdyAPSNFSIQLGDGQKYTIGP 155
Peptidase_M54 cd11375
Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 ...
 153-192 1.57e-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: 40.74  E-value: 1.57e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1895765417 153 TALHELGHAFGLwGHSDNPADAMapvQGSSPVLEpsaDDR 192
Cdd:cd11375   126 EAVHELGHLFGL-DHCPYYACVM---NFSNSLEE---TDR 158
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 152-173 7.77e-03

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: 35.40  E-value: 7.77e-03
                           10        20
                   ....*....|....*....|..
gi 1895765417  152 ATALHELGHAFGLWgHSDNPAD 173
Cdd:smart00235  86 GVAAHELGHALGLY-HEQSRSD 106
 
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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