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Conserved domains on  [gi|818241956|gb|KKP29095|]
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Peptidase M10A and M12B matrixin and adamalysin [Candidatus Nomurabacteria bacterium GW2011_GWE2_31_40]

Protein Classification

M10 family metallopeptidase domain-containing protein( domain architecture ID 1002428)

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
Peptidase_M10 super family cl37987
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 265-307 2.68e-08

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


The actual alignment was detected with superfamily member pfam00413:

Pssm-ID: 425668 [Multi-domain]  Cd Length: 159  Bit Score: 52.23  E-value: 2.68e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 818241956  265 VLTHEFGHALGLGHLESPESVM---YRLNNGVNEKLTIEDILALKK 307
Cdd:pfam00413 111 VAAHEIGHALGLGHSSDPGAIMyptYSPLDSKKFRLSQDDIKGIQQ 156
 
Name Accession Description Interval E-value
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 265-307 2.68e-08

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: 52.23  E-value: 2.68e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 818241956  265 VLTHEFGHALGLGHLESPESVM---YRLNNGVNEKLTIEDILALKK 307
Cdd:pfam00413 111 VAAHEIGHALGLGHSSDPGAIMyptYSPLDSKKFRLSQDDIKGIQQ 156
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 265-307 1.42e-07

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: 50.28  E-value: 1.42e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 818241956 265 VLTHEFGHALGLGHLESPESVMY--RLNNGVNEKLTIEDILALKK 307
Cdd:cd04278  110 VAAHEIGHALGLGHSSDPDSIMYpyYQGPVPKFKLSQDDIRGIQA 154
COG5549 COG5549
Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones]; ...
 268-307 5.98e-05

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


Pssm-ID: 444292 [Multi-domain]  Cd Length: 234  Bit Score: 43.52  E-value: 5.98e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 818241956 268 HEFGHALGL-GHLESPESVMYRLNNGVNEKLTIEDILALKK 307
Cdd:COG5549  188 HELGHALGIwGHSPSPTDAMYFSQVRNPPPISPRDINTLKR 228
archmetzin NF033823
archaemetzincin family Zn-dependent metalloprotease;
264-295 1.25e-03

archaemetzincin family Zn-dependent metalloprotease;


Pssm-ID: 468195  Cd Length: 170  Bit Score: 38.75  E-value: 1.25e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 818241956 264 RVL---THEFGHALGLGHLESPESVMYRlNNGVNE 295
Cdd:NF033823 121 RLAkeaVHELGHLLGLGHCPNPRCVMHF-SNSLDD 154
 
Name Accession Description Interval E-value
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 265-307 2.68e-08

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: 52.23  E-value: 2.68e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 818241956  265 VLTHEFGHALGLGHLESPESVM---YRLNNGVNEKLTIEDILALKK 307
Cdd:pfam00413 111 VAAHEIGHALGLGHSSDPGAIMyptYSPLDSKKFRLSQDDIKGIQQ 156
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 265-307 1.42e-07

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: 50.28  E-value: 1.42e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 818241956 265 VLTHEFGHALGLGHLESPESVMY--RLNNGVNEKLTIEDILALKK 307
Cdd:cd04278  110 VAAHEIGHALGLGHSSDPDSIMYpyYQGPVPKFKLSQDDIRGIQA 154
COG5549 COG5549
Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones]; ...
 268-307 5.98e-05

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


Pssm-ID: 444292 [Multi-domain]  Cd Length: 234  Bit Score: 43.52  E-value: 5.98e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 818241956 268 HEFGHALGL-GHLESPESVMYRLNNGVNEKLTIEDILALKK 307
Cdd:COG5549  188 HELGHALGIwGHSPSPTDAMYFSQVRNPPPISPRDINTLKR 228
ZnMc_MMP_like_1 cd04279
Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ...
 262-287 2.11e-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: 40.90  E-value: 2.11e-04
                         10        20
                 ....*....|....*....|....*..
gi 818241956 262 LARVLTHEFGHALGLGHLES-PESVMY 287
Cdd:cd04279  104 LQAIALHELGHALGLWHHSDrPEDAMY 130
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 262-307 2.66e-04

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: 40.94  E-value: 2.66e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818241956 262 LARVLTHEFGHALGLGH----------------LESPESVMY------RLNNGVNEKLTIE--DILALKK 307
Cdd:cd04268   94 LRNTAEHELGHALGLRHnfaasdrddnvdllaeKGDTSSVMDyapsnfSIQLGDGQKYTIGpyDIAAIKK 163
archmetzin NF033823
archaemetzincin family Zn-dependent metalloprotease;
264-295 1.25e-03

archaemetzincin family Zn-dependent metalloprotease;


Pssm-ID: 468195  Cd Length: 170  Bit Score: 38.75  E-value: 1.25e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 818241956 264 RVL---THEFGHALGLGHLESPESVMYRlNNGVNE 295
Cdd:NF033823 121 RLAkeaVHELGHLLGLGHCPNPRCVMHF-SNSLDD 154
Peptidase_M54 cd11375
Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 ...
 262-287 3.15e-03

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: 37.66  E-value: 3.15e-03
                         10        20
                 ....*....|....*....|....*.
gi 818241956 262 LARVLTHEFGHALGLGHLESPESVMY 287
Cdd:cd11375  123 LLKEAVHELGHLFGLDHCPYYACVMN 148
ZnMc_serralysin_like cd04277
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
 265-307 3.59e-03

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: 37.78  E-value: 3.59e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 818241956 265 VLTHEFGHALGLGH---------------LESPE-SVM-YR--LNNGVNEK------LTIEDILALKK 307
Cdd:cd04277  116 TIIHEIGHALGLEHpgdynggdpvpptyaLDSREyTVMsYNsgYGNGASAGggypqtPMLLDIAALQY 183
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
264-287 4.48e-03

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


Pssm-ID: 441517  Cd Length: 175  Bit Score: 37.24  E-value: 4.48e-03
                         10        20
                 ....*....|....*....|....*..
gi 818241956 264 RVL---THEFGHALGLGHLESPESVMY 287
Cdd:COG1913  122 RVLkeaVHELGHLFGLGHCPNPRCVMH 148
 
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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