NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2785235988|ref|WP_369680545|]
View 

matrixin family metalloprotease [Thomasclavelia spiroformis]

Protein Classification

zinc metalloprotease( domain architecture ID 1881)

zinc metalloprotease may be a member of the astacin-like protease family or the adamalysin/reprolysin-like protease family

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
ZnMc super family cl00064
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
22-68 3.67e-07

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.


The actual alignment was detected with superfamily member cd04278:

Pssm-ID: 469599 [Multi-domain]  Cd Length: 157  Bit Score: 44.12  E-value: 3.67e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2785235988  22 SVAAHQLGHPYGLGDLSSGNSLMS-HARNRNTIYKPQTDDINGIKRIY 68
Cdd:cd04278   109 SVAAHEIGHALGLGHSSDPDSIMYpYYQGPVPKFKLSQDDIRGIQALY 156
 
Name Accession Description Interval E-value
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
22-68 3.67e-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: 44.12  E-value: 3.67e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2785235988  22 SVAAHQLGHPYGLGDLSSGNSLMS-HARNRNTIYKPQTDDINGIKRIY 68
Cdd:cd04278   109 SVAAHEIGHALGLGHSSDPDSIMYpYYQGPVPKFKLSQDDIRGIQALY 156
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
17-68 2.38e-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: 42.22  E-value: 2.38e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2785235988  17 GNVYQSVAAHQLGHPYGLGDLSSGNSLM----SHARNRNtiYKPQTDDINGIKRIY 68
Cdd:pfam00413 105 GINLFLVAAHEIGHALGLGHSSDPGAIMyptySPLDSKK--FRLSQDDIKGIQQLY 158
COG5549 COG5549
Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones]; ...
12-68 2.79e-03

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


Pssm-ID: 444292 [Multi-domain]  Cd Length: 234  Bit Score: 33.89  E-value: 2.79e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2785235988  12 NTNITGNVYQSVAAHQLGHPYGL-GDLSSGNSLMSHARNRNtIYKPQTDDINGIKRIY 68
Cdd:COG5549   174 SPNQTGKYLLATARHELGHALGIwGHSPSPTDAMYFSQVRN-PPPISPRDINTLKRIY 230
 
Name Accession Description Interval E-value
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
22-68 3.67e-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: 44.12  E-value: 3.67e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2785235988  22 SVAAHQLGHPYGLGDLSSGNSLMS-HARNRNTIYKPQTDDINGIKRIY 68
Cdd:cd04278   109 SVAAHEIGHALGLGHSSDPDSIMYpYYQGPVPKFKLSQDDIRGIQALY 156
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
17-68 2.38e-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: 42.22  E-value: 2.38e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2785235988  17 GNVYQSVAAHQLGHPYGLGDLSSGNSLM----SHARNRNtiYKPQTDDINGIKRIY 68
Cdd:pfam00413 105 GINLFLVAAHEIGHALGLGHSSDPGAIMyptySPLDSKK--FRLSQDDIKGIQQLY 158
COG5549 COG5549
Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones]; ...
12-68 2.79e-03

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


Pssm-ID: 444292 [Multi-domain]  Cd Length: 234  Bit Score: 33.89  E-value: 2.79e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2785235988  12 NTNITGNVYQSVAAHQLGHPYGL-GDLSSGNSLMSHARNRNtIYKPQTDDINGIKRIY 68
Cdd:COG5549   174 SPNQTGKYLLATARHELGHALGIwGHSPSPTDAMYFSQVRN-PPPISPRDINTLKRIY 230
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH