NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1126537926|ref|WP_075175488|]
View 

matrixin family metalloprotease [Acinetobacter indicus]

Protein Classification

M10 family metallopeptidase domain-containing protein( domain architecture ID 1029656)

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 250-302 1.09e-14

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: 70.34  E-value: 1.09e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1126537926 250 SAADLRLTLAHEFGHALGLGHTHDPHALMHPLMQEQNLDHFQLTATDLALLQQ 302
Cdd:pfam00413 104 HGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFRLSQDDIKGIQQ 156
ZnMc super family cl00064
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 217-270 7.15e-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.


The actual alignment was detected with superfamily member cd04276:

Pssm-ID: 469599  Cd Length: 197  Bit Score: 40.00  E-value: 7.15e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1126537926 217 IDASVQQFNQRFQPRlfdkgsfdgktIRIYEFQSAADLRLTLAHEFGHALGLGH 270
Cdd:cd04276    90 LKADVILYSGFLRQD-----------QLWYEDLLAASLRYLLAHEVGHTLGLRH 132
 
Name Accession Description Interval E-value
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 250-302 1.09e-14

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: 70.34  E-value: 1.09e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1126537926 250 SAADLRLTLAHEFGHALGLGHTHDPHALMHPLMQEQNLDHFQLTATDLALLQQ 302
Cdd:pfam00413 104 HGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFRLSQDDIKGIQQ 156
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 253-302 4.18e-12

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: 62.99  E-value: 4.18e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1126537926 253 DLRLTLAHEFGHALGLGHTHDPHALMHPLMQEQNlDHFQLTATDLALLQQ 302
Cdd:cd04278   106 DLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPV-PKFKLSQDDIRGIQA 154
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 257-301 1.50e-07

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: 49.66  E-value: 1.50e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1126537926  257 TLAHEFGHALGLGHTHDPHA---LMHPLMQEQNLDHFQLTATDLALLQ 301
Cdd:smart00235  87 VAAHELGHALGLYHEQSRSDrdnYMYINYTNIDTRNFDLSEDDSLGIP 134
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
259-280 4.38e-04

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


Pssm-ID: 441517  Cd Length: 175  Bit Score: 40.33  E-value: 4.38e-04
                          10        20
                  ....*....|....*....|..
gi 1126537926 259 AHEFGHALGLGHTHDPHALMHP 280
Cdd:COG1913   128 VHELGHLFGLGHCPNPRCVMHF 149
ZnMc_MMP_like_2 cd04276
Zinc-dependent metalloprotease; MMP_like sub-family 2. A group of bacterial metalloproteinase ...
 217-270 7.15e-04

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: 40.00  E-value: 7.15e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1126537926 217 IDASVQQFNQRFQPRlfdkgsfdgktIRIYEFQSAADLRLTLAHEFGHALGLGH 270
Cdd:cd04276    90 LKADVILYSGFLRQD-----------QLWYEDLLAASLRYLLAHEVGHTLGLRH 132
 
Name Accession Description Interval E-value
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 250-302 1.09e-14

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: 70.34  E-value: 1.09e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1126537926 250 SAADLRLTLAHEFGHALGLGHTHDPHALMHPLMQEQNLDHFQLTATDLALLQQ 302
Cdd:pfam00413 104 HGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFRLSQDDIKGIQQ 156
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 253-302 4.18e-12

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: 62.99  E-value: 4.18e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1126537926 253 DLRLTLAHEFGHALGLGHTHDPHALMHPLMQEQNlDHFQLTATDLALLQQ 302
Cdd:cd04278   106 DLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPV-PKFKLSQDDIRGIQA 154
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 257-301 1.50e-07

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: 49.66  E-value: 1.50e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1126537926  257 TLAHEFGHALGLGHTHDPHA---LMHPLMQEQNLDHFQLTATDLALLQ 301
Cdd:smart00235  87 VAAHELGHALGLYHEQSRSDrdnYMYINYTNIDTRNFDLSEDDSLGIP 134
ZnMc_serralysin_like cd04277
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
 255-276 2.30e-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: 44.33  E-value: 2.30e-05
                          10        20
                  ....*....|....*....|..
gi 1126537926 255 RLTLAHEFGHALGLGHTHDPHA 276
Cdd:cd04277   114 YQTIIHEIGHALGLEHPGDYNG 135
ZnMc_MMP_like_1 cd04279
Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ...
 249-301 1.01e-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: 42.06  E-value: 1.01e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1126537926 249 QSAADLRLTLAHEFGHALGLGHTHD-PHALMHPlMQEQNLDHF-QLTATDLALLQ 301
Cdd:cd04279    99 RGAENLQAIALHELGHALGLWHHSDrPEDAMYP-SQGQGPDGNpTLSARDVATLK 152
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 250-273 3.04e-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: 40.56  E-value: 3.04e-04
                          10        20
                  ....*....|....*....|....
gi 1126537926 250 SAADLRLTLAHEFGHALGLGHTHD 273
Cdd:cd04268    90 SGARLRNTAEHELGHALGLRHNFA 113
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
259-280 4.38e-04

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


Pssm-ID: 441517  Cd Length: 175  Bit Score: 40.33  E-value: 4.38e-04
                          10        20
                  ....*....|....*....|..
gi 1126537926 259 AHEFGHALGLGHTHDPHALMHP 280
Cdd:COG1913   128 VHELGHLFGLGHCPNPRCVMHF 149
ZnMc_MMP_like_2 cd04276
Zinc-dependent metalloprotease; MMP_like sub-family 2. A group of bacterial metalloproteinase ...
 217-270 7.15e-04

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: 40.00  E-value: 7.15e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1126537926 217 IDASVQQFNQRFQPRlfdkgsfdgktIRIYEFQSAADLRLTLAHEFGHALGLGH 270
Cdd:cd04276    90 LKADVILYSGFLRQD-----------QLWYEDLLAASLRYLLAHEVGHTLGLRH 132
COG5549 COG5549
Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones]; ...
 242-282 2.33e-03

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


Pssm-ID: 444292 [Multi-domain]  Cd Length: 234  Bit Score: 38.51  E-value: 2.33e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1126537926 242 TIRIYEFQSAADLRLTLAHEFGHALGL-GHTHDPHALMHPLM 282
Cdd:COG5549   170 TILLSPNQTGKYLLATARHELGHALGIwGHSPSPTDAMYFSQ 211
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 253-274 3.88e-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: 37.50  E-value: 3.88e-03
                          10        20
                  ....*....|....*....|..
gi 1126537926 253 DLRLTLAHEFGHALGLGHTHDP 274
Cdd:cd00203    95 EGAQTIAHELGHALGFYHDHDR 116
 
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