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Conserved domains on  [gi|17553904|ref|NP_497594|]
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Matrix metalloproteinase-B [Caenorhabditis elegans]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 134-321 3.33e-62

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: 200.51  E-value: 3.33e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17553904 134 KWAHasgqsVTLKWYISDYTSDIDRLETRKVVEKAFKLWSSQSyiknekkvTLTFQEASSKDEADINILWAEGNHGDEHD 213
Cdd:cd04278   1 KWSK-----TNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVT--------PLTFREVTSGQEADIRISFARGNHGDGYP 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17553904 214 FDGANGkiegnkkenVLAHTFFPGyarPLNGDIHFDDAEDWEIDVDqvGHGSNkrfFPYVLAHEIGHALGLDHSQKADAL 293
Cdd:cd04278  68 FDGPGG---------TLAHAFFPG---GIGGDIHFDDDEQWTLGSD--SGGTD---LFSVAAHEIGHALGLGHSSDPDSI 130

                       170       180
                ....*....|....*....|....*...
gi 17553904 294 MHPYYKNvPINEIQLDIDDKCGVIWNYG 321
Cdd:cd04278 131 MYPYYQG-PVPKFKLSQDDIRGIQALYG 157
 
Name Accession Description Interval E-value
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 134-321 3.33e-62

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: 200.51  E-value: 3.33e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17553904 134 KWAHasgqsVTLKWYISDYTSDIDRLETRKVVEKAFKLWSSQSyiknekkvTLTFQEASSKDEADINILWAEGNHGDEHD 213
Cdd:cd04278   1 KWSK-----TNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVT--------PLTFREVTSGQEADIRISFARGNHGDGYP 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17553904 214 FDGANGkiegnkkenVLAHTFFPGyarPLNGDIHFDDAEDWEIDVDqvGHGSNkrfFPYVLAHEIGHALGLDHSQKADAL 293
Cdd:cd04278  68 FDGPGG---------TLAHAFFPG---GIGGDIHFDDDEQWTLGSD--SGGTD---LFSVAAHEIGHALGLGHSSDPDSI 130

                       170       180
                ....*....|....*....|....*...
gi 17553904 294 MHPYYKNvPINEIQLDIDDKCGVIWNYG 321
Cdd:cd04278 131 MYPYYQG-PVPKFKLSQDDIRGIQALYG 157
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 144-321 9.83e-61

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: 196.68  E-value: 9.83e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17553904   144 TLKWYISDYTSDIDRLETRKVVEKAFKLWSSQSyiknekkvTLTFQEASSkDEADINILWAEGNHGDEHDFDGANGkieg 223
Cdd:pfam00413   6 NLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVT--------PLTFTEVST-GEADIMIGFGRGDHGDGYPFDGPGG---- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17553904   224 nkkenVLAHTFFPGyaRPLNGDIHFDDAEDWEIDvDQVGHGSNkrfFPYVLAHEIGHALGLDHSQKADALMHPYYKNVPI 303
Cdd:pfam00413  73 -----VLAHAFFPG--PGLGGDIHFDDDETWTVG-SDPPHGIN---LFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDS 141

                         170
                  ....*....|....*...
gi 17553904   304 NEIQLDIDDKCGVIWNYG 321
Cdd:pfam00413 142 KKFRLSQDDIKGIQQLYG 159
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 134-321 5.92e-21

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: 88.95  E-value: 5.92e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17553904    134 KWAHAsgqsvTLKWYIsdYTSDIDRlETRKVVEKAFKLWSSQSyiknekkvTLTFQEASSkdEADINILWAEGNHGdehd 213
Cdd:smart00235   4 KWPKG-----TVPYVI--DSSSLSP-EEREAIAKALAEWSDVT--------CIRFVERTG--TADIYISFGSGDSG---- 61

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17553904    214 fdgangkiegnkkeNVLAHTFFPGyarplnGDIHFDDaEDWEIDVDqvghgsnkrffpyVLAHEIGHALGLDHSQKA--- 290
Cdd:smart00235  62 --------------CTLSHAGRPG------GDQHLSL-GNGCINTG-------------VAAHELGHALGLYHEQSRsdr 107

                          170       180       190
                   ....*....|....*....|....*....|.
gi 17553904    291 DALMHPYYKNVPINEIQLDIDDKCGVIWNYG 321
Cdd:smart00235 108 DNYMYINYTNIDTRNFDLSEDDSLGIPYDYG 138
fragilysin TIGR03935
fragilysin; Members of this family are fragilysin, the Bacteroides fragilis enterotoxin. This ...
 262-298 6.31e-03

fragilysin; Members of this family are fragilysin, the Bacteroides fragilis enterotoxin. This enzyme is a Zn metalloprotease. Three distinct subtypes included in this family all are produced by enterotoxigenic (by definition) strains of Bacteroides fragilis. [Cellular processes, Pathogenesis]


Pssm-ID: 188450 [Multi-domain]  Cd Length: 386  Bit Score: 38.79  E-value: 6.31e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 17553904   262 GHGSNKRFFPYVLAHEIGHALGLDHSQKADALMHPYY 298
Cdd:TIGR03935 330 GMSTTQLMYPGTLAHELGHILGAEHTDNEKDLMYTWY 366
 
Name Accession Description Interval E-value
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 134-321 3.33e-62

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: 200.51  E-value: 3.33e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17553904 134 KWAHasgqsVTLKWYISDYTSDIDRLETRKVVEKAFKLWSSQSyiknekkvTLTFQEASSKDEADINILWAEGNHGDEHD 213
Cdd:cd04278   1 KWSK-----TNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVT--------PLTFREVTSGQEADIRISFARGNHGDGYP 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17553904 214 FDGANGkiegnkkenVLAHTFFPGyarPLNGDIHFDDAEDWEIDVDqvGHGSNkrfFPYVLAHEIGHALGLDHSQKADAL 293
Cdd:cd04278  68 FDGPGG---------TLAHAFFPG---GIGGDIHFDDDEQWTLGSD--SGGTD---LFSVAAHEIGHALGLGHSSDPDSI 130

                       170       180
                ....*....|....*....|....*...
gi 17553904 294 MHPYYKNvPINEIQLDIDDKCGVIWNYG 321
Cdd:cd04278 131 MYPYYQG-PVPKFKLSQDDIRGIQALYG 157
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 144-321 9.83e-61

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: 196.68  E-value: 9.83e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17553904   144 TLKWYISDYTSDIDRLETRKVVEKAFKLWSSQSyiknekkvTLTFQEASSkDEADINILWAEGNHGDEHDFDGANGkieg 223
Cdd:pfam00413   6 NLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVT--------PLTFTEVST-GEADIMIGFGRGDHGDGYPFDGPGG---- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17553904   224 nkkenVLAHTFFPGyaRPLNGDIHFDDAEDWEIDvDQVGHGSNkrfFPYVLAHEIGHALGLDHSQKADALMHPYYKNVPI 303
Cdd:pfam00413  73 -----VLAHAFFPG--PGLGGDIHFDDDETWTVG-SDPPHGIN---LFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDS 141

                         170
                  ....*....|....*...
gi 17553904   304 NEIQLDIDDKCGVIWNYG 321
Cdd:pfam00413 142 KKFRLSQDDIKGIQQLYG 159
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 134-321 5.92e-21

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: 88.95  E-value: 5.92e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17553904    134 KWAHAsgqsvTLKWYIsdYTSDIDRlETRKVVEKAFKLWSSQSyiknekkvTLTFQEASSkdEADINILWAEGNHGdehd 213
Cdd:smart00235   4 KWPKG-----TVPYVI--DSSSLSP-EEREAIAKALAEWSDVT--------CIRFVERTG--TADIYISFGSGDSG---- 61

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17553904    214 fdgangkiegnkkeNVLAHTFFPGyarplnGDIHFDDaEDWEIDVDqvghgsnkrffpyVLAHEIGHALGLDHSQKA--- 290
Cdd:smart00235  62 --------------CTLSHAGRPG------GDQHLSL-GNGCINTG-------------VAAHELGHALGLYHEQSRsdr 107

                          170       180       190
                   ....*....|....*....|....*....|.
gi 17553904    291 DALMHPYYKNVPINEIQLDIDDKCGVIWNYG 321
Cdd:smart00235 108 DNYMYINYTNIDTRNFDLSEDDSLGIPYDYG 138
ZnMc_serralysin_like cd04277
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
 160-288 1.45e-11

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: 63.20  E-value: 1.45e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17553904 160 ETRKVVEKAFKLWSSqsyiknekkVT-LTFQEASSKDEADINILWaegnhgdehdFDGANGkiegnkkeNVLAHTFFPG- 237
Cdd:cd04277  34 AQQAAARDALEAWED---------VAdIDFVEVSDNSGADIRFGN----------SSDPDG--------NTAGYAYYPGs 86

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 17553904 238 -YARPLNGDIHFDDAEDWEIDVDqvghGSnkrFFPYVLAHEIGHALGLDHSQ 288
Cdd:cd04277  87 gSGTAYGGDIWFNSSYDTNSDSP----GS---YGYQTIIHEIGHALGLEHPG 131
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 144-290 5.49e-09

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: 55.20  E-value: 5.49e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17553904 144 TLKWYISDYTSDidrlETRKVVEKAFKLWssqsyiknEKKVTLTFQEASSKDEADINIlwaeGNHGDEHDFDGANGkieg 223
Cdd:cd04268   3 PITYYIDDSVPD----KLRAAILDAIEAW--------NKAFAIGFKNANDVDPADIRY----SVIRWIPYNDGTWS---- 62

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17553904 224 nkkenvlahtFFPGYARPLNGDIHFDDaedweIDVDQVGHGSNKRFFPYVLAHEIGHALGLDHSQKA 290
Cdd:cd04268  63 ----------YGPSQVDPLTGEILLAR-----VYLYSSFVEYSGARLRNTAEHELGHALGLRHNFAA 114
ZnMc_MMP_like_1 cd04279
Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ...
 143-321 6.84e-09

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: 54.77  E-value: 6.84e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17553904 143 VTLKWYISDYTSDIDRLETR--KVVEKAFKLWSSQSyiknekkvTLTF-QEASSKDEADINILWaegnhgdehDFDGANG 219
Cdd:cd04279   2 SPIRVYIDPTPAPPDSRAQSwlQAVKQAAAEWENVG--------PLKFvYNPEEDNDADIVIFF---------DRPPPVG 64

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17553904 220 KIEGnkkenVLAHTFFPGYARPLNGDIHFDDaedweiDVDQVGHGSNKRFFPYVLAHEIGHALGLDHS--QKADAlMHPY 297
Cdd:cd04279  65 GAGG-----GLARAGFPLISDGNRKLFNRTD------INLGPGQPRGAENLQAIALHELGHALGLWHHsdRPEDA-MYPS 132

                       170       180
                ....*....|....*....|....
gi 17553904 298 YKNVPINEIQLDIDDKCGVIWNYG 321
Cdd:cd04279 133 QGQGPDGNPTLSARDVATLKRLYG 156
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 223-288 2.49e-05

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: 2.49e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17553904 223 GNKKENVLAHTFFPGYARPLNGDIHFDDaedweidvdqvgHGSNKRFFPYVLAHEIGHALGLDHSQ 288
Cdd:cd00203  61 QDFDGGTGGWAYLGRVCDSLRGVGVLQD------------NQSGTKEGAQTIAHELGHALGFYHDH 114
ZnMc_MMP_like_2 cd04276
Zinc-dependent metalloprotease; MMP_like sub-family 2. A group of bacterial metalloproteinase ...
 242-302 1.14e-03

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: 40.39  E-value: 1.14e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17553904 242 LNGDIHFDDA---EDWEIDVDQVGHgsnkrFFPYVLAHEIGHALGLDHSQKADALMHPYYKNVP 302
Cdd:cd04276  90 LKADVILYSGflrQDQLWYEDLLAA-----SLRYLLAHEVGHTLGLRHNFKASSDGSNEELEDP 148
fragilysin TIGR03935
fragilysin; Members of this family are fragilysin, the Bacteroides fragilis enterotoxin. This ...
 262-298 6.31e-03

fragilysin; Members of this family are fragilysin, the Bacteroides fragilis enterotoxin. This enzyme is a Zn metalloprotease. Three distinct subtypes included in this family all are produced by enterotoxigenic (by definition) strains of Bacteroides fragilis. [Cellular processes, Pathogenesis]


Pssm-ID: 188450 [Multi-domain]  Cd Length: 386  Bit Score: 38.79  E-value: 6.31e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 17553904   262 GHGSNKRFFPYVLAHEIGHALGLDHSQKADALMHPYY 298
Cdd:TIGR03935 330 GMSTTQLMYPGTLAHELGHILGAEHTDNEKDLMYTWY 366
DUF4953 pfam16313
Met-zincin; This is a family of uncharacterized proteins that carry the highly characteriztic ...
 272-290 8.72e-03

Met-zincin; This is a family of uncharacterized proteins that carry the highly characteriztic met-zincin mmotif HExxHxxGxxH, the extended zinc-binding domain of metallopeptidases.


Pssm-ID: 435269  Cd Length: 319  Bit Score: 38.39  E-value: 8.72e-03
                          10
                  ....*....|....*....
gi 17553904   272 YVLAHEIGHALGLDHSQKA 290
Cdd:pfam16313  15 FVSAHEVGHTLGLRHNFAA 33
 
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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