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Conserved domains on  [gi|1944647358|ref|WP_197868755|]
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MULTISPECIES: M12 family metallopeptidase [Pseudomonas]

Protein Classification

ZnMc_MMP_like_3 domain-containing protein( domain architecture ID 10137789)

ZnMc_MMP_like_3 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ZnMc_MMP_like_3 cd04327
Zinc-dependent metalloprotease; MMP_like sub-family 3. A group of bacterial and fungal ...
 49-243 9.67e-100

Zinc-dependent metalloprotease; MMP_like sub-family 3. A group of bacterial and fungal metalloproteinase domains similar to matrix metalloproteinases and astacin.


:

Pssm-ID: 239819 [Multi-domain]  Cd Length: 198  Bit Score: 288.51  E-value: 9.67e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944647358  49 KLWANGRTLKIAFMDAPDADHKTRIINAARKWLAYINLNFEFVDDLKGDIRIATRNND-NSSMLGTDALLIHPDHPTMNL 127
Cdd:cd04327     1 KLWRNGTVLRIAFLGGPDAFLKDKVRAAAREWLPYANLKFKFVTDADADIRISFTPGDgYWSYVGTDALLIGADAPTMNL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944647358 128 GVKPE---HPDFETIVIHEFGHALGALHEHQHPQANIPWDKPKVYAFYRNREMNplTREQVDR-NLFATFDTLDAIYTNY 203
Cdd:cd04327    81 GWFTDdtpDPEFSRVVLHEFGHALGFIHEHQSPAANIPWDKEAVYAYFSGPPNW--DRETVINhNVFAKLDDGDVAYSPY 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1944647358 204 DRRSIMHHPVSNDLTIGNWEVPINRKISKKDKQLMKLLYP 243
Cdd:cd04327   159 DPDSIMHYPFPGSLTLDGEEVPPNRTLSDKDKAFMRLLYP 198
 
Name Accession Description Interval E-value
ZnMc_MMP_like_3 cd04327
Zinc-dependent metalloprotease; MMP_like sub-family 3. A group of bacterial and fungal ...
 49-243 9.67e-100

Zinc-dependent metalloprotease; MMP_like sub-family 3. A group of bacterial and fungal metalloproteinase domains similar to matrix metalloproteinases and astacin.


Pssm-ID: 239819 [Multi-domain]  Cd Length: 198  Bit Score: 288.51  E-value: 9.67e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944647358  49 KLWANGRTLKIAFMDAPDADHKTRIINAARKWLAYINLNFEFVDDLKGDIRIATRNND-NSSMLGTDALLIHPDHPTMNL 127
Cdd:cd04327     1 KLWRNGTVLRIAFLGGPDAFLKDKVRAAAREWLPYANLKFKFVTDADADIRISFTPGDgYWSYVGTDALLIGADAPTMNL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944647358 128 GVKPE---HPDFETIVIHEFGHALGALHEHQHPQANIPWDKPKVYAFYRNREMNplTREQVDR-NLFATFDTLDAIYTNY 203
Cdd:cd04327    81 GWFTDdtpDPEFSRVVLHEFGHALGFIHEHQSPAANIPWDKEAVYAYFSGPPNW--DRETVINhNVFAKLDDGDVAYSPY 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1944647358 204 DRRSIMHHPVSNDLTIGNWEVPINRKISKKDKQLMKLLYP 243
Cdd:cd04327   159 DPDSIMHYPFPGSLTLDGEEVPPNRTLSDKDKAFMRLLYP 198
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 63-152 7.89e-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: 44.53  E-value: 7.89e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944647358  63 DAPDADHKTRIINAARKWLAYINLNFEFVDDLKGDIRI--ATRN-NDNSSMLGTDALLIHPDHPTMNLG----------- 128
Cdd:pfam00413  17 DLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIgfGRGDhGDGYPFDGPGGVLAHAFFPGPGLGgdihfdddetw 96

                          90       100
                  ....*....|....*....|....*...
gi 1944647358 129 -VKPEHP---DFETIVIHEFGHALGALH 152
Cdd:pfam00413  97 tVGSDPPhgiNLFLVAAHEIGHALGLGH 124
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 139-179 6.47e-04

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: 38.87  E-value: 6.47e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1944647358  139 IVIHEFGHALGALHEHQhpqaniPWDKPK-VYAFYRNREMNP 179
Cdd:smart00235  87 VAAHELGHALGLYHEQS------RSDRDNyMYINYTNIDTRN 122
 
Name Accession Description Interval E-value
ZnMc_MMP_like_3 cd04327
Zinc-dependent metalloprotease; MMP_like sub-family 3. A group of bacterial and fungal ...
 49-243 9.67e-100

Zinc-dependent metalloprotease; MMP_like sub-family 3. A group of bacterial and fungal metalloproteinase domains similar to matrix metalloproteinases and astacin.


Pssm-ID: 239819 [Multi-domain]  Cd Length: 198  Bit Score: 288.51  E-value: 9.67e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944647358  49 KLWANGRTLKIAFMDAPDADHKTRIINAARKWLAYINLNFEFVDDLKGDIRIATRNND-NSSMLGTDALLIHPDHPTMNL 127
Cdd:cd04327     1 KLWRNGTVLRIAFLGGPDAFLKDKVRAAAREWLPYANLKFKFVTDADADIRISFTPGDgYWSYVGTDALLIGADAPTMNL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944647358 128 GVKPE---HPDFETIVIHEFGHALGALHEHQHPQANIPWDKPKVYAFYRNREMNplTREQVDR-NLFATFDTLDAIYTNY 203
Cdd:cd04327    81 GWFTDdtpDPEFSRVVLHEFGHALGFIHEHQSPAANIPWDKEAVYAYFSGPPNW--DRETVINhNVFAKLDDGDVAYSPY 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1944647358 204 DRRSIMHHPVSNDLTIGNWEVPINRKISKKDKQLMKLLYP 243
Cdd:cd04327   159 DPDSIMHYPFPGSLTLDGEEVPPNRTLSDKDKAFMRLLYP 198
ZnMc_MMP_like_1 cd04279
Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ...
 71-158 4.00e-06

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: 45.53  E-value: 4.00e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944647358  71 TRIINAARKWLAYINLNFEFVD--DLKGDIRIATRNNDNSSMLG-----------TDALLIHPDHPTMNLGV--KPEHPD 135
Cdd:cd04279    24 QAVKQAAAEWENVGPLKFVYNPeeDNDADIVIFFDRPPPVGGAGgglaragfpliSDGNRKLFNRTDINLGPgqPRGAEN 103

                          90       100
                  ....*....|....*....|...
gi 1944647358 136 FETIVIHEFGHALGALHEHQHPQ 158
Cdd:cd04279   104 LQAIALHELGHALGLWHHSDRPE 126
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 63-152 7.89e-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: 44.53  E-value: 7.89e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944647358  63 DAPDADHKTRIINAARKWLAYINLNFEFVDDLKGDIRI--ATRN-NDNSSMLGTDALLIHPDHPTMNLG----------- 128
Cdd:pfam00413  17 DLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIgfGRGDhGDGYPFDGPGGVLAHAFFPGPGLGgdihfdddetw 96

                          90       100
                  ....*....|....*....|....*...
gi 1944647358 129 -VKPEHP---DFETIVIHEFGHALGALH 152
Cdd:pfam00413  97 tVGSDPPhgiNLFLVAAHEIGHALGLGH 124
Astacin pfam01400
Astacin (Peptidase family M12A); The members of this family are enzymes that cleave peptides. ...
 139-242 8.15e-06

Astacin (Peptidase family M12A); The members of this family are enzymes that cleave peptides. These proteases require zinc for catalysis. Members of this family contain two conserved disulphide bridges, these are joined 1-4 and 2-3. Members of this family have an amino terminal propeptide which is cleaved to give the active protease domain. All other linked domains are found to the carboxyl terminus of this domain. This family includes: Astacin, a digestive enzyme from Crayfish. Meprin, a multiple domain membrane component that is constructed from a homologous alpha and beta chain. Proteins involved in morphogenesis such as Swiss:P13497, and Tolloid from drosophila.


Pssm-ID: 426242 [Multi-domain]  Cd Length: 192  Bit Score: 44.96  E-value: 8.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944647358 139 IVIHEFGHALGALHEHQHPQA----NIPWDkpkvyafyrnremnpltreQVDRNLFATFDTLDA-IYTN----YDRRSIM 209
Cdd:pfam01400  83 IIVHELGHALGFFHEQSRPDRddyvSINWD-------------------NIDPGQEGNFDKYDPsEVDSygvpYDYGSIM 143

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1944647358 210 HH---------------PVSNDL--TIGNwevpiNRKISKKDKQLMKLLY 242
Cdd:pfam01400 144 HYgpnafskngslptivPKDNDYqaTIGQ-----RVKLSFYDIKKINKLY 188
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 63-149 5.54e-05

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: 42.19  E-value: 5.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944647358  63 DAPDADHKTRIINAARKWLAYINLNFEFV-DDLKGDIRI--ATRN-NDNSSMLGTDALLIHP-------------DHPTM 125
Cdd:cd04278    17 DLPRDDVRRAIARAFRVWSDVTPLTFREVtSGQEADIRIsfARGNhGDGYPFDGPGGTLAHAffpggiggdihfdDDEQW 96

                          90       100
                  ....*....|....*....|....
gi 1944647358 126 NLGVKPEHPDFETIVIHEFGHALG 149
Cdd:cd04278    97 TLGSDSGGTDLFSVAAHEIGHALG 120
ZnMc_astacin_like cd04280
Zinc-dependent metalloprotease, astacin_like subfamily or peptidase family M12A, a group of ...
 61-242 6.20e-05

Zinc-dependent metalloprotease, astacin_like subfamily or peptidase family M12A, a group of zinc-dependent proteolytic enzymes with a HExxH zinc-binding site/active site. Members of this family may have an amino terminal propeptide, which is cleaved to yield the active protease domain, which is consequently always found at the N-terminus in multi-domain architectures. This family includes: astacin, a digestive enzyme from Crayfish; meprin, a multiple domain membrane component that is constructed from a homologous alpha and beta chain, proteins involved in (bone) morphogenesis, tolloid from drosophila, and the sea urchin SPAN protein, which may also play a role in development.


Pssm-ID: 239807 [Multi-domain]  Cd Length: 180  Bit Score: 42.56  E-value: 6.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944647358  61 FMDAPDADHKTRIINAARKWLAYINLNFEFVDDLKGDIRIaTRNNDNSSMLGtdalliHPDHP-TMNLGVKPEHpdfETI 139
Cdd:cd04280     8 IDGSFDESDRSLILRAMREIESNTCIRFVPRTTEKDYIRI-VKGSGCWSYVG------RVGGRqVVSLGSGCFS---LGT 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944647358 140 VIHEFGHALGALHEHQHPQAN----IPWD--KP-KVYAFYRNREmnpltreqvdrnlfatfDTLDAIYTNYDRRSIMHHP 212
Cdd:cd04280    78 IVHELMHALGFYHEQSRPDRDdyvtINWEniQPgYEHNFDKYSP-----------------DTVTTYGVPYDYGSVMHYG 140

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1944647358 213 -----VSNDLTIgnweVPIN---------RKISKKDKQLMKLLY 242
Cdd:cd04280   141 ptafsKNGKPTI----VPKDpgyqiigqrEGLSFLDIKKINKMY 180
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 63-242 1.68e-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: 1.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944647358  63 DAPDADHKTRIINAARKWLAYINLNFEFVDD-LKGDIRI-----ATRNNDNSSMLGTDAlliHPDHPTMNLG-------- 128
Cdd:cd04268    10 DSVPDKLRAAILDAIEAWNKAFAIGFKNANDvDPADIRYsvirwIPYNDGTWSYGPSQV---DPLTGEILLArvylyssf 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944647358 129 VKPEHPDFETIVIHEFGHALGALHEHQHPqanipwdkpkvyafyrnremnpltreqvdrnlfATFDTLDAIYTNYDRRSI 208
Cdd:cd04268    87 VEYSGARLRNTAEHELGHALGLRHNFAAS---------------------------------DRDDNVDLLAEKGDTSSV 133

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1944647358 209 MHHPVSNDltIGNWEVPINRKISKKDKQLMKLLY 242
Cdd:cd04268   134 MDYAPSNF--SIQLGDGQKYTIGPYDIAAIKKLY 165
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 63-242 2.16e-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.


Pssm-ID: 238124 [Multi-domain]  Cd Length: 167  Bit Score: 40.58  E-value: 2.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944647358  63 DAPDADHKTRIINAARKWLAYINLNF--EFVDDLKGDIRIATRNNDNSSMLGTDALL---IHPDHPTMNLGVKPEHP-DF 136
Cdd:cd00203    17 ENLSAQIQSLILIAMQIWRDYLNIRFvlVGVEIDKADIAILVTRQDFDGGTGGWAYLgrvCDSLRGVGVLQDNQSGTkEG 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944647358 137 ETIVIHEFGHALGALHEHqhpqanipwdkpkvyafyrnremnpltreqvDRNLFATFDTLDAIYTN--YDRRSIMhHPVS 214
Cdd:cd00203    97 AQTIAHELGHALGFYHDH-------------------------------DRKDRDDYPTIDDTLNAedDDYYSVM-SYTK 144

                         170       180
                  ....*....|....*....|....*...
gi 1944647358 215 NDLTIGNwevpiNRKISKKDKQLMKLLY 242
Cdd:cd00203   145 GSFSDGQ-----RKDFSQCDIDQINKLY 167
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 139-179 6.47e-04

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: 38.87  E-value: 6.47e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1944647358  139 IVIHEFGHALGALHEHQhpqaniPWDKPK-VYAFYRNREMNP 179
Cdd:smart00235  87 VAAHELGHALGLYHEQS------RSDRDNyMYINYTNIDTRN 122
ZnMc_BMP1_TLD cd04281
Zinc-dependent metalloprotease; BMP1/TLD-like subfamily. BMP1 (Bone morphogenetic protein 1) ...
 139-211 6.26e-03

Zinc-dependent metalloprotease; BMP1/TLD-like subfamily. BMP1 (Bone morphogenetic protein 1) and TLD (tolloid)-like metalloproteases play vital roles in extracellular matrix formation, by cleaving precursor proteins such as enzymes, structural proteins, and proteins involved in the mineralization of the extracellular matrix. The drosophila protein tolloid and its Xenopus homologue xolloid cleave and inactivate Sog and chordin, respectively, which are inhibitors of Dpp (the Drosophila decapentaplegic gene product) and its homologue BMP4, involved in dorso-ventral patterning.


Pssm-ID: 239808 [Multi-domain]  Cd Length: 200  Bit Score: 36.65  E-value: 6.26e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1944647358 139 IVIHEFGHALGALHEHQHPqanipwdkpkvyafyrNREMN-PLTREQVDRNLFATFDTLDAIYTN-----YDRRSIMHH 211
Cdd:cd04281    90 IVVHELGHVIGFWHEHTRP----------------DRDDHvTIIRENIQPGQEYNFLKMEPEEVDslgepYDFDSIMHY 152
 
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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