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Conserved domains on  [gi|24649626|ref|NP_651242|]
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uncharacterized protein Dmel_CG5715 [Drosophila melanogaster]

Protein Classification

M12 family metallopeptidase( domain architecture ID 10136691)

M12 family metallopeptidase such as astacin, a digestive enzyme isolated from crayfish, belongs to a group of zinc-dependent proteolytic enzymes with an HExxH zinc-binding site/active site

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ZnMc_astacin_like cd04280
Zinc-dependent metalloprotease, astacin_like subfamily or peptidase family M12A, a group of ...
107-291 1.73e-94

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: 276.76  E-value: 1.73e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649626 107 GGVVPYEIKGPFTSQELGNINHAFKEYHTKTCVRFKPRTTEKDYISIGSGkSGCWSSIGRLGGRQEVNLQsPNCLRtYGT 186
Cdd:cd04280   1 NGTVPYVIDGSFDESDRSLILRAMREIESNTCIRFVPRTTEKDYIRIVKG-SGCWSYVGRVGGRQVVSLG-SGCFS-LGT 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649626 187 PIHELMHALGFFHEQNRHERDSYVRVMKDNIKPEMMVNFEKSSSRTQYGFGVEYDYGSVMHYSPTSFTRNGQPTLKALRa 266
Cdd:cd04280  78 IVHELMHALGFYHEQSRPDRDDYVTINWENIQPGYEHNFDKYSPDTVTTYGVPYDYGSVMHYGPTAFSKNGKPTIVPKD- 156
                       170       180
                ....*....|....*....|....*
gi 24649626 267 tSDASQMGQRKGFSAGDVRKINAMY 291
Cdd:cd04280 157 -PGYQIIGQREGLSFLDIKKINKMY 180
 
Name Accession Description Interval E-value
ZnMc_astacin_like cd04280
Zinc-dependent metalloprotease, astacin_like subfamily or peptidase family M12A, a group of ...
107-291 1.73e-94

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: 276.76  E-value: 1.73e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649626 107 GGVVPYEIKGPFTSQELGNINHAFKEYHTKTCVRFKPRTTEKDYISIGSGkSGCWSSIGRLGGRQEVNLQsPNCLRtYGT 186
Cdd:cd04280   1 NGTVPYVIDGSFDESDRSLILRAMREIESNTCIRFVPRTTEKDYIRIVKG-SGCWSYVGRVGGRQVVSLG-SGCFS-LGT 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649626 187 PIHELMHALGFFHEQNRHERDSYVRVMKDNIKPEMMVNFEKSSSRTQYGFGVEYDYGSVMHYSPTSFTRNGQPTLKALRa 266
Cdd:cd04280  78 IVHELMHALGFYHEQSRPDRDDYVTINWENIQPGYEHNFDKYSPDTVTTYGVPYDYGSVMHYGPTAFSKNGKPTIVPKD- 156
                       170       180
                ....*....|....*....|....*
gi 24649626 267 tSDASQMGQRKGFSAGDVRKINAMY 291
Cdd:cd04280 157 -PGYQIIGQREGLSFLDIKKINKMY 180
Astacin pfam01400
Astacin (Peptidase family M12A); The members of this family are enzymes that cleave peptides. ...
104-295 8.06e-77

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: 232.17  E-value: 8.06e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649626   104 RWPGGVVPYEIKGPFTSQELGNINHAFKEYHTKTCVRFKPRTTEK--DYISIGSGkSGCWSSIGRLGGRQEVNLqSPNCL 181
Cdd:pfam01400   2 KWPNGPIPYVIDGSLTGLARALIRQAMRHWENKTCIRFVERTPAPdnNYLFFFKG-DGCYSYVGRVGGRQPVSI-GDGCD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649626   182 RtYGTPIHELMHALGFFHEQNRHERDSYVRVMKDNIKPEMMVNFEKSSSRTQYGFGVEYDYGSVMHYSPTSFTRNG-QPT 260
Cdd:pfam01400  80 K-FGIIVHELGHALGFFHEQSRPDRDDYVSINWDNIDPGQEGNFDKYDPSEVDSYGVPYDYGSIMHYGPNAFSKNGsLPT 158
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 24649626   261 LKAlRATSDASQMGQRKGFSAGDVRKINAMYKCKV 295
Cdd:pfam01400 159 IVP-KDNDYQATIGQRVKLSFYDIKKINKLYKCPS 192
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
101-244 6.23e-39

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: 133.63  E-value: 6.23e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649626    101 LSSRWPGGVVPYEI-KGPFTSQELGNINHAFKEYHTKTCVRFKPRT-TEKDYISIGSGKSGCW-SSIGRLGGRQEVNLQS 177
Cdd:smart00235   1 GSKKWPKGTVPYVIdSSSLSPEEREAIAKALAEWSDVTCIRFVERTgTADIYISFGSGDSGCTlSHAGRPGGDQHLSLGN 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24649626    178 pNCLRTyGTPIHELMHALGFFHEQNRHERDSYVRVMKDNIkPEMMVNFEKSSSRtqygfGVEYDYGS 244
Cdd:smart00235  81 -GCINT-GVAAHELGHALGLYHEQSRSDRDNYMYINYTNI-DTRNFDLSEDDSL-----GIPYDYGS 139
 
Name Accession Description Interval E-value
ZnMc_astacin_like cd04280
Zinc-dependent metalloprotease, astacin_like subfamily or peptidase family M12A, a group of ...
107-291 1.73e-94

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: 276.76  E-value: 1.73e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649626 107 GGVVPYEIKGPFTSQELGNINHAFKEYHTKTCVRFKPRTTEKDYISIGSGkSGCWSSIGRLGGRQEVNLQsPNCLRtYGT 186
Cdd:cd04280   1 NGTVPYVIDGSFDESDRSLILRAMREIESNTCIRFVPRTTEKDYIRIVKG-SGCWSYVGRVGGRQVVSLG-SGCFS-LGT 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649626 187 PIHELMHALGFFHEQNRHERDSYVRVMKDNIKPEMMVNFEKSSSRTQYGFGVEYDYGSVMHYSPTSFTRNGQPTLKALRa 266
Cdd:cd04280  78 IVHELMHALGFYHEQSRPDRDDYVTINWENIQPGYEHNFDKYSPDTVTTYGVPYDYGSVMHYGPTAFSKNGKPTIVPKD- 156
                       170       180
                ....*....|....*....|....*
gi 24649626 267 tSDASQMGQRKGFSAGDVRKINAMY 291
Cdd:cd04280 157 -PGYQIIGQREGLSFLDIKKINKMY 180
Astacin pfam01400
Astacin (Peptidase family M12A); The members of this family are enzymes that cleave peptides. ...
104-295 8.06e-77

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: 232.17  E-value: 8.06e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649626   104 RWPGGVVPYEIKGPFTSQELGNINHAFKEYHTKTCVRFKPRTTEK--DYISIGSGkSGCWSSIGRLGGRQEVNLqSPNCL 181
Cdd:pfam01400   2 KWPNGPIPYVIDGSLTGLARALIRQAMRHWENKTCIRFVERTPAPdnNYLFFFKG-DGCYSYVGRVGGRQPVSI-GDGCD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649626   182 RtYGTPIHELMHALGFFHEQNRHERDSYVRVMKDNIKPEMMVNFEKSSSRTQYGFGVEYDYGSVMHYSPTSFTRNG-QPT 260
Cdd:pfam01400  80 K-FGIIVHELGHALGFFHEQSRPDRDDYVSINWDNIDPGQEGNFDKYDPSEVDSYGVPYDYGSIMHYGPNAFSKNGsLPT 158
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 24649626   261 LKAlRATSDASQMGQRKGFSAGDVRKINAMYKCKV 295
Cdd:pfam01400 159 IVP-KDNDYQATIGQRVKLSFYDIKKINKLYKCPS 192
ZnMc_hatching_enzyme cd04283
Zinc-dependent metalloprotease, hatching enzyme-like subfamily. Hatching enzymes are secreted ...
110-293 2.17e-74

Zinc-dependent metalloprotease, hatching enzyme-like subfamily. Hatching enzymes are secreted by teleost embryos to digest the egg envelope or chorion. In some teleosts, the hatching enzyme may be a system consisting of two evolutionary related metalloproteases, high choriolytic enzyme and low choriolytic enzyme (HCE and LCE), which may have different substrate specificities and cooperatively digest the chorion.


Pssm-ID: 239810 [Multi-domain]  Cd Length: 182  Bit Score: 225.60  E-value: 2.17e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649626 110 VPYEIKGPFTSQELGNINHAFKEYHTKTCVRFKPRTTEKDYISIGSgKSGCWSSIGRLGGRQEVNLQSPNCLRTyGTPIH 189
Cdd:cd04283   6 VPYVISPQYSENERAVIEKAMQEFETLTCVRFVPRTTERDYLNIES-RSGCWSYIGRQGGRQTVSLQKQGCMYK-GIIQH 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649626 190 ELMHALGFFHEQNRHERDSYVRVMKDNIKPEMMVNFEKSSSRTQygfGVEYDYGSVMHYSPTSFTRNGQPTLKALRatsD 269
Cdd:cd04283  84 ELLHALGFYHEQTRSDRDKYVRINWENIIPDQLYNFDKQDTNNL---GTPYDYSSVMHYGRYAFSINGKPTIVPIP---D 157
                       170       180
                ....*....|....*....|....*
gi 24649626 270 AS-QMGQRKGFSAGDVRKINAMYKC 293
Cdd:cd04283 158 PNvPIGQRQGMSNLDILRINKLYNC 182
ZnMc_meprin cd04282
Zinc-dependent metalloprotease, meprin_like subfamily. Meprins are membrane-bound or secreted ...
77-293 8.89e-49

Zinc-dependent metalloprotease, meprin_like subfamily. Meprins are membrane-bound or secreted extracellular proteases, which cleave a variety of targets, including peptides such as parathyroid hormone, gastrin, and cholecystokinin, cytokines such as osteopontin, and proteins such as collagen IV, fibronectin, casein and gelatin. Meprins may also be able to release proteins from the cell surface. Closely related meprin alpha- and beta-subunits form homo- and hetero-oligomers; these complexes are found on epithelial cells of the intestine, for example, and are also expressed in certain cancer cells.


Pssm-ID: 239809 [Multi-domain]  Cd Length: 230  Bit Score: 161.87  E-value: 8.89e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649626  77 EGDILIPLSyrdarfnGTRNGILALSSRWPGgVVPYEIKGPFTSQELGNINHAFKEYHTKTCVRFKPRTTEKDYISIGSG 156
Cdd:cd04282  25 EGDILLDEG-------QSRNGLIGDTYRWPF-PIPYILDDSLDLNAKGVILKAFEMYRLKSCVDFKPYEGESNYIFFFKG 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649626 157 kSGCWSSIGRLGGRQEVNLqSPNCLRTyGTPIHELMHALGFFHEQNRHERDSYVRVMKDNIKPEMMVNFEKSSSRTQYGF 236
Cdd:cd04282  97 -SGCWSMVGDQQGGQNLSI-GAGCDYK-ATVEHEFLHALGFYHEQSRSDRDDYVKIWWDQILSGREHNFNKYDDSFSTDL 173
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 24649626 237 GVEYDYGSVMHYSPTSFTRNG-QPTLKAlRATSDASQMGQRKGFSAGDVRKINAMYKC 293
Cdd:cd04282 174 NTPYDYESVMHYSPFSFNKGAsEPTITT-KIPEFNDIIGQRLDFSDIDLERLNRMYNC 230
ZnMc_BMP1_TLD cd04281
Zinc-dependent metalloprotease; BMP1/TLD-like subfamily. BMP1 (Bone morphogenetic protein 1) ...
104-293 2.82e-46

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: 154.52  E-value: 2.82e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649626 104 RWPGGVVPYEIKGPFTSQELGNINHAFKEYHTKTCVRFKPRTTEKDYISIGSGKSGCWSSIGRLG-GRQEVNLqSPNCLR 182
Cdd:cd04281   9 IWPGGVIPYVIDGNFTGSQRAMFKQAMRHWENFTCVTFVERTPEENYIVFTYRPCGCCSYVGRRGnGPQAISI-GKNCDK 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649626 183 tYGTPIHELMHALGFFHEQNRHERDSYVRVMKDNIKPEMMVNFEKSSSRTQYGFGVEYDYGSVMHYSPTSFTRNgqPTLK 262
Cdd:cd04281  88 -FGIVVHELGHVIGFWHEHTRPDRDDHVTIIRENIQPGQEYNFLKMEPEEVDSLGEPYDFDSIMHYARNTFSRG--MFLD 164
                       170       180       190
                ....*....|....*....|....*....|....*
gi 24649626 263 ALRATSDASQM----GQRKGFSAGDVRKINAMYKC 293
Cdd:cd04281 165 TILPKRDPNGVrpeiGQRTRLSEGDIIQANKLYKC 199
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
101-244 6.23e-39

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: 133.63  E-value: 6.23e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649626    101 LSSRWPGGVVPYEI-KGPFTSQELGNINHAFKEYHTKTCVRFKPRT-TEKDYISIGSGKSGCW-SSIGRLGGRQEVNLQS 177
Cdd:smart00235   1 GSKKWPKGTVPYVIdSSSLSPEEREAIAKALAEWSDVTCIRFVERTgTADIYISFGSGDSGCTlSHAGRPGGDQHLSLGN 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24649626    178 pNCLRTyGTPIHELMHALGFFHEQNRHERDSYVRVMKDNIkPEMMVNFEKSSSRtqygfGVEYDYGS 244
Cdd:smart00235  81 -GCINT-GVAAHELGHALGLYHEQSRSDRDNYMYINYTNI-DTRNFDLSEDDSL-----GIPYDYGS 139
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
126-291 7.70e-20

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: 84.50  E-value: 7.70e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649626 126 INHAFKEYHTKTCVRFKPRTTE--KDYISIG------SGKSGCWSSIGR--LGGRQEVNLQSPNC--LRTYGTPIHELMH 193
Cdd:cd00203  27 ILIAMQIWRDYLNIRFVLVGVEidKADIAILvtrqdfDGGTGGWAYLGRvcDSLRGVGVLQDNQSgtKEGAQTIAHELGH 106
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649626 194 ALGFFHEQNRHERDSYVRVMKDNikpemmvnfeksssrtqygFGVEYDYGSVMHYSPTSFTrngqptlkalratsdasqM 273
Cdd:cd00203 107 ALGFYHDHDRKDRDDYPTIDDTL-------------------NAEDDDYYSVMSYTKGSFS------------------D 149
                       170
                ....*....|....*...
gi 24649626 274 GQRKGFSAGDVRKINAMY 291
Cdd:cd00203 150 GQRKDFSQCDIDQINKLY 167
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
108-291 1.33e-10

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: 59.05  E-value: 1.33e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649626 108 GVVPYEIKGPFTSQELGNINHAFKEYHTKTCVRFKPRTTE-KDYISIGSGK-----SGCWSSIGRL--GGRQEVNLQSPN 179
Cdd:cd04268   2 KPITYYIDDSVPDKLRAAILDAIEAWNKAFAIGFKNANDVdPADIRYSVIRwipynDGTWSYGPSQvdPLTGEILLARVY 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649626 180 CLRTY---------GTPIHELMHALGFFHEQNRHERDSYVRVMKDnikpemmvnfeksssrtqygfgvEYDYGSVMHYSP 250
Cdd:cd04268  82 LYSSFveysgarlrNTAEHELGHALGLRHNFAASDRDDNVDLLAE-----------------------KGDTSSVMDYAP 138
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 24649626 251 TSFTRNGQPtlkalratsdasqmGQRKGFSAGDVRKINAMY 291
Cdd:cd04268 139 SNFSIQLGD--------------GQKYTIGPYDIAAIKKLY 165
ZnMc_MMP_like_3 cd04327
Zinc-dependent metalloprotease; MMP_like sub-family 3. A group of bacterial and fungal ...
159-260 2.08e-04

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: 41.60  E-value: 2.08e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649626 159 GCWSSIGR--LGGRQE---VNLQSPNcLRT-----YGTPIHELMHALGFFHEQNRHERdsyvrvmkdNI---KPEMMVNF 225
Cdd:cd04327  59 GYWSYVGTdaLLIGADaptMNLGWFT-DDTpdpefSRVVLHEFGHALGFIHEHQSPAA---------NIpwdKEAVYAYF 128
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 24649626 226 EKS--SSRTQYGFGV-------------EYDYGSVMHYS-PTSFTRNGQPT 260
Cdd:cd04327 129 SGPpnWDRETVINHNvfaklddgdvaysPYDPDSIMHYPfPGSLTLDGEEV 179
 
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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