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Conserved domains on  [gi|19921390|ref|NP_609760|]
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uncharacterized protein Dmel_CG7631 [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 ...
 61-248 4.74e-87

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: 256.34  E-value: 4.74e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921390  61 NATVPYRISEEFDAPHVEYIKLGMQFIEYSSCIRFVPADEdEENYLFVLPStSGCSSKVGYQPGERTVklkpgSLDTGCF 140
Cdd:cd04280   1 NGTVPYVIDGSFDESDRSLILRAMREIESNTCIRFVPRTT-EKDYIRIVKG-SGCWSYVGRVGGRQVV-----SLGSGCF 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921390 141 KLGTIQHELLHTLGFHHQQCSPNRDEFVKIVEENISEGHEKNFVKYEEDEVGDFDQPYDYGSILHYSSLAFSINGEATIV 220
Cdd:cd04280  74 SLGTIVHELMHALGFYHEQSRPDRDDYVTINWENIQPGYEHNFDKYSPDTVTTYGVPYDYGSVMHYGPTAFSKNGKPTIV 153

                       170       180
                ....*....|....*....|....*...
gi 19921390 221 ALNPeGQEQMGQRLMMSDTDVKRLNTMY 248
Cdd:cd04280 154 PKDP-GYQIIGQREGLSFLDIKKINKMY 180
 
Name Accession Description Interval E-value
ZnMc_astacin_like cd04280
Zinc-dependent metalloprotease, astacin_like subfamily or peptidase family M12A, a group of ...
 61-248 4.74e-87

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: 256.34  E-value: 4.74e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921390  61 NATVPYRISEEFDAPHVEYIKLGMQFIEYSSCIRFVPADEdEENYLFVLPStSGCSSKVGYQPGERTVklkpgSLDTGCF 140
Cdd:cd04280   1 NGTVPYVIDGSFDESDRSLILRAMREIESNTCIRFVPRTT-EKDYIRIVKG-SGCWSYVGRVGGRQVV-----SLGSGCF 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921390 141 KLGTIQHELLHTLGFHHQQCSPNRDEFVKIVEENISEGHEKNFVKYEEDEVGDFDQPYDYGSILHYSSLAFSINGEATIV 220
Cdd:cd04280  74 SLGTIVHELMHALGFYHEQSRPDRDDYVTINWENIQPGYEHNFDKYSPDTVTTYGVPYDYGSVMHYGPTAFSKNGKPTIV 153

                       170       180
                ....*....|....*....|....*...
gi 19921390 221 ALNPeGQEQMGQRLMMSDTDVKRLNTMY 248
Cdd:cd04280 154 PKDP-GYQIIGQREGLSFLDIKKINKMY 180
Astacin pfam01400
Astacin (Peptidase family M12A); The members of this family are enzymes that cleave peptides. ...
 57-251 2.74e-74

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: 224.47  E-value: 2.74e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921390    57 RRWPNATVPYRISEEFDAPHVEYIKLGMQFIEYSSCIRFVP-ADEDEENYLFVLpSTSGCSSKVGYQPGERTVklkpgSL 135
Cdd:pfam01400   1 KKWPNGPIPYVIDGSLTGLARALIRQAMRHWENKTCIRFVErTPAPDNNYLFFF-KGDGCYSYVGRVGGRQPV-----SI 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921390   136 DTGCFKLGTIQHELLHTLGFHHQQCSPNRDEFVKIVEENISEGHEKNFVKYEEDEVGDFDQPYDYGSILHYSSLAFSING 215
Cdd:pfam01400  75 GDGCDKFGIIVHELGHALGFFHEQSRPDRDDYVSINWDNIDPGQEGNFDKYDPSEVDSYGVPYDYGSIMHYGPNAFSKNG 154

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 19921390   216 -EATIVALNPEGQEQMGQRLMMSDTDVKRLNTMYKCP 251
Cdd:pfam01400 155 sLPTIVPKDNDYQATIGQRVKLSFYDIKKINKLYKCP 191
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 57-202 1.11e-34

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: 121.30  E-value: 1.11e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921390     57 RRWPNATVPYRISEEFDAPHVEY-IKLGMQFIEYSSCIRFVPADEDEENYLFVLPSTSGCSSKVGYQPGERTVKlkpgSL 135
Cdd:smart00235   3 KKWPKGTVPYVIDSSSLSPEEREaIAKALAEWSDVTCIRFVERTGTADIYISFGSGDSGCTLSHAGRPGGDQHL----SL 78

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19921390    136 DTGCFKLGTIQHELLHTLGFHHQQCSPNRDEFVKIVEENISEGhekNFVKYEEDEVGdfdQPYDYGS 202
Cdd:smart00235  79 GNGCINTGVAAHELGHALGLYHEQSRSDRDNYMYINYTNIDTR---NFDLSEDDSLG---IPYDYGS 139
 
Name Accession Description Interval E-value
ZnMc_astacin_like cd04280
Zinc-dependent metalloprotease, astacin_like subfamily or peptidase family M12A, a group of ...
 61-248 4.74e-87

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: 256.34  E-value: 4.74e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921390  61 NATVPYRISEEFDAPHVEYIKLGMQFIEYSSCIRFVPADEdEENYLFVLPStSGCSSKVGYQPGERTVklkpgSLDTGCF 140
Cdd:cd04280   1 NGTVPYVIDGSFDESDRSLILRAMREIESNTCIRFVPRTT-EKDYIRIVKG-SGCWSYVGRVGGRQVV-----SLGSGCF 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921390 141 KLGTIQHELLHTLGFHHQQCSPNRDEFVKIVEENISEGHEKNFVKYEEDEVGDFDQPYDYGSILHYSSLAFSINGEATIV 220
Cdd:cd04280  74 SLGTIVHELMHALGFYHEQSRPDRDDYVTINWENIQPGYEHNFDKYSPDTVTTYGVPYDYGSVMHYGPTAFSKNGKPTIV 153

                       170       180
                ....*....|....*....|....*...
gi 19921390 221 ALNPeGQEQMGQRLMMSDTDVKRLNTMY 248
Cdd:cd04280 154 PKDP-GYQIIGQREGLSFLDIKKINKMY 180
Astacin pfam01400
Astacin (Peptidase family M12A); The members of this family are enzymes that cleave peptides. ...
 57-251 2.74e-74

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: 224.47  E-value: 2.74e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921390    57 RRWPNATVPYRISEEFDAPHVEYIKLGMQFIEYSSCIRFVP-ADEDEENYLFVLpSTSGCSSKVGYQPGERTVklkpgSL 135
Cdd:pfam01400   1 KKWPNGPIPYVIDGSLTGLARALIRQAMRHWENKTCIRFVErTPAPDNNYLFFF-KGDGCYSYVGRVGGRQPV-----SI 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921390   136 DTGCFKLGTIQHELLHTLGFHHQQCSPNRDEFVKIVEENISEGHEKNFVKYEEDEVGDFDQPYDYGSILHYSSLAFSING 215
Cdd:pfam01400  75 GDGCDKFGIIVHELGHALGFFHEQSRPDRDDYVSINWDNIDPGQEGNFDKYDPSEVDSYGVPYDYGSIMHYGPNAFSKNG 154

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 19921390   216 -EATIVALNPEGQEQMGQRLMMSDTDVKRLNTMYKCP 251
Cdd:pfam01400 155 sLPTIVPKDNDYQATIGQRVKLSFYDIKKINKLYKCP 191
ZnMc_hatching_enzyme cd04283
Zinc-dependent metalloprotease, hatching enzyme-like subfamily. Hatching enzymes are secreted ...
 64-250 2.39e-63

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: 195.94  E-value: 2.39e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921390  64 VPYRISEEFDAPHVEYIKLGMQFIEYSSCIRFVPAdEDEENYLFVlPSTSGCSSKVGYQPGERTVKLKPGsldtGCFKLG 143
Cdd:cd04283   6 VPYVISPQYSENERAVIEKAMQEFETLTCVRFVPR-TTERDYLNI-ESRSGCWSYIGRQGGRQTVSLQKQ----GCMYKG 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921390 144 TIQHELLHTLGFHHQQCSPNRDEFVKIVEENISEGHEKNFVKYEEDEVGdfdQPYDYGSILHYSSLAFSINGEATIVALn 223
Cdd:cd04283  80 IIQHELLHALGFYHEQTRSDRDKYVRINWENIIPDQLYNFDKQDTNNLG---TPYDYSSVMHYGRYAFSINGKPTIVPI- 155

                       170       180
                ....*....|....*....|....*..
gi 19921390 224 PEGQEQMGQRLMMSDTDVKRLNTMYKC 250
Cdd:cd04283 156 PDPNVPIGQRQGMSNLDILRINKLYNC 182
ZnMc_meprin cd04282
Zinc-dependent metalloprotease, meprin_like subfamily. Meprins are membrane-bound or secreted ...
 21-250 1.09e-47

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: 157.63  E-value: 1.09e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921390  21 APFNTHYDETDPELTAGYFQGDMDVDYA--RNGQLSETRRWPNaTVPYRISEEFDAPHVEYIKLGMQFIEYSSCIRFVPA 98
Cdd:cd04282   6 EGIDQDIFEINLGAGLDLFEGDILLDEGqsRNGLIGDTYRWPF-PIPYILDDSLDLNAKGVILKAFEMYRLKSCVDFKPY 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921390  99 dEDEENYLFVLPStSGCSSKVGYQPGERTVklkpgSLDTGCFKLGTIQHELLHTLGFHHQQCSPNRDEFVKIVEENISEG 178
Cdd:cd04282  85 -EGESNYIFFFKG-SGCWSMVGDQQGGQNL-----SIGAGCDYKATVEHEFLHALGFYHEQSRSDRDDYVKIWWDQILSG 157

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19921390 179 HEKNFVKYEEDEVGDFDQPYDYGSILHYSSLAFSING-EATIVALNPEGQEQMGQRLMMSDTDVKRLNTMYKC 250
Cdd:cd04282 158 REHNFNKYDDSFSTDLNTPYDYESVMHYSPFSFNKGAsEPTITTKIPEFNDIIGQRLDFSDIDLERLNRMYNC 230
ZnMc_BMP1_TLD cd04281
Zinc-dependent metalloprotease; BMP1/TLD-like subfamily. BMP1 (Bone morphogenetic protein 1) ...
 57-251 1.35e-43

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: 146.43  E-value: 1.35e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921390  57 RRWPNATVPYRISEEFDAPHVEYIKLGMQFIEYSSCIRFVPADeDEENYLFVLPSTSGCSSKVGYQPGERtvklKPGSLD 136
Cdd:cd04281   8 RIWPGGVIPYVIDGNFTGSQRAMFKQAMRHWENFTCVTFVERT-PEENYIVFTYRPCGCCSYVGRRGNGP----QAISIG 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921390 137 TGCFKLGTIQHELLHTLGFHHQQCSPNRDEFVKIVEENISEGHEKNFVKYEEDEVGDFDQPYDYGSILHYSSLAFS--IN 214
Cdd:cd04281  83 KNCDKFGIVVHELGHVIGFWHEHTRPDRDDHVTIIRENIQPGQEYNFLKMEPEEVDSLGEPYDFDSIMHYARNTFSrgMF 162

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 19921390 215 GEATIVALNPEG-QEQMGQRLMMSDTDVKRLNTMYKCP 251
Cdd:cd04281 163 LDTILPKRDPNGvRPEIGQRTRLSEGDIIQANKLYKCP 200
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 57-202 1.11e-34

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: 121.30  E-value: 1.11e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921390     57 RRWPNATVPYRISEEFDAPHVEY-IKLGMQFIEYSSCIRFVPADEDEENYLFVLPSTSGCSSKVGYQPGERTVKlkpgSL 135
Cdd:smart00235   3 KKWPKGTVPYVIDSSSLSPEEREaIAKALAEWSDVTCIRFVERTGTADIYISFGSGDSGCTLSHAGRPGGDQHL----SL 78

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19921390    136 DTGCFKLGTIQHELLHTLGFHHQQCSPNRDEFVKIVEENISEGhekNFVKYEEDEVGdfdQPYDYGS 202
Cdd:smart00235  79 GNGCINTGVAAHELGHALGLYHEQSRSDRDNYMYINYTNIDTR---NFDLSEDDSLG---IPYDYGS 139
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 63-248 2.31e-14

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: 68.70  E-value: 2.31e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921390  63 TVPYRI--------SEEFDAPHVEYIKLGMQFIEYSSCIRFVPADEDEE---NYLFVLPST----SGCSSKVGYQPGERT 127
Cdd:cd00203   2 VIPYVVvaddrdveEENLSAQIQSLILIAMQIWRDYLNIRFVLVGVEIDkadIAILVTRQDfdggTGGWAYLGRVCDSLR 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921390 128 vklKPGSLDTGCF----KLGTIQHELLHTLGFHHQQCSPNRDEFVKIVEENISEgheknfvkyeedevgdfdqPYDYGSI 203
Cdd:cd00203  82 ---GVGVLQDNQSgtkeGAQTIAHELGHALGFYHDHDRKDRDDYPTIDDTLNAE-------------------DDDYYSV 139

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 19921390 204 LHYSSLAFSIngeativalnpegqeqmGQRLMMSDTDVKRLNTMY 248
Cdd:cd00203 140 MSYTKGSFSD-----------------GQRKDFSQCDIDQINKLY 167
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 61-248 3.96e-11

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: 59.82  E-value: 3.96e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921390  61 NATVPYRISEEFDAPHVEYIKLGMQFIEYSSCIRFVPADEDEENYLFV-----LPSTSGCSSKVGYQPGERT--VKLKPG 133
Cdd:cd04268   1 KKPITYYIDDSVPDKLRAAILDAIEAWNKAFAIGFKNANDVDPADIRYsvirwIPYNDGTWSYGPSQVDPLTgeILLARV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921390 134 SLDTGCFKL------GTIQHELLHTLGFHHQQCSPNRDEFVKIVEEnisegheknfvkyeedevgdfdqPYDYGSILHYS 207
Cdd:cd04268  81 YLYSSFVEYsgarlrNTAEHELGHALGLRHNFAASDRDDNVDLLAE-----------------------KGDTSSVMDYA 137

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 19921390 208 SLAFSINGEAtivalnpegqeqmGQRLMMSDTDVKRLNTMY 248
Cdd:cd04268 138 PSNFSIQLGD-------------GQKYTIGPYDIAAIKKLY 165
ZnMc_MMP_like_3 cd04327
Zinc-dependent metalloprotease; MMP_like sub-family 3. A group of bacterial and fungal ...
 144-207 1.90e-03

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: 38.13  E-value: 1.90e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19921390 144 TIQHELLHTLGFHHQQCSP--NR---DEFVK---IVEENISEGHEKNFVKYEEDEVGDFD-QPYDYGSILHYS 207
Cdd:cd04327  95 VVLHEFGHALGFIHEHQSPaaNIpwdKEAVYayfSGPPNWDRETVINHNVFAKLDDGDVAySPYDPDSIMHYP 167
 
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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