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Conserved domains on  [gi|665408167|ref|NP_001285958|]
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uncharacterized protein Dmel_CG15255, isoform B [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 ...
70-255 1.87e-85

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: 252.49  E-value: 1.87e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408167  70 GNVVVYRISDDFDTAHKKAIQTGIDTLELHTCLRFREATdEDKAYLTVTaKSGGCYTAVGYQGAPQEMNLeiyplGEGCF 149
Cdd:cd04280    1 NGTVPYVIDGSFDESDRSLILRAMREIESNTCIRFVPRT-TEKDYIRIV-KGSGCWSYVGRVGGRQVVSL-----GSGCF 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408167 150 RPGTILHEFMHALGFYHQQSSSIRDDFINVIYENIVPGKEFNFQKYADTVVTDFEVGYDYDSCLHYRPGAFSINGEDTIV 229
Cdd:cd04280   74 SLGTIVHELMHALGFYHEQSRPDRDDYVTINWENIQPGYEHNFDKYSPDTVTTYGVPYDYGSVMHYGPTAFSKNGKPTIV 153
                        170       180
                 ....*....|....*....|....*..
gi 665408167 230 PLDSSAV-IGQRVGLSSKDIDKINIMY 255
Cdd:cd04280  154 PKDPGYQiIGQREGLSFLDIKKINKMY 180
 
Name Accession Description Interval E-value
ZnMc_astacin_like cd04280
Zinc-dependent metalloprotease, astacin_like subfamily or peptidase family M12A, a group of ...
70-255 1.87e-85

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: 252.49  E-value: 1.87e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408167  70 GNVVVYRISDDFDTAHKKAIQTGIDTLELHTCLRFREATdEDKAYLTVTaKSGGCYTAVGYQGAPQEMNLeiyplGEGCF 149
Cdd:cd04280    1 NGTVPYVIDGSFDESDRSLILRAMREIESNTCIRFVPRT-TEKDYIRIV-KGSGCWSYVGRVGGRQVVSL-----GSGCF 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408167 150 RPGTILHEFMHALGFYHQQSSSIRDDFINVIYENIVPGKEFNFQKYADTVVTDFEVGYDYDSCLHYRPGAFSINGEDTIV 229
Cdd:cd04280   74 SLGTIVHELMHALGFYHEQSRPDRDDYVTINWENIQPGYEHNFDKYSPDTVTTYGVPYDYGSVMHYGPTAFSKNGKPTIV 153
                        170       180
                 ....*....|....*....|....*..
gi 665408167 230 PLDSSAV-IGQRVGLSSKDIDKINIMY 255
Cdd:cd04280  154 PKDPGYQiIGQREGLSFLDIKKINKMY 180
Astacin pfam01400
Astacin (Peptidase family M12A); The members of this family are enzymes that cleave peptides. ...
66-258 9.41e-68

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: 207.90  E-value: 9.41e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408167   66 KRWPGNVVVYRISDDFDTAHKKAIQTGIDTLELHTCLRFREATDEDKAYLTVTAKSGGCYTAVGYQGAPQEMNLeiyplG 145
Cdd:pfam01400   1 KKWPNGPIPYVIDGSLTGLARALIRQAMRHWENKTCIRFVERTPAPDNNYLFFFKGDGCYSYVGRVGGRQPVSI-----G 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408167  146 EGCFRPGTILHEFMHALGFYHQQSSSIRDDFINVIYENIVPGKEFNFQKYADTVVTDFEVGYDYDSCLHYRPGAFSING- 224
Cdd:pfam01400  76 DGCDKFGIIVHELGHALGFFHEQSRPDRDDYVSINWDNIDPGQEGNFDKYDPSEVDSYGVPYDYGSIMHYGPNAFSKNGs 155
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 665408167  225 EDTIVPLDS--SAVIGQRVGLSSKDIDKINIMYKCP 258
Cdd:pfam01400 156 LPTIVPKDNdyQATIGQRVKLSFYDIKKINKLYKCP 191
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
65-211 3.69e-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: 120.15  E-value: 3.69e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408167    65 EKRWPGNVVVYRI-SDDFDTAHKKAIQTGIDTLELHTCLRFREATDEDKAYLTVTAKSGGCYTA-VGYQGAPQEMNLEiy 142
Cdd:smart00235   2 SKKWPKGTVPYVIdSSSLSPEEREAIAKALAEWSDVTCIRFVERTGTADIYISFGSGDSGCTLShAGRPGGDQHLSLG-- 79
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 665408167   143 plgEGCFRPGTILHEFMHALGFYHQQSSSIRDDFINVIYENIVPGkefNFQKYADTVVTdfeVGYDYDS 211
Cdd:smart00235  80 ---NGCINTGVAAHELGHALGLYHEQSRSDRDNYMYINYTNIDTR---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 ...
70-255 1.87e-85

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: 252.49  E-value: 1.87e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408167  70 GNVVVYRISDDFDTAHKKAIQTGIDTLELHTCLRFREATdEDKAYLTVTaKSGGCYTAVGYQGAPQEMNLeiyplGEGCF 149
Cdd:cd04280    1 NGTVPYVIDGSFDESDRSLILRAMREIESNTCIRFVPRT-TEKDYIRIV-KGSGCWSYVGRVGGRQVVSL-----GSGCF 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408167 150 RPGTILHEFMHALGFYHQQSSSIRDDFINVIYENIVPGKEFNFQKYADTVVTDFEVGYDYDSCLHYRPGAFSINGEDTIV 229
Cdd:cd04280   74 SLGTIVHELMHALGFYHEQSRPDRDDYVTINWENIQPGYEHNFDKYSPDTVTTYGVPYDYGSVMHYGPTAFSKNGKPTIV 153
                        170       180
                 ....*....|....*....|....*..
gi 665408167 230 PLDSSAV-IGQRVGLSSKDIDKINIMY 255
Cdd:cd04280  154 PKDPGYQiIGQREGLSFLDIKKINKMY 180
Astacin pfam01400
Astacin (Peptidase family M12A); The members of this family are enzymes that cleave peptides. ...
66-258 9.41e-68

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: 207.90  E-value: 9.41e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408167   66 KRWPGNVVVYRISDDFDTAHKKAIQTGIDTLELHTCLRFREATDEDKAYLTVTAKSGGCYTAVGYQGAPQEMNLeiyplG 145
Cdd:pfam01400   1 KKWPNGPIPYVIDGSLTGLARALIRQAMRHWENKTCIRFVERTPAPDNNYLFFFKGDGCYSYVGRVGGRQPVSI-----G 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408167  146 EGCFRPGTILHEFMHALGFYHQQSSSIRDDFINVIYENIVPGKEFNFQKYADTVVTDFEVGYDYDSCLHYRPGAFSING- 224
Cdd:pfam01400  76 DGCDKFGIIVHELGHALGFFHEQSRPDRDDYVSINWDNIDPGQEGNFDKYDPSEVDSYGVPYDYGSIMHYGPNAFSKNGs 155
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 665408167  225 EDTIVPLDS--SAVIGQRVGLSSKDIDKINIMYKCP 258
Cdd:pfam01400 156 LPTIVPKDNdyQATIGQRVKLSFYDIKKINKLYKCP 191
ZnMc_hatching_enzyme cd04283
Zinc-dependent metalloprotease, hatching enzyme-like subfamily. Hatching enzymes are secreted ...
70-257 4.64e-60

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: 187.85  E-value: 4.64e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408167  70 GNVVV-YRISDDFDTAHKKAIQTGIDTLELHTCLRFREATDEDkAYLTVTAKSGgCYTAVGYQGAPQEMNLEIYplgeGC 148
Cdd:cd04283    2 GIVYVpYVISPQYSENERAVIEKAMQEFETLTCVRFVPRTTER-DYLNIESRSG-CWSYIGRQGGRQTVSLQKQ----GC 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408167 149 FRPGTILHEFMHALGFYHQQSSSIRDDFINVIYENIVPGKEFNFQKYaDTvvTDFEVGYDYDSCLHYRPGAFSINGEDTI 228
Cdd:cd04283   76 MYKGIIQHELLHALGFYHEQTRSDRDKYVRINWENIIPDQLYNFDKQ-DT--NNLGTPYDYSSVMHYGRYAFSINGKPTI 152
                        170       180       190
                 ....*....|....*....|....*....|
gi 665408167 229 VPL-DSSAVIGQRVGLSSKDIDKINIMYKC 257
Cdd:cd04283  153 VPIpDPNVPIGQRQGMSNLDILRINKLYNC 182
ZnMc_meprin cd04282
Zinc-dependent metalloprotease, meprin_like subfamily. Meprins are membrane-bound or secreted ...
36-257 3.29e-50

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: 164.57  E-value: 3.29e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408167  36 VEGDMMLTEEQQRNleqgapkarnGLINTEKRWPgNVVVYRISDDFDTAHKKAIQTGIDTLELHTCLRFREATDEdKAYL 115
Cdd:cd04282   24 FEGDILLDEGQSRN----------GLIGDTYRWP-FPIPYILDDSLDLNAKGVILKAFEMYRLKSCVDFKPYEGE-SNYI 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408167 116 TVTaKSGGCYTAVGYQGAPQEMNLeiyplGEGCFRPGTILHEFMHALGFYHQQSSSIRDDFINVIYENIVPGKEFNFQKY 195
Cdd:cd04282   92 FFF-KGSGCWSMVGDQQGGQNLSI-----GAGCDYKATVEHEFLHALGFYHEQSRSDRDDYVKIWWDQILSGREHNFNKY 165
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 665408167 196 ADTVVTDFEVGYDYDSCLHYRPGAFSING-EDTIVPL--DSSAVIGQRVGLSSKDIDKINIMYKC 257
Cdd:cd04282  166 DDSFSTDLNTPYDYESVMHYSPFSFNKGAsEPTITTKipEFNDIIGQRLDFSDIDLERLNRMYNC 230
ZnMc_BMP1_TLD cd04281
Zinc-dependent metalloprotease; BMP1/TLD-like subfamily. BMP1 (Bone morphogenetic protein 1) ...
64-258 4.99e-44

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: 147.59  E-value: 4.99e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408167  64 TEKRWPGNVVVYRISDDFDTAHKKAIQTGIDTLELHTCLRFREATDEDKaYLTVTAKSGGCYTAVGYQG-APQEMNLeiy 142
Cdd:cd04281    6 KERIWPGGVIPYVIDGNFTGSQRAMFKQAMRHWENFTCVTFVERTPEEN-YIVFTYRPCGCCSYVGRRGnGPQAISI--- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408167 143 plGEGCFRPGTILHEFMHALGFYHQQSSSIRDDFINVIYENIVPGKEFNFQKYADTVVTDFEVGYDYDSCLHYRPGAFSI 222
Cdd:cd04281   82 --GKNCDKFGIVVHELGHVIGFWHEHTRPDRDDHVTIIRENIQPGQEYNFLKMEPEEVDSLGEPYDFDSIMHYARNTFSR 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 665408167 223 NGE-DTIVPL-DSSAV---IGQRVGLSSKDIDKINIMYKCP 258
Cdd:cd04281  160 GMFlDTILPKrDPNGVrpeIGQRTRLSEGDIIQANKLYKCP 200
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
65-211 3.69e-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: 120.15  E-value: 3.69e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408167    65 EKRWPGNVVVYRI-SDDFDTAHKKAIQTGIDTLELHTCLRFREATDEDKAYLTVTAKSGGCYTA-VGYQGAPQEMNLEiy 142
Cdd:smart00235   2 SKKWPKGTVPYVIdSSSLSPEEREAIAKALAEWSDVTCIRFVERTGTADIYISFGSGDSGCTLShAGRPGGDQHLSLG-- 79
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 665408167   143 plgEGCFRPGTILHEFMHALGFYHQQSSSIRDDFINVIYENIVPGkefNFQKYADTVVTdfeVGYDYDS 211
Cdd:smart00235  80 ---NGCINTGVAAHELGHALGLYHEQSRSDRDNYMYINYTNIDTR---NFDLSEDDSLG---IPYDYGS 139
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
71-255 1.88e-15

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: 71.76  E-value: 1.88e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408167  71 NVVVYRISDDFDTAHKKAIQTGIDTLELHTCLRFREATDEDKAYLTVTAK-----SGGCYTAVGYQGAP--QEMNLEIYP 143
Cdd:cd04268    2 KPITYYIDDSVPDKLRAAILDAIEAWNKAFAIGFKNANDVDPADIRYSVIrwipyNDGTWSYGPSQVDPltGEILLARVY 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408167 144 LG------EGCFRPGTILHEFMHALGFYHQQSSSIRDDFINVIYEnivpgkefnfqkyadtvvtdfevGYDYDSCLHYRP 217
Cdd:cd04268   82 LYssfveySGARLRNTAEHELGHALGLRHNFAASDRDDNVDLLAE-----------------------KGDTSSVMDYAP 138
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 665408167 218 GAFSINGEDtivpldssaviGQRVGLSSKDIDKINIMY 255
Cdd:cd04268  139 SNFSIQLGD-----------GQKYTIGPYDIAAIKKLY 165
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
78-255 6.17e-12

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: 62.15  E-value: 6.17e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408167  78 SDDFDTAHKKAIQTGIDTLELHTCLRFREAT-DEDKAYLTV----TAKSGGC----YTAVGYQGAPQEMNLEIYPLGEGC 148
Cdd:cd00203   16 EENLSAQIQSLILIAMQIWRDYLNIRFVLVGvEIDKADIAIlvtrQDFDGGTggwaYLGRVCDSLRGVGVLQDNQSGTKE 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408167 149 FRpGTILHEFMHALGFYHQQSSSIRDDFINViyenivpgkefnfqkyadtVVTDFEVGYDYDSCLHYRPGAFSingedti 228
Cdd:cd00203   96 GA-QTIAHELGHALGFYHDHDRKDRDDYPTI-------------------DDTLNAEDDDYYSVMSYTKGSFS------- 148
                        170       180
                 ....*....|....*....|....*..
gi 665408167 229 vpldssavIGQRVGLSSKDIDKINIMY 255
Cdd:cd00203  149 --------DGQRKDFSQCDIDQINKLY 167
ZnMc_MMP_like_3 cd04327
Zinc-dependent metalloprotease; MMP_like sub-family 3. A group of bacterial and fungal ...
66-255 6.75e-09

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: 54.31  E-value: 6.75e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408167  66 KRWP-GNVVVYRISDDFDTAHKKAIQTGIDTLELHTCLRFREATDEDKAYLTVTAKSGGCYTAVG----YQGAPQE-MNL 139
Cdd:cd04327    1 KLWRnGTVLRIAFLGGPDAFLKDKVRAAAREWLPYANLKFKFVTDADADIRISFTPGDGYWSYVGtdalLIGADAPtMNL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408167 140 EIYPL-GEGCFRPGTILHEFMHALGFYHQQSS---SIRDDFINVI-YENIVPG------KEFNFQKYADTVVTDFEVgYD 208
Cdd:cd04327   81 GWFTDdTPDPEFSRVVLHEFGHALGFIHEHQSpaaNIPWDKEAVYaYFSGPPNwdretvINHNVFAKLDDGDVAYSP-YD 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 665408167 209 YDSCLHYR-PGAFSINGEDtiVPLDSsavigqrvGLSSKDIDKINIMY 255
Cdd:cd04327  160 PDSIMHYPfPGSLTLDGEE--VPPNR--------TLSDKDKAFMRLLY 197
 
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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