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Conserved domains on  [gi|386765203|ref|NP_001246942|]
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uncharacterized protein Dmel_CG10280, 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 ...
151-342 4.70e-80

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: 242.48  E-value: 4.70e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765203 151 NGTIPFEISPRYANQERQAIIQAVKTFNSLTCVHFVPYDGEVDdYLLIEPPlegpQGCWSYVGRRGGEQVVSLQRpdens 230
Cdd:cd04280    1 NGTVPYVIDGSFDESDRSLILRAMREIESNTCIRFVPRTTEKD-YIRIVKG----SGCWSYVGRVGGRQVVSLGS----- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765203 231 aHCFSsEGRIMHELMHAIGIYHEQSRADRDNFVKIHWDNIVPRFRKNFKLVSKKKG-KYAFDYDYNSVMHYGEFYFSkrK 309
Cdd:cd04280   71 -GCFS-LGTIVHELMHALGFYHEQSRPDRDDYVTINWENIQPGYEHNFDKYSPDTVtTYGVPYDYGSVMHYGPTAFS--K 146
                        170       180       190
                 ....*....|....*....|....*....|....
gi 386765203 310 GEKPTMTPLQPGV-RIGQRKTISKIDCLKINELY 342
Cdd:cd04280  147 NGKPTIVPKDPGYqIIGQREGLSFLDIKKINKMY 180
 
Name Accession Description Interval E-value
ZnMc_astacin_like cd04280
Zinc-dependent metalloprotease, astacin_like subfamily or peptidase family M12A, a group of ...
151-342 4.70e-80

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: 242.48  E-value: 4.70e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765203 151 NGTIPFEISPRYANQERQAIIQAVKTFNSLTCVHFVPYDGEVDdYLLIEPPlegpQGCWSYVGRRGGEQVVSLQRpdens 230
Cdd:cd04280    1 NGTVPYVIDGSFDESDRSLILRAMREIESNTCIRFVPRTTEKD-YIRIVKG----SGCWSYVGRVGGRQVVSLGS----- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765203 231 aHCFSsEGRIMHELMHAIGIYHEQSRADRDNFVKIHWDNIVPRFRKNFKLVSKKKG-KYAFDYDYNSVMHYGEFYFSkrK 309
Cdd:cd04280   71 -GCFS-LGTIVHELMHALGFYHEQSRPDRDDYVTINWENIQPGYEHNFDKYSPDTVtTYGVPYDYGSVMHYGPTAFS--K 146
                        170       180       190
                 ....*....|....*....|....*....|....
gi 386765203 310 GEKPTMTPLQPGV-RIGQRKTISKIDCLKINELY 342
Cdd:cd04280  147 NGKPTIVPKDPGYqIIGQREGLSFLDIKKINKMY 180
Astacin pfam01400
Astacin (Peptidase family M12A); The members of this family are enzymes that cleave peptides. ...
147-344 3.18e-65

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: 205.21  E-value: 3.18e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765203  147 RLWPNGTIPFEISPRYANQERQAIIQAVKTFNSLTCVHFVPYDGEVD-DYLLIEPPlegpQGCWSYVGRRGGEQVVSLqr 225
Cdd:pfam01400   1 KKWPNGPIPYVIDGSLTGLARALIRQAMRHWENKTCIRFVERTPAPDnNYLFFFKG----DGCYSYVGRVGGRQPVSI-- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765203  226 pdenSAHCFSsEGRIMHELMHAIGIYHEQSRADRDNFVKIHWDNIVPRFRKNF-KLVSKKKGKYAFDYDYNSVMHYGEFY 304
Cdd:pfam01400  75 ----GDGCDK-FGIIVHELGHALGFFHEQSRPDRDDYVSINWDNIDPGQEGNFdKYDPSEVDSYGVPYDYGSIMHYGPNA 149
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 386765203  305 FSKrKGEKPTMTPLQPGVR--IGQRKTISKIDCLKINELYGC 344
Cdd:pfam01400 150 FSK-NGSLPTIVPKDNDYQatIGQRVKLSFYDIKKINKLYKC 190
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
145-296 3.51e-36

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: 128.24  E-value: 3.51e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765203   145 PKRLWPNGTIPFEI-SPRYANQERQAIIQAVKTFNSLTCVHFVPYDGEVDDYLLIEPpleGPQGCW-SYVGRRGGEQVVS 222
Cdd:smart00235   1 GSKKWPKGTVPYVIdSSSLSPEEREAIAKALAEWSDVTCIRFVERTGTADIYISFGS---GDSGCTlSHAGRPGGDQHLS 77
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386765203   223 LqrpdENSAhcfSSEGRIMHELMHAIGIYHEQSRADRDNFVKIHWDNIVPRfrkNFKLVskKKGKYAFDYDYNS 296
Cdd:smart00235  78 L----GNGC---INTGVAAHELGHALGLYHEQSRSDRDNYMYINYTNIDTR---NFDLS--EDDSLGIPYDYGS 139
 
Name Accession Description Interval E-value
ZnMc_astacin_like cd04280
Zinc-dependent metalloprotease, astacin_like subfamily or peptidase family M12A, a group of ...
151-342 4.70e-80

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: 242.48  E-value: 4.70e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765203 151 NGTIPFEISPRYANQERQAIIQAVKTFNSLTCVHFVPYDGEVDdYLLIEPPlegpQGCWSYVGRRGGEQVVSLQRpdens 230
Cdd:cd04280    1 NGTVPYVIDGSFDESDRSLILRAMREIESNTCIRFVPRTTEKD-YIRIVKG----SGCWSYVGRVGGRQVVSLGS----- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765203 231 aHCFSsEGRIMHELMHAIGIYHEQSRADRDNFVKIHWDNIVPRFRKNFKLVSKKKG-KYAFDYDYNSVMHYGEFYFSkrK 309
Cdd:cd04280   71 -GCFS-LGTIVHELMHALGFYHEQSRPDRDDYVTINWENIQPGYEHNFDKYSPDTVtTYGVPYDYGSVMHYGPTAFS--K 146
                        170       180       190
                 ....*....|....*....|....*....|....
gi 386765203 310 GEKPTMTPLQPGV-RIGQRKTISKIDCLKINELY 342
Cdd:cd04280  147 NGKPTIVPKDPGYqIIGQREGLSFLDIKKINKMY 180
ZnMc_hatching_enzyme cd04283
Zinc-dependent metalloprotease, hatching enzyme-like subfamily. Hatching enzymes are secreted ...
154-344 2.95e-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: 227.92  E-value: 2.95e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765203 154 IPFEISPRYANQERQAIIQAVKTFNSLTCVHFVPYDGEvDDYLLIEPPlegpQGCWSYVGRRGGEQVVSLQRPDensahC 233
Cdd:cd04283    6 VPYVISPQYSENERAVIEKAMQEFETLTCVRFVPRTTE-RDYLNIESR----SGCWSYIGRQGGRQTVSLQKQG-----C 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765203 234 FSsEGRIMHELMHAIGIYHEQSRADRDNFVKIHWDNIVPRFRKNFKlvskkkgKYAFD-----YDYNSVMHYGEFYFSKR 308
Cdd:cd04283   76 MY-KGIIQHELLHALGFYHEQTRSDRDKYVRINWENIIPDQLYNFD-------KQDTNnlgtpYDYSSVMHYGRYAFSIN 147
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 386765203 309 KgeKPTMTPL-QPGVRIGQRKTISKIDCLKINELYGC 344
Cdd:cd04283  148 G--KPTIVPIpDPNVPIGQRQGMSNLDILRINKLYNC 182
Astacin pfam01400
Astacin (Peptidase family M12A); The members of this family are enzymes that cleave peptides. ...
147-344 3.18e-65

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: 205.21  E-value: 3.18e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765203  147 RLWPNGTIPFEISPRYANQERQAIIQAVKTFNSLTCVHFVPYDGEVD-DYLLIEPPlegpQGCWSYVGRRGGEQVVSLqr 225
Cdd:pfam01400   1 KKWPNGPIPYVIDGSLTGLARALIRQAMRHWENKTCIRFVERTPAPDnNYLFFFKG----DGCYSYVGRVGGRQPVSI-- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765203  226 pdenSAHCFSsEGRIMHELMHAIGIYHEQSRADRDNFVKIHWDNIVPRFRKNF-KLVSKKKGKYAFDYDYNSVMHYGEFY 304
Cdd:pfam01400  75 ----GDGCDK-FGIIVHELGHALGFFHEQSRPDRDDYVSINWDNIDPGQEGNFdKYDPSEVDSYGVPYDYGSIMHYGPNA 149
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 386765203  305 FSKrKGEKPTMTPLQPGVR--IGQRKTISKIDCLKINELYGC 344
Cdd:pfam01400 150 FSK-NGSLPTIVPKDNDYQatIGQRVKLSFYDIKKINKLYKC 190
ZnMc_meprin cd04282
Zinc-dependent metalloprotease, meprin_like subfamily. Meprins are membrane-bound or secreted ...
119-344 2.09e-41

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: 144.92  E-value: 2.09e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765203 119 RLFQGDIAIDPYTyitlrlGVNPMRHPKRLWPNgTIPFEISPRYANQERQAIIQAVKTFNSLTCVHFVPYDGEvDDYLLI 198
Cdd:cd04282   22 DLFEGDILLDEGQ------SRNGLIGDTYRWPF-PIPYILDDSLDLNAKGVILKAFEMYRLKSCVDFKPYEGE-SNYIFF 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765203 199 EPPlegpQGCWSYVGRRGGEQVVSLqrpdenSAHCfSSEGRIMHELMHAIGIYHEQSRADRDNFVKIHWDNIVPRFRKNF 278
Cdd:cd04282   94 FKG----SGCWSMVGDQQGGQNLSI------GAGC-DYKATVEHEFLHALGFYHEQSRSDRDDYVKIWWDQILSGREHNF 162
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386765203 279 klvSKKKGKYAFD----YDYNSVMHYGEFYFSKRKGEkPTMTPLQPGVR--IGQRKTISKIDCLKINELYGC 344
Cdd:cd04282  163 ---NKYDDSFSTDlntpYDYESVMHYSPFSFNKGASE-PTITTKIPEFNdiIGQRLDFSDIDLERLNRMYNC 230
ZnMc_BMP1_TLD cd04281
Zinc-dependent metalloprotease; BMP1/TLD-like subfamily. BMP1 (Bone morphogenetic protein 1) ...
145-344 2.32e-39

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: 138.73  E-value: 2.32e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765203 145 PKRLWPNGTIPFEISPRYANQERQAIIQAVKTFNSLTCVHFVPYDGEvDDYLLIEpplEGPQGCWSYVGRRG-GEQVVSL 223
Cdd:cd04281    6 KERIWPGGVIPYVIDGNFTGSQRAMFKQAMRHWENFTCVTFVERTPE-ENYIVFT---YRPCGCCSYVGRRGnGPQAISI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765203 224 QRpdensaHCfSSEGRIMHELMHAIGIYHEQSRADRDNFVKIHWDNIVPRFRKNF-KLVSKKKGKYAFDYDYNSVMHYGE 302
Cdd:cd04281   82 GK------NC-DKFGIVVHELGHVIGFWHEHTRPDRDDHVTIIRENIQPGQEYNFlKMEPEEVDSLGEPYDFDSIMHYAR 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 386765203 303 FYFSkRKGEKPTMTP--LQPGVR--IGQRKTISKIDCLKINELYGC 344
Cdd:cd04281  155 NTFS-RGMFLDTILPkrDPNGVRpeIGQRTRLSEGDIIQANKLYKC 199
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
145-296 3.51e-36

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: 128.24  E-value: 3.51e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765203   145 PKRLWPNGTIPFEI-SPRYANQERQAIIQAVKTFNSLTCVHFVPYDGEVDDYLLIEPpleGPQGCW-SYVGRRGGEQVVS 222
Cdd:smart00235   1 GSKKWPKGTVPYVIdSSSLSPEEREAIAKALAEWSDVTCIRFVERTGTADIYISFGS---GDSGCTlSHAGRPGGDQHLS 77
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386765203   223 LqrpdENSAhcfSSEGRIMHELMHAIGIYHEQSRADRDNFVKIHWDNIVPRfrkNFKLVskKKGKYAFDYDYNS 296
Cdd:smart00235  78 L----GNGC---INTGVAAHELGHALGLYHEQSRSDRDNYMYINYTNIDTR---NFDLS--EDDSLGIPYDYGS 139
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
164-342 6.58e-21

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: 88.35  E-value: 6.58e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765203 164 NQERQAIIQAVKTFNSLTCVHFVPYDGEVDD----YLLIEPPLEGPQGCWSYVGR--RGGEQVVSLQRpdeNSAHCFSSE 237
Cdd:cd00203   21 AQIQSLILIAMQIWRDYLNIRFVLVGVEIDKadiaILVTRQDFDGGTGGWAYLGRvcDSLRGVGVLQD---NQSGTKEGA 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765203 238 GRIMHELMHAIGIYHEQSRADRDNFVKIHWDNivprfrknfklvskkkgkYAFDYDYNSVMHYGEFYFSkrkgekptmtp 317
Cdd:cd00203   98 QTIAHELGHALGFYHDHDRKDRDDYPTIDDTL------------------NAEDDDYYSVMSYTKGSFS----------- 148
                        170       180
                 ....*....|....*....|....*
gi 386765203 318 lqpgvrIGQRKTISKIDCLKINELY 342
Cdd:cd00203  149 ------DGQRKDFSQCDIDQINKLY 167
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
151-342 2.10e-17

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: 78.69  E-value: 2.10e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765203 151 NGTIPFEISPRYANQERQAIIQAVKTFNSLTCVHFVPYDGEVDDYLLIE--PPLEGPQGCWSYVGRR--GGEQVVSLQRP 226
Cdd:cd04268    1 KKPITYYIDDSVPDKLRAAILDAIEAWNKAFAIGFKNANDVDPADIRYSviRWIPYNDGTWSYGPSQvdPLTGEILLARV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765203 227 DENSAHCFSSEGRI----MHELMHAIGIYHEQSRADRDNFVKIhwdnivprfrknfklvskkkgkYAFDYDYNSVMHYGE 302
Cdd:cd04268   81 YLYSSFVEYSGARLrntaEHELGHALGLRHNFAASDRDDNVDL----------------------LAEKGDTSSVMDYAP 138
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 386765203 303 FYFSKRKGekptmtplqpgvrIGQRKTISKIDCLKINELY 342
Cdd:cd04268  139 SNFSIQLG-------------DGQKYTIGPYDIAAIKKLY 165
ZnMc_MMP_like_1 cd04279
Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ...
155-256 3.97e-04

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: 40.52  E-value: 3.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765203 155 PFEISPRYANQERQAIIQAVKTFNSLTCVHFVPYDGEVDDY----LLIEPPLEGPQGCW---SYVGRRGGEQVVSLQRPD 227
Cdd:cd04279   11 TPAPPDSRAQSWLQAVKQAAAEWENVGPLKFVYNPEEDNDAdiviFFDRPPPVGGAGGGlarAGFPLISDGNRKLFNRTD 90
                         90       100       110
                 ....*....|....*....|....*....|....
gi 386765203 228 ENSAHCFSSEGRIM-----HELMHAIGIYHEQSR 256
Cdd:cd04279   91 INLGPGQPRGAENLqaialHELGHALGLWHHSDR 124
ZnMc_MMP_like_3 cd04327
Zinc-dependent metalloprotease; MMP_like sub-family 3. A group of bacterial and fungal ...
147-300 2.60e-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: 38.52  E-value: 2.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765203 147 RLWPNGT---IPFEISPRYAnqERQAIIQAVKTFNSLTCVHFVpydgEVDDyllIEPPL----EGPQGCWSYVGR----- 214
Cdd:cd04327    1 KLWRNGTvlrIAFLGGPDAF--LKDKVRAAAREWLPYANLKFK----FVTD---ADADIrisfTPGDGYWSYVGTdalli 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765203 215 RGGE-----QVVSLQRPDENSAHCfssegrIMHELMHAIGIYHEQSRAdrdnFVKIHWDN--IVPRFR----------KN 277
Cdd:cd04327   72 GADAptmnlGWFTDDTPDPEFSRV------VLHEFGHALGFIHEHQSP----AANIPWDKeaVYAYFSgppnwdretvIN 141
                        170       180
                 ....*....|....*....|....*
gi 386765203 278 FKLVSKKKGKYAF--DYDYNSVMHY 300
Cdd:cd04327  142 HNVFAKLDDGDVAysPYDPDSIMHY 166
 
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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