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Conserved domains on  [gi|351058830|emb|CCD66603|]
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Zinc metalloproteinase nas-8 [Caenorhabditis elegans]

Protein Classification

ZnMc_astacin_like and ShK domain-containing protein( domain architecture ID 12019273)

ZnMc_astacin_like and ShK domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Astacin pfam01400
Astacin (Peptidase family M12A); The members of this family are enzymes that cleave peptides. ...
 119-308 4.63e-105

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: 308.06  E-value: 4.63e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351058830  119 RKWPNGRIPYVISNQYNDRERAVLARSFQAYHDKTCVRFVPRT-AVDNDYLYIGKIDGCYSDVGRAGGRQELSLDNGCLQ 197
Cdd:pfam01400   1 KKWPNGPIPYVIDGSLTGLARALIRQAMRHWENKTCIRFVERTpAPDNNYLFFFKGDGCYSYVGRVGGRQPVSIGDGCDK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351058830  198 YDTAIHELMHSVGFYHEHERWDRDEHITILWHNIDREAYDQFGKVDLAESSYYGQLYDYYSIMHYDSLAFSKNG-FETMV 276
Cdd:pfam01400  81 FGIIVHELGHALGFFHEQSRPDRDDYVSINWDNIDPGQEGNFDKYDPSEVDSYGVPYDYGSIMHYGPNAFSKNGsLPTIV 160

                         170       180       190
                  ....*....|....*....|....*....|..
gi 351058830  277 AKQSEMTAVIGAAIDFSPIDILKMNLMYQCSD 308
Cdd:pfam01400 161 PKDNDYQATIGQRVKLSFYDIKKINKLYKCPS 192
ShK pfam01549
ShK domain-like; This domain of is found in several C. elegans proteins. The domain is 30 ...
 337-372 4.89e-07

ShK domain-like; This domain of is found in several C. elegans proteins. The domain is 30 amino acids long and rich in cysteine residues. There are 6 conserved cysteine positions in the domain that form three disulphide bridges. The domain is found in the potassium channel inhibitor ShK in sea anemone.


:

Pssm-ID: 426319  Cd Length: 37  Bit Score: 45.85  E-value: 4.89e-07
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 351058830  337 DCRDRTNLCWRWIDR-CKSFFFEQIMKEFCSLSCGYC 372
Cdd:pfam01549   1 SCVDPHSDCASWAALgCTSPFYQDFMKENCPKTCGFC 37
 
Name Accession Description Interval E-value
Astacin pfam01400
Astacin (Peptidase family M12A); The members of this family are enzymes that cleave peptides. ...
 119-308 4.63e-105

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: 308.06  E-value: 4.63e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351058830  119 RKWPNGRIPYVISNQYNDRERAVLARSFQAYHDKTCVRFVPRT-AVDNDYLYIGKIDGCYSDVGRAGGRQELSLDNGCLQ 197
Cdd:pfam01400   1 KKWPNGPIPYVIDGSLTGLARALIRQAMRHWENKTCIRFVERTpAPDNNYLFFFKGDGCYSYVGRVGGRQPVSIGDGCDK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351058830  198 YDTAIHELMHSVGFYHEHERWDRDEHITILWHNIDREAYDQFGKVDLAESSYYGQLYDYYSIMHYDSLAFSKNG-FETMV 276
Cdd:pfam01400  81 FGIIVHELGHALGFFHEQSRPDRDDYVSINWDNIDPGQEGNFDKYDPSEVDSYGVPYDYGSIMHYGPNAFSKNGsLPTIV 160

                         170       180       190
                  ....*....|....*....|....*....|..
gi 351058830  277 AKQSEMTAVIGAAIDFSPIDILKMNLMYQCSD 308
Cdd:pfam01400 161 PKDNDYQATIGQRVKLSFYDIKKINKLYKCPS 192
ZnMc_astacin_like cd04280
Zinc-dependent metalloprotease, astacin_like subfamily or peptidase family M12A, a group of ...
 123-304 9.96e-82

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: 248.25  E-value: 9.96e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351058830 123 NGRIPYVISNQYNDRERAVLARSFQAYHDKTCVRFVPRTAvDNDYLYIGKIDGCYSDVGRAGGRQELSLDNGCLQYDTAI 202
Cdd:cd04280    1 NGTVPYVIDGSFDESDRSLILRAMREIESNTCIRFVPRTT-EKDYIRIVKGSGCWSYVGRVGGRQVVSLGSGCFSLGTIV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351058830 203 HELMHSVGFYHEHERWDRDEHITILWHNIDREAYDQFGKVDLAESSYYGQLYDYYSIMHYDSLAFSKNGFETMVAKQSEM 282
Cdd:cd04280   80 HELMHALGFYHEQSRPDRDDYVTINWENIQPGYEHNFDKYSPDTVTTYGVPYDYGSVMHYGPTAFSKNGKPTIVPKDPGY 159

                        170       180
                 ....*....|....*....|..
gi 351058830 283 TaVIGAAIDFSPIDILKMNLMY 304
Cdd:cd04280  160 Q-IIGQREGLSFLDIKKINKMY 180
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 117-256 2.63e-47

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: 158.28  E-value: 2.63e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351058830   117 GTRKWPNGRIPYVI-SNQYNDRERAVLARSFQAYHDKTCVRFVPRTAVDNDYLYIGKID-GC-YSDVGRAGGRQELSLDN 193
Cdd:smart00235   1 GSKKWPKGTVPYVIdSSSLSPEEREAIAKALAEWSDVTCIRFVERTGTADIYISFGSGDsGCtLSHAGRPGGDQHLSLGN 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 351058830   194 GCLQYDTAIHELMHSVGFYHEHERWDRDEHITILWHNIDREAYdqfgkvDLAESSYYGQLYDY 256
Cdd:smart00235  81 GCINTGVAAHELGHALGLYHEQSRSDRDNYMYINYTNIDTRNF------DLSEDDSLGIPYDY 137
ShK pfam01549
ShK domain-like; This domain of is found in several C. elegans proteins. The domain is 30 ...
 337-372 4.89e-07

ShK domain-like; This domain of is found in several C. elegans proteins. The domain is 30 amino acids long and rich in cysteine residues. There are 6 conserved cysteine positions in the domain that form three disulphide bridges. The domain is found in the potassium channel inhibitor ShK in sea anemone.


Pssm-ID: 426319  Cd Length: 37  Bit Score: 45.85  E-value: 4.89e-07
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 351058830  337 DCRDRTNLCWRWIDR-CKSFFFEQIMKEFCSLSCGYC 372
Cdd:pfam01549   1 SCVDPHSDCASWAALgCTSPFYQDFMKENCPKTCGFC 37
ShKT smart00254
ShK toxin domain; ShK toxin domain
 338-372 3.72e-05

ShK toxin domain; ShK toxin domain


Pssm-ID: 214586 [Multi-domain]  Cd Length: 33  Bit Score: 40.44  E-value: 3.72e-05
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 351058830   338 CRDRTNLCWRW-IDRCKSFFFeqiMKEFCSLSCGYC 372
Cdd:smart00254   1 CVDRHPDCAAWaKGFCTNPFY---MKSNCPKTCGFC 33
 
Name Accession Description Interval E-value
Astacin pfam01400
Astacin (Peptidase family M12A); The members of this family are enzymes that cleave peptides. ...
 119-308 4.63e-105

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: 308.06  E-value: 4.63e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351058830  119 RKWPNGRIPYVISNQYNDRERAVLARSFQAYHDKTCVRFVPRT-AVDNDYLYIGKIDGCYSDVGRAGGRQELSLDNGCLQ 197
Cdd:pfam01400   1 KKWPNGPIPYVIDGSLTGLARALIRQAMRHWENKTCIRFVERTpAPDNNYLFFFKGDGCYSYVGRVGGRQPVSIGDGCDK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351058830  198 YDTAIHELMHSVGFYHEHERWDRDEHITILWHNIDREAYDQFGKVDLAESSYYGQLYDYYSIMHYDSLAFSKNG-FETMV 276
Cdd:pfam01400  81 FGIIVHELGHALGFFHEQSRPDRDDYVSINWDNIDPGQEGNFDKYDPSEVDSYGVPYDYGSIMHYGPNAFSKNGsLPTIV 160

                         170       180       190
                  ....*....|....*....|....*....|..
gi 351058830  277 AKQSEMTAVIGAAIDFSPIDILKMNLMYQCSD 308
Cdd:pfam01400 161 PKDNDYQATIGQRVKLSFYDIKKINKLYKCPS 192
ZnMc_astacin_like cd04280
Zinc-dependent metalloprotease, astacin_like subfamily or peptidase family M12A, a group of ...
 123-304 9.96e-82

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: 248.25  E-value: 9.96e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351058830 123 NGRIPYVISNQYNDRERAVLARSFQAYHDKTCVRFVPRTAvDNDYLYIGKIDGCYSDVGRAGGRQELSLDNGCLQYDTAI 202
Cdd:cd04280    1 NGTVPYVIDGSFDESDRSLILRAMREIESNTCIRFVPRTT-EKDYIRIVKGSGCWSYVGRVGGRQVVSLGSGCFSLGTIV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351058830 203 HELMHSVGFYHEHERWDRDEHITILWHNIDREAYDQFGKVDLAESSYYGQLYDYYSIMHYDSLAFSKNGFETMVAKQSEM 282
Cdd:cd04280   80 HELMHALGFYHEQSRPDRDDYVTINWENIQPGYEHNFDKYSPDTVTTYGVPYDYGSVMHYGPTAFSKNGKPTIVPKDPGY 159

                        170       180
                 ....*....|....*....|..
gi 351058830 283 TaVIGAAIDFSPIDILKMNLMY 304
Cdd:cd04280  160 Q-IIGQREGLSFLDIKKINKMY 180
ZnMc_hatching_enzyme cd04283
Zinc-dependent metalloprotease, hatching enzyme-like subfamily. Hatching enzymes are secreted ...
 125-306 3.19e-67

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: 211.35  E-value: 3.19e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351058830 125 RIPYVISNQYNDRERAVLARSFQAYHDKTCVRFVPRTAvDNDYLYIGKIDGCYSDVGRAGGRQELSLD-NGCLQYDTAIH 203
Cdd:cd04283    5 YVPYVISPQYSENERAVIEKAMQEFETLTCVRFVPRTT-ERDYLNIESRSGCWSYIGRQGGRQTVSLQkQGCMYKGIIQH 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351058830 204 ELMHSVGFYHEHERWDRDEHITILWHNIDREAYDQFGKVDlaeSSYYGQLYDYYSIMHYDSLAFSKNGFETMVAKQSEmT 283
Cdd:cd04283   84 ELLHALGFYHEQTRSDRDKYVRINWENIIPDQLYNFDKQD---TNNLGTPYDYSSVMHYGRYAFSINGKPTIVPIPDP-N 159

                        170       180
                 ....*....|....*....|...
gi 351058830 284 AVIGAAIDFSPIDILKMNLMYQC 306
Cdd:cd04283  160 VPIGQRQGMSNLDILRINKLYNC 182
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 117-256 2.63e-47

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: 158.28  E-value: 2.63e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351058830   117 GTRKWPNGRIPYVI-SNQYNDRERAVLARSFQAYHDKTCVRFVPRTAVDNDYLYIGKID-GC-YSDVGRAGGRQELSLDN 193
Cdd:smart00235   1 GSKKWPKGTVPYVIdSSSLSPEEREAIAKALAEWSDVTCIRFVERTGTADIYISFGSGDsGCtLSHAGRPGGDQHLSLGN 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 351058830   194 GCLQYDTAIHELMHSVGFYHEHERWDRDEHITILWHNIDREAYdqfgkvDLAESSYYGQLYDY 256
Cdd:smart00235  81 GCINTGVAAHELGHALGLYHEQSRSDRDNYMYINYTNIDTRNF------DLSEDDSLGIPYDY 137
ZnMc_BMP1_TLD cd04281
Zinc-dependent metalloprotease; BMP1/TLD-like subfamily. BMP1 (Bone morphogenetic protein 1) ...
 119-306 1.35e-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: 153.37  E-value: 1.35e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351058830 119 RKWPNGRIPYVISNQYNDRERAVLARSFQAYHDKTCVRFVPRTAVDNDYLYIGKIDGCYSDVGRAG-GRQELSLDNGCLQ 197
Cdd:cd04281    8 RIWPGGVIPYVIDGNFTGSQRAMFKQAMRHWENFTCVTFVERTPEENYIVFTYRPCGCCSYVGRRGnGPQAISIGKNCDK 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351058830 198 YDTAIHELMHSVGFYHEHERWDRDEHITILWHNIDREAYDQFGKVDLAESSYYGQLYDYYSIMHYDSLAFSKNGF-ETMV 276
Cdd:cd04281   88 FGIVVHELGHVIGFWHEHTRPDRDDHVTIIRENIQPGQEYNFLKMEPEEVDSLGEPYDFDSIMHYARNTFSRGMFlDTIL 167

                        170       180       190
                 ....*....|....*....|....*....|..
gi 351058830 277 AKQSE--MTAVIGAAIDFSPIDILKMNLMYQC 306
Cdd:cd04281  168 PKRDPngVRPEIGQRTRLSEGDIIQANKLYKC 199
ZnMc_meprin cd04282
Zinc-dependent metalloprotease, meprin_like subfamily. Meprins are membrane-bound or secreted ...
 90-306 4.16e-44

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: 153.01  E-value: 4.16e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351058830  90 KGDIrgkaawKLDPKNSeslrRNGVITGTRKWPNgRIPYVISNQYNDRERAVLARSFQAYHDKTCVRFVPRTAVDNdYLY 169
Cdd:cd04282   25 EGDI------LLDEGQS----RNGLIGDTYRWPF-PIPYILDDSLDLNAKGVILKAFEMYRLKSCVDFKPYEGESN-YIF 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351058830 170 IGKIDGCYSDVGRAGGRQELSLDNGCLQYDTAIHELMHSVGFYHEHERWDRDEHITILWHNIDREAYDQFGKVDLAESSY 249
Cdd:cd04282   93 FFKGSGCWSMVGDQQGGQNLSIGAGCDYKATVEHEFLHALGFYHEQSRSDRDDYVKIWWDQILSGREHNFNKYDDSFSTD 172

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 351058830 250 YGQLYDYYSIMHYDSLAFSKNGFE-TMVAKQSEMTAVIGAAIDFSPIDILKMNLMYQC 306
Cdd:cd04282  173 LNTPYDYESVMHYSPFSFNKGASEpTITTKIPEFNDIIGQRLDFSDIDLERLNRMYNC 230
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 126-304 1.27e-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: 74.07  E-value: 1.27e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351058830 126 IPYVISNQYNDRERAVLARSFQAYHDKTCVRFVPRTAVDNDYLYIGKI------DGCYSDVGRA--GGRQELSLDNGCL- 196
Cdd:cd04268    4 ITYYIDDSVPDKLRAAILDAIEAWNKAFAIGFKNANDVDPADIRYSVIrwipynDGTWSYGPSQvdPLTGEILLARVYLy 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351058830 197 ----------QYDTAIHELMHSVGFYHEHERWDRDEHITilwhnidreaydqfgkvdlaessYYGQLYDYYSIMHYDSLA 266
Cdd:cd04268   84 ssfveysgarLRNTAEHELGHALGLRHNFAASDRDDNVD-----------------------LLAEKGDTSSVMDYAPSN 140

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 351058830 267 FSKNGfetmvakqsemtaVIGAAIDFSPIDILKMNLMY 304
Cdd:cd04268  141 FSIQL-------------GDGQKYTIGPYDIAAIKKLY 165
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 126-304 2.40e-15

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: 73.33  E-value: 2.40e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351058830 126 IPYVISNQYNDRE--------RAVLARSFQAYHDKTCVRFVPRTA-VDNDYLYIG-------KIDGCYSDVGR---AGGR 186
Cdd:cd00203    3 IPYVVVADDRDVEeenlsaqiQSLILIAMQIWRDYLNIRFVLVGVeIDKADIAILvtrqdfdGGTGGWAYLGRvcdSLRG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351058830 187 QELSLDNGCLQYD---TAIHELMHSVGFYHEHERWDRDEHITIlwhnidreaydqfgkvdlaESSYYGQLYDYYSIMHYD 263
Cdd:cd00203   83 VGVLQDNQSGTKEgaqTIAHELGHALGFYHDHDRKDRDDYPTI-------------------DDTLNAEDDDYYSVMSYT 143

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 351058830 264 SLAFSkngfetmvakqsemtavIGAAIDFSPIDILKMNLMY 304
Cdd:cd00203  144 KGSFS-----------------DGQRKDFSQCDIDQINKLY 167
ShK pfam01549
ShK domain-like; This domain of is found in several C. elegans proteins. The domain is 30 ...
 337-372 4.89e-07

ShK domain-like; This domain of is found in several C. elegans proteins. The domain is 30 amino acids long and rich in cysteine residues. There are 6 conserved cysteine positions in the domain that form three disulphide bridges. The domain is found in the potassium channel inhibitor ShK in sea anemone.


Pssm-ID: 426319  Cd Length: 37  Bit Score: 45.85  E-value: 4.89e-07
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 351058830  337 DCRDRTNLCWRWIDR-CKSFFFEQIMKEFCSLSCGYC 372
Cdd:pfam01549   1 SCVDPHSDCASWAALgCTSPFYQDFMKENCPKTCGFC 37
ZnMc_MMP_like_3 cd04327
Zinc-dependent metalloprotease; MMP_like sub-family 3. A group of bacterial and fungal ...
 198-304 1.14e-05

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: 45.83  E-value: 1.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351058830 198 YDTAIHELMHSVGFYHEHE------RWDRDEHITILW--HNIDREAYDQFGKVDLAESSY-YGQLYDYYSIMHYD-SLAF 267
Cdd:cd04327   93 SRVVLHEFGHALGFIHEHQspaaniPWDKEAVYAYFSgpPNWDRETVINHNVFAKLDDGDvAYSPYDPDSIMHYPfPGSL 172

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 351058830 268 SKNGFEtmvakqsemtavIGAAIDFSPIDILKMNLMY 304
Cdd:cd04327  173 TLDGEE------------VPPNRTLSDKDKAFMRLLY 197
ShKT smart00254
ShK toxin domain; ShK toxin domain
 338-372 3.72e-05

ShK toxin domain; ShK toxin domain


Pssm-ID: 214586 [Multi-domain]  Cd Length: 33  Bit Score: 40.44  E-value: 3.72e-05
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 351058830   338 CRDRTNLCWRW-IDRCKSFFFeqiMKEFCSLSCGYC 372
Cdd:smart00254   1 CVDRHPDCAAWaKGFCTNPFY---MKSNCPKTCGFC 33
 
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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