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Conserved domains on  [gi|392895294|ref|NP_001254939|]
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Zinc metalloproteinase nas-4 [Caenorhabditis elegans]

Protein Classification

astacin family metallopeptidase( domain architecture ID 12019253)

astacin (M12A) 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

EC:  3.4.24.21
Gene Ontology:  GO:0004222|GO:0008270|GO:0006508
PubMed:  9016826|8445658|7670368

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. ...
 102-290 4.35e-106

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: 307.29  E-value: 4.35e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895294  102 RRWPNNEIPYTLSSQYGSYARSVIANAMNEYHTKTCVKFVARDPSKHHDYLWIHPDEGCYSLVGKTGGKQPVSLDSGCIQ 181
Cdd:pfam01400   1 KKWPNGPIPYVIDGSLTGLARALIRQAMRHWENKTCIRFVERTPAPDNNYLFFFKGDGCYSYVGRVGGRQPVSIGDGCDK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895294  182 VGTIVHELMHAVGFFHEQSRQDRDSYIDVVWQNVMNGADDQFEKYNLNVISHLDEPYDYASIMHYGPYAFS-GSGKKTLV 260
Cdd:pfam01400  81 FGIIVHELGHALGFFHEQSRPDRDDYVSINWDNIDPGQEGNFDKYDPSEVDSYGVPYDYGSIMHYGPNAFSkNGSLPTIV 160

                         170       180       190
                  ....*....|....*....|....*....|.
gi 392895294  261 PKKSG-SERMGQRVKFSDIDVRKINKLYNCP 290
Cdd:pfam01400 161 PKDNDyQATIGQRVKLSFYDIKKINKLYKCP 191
 
Name Accession Description Interval E-value
Astacin pfam01400
Astacin (Peptidase family M12A); The members of this family are enzymes that cleave peptides. ...
 102-290 4.35e-106

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: 307.29  E-value: 4.35e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895294  102 RRWPNNEIPYTLSSQYGSYARSVIANAMNEYHTKTCVKFVARDPSKHHDYLWIHPDEGCYSLVGKTGGKQPVSLDSGCIQ 181
Cdd:pfam01400   1 KKWPNGPIPYVIDGSLTGLARALIRQAMRHWENKTCIRFVERTPAPDNNYLFFFKGDGCYSYVGRVGGRQPVSIGDGCDK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895294  182 VGTIVHELMHAVGFFHEQSRQDRDSYIDVVWQNVMNGADDQFEKYNLNVISHLDEPYDYASIMHYGPYAFS-GSGKKTLV 260
Cdd:pfam01400  81 FGIIVHELGHALGFFHEQSRPDRDDYVSINWDNIDPGQEGNFDKYDPSEVDSYGVPYDYGSIMHYGPNAFSkNGSLPTIV 160

                         170       180       190
                  ....*....|....*....|....*....|.
gi 392895294  261 PKKSG-SERMGQRVKFSDIDVRKINKLYNCP 290
Cdd:pfam01400 161 PKDNDyQATIGQRVKLSFYDIKKINKLYKCP 191
ZnMc_astacin_like cd04280
Zinc-dependent metalloprotease, astacin_like subfamily or peptidase family M12A, a group of ...
 106-287 3.03e-95

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: 279.46  E-value: 3.03e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895294 106 NNEIPYTLSSQYGSYARSVIANAMNEYHTKTCVKFVARDPskHHDYLWIHPDEGCYSLVGKTGGKQPVSLDSGCIQVGTI 185
Cdd:cd04280    1 NGTVPYVIDGSFDESDRSLILRAMREIESNTCIRFVPRTT--EKDYIRIVKGSGCWSYVGRVGGRQVVSLGSGCFSLGTI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895294 186 VHELMHAVGFFHEQSRQDRDSYIDVVWQNVMNGADDQFEKYNLNVISHLDEPYDYASIMHYGPYAFSGSGKKTLVPKKSG 265
Cdd:cd04280   79 VHELMHALGFYHEQSRPDRDDYVTINWENIQPGYEHNFDKYSPDTVTTYGVPYDYGSVMHYGPTAFSKNGKPTIVPKDPG 158

                        170       180
                 ....*....|....*....|..
gi 392895294 266 SERMGQRVKFSDIDVRKINKLY 287
Cdd:cd04280  159 YQIIGQREGLSFLDIKKINKMY 180
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 101-242 5.36e-46

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: 152.50  E-value: 5.36e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895294   101 YRRWPNNEIPYTL-SSQYGSYARSVIANAMNEYHTKTCVKFVARDPsKHHDYLWIHP-DEGC-YSLVGKTGGKQPVSLDS 177
Cdd:smart00235   2 SKKWPKGTVPYVIdSSSLSPEEREAIAKALAEWSDVTCIRFVERTG-TADIYISFGSgDSGCtLSHAGRPGGDQHLSLGN 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 392895294   178 GCIQVGTIVHELMHAVGFFHEQSRQDRDSYIDVVWQNVMngaddqFEKYNLNVISHLDEPYDYAS 242
Cdd:smart00235  81 GCINTGVAAHELGHALGLYHEQSRSDRDNYMYINYTNID------TRNFDLSEDDSLGIPYDYGS 139
 
Name Accession Description Interval E-value
Astacin pfam01400
Astacin (Peptidase family M12A); The members of this family are enzymes that cleave peptides. ...
 102-290 4.35e-106

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: 307.29  E-value: 4.35e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895294  102 RRWPNNEIPYTLSSQYGSYARSVIANAMNEYHTKTCVKFVARDPSKHHDYLWIHPDEGCYSLVGKTGGKQPVSLDSGCIQ 181
Cdd:pfam01400   1 KKWPNGPIPYVIDGSLTGLARALIRQAMRHWENKTCIRFVERTPAPDNNYLFFFKGDGCYSYVGRVGGRQPVSIGDGCDK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895294  182 VGTIVHELMHAVGFFHEQSRQDRDSYIDVVWQNVMNGADDQFEKYNLNVISHLDEPYDYASIMHYGPYAFS-GSGKKTLV 260
Cdd:pfam01400  81 FGIIVHELGHALGFFHEQSRPDRDDYVSINWDNIDPGQEGNFDKYDPSEVDSYGVPYDYGSIMHYGPNAFSkNGSLPTIV 160

                         170       180       190
                  ....*....|....*....|....*....|.
gi 392895294  261 PKKSG-SERMGQRVKFSDIDVRKINKLYNCP 290
Cdd:pfam01400 161 PKDNDyQATIGQRVKLSFYDIKKINKLYKCP 191
ZnMc_astacin_like cd04280
Zinc-dependent metalloprotease, astacin_like subfamily or peptidase family M12A, a group of ...
 106-287 3.03e-95

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: 279.46  E-value: 3.03e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895294 106 NNEIPYTLSSQYGSYARSVIANAMNEYHTKTCVKFVARDPskHHDYLWIHPDEGCYSLVGKTGGKQPVSLDSGCIQVGTI 185
Cdd:cd04280    1 NGTVPYVIDGSFDESDRSLILRAMREIESNTCIRFVPRTT--EKDYIRIVKGSGCWSYVGRVGGRQVVSLGSGCFSLGTI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895294 186 VHELMHAVGFFHEQSRQDRDSYIDVVWQNVMNGADDQFEKYNLNVISHLDEPYDYASIMHYGPYAFSGSGKKTLVPKKSG 265
Cdd:cd04280   79 VHELMHALGFYHEQSRPDRDDYVTINWENIQPGYEHNFDKYSPDTVTTYGVPYDYGSVMHYGPTAFSKNGKPTIVPKDPG 158

                        170       180
                 ....*....|....*....|..
gi 392895294 266 SERMGQRVKFSDIDVRKINKLY 287
Cdd:cd04280  159 YQIIGQREGLSFLDIKKINKMY 180
ZnMc_hatching_enzyme cd04283
Zinc-dependent metalloprotease, hatching enzyme-like subfamily. Hatching enzymes are secreted ...
 108-289 5.01e-78

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: 235.62  E-value: 5.01e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895294 108 EIPYTLSSQYGSYARSVIANAMNEYHTKTCVKFVARdpSKHHDYLWIHPDEGCYSLVGKTGGKQPVSLD-SGCIQVGTIV 186
Cdd:cd04283    5 YVPYVISPQYSENERAVIEKAMQEFETLTCVRFVPR--TTERDYLNIESRSGCWSYIGRQGGRQTVSLQkQGCMYKGIIQ 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895294 187 HELMHAVGFFHEQSRQDRDSYIDVVWQNVMNGADDQFEKYNLNvisHLDEPYDYASIMHYGPYAFSGSGKKTLVPKKSGS 266
Cdd:cd04283   83 HELLHALGFYHEQTRSDRDKYVRINWENIIPDQLYNFDKQDTN---NLGTPYDYSSVMHYGRYAFSINGKPTIVPIPDPN 159

                        170       180
                 ....*....|....*....|...
gi 392895294 267 ERMGQRVKFSDIDVRKINKLYNC 289
Cdd:cd04283  160 VPIGQRQGMSNLDILRINKLYNC 182
ZnMc_meprin cd04282
Zinc-dependent metalloprotease, meprin_like subfamily. Meprins are membrane-bound or secreted ...
 74-289 3.50e-54

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: 176.51  E-value: 3.50e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895294  74 EGDILLESPKkfveennklGRNAIKQIYRRWPNnEIPYTLSSQYGSYARSVIANAMNEYHTKTCVKFVARDPSKhhDYLW 153
Cdd:cd04282   25 EGDILLDEGQ---------SRNGLIGDTYRWPF-PIPYILDDSLDLNAKGVILKAFEMYRLKSCVDFKPYEGES--NYIF 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895294 154 IHPDEGCYSLVGKTGGKQPVSLDSGCIQVGTIVHELMHAVGFFHEQSRQDRDSYIDVVWQNVMNGADDQFEKYNLNVISH 233
Cdd:cd04282   93 FFKGSGCWSMVGDQQGGQNLSIGAGCDYKATVEHEFLHALGFYHEQSRSDRDDYVKIWWDQILSGREHNFNKYDDSFSTD 172

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 392895294 234 LDEPYDYASIMHYGPYAFS-GSGKKTLVPKKSGSER-MGQRVKFSDIDVRKINKLYNC 289
Cdd:cd04282  173 LNTPYDYESVMHYSPFSFNkGASEPTITTKIPEFNDiIGQRLDFSDIDLERLNRMYNC 230
ZnMc_BMP1_TLD cd04281
Zinc-dependent metalloprotease; BMP1/TLD-like subfamily. BMP1 (Bone morphogenetic protein 1) ...
 102-290 1.24e-52

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: 171.47  E-value: 1.24e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895294 102 RRWPNNEIPYTLSSQYGSYARSVIANAMNEYHTKTCVKFVARDPSKHHDYLWIHPDeGCYSLVGKTG-GKQPVSLDSGCI 180
Cdd:cd04281    8 RIWPGGVIPYVIDGNFTGSQRAMFKQAMRHWENFTCVTFVERTPEENYIVFTYRPC-GCCSYVGRRGnGPQAISIGKNCD 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895294 181 QVGTIVHELMHAVGFFHEQSRQDRDSYIDVVWQNVMNGADDQFEKYNLNVISHLDEPYDYASIMHYGPYAFS-GSGKKTL 259
Cdd:cd04281   87 KFGIVVHELGHVIGFWHEHTRPDRDDHVTIIRENIQPGQEYNFLKMEPEEVDSLGEPYDFDSIMHYARNTFSrGMFLDTI 166

                        170       180       190
                 ....*....|....*....|....*....|....
gi 392895294 260 VPKKSGS---ERMGQRVKFSDIDVRKINKLYNCP 290
Cdd:cd04281  167 LPKRDPNgvrPEIGQRTRLSEGDIIQANKLYKCP 200
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 101-242 5.36e-46

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: 152.50  E-value: 5.36e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895294   101 YRRWPNNEIPYTL-SSQYGSYARSVIANAMNEYHTKTCVKFVARDPsKHHDYLWIHP-DEGC-YSLVGKTGGKQPVSLDS 177
Cdd:smart00235   2 SKKWPKGTVPYVIdSSSLSPEEREAIAKALAEWSDVTCIRFVERTG-TADIYISFGSgDSGCtLSHAGRPGGDQHLSLGN 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 392895294   178 GCIQVGTIVHELMHAVGFFHEQSRQDRDSYIDVVWQNVMngaddqFEKYNLNVISHLDEPYDYAS 242
Cdd:smart00235  81 GCINTGVAAHELGHALGLYHEQSRSDRDNYMYINYTNID------TRNFDLSEDDSLGIPYDYGS 139
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 107-287 1.19e-18

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: 81.41  E-value: 1.19e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895294 107 NEIPYTL--------SSQYGSYARSVIANAMNEYHTKTCVKFVARDPSKHHDYLWI-------HPDEGCYSLVGKT--GG 169
Cdd:cd00203    1 KVIPYVVvaddrdveEENLSAQIQSLILIAMQIWRDYLNIRFVLVGVEIDKADIAIlvtrqdfDGGTGGWAYLGRVcdSL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895294 170 KQPVSLDSGCIQ----VGTIVHELMHAVGFFHEQSRQDRDSYIDVvwqnvmngaddqfekynlnVISHLDEPYDYASIMH 245
Cdd:cd00203   81 RGVGVLQDNQSGtkegAQTIAHELGHALGFYHDHDRKDRDDYPTI-------------------DDTLNAEDDDYYSVMS 141

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 392895294 246 YGPYAFSGsgkktlvpkksgsermGQRVKFSDIDVRKINKLY 287
Cdd:cd00203  142 YTKGSFSD----------------GQRKDFSQCDIDQINKLY 167
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 106-287 2.17e-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: 72.53  E-value: 2.17e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895294 106 NNEIPYTLSSQYGSYARSVIANAMNEYHTKTCVKFVARDPSKHHD-----YLWIHPDEGCYSLVGKTGG-------KQPV 173
Cdd:cd04268    1 KKPITYYIDDSVPDKLRAAILDAIEAWNKAFAIGFKNANDVDPADirysvIRWIPYNDGTWSYGPSQVDpltgeilLARV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895294 174 SLDSGCIQ------VGTIVHELMHAVGFFHEQSRQDRDSYIDVvwqnvmngaddqfekynlnvishLDEPYDYASIMHYG 247
Cdd:cd04268   81 YLYSSFVEysgarlRNTAEHELGHALGLRHNFAASDRDDNVDL-----------------------LAEKGDTSSVMDYA 137

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 392895294 248 PYAFSGSGKKtlvpkksgsermGQRVKFSDIDVRKINKLY 287
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 ...
 184-254 2.80e-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: 44.29  E-value: 2.80e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392895294 184 TIVHELMHAVGFFHEQSRQDRDSYIDV--VWQNVMN--GADDQfEKYNLNVISHLDE------PYDYASIMHygpYAFSG 253
Cdd:cd04327   95 VVLHEFGHALGFIHEHQSPAANIPWDKeaVYAYFSGppNWDRE-TVINHNVFAKLDDgdvaysPYDPDSIMH---YPFPG 170


                 .
gi 392895294 254 S 254
Cdd:cd04327  171 S 171
 
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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