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Conserved domains on  [gi|19921384|ref|NP_609756|]
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seminal metalloprotease-1 [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 ...
55-245 1.15e-72

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: 219.75  E-value: 1.15e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921384  55 NRTVPYMIeDDAFADSHYREILRAISIIEENSCVIFKPAT-EMDFpmaLVITsKGLGCNTvHLGYRNKTQVVNLeiyplG 133
Cdd:cd04280   1 NGTVPYVI-DGSFDESDRSLILRAMREIESNTCIRFVPRTtEKDY---IRIV-KGSGCWS-YVGRVGGRQVVSL-----G 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921384 134 EGCFRIGSIIHELLHVLGFEHQHVSQNRDQYVSIQWKNINPQYNINFVNNDNSTAWHdFDEGYDYESVMHYVPRAFSRNG 213
Cdd:cd04280  70 SGCFSLGTIVHELMHALGFYHEQSRPDRDDYVTINWENIQPGYEHNFDKYSPDTVTT-YGVPYDYGSVMHYGPTAFSKNG 148
                       170       180       190
                ....*....|....*....|....*....|..
gi 19921384 214 QPTIVPLREGAENMGQRFYMSEKDIRKLNKMY 245
Cdd:cd04280 149 KPTIVPKDPGYQIIGQREGLSFLDIKKINKMY 180
 
Name Accession Description Interval E-value
ZnMc_astacin_like cd04280
Zinc-dependent metalloprotease, astacin_like subfamily or peptidase family M12A, a group of ...
55-245 1.15e-72

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: 219.75  E-value: 1.15e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921384  55 NRTVPYMIeDDAFADSHYREILRAISIIEENSCVIFKPAT-EMDFpmaLVITsKGLGCNTvHLGYRNKTQVVNLeiyplG 133
Cdd:cd04280   1 NGTVPYVI-DGSFDESDRSLILRAMREIESNTCIRFVPRTtEKDY---IRIV-KGSGCWS-YVGRVGGRQVVSL-----G 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921384 134 EGCFRIGSIIHELLHVLGFEHQHVSQNRDQYVSIQWKNINPQYNINFVNNDNSTAWHdFDEGYDYESVMHYVPRAFSRNG 213
Cdd:cd04280  70 SGCFSLGTIVHELMHALGFYHEQSRPDRDDYVTINWENIQPGYEHNFDKYSPDTVTT-YGVPYDYGSVMHYGPTAFSKNG 148
                       170       180       190
                ....*....|....*....|....*....|..
gi 19921384 214 QPTIVPLREGAENMGQRFYMSEKDIRKLNKMY 245
Cdd:cd04280 149 KPTIVPKDPGYQIIGQREGLSFLDIKKINKMY 180
Astacin pfam01400
Astacin (Peptidase family M12A); The members of this family are enzymes that cleave peptides. ...
53-249 2.37e-52

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: 168.23  E-value: 2.37e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921384    53 WPNRTVPYMIeDDAFADSHYREILRAISIIEENSCVIFKPATEMDFPMALVITsKGLGCNTvHLGYRNKTQVVNLeiypl 132
Cdd:pfam01400   3 WPNGPIPYVI-DGSLTGLARALIRQAMRHWENKTCIRFVERTPAPDNNYLFFF-KGDGCYS-YVGRVGGRQPVSI----- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921384   133 GEGCFRIGSIIHELLHVLGFEHQHVSQNRDQYVSIQWKNINPQYNINFVNNDNSTAwHDFDEGYDYESVMHYVPRAFSRN 212
Cdd:pfam01400  75 GDGCDKFGIIVHELGHALGFFHEQSRPDRDDYVSINWDNIDPGQEGNFDKYDPSEV-DSYGVPYDYGSIMHYGPNAFSKN 153
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 19921384   213 G-QPTIVPLREGAEN-MGQRFYMSEKDIRKLNKMYRCPD 249
Cdd:pfam01400 154 GsLPTIVPKDNDYQAtIGQRVKLSFYDIKKINKLYKCPS 192
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
53-200 1.86e-25

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: 97.42  E-value: 1.86e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921384     53 WPNRTVPYMIEDDAFADSHYREILRAISIIEENSCVIFKPATEMDFPMaLVITSKGLGCNTVHLGYRNKTQVVNLEiypl 132
Cdd:smart00235   5 WPKGTVPYVIDSSSLSPEEREAIAKALAEWSDVTCIRFVERTGTADIY-ISFGSGDSGCTLSHAGRPGGDQHLSLG---- 79
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19921384    133 gEGCFRIGSIIHELLHVLGFEHQHVSQNRDQYVSIQWKNINP-QYNINFVNNDNstawhdfdEGYDYES 200
Cdd:smart00235  80 -NGCINTGVAAHELGHALGLYHEQSRSDRDNYMYINYTNIDTrNFDLSEDDSLG--------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 ...
55-245 1.15e-72

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: 219.75  E-value: 1.15e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921384  55 NRTVPYMIeDDAFADSHYREILRAISIIEENSCVIFKPAT-EMDFpmaLVITsKGLGCNTvHLGYRNKTQVVNLeiyplG 133
Cdd:cd04280   1 NGTVPYVI-DGSFDESDRSLILRAMREIESNTCIRFVPRTtEKDY---IRIV-KGSGCWS-YVGRVGGRQVVSL-----G 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921384 134 EGCFRIGSIIHELLHVLGFEHQHVSQNRDQYVSIQWKNINPQYNINFVNNDNSTAWHdFDEGYDYESVMHYVPRAFSRNG 213
Cdd:cd04280  70 SGCFSLGTIVHELMHALGFYHEQSRPDRDDYVTINWENIQPGYEHNFDKYSPDTVTT-YGVPYDYGSVMHYGPTAFSKNG 148
                       170       180       190
                ....*....|....*....|....*....|..
gi 19921384 214 QPTIVPLREGAENMGQRFYMSEKDIRKLNKMY 245
Cdd:cd04280 149 KPTIVPKDPGYQIIGQREGLSFLDIKKINKMY 180
Astacin pfam01400
Astacin (Peptidase family M12A); The members of this family are enzymes that cleave peptides. ...
53-249 2.37e-52

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: 168.23  E-value: 2.37e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921384    53 WPNRTVPYMIeDDAFADSHYREILRAISIIEENSCVIFKPATEMDFPMALVITsKGLGCNTvHLGYRNKTQVVNLeiypl 132
Cdd:pfam01400   3 WPNGPIPYVI-DGSLTGLARALIRQAMRHWENKTCIRFVERTPAPDNNYLFFF-KGDGCYS-YVGRVGGRQPVSI----- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921384   133 GEGCFRIGSIIHELLHVLGFEHQHVSQNRDQYVSIQWKNINPQYNINFVNNDNSTAwHDFDEGYDYESVMHYVPRAFSRN 212
Cdd:pfam01400  75 GDGCDKFGIIVHELGHALGFFHEQSRPDRDDYVSINWDNIDPGQEGNFDKYDPSEV-DSYGVPYDYGSIMHYGPNAFSKN 153
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 19921384   213 G-QPTIVPLREGAEN-MGQRFYMSEKDIRKLNKMYRCPD 249
Cdd:pfam01400 154 GsLPTIVPKDNDYQAtIGQRVKLSFYDIKKINKLYKCPS 192
ZnMc_hatching_enzyme cd04283
Zinc-dependent metalloprotease, hatching enzyme-like subfamily. Hatching enzymes are secreted ...
44-247 1.18e-48

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: 158.58  E-value: 1.18e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921384  44 NGIVnqiyhwpnrTVPYMIeDDAFADSHYREILRAISIIEENSCVIFKP-ATEMDFpmaLVITSKGlGCNTvHLGYRNKT 122
Cdd:cd04283   1 NGIV---------YVPYVI-SPQYSENERAVIEKAMQEFETLTCVRFVPrTTERDY---LNIESRS-GCWS-YIGRQGGR 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921384 123 QVVNLEIYplgeGCFRIGSIIHELLHVLGFEHQHVSQNRDQYVSIQWKNINPQYNINFVNNDNSTawhdFDEGYDYESVM 202
Cdd:cd04283  66 QTVSLQKQ----GCMYKGIIQHELLHALGFYHEQTRSDRDKYVRINWENIIPDQLYNFDKQDTNN----LGTPYDYSSVM 137
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 19921384 203 HYVPRAFSRNGQPTIVPLREGAENMGQRFYMSEKDIRKLNKMYRC 247
Cdd:cd04283 138 HYGRYAFSINGKPTIVPIPDPNVPIGQRQGMSNLDILRINKLYNC 182
ZnMc_meprin cd04282
Zinc-dependent metalloprotease, meprin_like subfamily. Meprins are membrane-bound or secreted ...
31-247 1.42e-37

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: 131.44  E-value: 1.42e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921384  31 YQGDIKAHPIRTRNGIVNQIYHWPNrTVPYMIEDDAFADSHyREILRAISIIEENSCVIFKP-ATEMDFpmalVITSKGL 109
Cdd:cd04282  24 FEGDILLDEGQSRNGLIGDTYRWPF-PIPYILDDSLDLNAK-GVILKAFEMYRLKSCVDFKPyEGESNY----IFFFKGS 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921384 110 GCntvhlgYRNKTQVVNLEIYPLGEGCFRIGSIIHELLHVLGFEHQHVSQNRDQYVSIQWKNINPQYNINFVNNDNSTAw 189
Cdd:cd04282  98 GC------WSMVGDQQGGQNLSIGAGCDYKATVEHEFLHALGFYHEQSRSDRDDYVKIWWDQILSGREHNFNKYDDSFS- 170
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921384 190 HDFDEGYDYESVMHYVPRAFSRNG-QPTIVPLREGAEN-MGQRFYMSEKDIRKLNKMYRC 247
Cdd:cd04282 171 TDLNTPYDYESVMHYSPFSFNKGAsEPTITTKIPEFNDiIGQRLDFSDIDLERLNRMYNC 230
ZnMc_BMP1_TLD cd04281
Zinc-dependent metalloprotease; BMP1/TLD-like subfamily. BMP1 (Bone morphogenetic protein 1) ...
53-248 4.66e-31

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: 113.69  E-value: 4.66e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921384  53 WPNRTVPYMIeDDAFADSHYREILRAISIIEENSCVIFKPAT-EMDFpmaLVITSKGLGCNTvHLGYR-NKTQVVNLeiy 130
Cdd:cd04281  10 WPGGVIPYVI-DGNFTGSQRAMFKQAMRHWENFTCVTFVERTpEENY---IVFTYRPCGCCS-YVGRRgNGPQAISI--- 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921384 131 plGEGCFRIGSIIHELLHVLGFEHQHVSQNRDQYVSIQWKNINPQYNINFVNNDnSTAWHDFDEGYDYESVMHYVPRAFS 210
Cdd:cd04281  82 --GKNCDKFGIVVHELGHVIGFWHEHTRPDRDDHVTIIRENIQPGQEYNFLKME-PEEVDSLGEPYDFDSIMHYARNTFS 158
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 19921384 211 RNG-QPTIVPLREGA---ENMGQRFYMSEKDIRKLNKMYRCP 248
Cdd:cd04281 159 RGMfLDTILPKRDPNgvrPEIGQRTRLSEGDIIQANKLYKCP 200
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
53-200 1.86e-25

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: 97.42  E-value: 1.86e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921384     53 WPNRTVPYMIEDDAFADSHYREILRAISIIEENSCVIFKPATEMDFPMaLVITSKGLGCNTVHLGYRNKTQVVNLEiypl 132
Cdd:smart00235   5 WPKGTVPYVIDSSSLSPEEREAIAKALAEWSDVTCIRFVERTGTADIY-ISFGSGDSGCTLSHAGRPGGDQHLSLG---- 79
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19921384    133 gEGCFRIGSIIHELLHVLGFEHQHVSQNRDQYVSIQWKNINP-QYNINFVNNDNstawhdfdEGYDYES 200
Cdd:smart00235  80 -NGCINTGVAAHELGHALGLYHEQSRSDRDNYMYINYTNIDTrNFDLSEDDSLG--------IPYDYGS 139
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
56-245 9.22e-10

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: 55.99  E-value: 9.22e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921384  56 RTVPYMIEDDAFADS-------HYREILRAISIIEENSCVIFKPATEMDFP--MALVITSKGLGCNTVHLGYR-----NK 121
Cdd:cd00203   1 KVIPYVVVADDRDVEeenlsaqIQSLILIAMQIWRDYLNIRFVLVGVEIDKadIAILVTRQDFDGGTGGWAYLgrvcdSL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921384 122 TQVVNLEIYPLGEGCFRiGSIIHELLHVLGFEHQHVSQNRDQYVSIQWKNINpqyninfvnndnstawhdfdEGYDYESV 201
Cdd:cd00203  81 RGVGVLQDNQSGTKEGA-QTIAHELGHALGFYHDHDRKDRDDYPTIDDTLNA--------------------EDDDYYSV 139
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 19921384 202 MHYVPRAFSrngqptivplregaenMGQRFYMSEKDIRKLNKMY 245
Cdd:cd00203 140 MSYTKGSFS----------------DGQRKDFSQCDIDQINKLY 167
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
55-245 1.15e-05

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: 44.41  E-value: 1.15e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921384  55 NRTVPYMIeDDAFADSHYREILRAISIIEENSCVIFKPATEMDfPMALVITSK-----GLGCNTVHLGYRN-KTQVVNLE 128
Cdd:cd04268   1 KKPITYYI-DDSVPDKLRAAILDAIEAWNKAFAIGFKNANDVD-PADIRYSVIrwipyNDGTWSYGPSQVDpLTGEILLA 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921384 129 IYPLGEGCFRI------GSIIHELLHVLGFEHQHVSQNRDQYVsiqwkninpqyninfvnndnstawHDFDEGYDYESVM 202
Cdd:cd04268  79 RVYLYSSFVEYsgarlrNTAEHELGHALGLRHNFAASDRDDNV------------------------DLLAEKGDTSSVM 134
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 19921384 203 HYVPRAFSRNGQPtivplregaenmGQRFYMSEKDIRKLNKMY 245
Cdd:cd04268 135 DYAPSNFSIQLGD------------GQKYTIGPYDIAAIKKLY 165
ZnMc_MMP_like_3 cd04327
Zinc-dependent metalloprotease; MMP_like sub-family 3. A group of bacterial and fungal ...
142-216 6.32e-04

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: 39.67  E-value: 6.32e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921384 142 IIHELLHVLGFEHQHvsQNRDqyVSIQWkniNPQ----YNINFVNNDNSTAWHDF-----DEG------YDYESVMHY-V 205
Cdd:cd04327  96 VLHEFGHALGFIHEH--QSPA--ANIPW---DKEavyaYFSGPPNWDRETVINHNvfaklDDGdvayspYDPDSIMHYpF 168
                        90
                ....*....|.
gi 19921384 206 PRAFSRNGQPT 216
Cdd:cd04327 169 PGSLTLDGEEV 179
 
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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