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Conserved domains on  [gi|20129545|ref|NP_609758|]
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uncharacterized protein Dmel_CG15253 [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 ...
59-246 1.08e-85

Zinc-dependent metalloprotease, astacin_like subfamily or peptidase family M12A, a group of zinc-dependent proteolytic enzymes with a HExxH zinc-binding site/active site. Members of this family may have an amino terminal propeptide, which is cleaved to yield the active protease domain, which is consequently always found at the N-terminus in multi-domain architectures. This family includes: astacin, a digestive enzyme from Crayfish; meprin, a multiple domain membrane component that is constructed from a homologous alpha and beta chain, proteins involved in (bone) morphogenesis, tolloid from drosophila, and the sea urchin SPAN protein, which may also play a role in development.


:

Pssm-ID: 239807 [Multi-domain]  Cd Length: 180  Bit Score: 252.88  E-value: 1.08e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129545  59 NRIIYYHINSYIDEEHRNHIVSAIQKIESISCLTFKEATTdQKYYVNVTSEeGGCFSYIGYLNRVQQLNLQNneigvGCF 138
Cdd:cd04280   1 NGTVPYVIDGSFDESDRSLILRAMREIESNTCIRFVPRTT-EKDYIRIVKG-SGCWSYVGRVGGRQVVSLGS-----GCF 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129545 139 RLYTIVHEFLHALGFFHQQSAADRDDYVQIVEENITEGMEFNFDKYTEETVNDFGEKYDYGSVMHYGPYAFSKNGERTIL 218
Cdd:cd04280  74 SLGTIVHELMHALGFYHEQSRPDRDDYVTINWENIQPGYEHNFDKYSPDTVTTYGVPYDYGSVMHYGPTAFSKNGKPTIV 153
                       170       180
                ....*....|....*....|....*...
gi 20129545 219 ALEEGKEDvIGQRLELSETDIRKLNAIY 246
Cdd:cd04280 154 PKDPGYQI-IGQREGLSFLDIKKINKMY 180
 
Name Accession Description Interval E-value
ZnMc_astacin_like cd04280
Zinc-dependent metalloprotease, astacin_like subfamily or peptidase family M12A, a group of ...
59-246 1.08e-85

Zinc-dependent metalloprotease, astacin_like subfamily or peptidase family M12A, a group of zinc-dependent proteolytic enzymes with a HExxH zinc-binding site/active site. Members of this family may have an amino terminal propeptide, which is cleaved to yield the active protease domain, which is consequently always found at the N-terminus in multi-domain architectures. This family includes: astacin, a digestive enzyme from Crayfish; meprin, a multiple domain membrane component that is constructed from a homologous alpha and beta chain, proteins involved in (bone) morphogenesis, tolloid from drosophila, and the sea urchin SPAN protein, which may also play a role in development.


Pssm-ID: 239807 [Multi-domain]  Cd Length: 180  Bit Score: 252.88  E-value: 1.08e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129545  59 NRIIYYHINSYIDEEHRNHIVSAIQKIESISCLTFKEATTdQKYYVNVTSEeGGCFSYIGYLNRVQQLNLQNneigvGCF 138
Cdd:cd04280   1 NGTVPYVIDGSFDESDRSLILRAMREIESNTCIRFVPRTT-EKDYIRIVKG-SGCWSYVGRVGGRQVVSLGS-----GCF 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129545 139 RLYTIVHEFLHALGFFHQQSAADRDDYVQIVEENITEGMEFNFDKYTEETVNDFGEKYDYGSVMHYGPYAFSKNGERTIL 218
Cdd:cd04280  74 SLGTIVHELMHALGFYHEQSRPDRDDYVTINWENIQPGYEHNFDKYSPDTVTTYGVPYDYGSVMHYGPTAFSKNGKPTIV 153
                       170       180
                ....*....|....*....|....*...
gi 20129545 219 ALEEGKEDvIGQRLELSETDIRKLNAIY 246
Cdd:cd04280 154 PKDPGYQI-IGQREGLSFLDIKKINKMY 180
Astacin pfam01400
Astacin (Peptidase family M12A); The members of this family are enzymes that cleave peptides. ...
55-250 5.07e-71

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: 215.99  E-value: 5.07e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129545    55 YRWPNRIIYYHINSYIDEEHRNHIVSAIQKIESISCLTFKEATTDQKYYVNVTSEEGGCFSYIGYLNRVQQLNlqnneIG 134
Cdd:pfam01400   1 KKWPNGPIPYVIDGSLTGLARALIRQAMRHWENKTCIRFVERTPAPDNNYLFFFKGDGCYSYVGRVGGRQPVS-----IG 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129545   135 VGCFRLYTIVHEFLHALGFFHQQSAADRDDYVQIVEENITEGMEFNFDKYTEETVNDFGEKYDYGSVMHYGPYAFSKNG- 213
Cdd:pfam01400  76 DGCDKFGIIVHELGHALGFFHEQSRPDRDDYVSINWDNIDPGQEGNFDKYDPSEVDSYGVPYDYGSIMHYGPNAFSKNGs 155
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 20129545   214 ERTILALEEGKEDVIGQRLELSETDIRKLNAIYKCPT 250
Cdd:pfam01400 156 LPTIVPKDNDYQATIGQRVKLSFYDIKKINKLYKCPS 192
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
56-200 6.25e-32

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: 114.37  E-value: 6.25e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129545     56 RWPNRIIYYHINSY-IDEEHRNHIVSAIQKIESISCLTFKEATTDQKYYVNVTSEEGGCF-SYIGYLNRVQQLNLQNnei 133
Cdd:smart00235   4 KWPKGTVPYVIDSSsLSPEEREAIAKALAEWSDVTCIRFVERTGTADIYISFGSGDSGCTlSHAGRPGGDQHLSLGN--- 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 20129545    134 gvGCFRLYTIVHEFLHALGFFHQQSAADRDDYVQIVEENItegMEFNFDKYTEETVndfGEKYDYGS 200
Cdd:smart00235  81 --GCINTGVAAHELGHALGLYHEQSRSDRDNYMYINYTNI---DTRNFDLSEDDSL---GIPYDYGS 139
 
Name Accession Description Interval E-value
ZnMc_astacin_like cd04280
Zinc-dependent metalloprotease, astacin_like subfamily or peptidase family M12A, a group of ...
59-246 1.08e-85

Zinc-dependent metalloprotease, astacin_like subfamily or peptidase family M12A, a group of zinc-dependent proteolytic enzymes with a HExxH zinc-binding site/active site. Members of this family may have an amino terminal propeptide, which is cleaved to yield the active protease domain, which is consequently always found at the N-terminus in multi-domain architectures. This family includes: astacin, a digestive enzyme from Crayfish; meprin, a multiple domain membrane component that is constructed from a homologous alpha and beta chain, proteins involved in (bone) morphogenesis, tolloid from drosophila, and the sea urchin SPAN protein, which may also play a role in development.


Pssm-ID: 239807 [Multi-domain]  Cd Length: 180  Bit Score: 252.88  E-value: 1.08e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129545  59 NRIIYYHINSYIDEEHRNHIVSAIQKIESISCLTFKEATTdQKYYVNVTSEeGGCFSYIGYLNRVQQLNLQNneigvGCF 138
Cdd:cd04280   1 NGTVPYVIDGSFDESDRSLILRAMREIESNTCIRFVPRTT-EKDYIRIVKG-SGCWSYVGRVGGRQVVSLGS-----GCF 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129545 139 RLYTIVHEFLHALGFFHQQSAADRDDYVQIVEENITEGMEFNFDKYTEETVNDFGEKYDYGSVMHYGPYAFSKNGERTIL 218
Cdd:cd04280  74 SLGTIVHELMHALGFYHEQSRPDRDDYVTINWENIQPGYEHNFDKYSPDTVTTYGVPYDYGSVMHYGPTAFSKNGKPTIV 153
                       170       180
                ....*....|....*....|....*...
gi 20129545 219 ALEEGKEDvIGQRLELSETDIRKLNAIY 246
Cdd:cd04280 154 PKDPGYQI-IGQREGLSFLDIKKINKMY 180
Astacin pfam01400
Astacin (Peptidase family M12A); The members of this family are enzymes that cleave peptides. ...
55-250 5.07e-71

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: 215.99  E-value: 5.07e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129545    55 YRWPNRIIYYHINSYIDEEHRNHIVSAIQKIESISCLTFKEATTDQKYYVNVTSEEGGCFSYIGYLNRVQQLNlqnneIG 134
Cdd:pfam01400   1 KKWPNGPIPYVIDGSLTGLARALIRQAMRHWENKTCIRFVERTPAPDNNYLFFFKGDGCYSYVGRVGGRQPVS-----IG 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129545   135 VGCFRLYTIVHEFLHALGFFHQQSAADRDDYVQIVEENITEGMEFNFDKYTEETVNDFGEKYDYGSVMHYGPYAFSKNG- 213
Cdd:pfam01400  76 DGCDKFGIIVHELGHALGFFHEQSRPDRDDYVSINWDNIDPGQEGNFDKYDPSEVDSYGVPYDYGSIMHYGPNAFSKNGs 155
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 20129545   214 ERTILALEEGKEDVIGQRLELSETDIRKLNAIYKCPT 250
Cdd:pfam01400 156 LPTIVPKDNDYQATIGQRVKLSFYDIKKINKLYKCPS 192
ZnMc_hatching_enzyme cd04283
Zinc-dependent metalloprotease, hatching enzyme-like subfamily. Hatching enzymes are secreted ...
64-248 6.10e-56

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: 177.07  E-value: 6.10e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129545  64 YHINSYIDEEHRNHIVSAIQKIESISCLTFKEATTdQKYYVNVTSEeGGCFSYIGYLNRVQQLNLQNNeigvGCFRLYTI 143
Cdd:cd04283   8 YVISPQYSENERAVIEKAMQEFETLTCVRFVPRTT-ERDYLNIESR-SGCWSYIGRQGGRQTVSLQKQ----GCMYKGII 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129545 144 VHEFLHALGFFHQQSAADRDDYVQIVEENITEGMEFNFDKYteETvNDFGEKYDYGSVMHYGPYAFSKNGERTILALEEG 223
Cdd:cd04283  82 QHELLHALGFYHEQTRSDRDKYVRINWENIIPDQLYNFDKQ--DT-NNLGTPYDYSSVMHYGRYAFSINGKPTIVPIPDP 158
                       170       180
                ....*....|....*....|....*
gi 20129545 224 KEdVIGQRLELSETDIRKLNAIYKC 248
Cdd:cd04283 159 NV-PIGQRQGMSNLDILRINKLYNC 182
ZnMc_meprin cd04282
Zinc-dependent metalloprotease, meprin_like subfamily. Meprins are membrane-bound or secreted ...
36-248 5.43e-55

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: 5.43e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129545  36 IEGDMV-PSGSSRNIWRNETYRWPNRIIYYHINSyIDEEHRNHIVSAIQKIESISCLTFKEATTDQKYYVnvTSEEGGCF 114
Cdd:cd04282  24 FEGDILlDEGQSRNGLIGDTYRWPFPIPYILDDS-LDLNAKGVILKAFEMYRLKSCVDFKPYEGESNYIF--FFKGSGCW 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129545 115 SYIGylnrvQQLNLQNNEIGVGCFRLYTIVHEFLHALGFFHQQSAADRDDYVQIVEENITEGMEFNFDKYTEETVNDFGE 194
Cdd:cd04282 101 SMVG-----DQQGGQNLSIGAGCDYKATVEHEFLHALGFYHEQSRSDRDDYVKIWWDQILSGREHNFNKYDDSFSTDLNT 175
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 20129545 195 KYDYGSVMHYGPYAFSKNG-ERTILALEEGKEDVIGQRLELSETDIRKLNAIYKC 248
Cdd:cd04282 176 PYDYESVMHYSPFSFNKGAsEPTITTKIPEFNDIIGQRLDFSDIDLERLNRMYNC 230
ZnMc_BMP1_TLD cd04281
Zinc-dependent metalloprotease; BMP1/TLD-like subfamily. BMP1 (Bone morphogenetic protein 1) ...
56-249 1.37e-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: 148.74  E-value: 1.37e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129545  56 RWPNRIIYYHINSYIDEEHRNHIVSAIQKIESISCLTFKEaTTDQKYYVNVTSEEGGCFSYIGYLNRvqqlNLQNNEIGV 135
Cdd:cd04281   9 IWPGGVIPYVIDGNFTGSQRAMFKQAMRHWENFTCVTFVE-RTPEENYIVFTYRPCGCCSYVGRRGN----GPQAISIGK 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129545 136 GCFRLYTIVHEFLHALGFFHQQSAADRDDYVQIVEENITEGMEFNFDKYTEETVNDFGEKYDYGSVMHYGPYAFSKNGE- 214
Cdd:cd04281  84 NCDKFGIVVHELGHVIGFWHEHTRPDRDDHVTIIRENIQPGQEYNFLKMEPEEVDSLGEPYDFDSIMHYARNTFSRGMFl 163
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 20129545 215 RTIL--ALEEGKEDVIGQRLELSETDIRKLNAIYKCP 249
Cdd:cd04281 164 DTILpkRDPNGVRPEIGQRTRLSEGDIIQANKLYKCP 200
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
56-200 6.25e-32

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: 114.37  E-value: 6.25e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129545     56 RWPNRIIYYHINSY-IDEEHRNHIVSAIQKIESISCLTFKEATTDQKYYVNVTSEEGGCF-SYIGYLNRVQQLNLQNnei 133
Cdd:smart00235   4 KWPKGTVPYVIDSSsLSPEEREAIAKALAEWSDVTCIRFVERTGTADIYISFGSGDSGCTlSHAGRPGGDQHLSLGN--- 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 20129545    134 gvGCFRLYTIVHEFLHALGFFHQQSAADRDDYVQIVEENItegMEFNFDKYTEETVndfGEKYDYGS 200
Cdd:smart00235  81 --GCINTGVAAHELGHALGLYHEQSRSDRDNYMYINYTNI---DTRNFDLSEDDSL---GIPYDYGS 139
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
62-246 7.63e-16

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: 72.91  E-value: 7.63e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129545  62 IYYHINSYIDEEHRNHIVSAIQKIESISCLTFKEATTDQKYYVNV-----TSEEGGCFSYIG----------YLNRVQQL 126
Cdd:cd04268   4 ITYYIDDSVPDKLRAAILDAIEAWNKAFAIGFKNANDVDPADIRYsvirwIPYNDGTWSYGPsqvdpltgeiLLARVYLY 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129545 127 NlqNNEIGVGCFRLYTIVHEFLHALGFFHQQSAADRDDYvqiveenitegmefnfdkyteetVNDFGEKYDYGSVMHYGP 206
Cdd:cd04268  84 S--SFVEYSGARLRNTAEHELGHALGLRHNFAASDRDDN-----------------------VDLLAEKGDTSSVMDYAP 138
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 20129545 207 YAFSKNGertilaleegkedVIGQRLELSETDIRKLNAIY 246
Cdd:cd04268 139 SNFSIQL-------------GDGQKYTIGPYDIAAIKKLY 165
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
67-246 2.08e-11

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: 60.61  E-value: 2.08e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129545  67 NSYIDEEHRNHIVSAIQKIESISCLTFKEATTD-QKYYVNVT------SEEGGCFSYIG--YLNRVQQLNLQNNEIGVGC 137
Cdd:cd00203  16 EENLSAQIQSLILIAMQIWRDYLNIRFVLVGVEiDKADIAILvtrqdfDGGTGGWAYLGrvCDSLRGVGVLQDNQSGTKE 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129545 138 FRlYTIVHEFLHALGFFHQQSAADRDDYVQIveenitegmefnfdkyteeTVNDFGEKYDYGSVMHYGPYAFSkngerti 217
Cdd:cd00203  96 GA-QTIAHELGHALGFYHDHDRKDRDDYPTI-------------------DDTLNAEDDDYYSVMSYTKGSFS------- 148
                       170       180
                ....*....|....*....|....*....
gi 20129545 218 laleegkedvIGQRLELSETDIRKLNAIY 246
Cdd:cd00203 149 ----------DGQRKDFSQCDIDQINKLY 167
ZnMc_MMP_like_3 cd04327
Zinc-dependent metalloprotease; MMP_like sub-family 3. A group of bacterial and fungal ...
71-239 2.60e-06

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: 46.60  E-value: 2.60e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129545  71 DEEHRNHIVSAIQKIESISCLTFKEAT-TDQKYYVNVTsEEGGCFSYIG---YLNRVQQ--LNLQ-NNEIGVGCFRLYTI 143
Cdd:cd04327  18 DAFLKDKVRAAAREWLPYANLKFKFVTdADADIRISFT-PGDGYWSYVGtdaLLIGADAptMNLGwFTDDTPDPEFSRVV 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129545 144 VHEFLHALGFFH--QQSAADR--DD-----YVQIVEENITEGMEFN--FDKYTEETVNdfGEKYDYGSVMHYG-PYAFSK 211
Cdd:cd04327  97 LHEFGHALGFIHehQSPAANIpwDKeavyaYFSGPPNWDRETVINHnvFAKLDDGDVA--YSPYDPDSIMHYPfPGSLTL 174
                       170       180
                ....*....|....*....|....*...
gi 20129545 212 NGertilaleegkEDVIGQRlELSETDI 239
Cdd:cd04327 175 DG-----------EEVPPNR-TLSDKDK 190
ZnMc_serralysin_like cd04277
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
50-198 4.85e-03

Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases are important virulence factors in pathogenic bacteria. They may be secreted into the medium via a mechanism found in gram-negative bacteria, that does not require n-terminal signal sequences which are cleaved after the transmembrane translocation. A calcium-binding domain c-terminal to the metalloprotease domain, which contains multiple tandem repeats of a nine-residue motif including the pattern GGxGxD, and which forms a parallel beta roll may be involved in the translocation mechanism and/or substrate binding. Serralysin family members may have a broad spectrum of substrates each, including host immunoglobulins, complement proteins, cell matrix and cytoskeletal proteins, as well as antimicrobial peptides.


Pssm-ID: 239804 [Multi-domain]  Cd Length: 186  Bit Score: 37.01  E-value: 4.85e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129545  50 WRNETYRWPNRIIYYHINSYIDEEHRNHIVSAIQKIESISCLTFKEATTDQK---YYVNVTSEEGGCFSYIGYLNRVQQL 126
Cdd:cd04277  11 TGGPYSYGYGREEDTTNTAALSAAQQAAARDALEAWEDVADIDFVEVSDNSGadiRFGNSSDPDGNTAGYAYYPGSGSGT 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129545 127 NLQ----------NNEIGVGCFRLYTIVHEFLHALGFFHQQSAADRDDYVQIVEENITEG--MefnfdKYTEETVNDFGE 194
Cdd:cd04277  91 AYGgdiwfnssydTNSDSPGSYGYQTIIHEIGHALGLEHPGDYNGGDPVPPTYALDSREYtvM-----SYNSGYGNGASA 165

                ....
gi 20129545 195 KYDY 198
Cdd:cd04277 166 GGGY 169
 
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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