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Conserved domains on  [gi|71993835|ref|NP_001024789|]
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Zinc metalloproteinase nas-11 [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. ...
 339-537 3.81e-88

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: 270.69  E-value: 3.81e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71993835   339 KKWdPSSPIRYVLDSSLEDLDKNDVRAAIYEIEKNTCIRFKELSSPPtgsHIVYYKVDSPTFCGlSYVGRADPANPVYLS 418
Cdd:pfam01400   1 KKW-PNGPIPYVIDGSLTGLARALIRQAMRHWENKTCIRFVERTPAP---DNNYLFFFKGDGCY-SYVGRVGGRQPVSIG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71993835   419 FGCDNnKGVAIHETMHALGVAHQHLRNDRDQFITINWSNIDPQQYDAFVVVDSKLYTSYGVKYAYDSIMHYNGYTAAQNI 498
Cdd:pfam01400  76 DGCDK-FGIIVHELGHALGFFHEQSRPDRDDYVSINWDNIDPGQEGNFDKYDPSEVDSYGVPYDYGSIMHYGPNAFSKNG 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 71993835   499 AIPTMNPKTNsaVNLKVLGQRQKMGTTDIELLKKMY-CQP 537
Cdd:pfam01400 155 SLPTIVPKDN--DYQATIGQRVKLSFYDIKKINKLYkCPS 192
ShK pfam01549
ShK domain-like; This domain of is found in several C. elegans proteins. The domain is 30 ...
 538-575 9.44e-10

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: 53.94  E-value: 9.44e-10
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 71993835   538 GCDDKNVYCGAWAlKDLCKNPGHDQYMAANCKKSCGLC 575
Cdd:pfam01549   1 SCVDPHSDCASWA-ALGCTSPFYQDFMKENCPKTCGFC 37
 
Name Accession Description Interval E-value
Astacin pfam01400
Astacin (Peptidase family M12A); The members of this family are enzymes that cleave peptides. ...
 339-537 3.81e-88

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: 270.69  E-value: 3.81e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71993835   339 KKWdPSSPIRYVLDSSLEDLDKNDVRAAIYEIEKNTCIRFKELSSPPtgsHIVYYKVDSPTFCGlSYVGRADPANPVYLS 418
Cdd:pfam01400   1 KKW-PNGPIPYVIDGSLTGLARALIRQAMRHWENKTCIRFVERTPAP---DNNYLFFFKGDGCY-SYVGRVGGRQPVSIG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71993835   419 FGCDNnKGVAIHETMHALGVAHQHLRNDRDQFITINWSNIDPQQYDAFVVVDSKLYTSYGVKYAYDSIMHYNGYTAAQNI 498
Cdd:pfam01400  76 DGCDK-FGIIVHELGHALGFFHEQSRPDRDDYVSINWDNIDPGQEGNFDKYDPSEVDSYGVPYDYGSIMHYGPNAFSKNG 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 71993835   499 AIPTMNPKTNsaVNLKVLGQRQKMGTTDIELLKKMY-CQP 537
Cdd:pfam01400 155 SLPTIVPKDN--DYQATIGQRVKLSFYDIKKINKLYkCPS 192
ZnMc_astacin_like cd04280
Zinc-dependent metalloprotease, astacin_like subfamily or peptidase family M12A, a group of ...
 346-534 1.02e-57

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: 191.25  E-value: 1.02e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71993835 346 PIRYVLDSSLEDLDKNDVRAAIYEIEKNTCIRFKELSSPPtgSHIVYYKVDSptfCGlSYVGRADPANPVYLSFGCDNnK 425
Cdd:cd04280   3 TVPYVIDGSFDESDRSLILRAMREIESNTCIRFVPRTTEK--DYIRIVKGSG---CW-SYVGRVGGRQVVSLGSGCFS-L 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71993835 426 GVAIHETMHALGVAHQHLRNDRDQFITINWSNIDPQQYDAFVVVDSKLYTSYGVKYAYDSIMHYNGYTAAQNiAIPTMNP 505
Cdd:cd04280  76 GTIVHELMHALGFYHEQSRPDRDDYVTINWENIQPGYEHNFDKYSPDTVTTYGVPYDYGSVMHYGPTAFSKN-GKPTIVP 154

                       170       180
                ....*....|....*....|....*....
gi 71993835 506 KTNSAVNlkvLGQRQKMGTTDIELLKKMY 534
Cdd:cd04280 155 KDPGYQI---IGQREGLSFLDIKKINKMY 180
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 339-485 3.39e-35

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: 129.01  E-value: 3.39e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71993835    339 KKWdPSSPIRYVLD-SSLEDLDKNDVRAAIYEIEKNTCIRFKELSSPPTgSHIVYYKVDSptFCGLSYVGRADPANPVYL 417
Cdd:smart00235   3 KKW-PKGTVPYVIDsSSLSPEEREAIAKALAEWSDVTCIRFVERTGTAD-IYISFGSGDS--GCTLSHAGRPGGDQHLSL 78

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71993835    418 SFGCDNnKGVAIHETMHALGVAHQHLRNDRDQFITINWSNIDPQQYDAFvvvdskLYTSYGVKYAYDS 485
Cdd:smart00235  79 GNGCIN-TGVAAHELGHALGLYHEQSRSDRDNYMYINYTNIDTRNFDLS------EDDSLGIPYDYGS 139
ShK pfam01549
ShK domain-like; This domain of is found in several C. elegans proteins. The domain is 30 ...
 538-575 9.44e-10

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: 53.94  E-value: 9.44e-10
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 71993835   538 GCDDKNVYCGAWAlKDLCKNPGHDQYMAANCKKSCGLC 575
Cdd:pfam01549   1 SCVDPHSDCASWA-ALGCTSPFYQDFMKENCPKTCGFC 37
ShKT smart00254
ShK toxin domain; ShK toxin domain
 539-575 1.37e-08

ShK toxin domain; ShK toxin domain


Pssm-ID: 214586 [Multi-domain]  Cd Length: 33  Bit Score: 50.46  E-value: 1.37e-08
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 71993835    539 CDDKNVYCGAWAlKDLCKNPghdQYMAANCKKSCGLC 575
Cdd:smart00254   1 CVDRHPDCAAWA-KGFCTNP---FYMKSNCPKTCGFC 33
 
Name Accession Description Interval E-value
Astacin pfam01400
Astacin (Peptidase family M12A); The members of this family are enzymes that cleave peptides. ...
 339-537 3.81e-88

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: 270.69  E-value: 3.81e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71993835   339 KKWdPSSPIRYVLDSSLEDLDKNDVRAAIYEIEKNTCIRFKELSSPPtgsHIVYYKVDSPTFCGlSYVGRADPANPVYLS 418
Cdd:pfam01400   1 KKW-PNGPIPYVIDGSLTGLARALIRQAMRHWENKTCIRFVERTPAP---DNNYLFFFKGDGCY-SYVGRVGGRQPVSIG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71993835   419 FGCDNnKGVAIHETMHALGVAHQHLRNDRDQFITINWSNIDPQQYDAFVVVDSKLYTSYGVKYAYDSIMHYNGYTAAQNI 498
Cdd:pfam01400  76 DGCDK-FGIIVHELGHALGFFHEQSRPDRDDYVSINWDNIDPGQEGNFDKYDPSEVDSYGVPYDYGSIMHYGPNAFSKNG 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 71993835   499 AIPTMNPKTNsaVNLKVLGQRQKMGTTDIELLKKMY-CQP 537
Cdd:pfam01400 155 SLPTIVPKDN--DYQATIGQRVKLSFYDIKKINKLYkCPS 192
ZnMc_astacin_like cd04280
Zinc-dependent metalloprotease, astacin_like subfamily or peptidase family M12A, a group of ...
 346-534 1.02e-57

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: 191.25  E-value: 1.02e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71993835 346 PIRYVLDSSLEDLDKNDVRAAIYEIEKNTCIRFKELSSPPtgSHIVYYKVDSptfCGlSYVGRADPANPVYLSFGCDNnK 425
Cdd:cd04280   3 TVPYVIDGSFDESDRSLILRAMREIESNTCIRFVPRTTEK--DYIRIVKGSG---CW-SYVGRVGGRQVVSLGSGCFS-L 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71993835 426 GVAIHETMHALGVAHQHLRNDRDQFITINWSNIDPQQYDAFVVVDSKLYTSYGVKYAYDSIMHYNGYTAAQNiAIPTMNP 505
Cdd:cd04280  76 GTIVHELMHALGFYHEQSRPDRDDYVTINWENIQPGYEHNFDKYSPDTVTTYGVPYDYGSVMHYGPTAFSKN-GKPTIVP 154

                       170       180
                ....*....|....*....|....*....
gi 71993835 506 KTNSAVNlkvLGQRQKMGTTDIELLKKMY 534
Cdd:cd04280 155 KDPGYQI---IGQREGLSFLDIKKINKMY 180
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 339-485 3.39e-35

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: 129.01  E-value: 3.39e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71993835    339 KKWdPSSPIRYVLD-SSLEDLDKNDVRAAIYEIEKNTCIRFKELSSPPTgSHIVYYKVDSptFCGLSYVGRADPANPVYL 417
Cdd:smart00235   3 KKW-PKGTVPYVIDsSSLSPEEREAIAKALAEWSDVTCIRFVERTGTAD-IYISFGSGDS--GCTLSHAGRPGGDQHLSL 78

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71993835    418 SFGCDNnKGVAIHETMHALGVAHQHLRNDRDQFITINWSNIDPQQYDAFvvvdskLYTSYGVKYAYDS 485
Cdd:smart00235  79 GNGCIN-TGVAAHELGHALGLYHEQSRSDRDNYMYINYTNIDTRNFDLS------EDDSLGIPYDYGS 139
ZnMc_hatching_enzyme cd04283
Zinc-dependent metalloprotease, hatching enzyme-like subfamily. Hatching enzymes are secreted ...
 346-535 1.20e-34

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: 129.30  E-value: 1.20e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71993835 346 PIRYVLDSSLEDLDKNDVRAAIYEIEKNTCIRFKelsspPTGSHIVYYKVDSPTFCGlSYVGRADPANPVYLS-FGCdNN 424
Cdd:cd04283   5 YVPYVISPQYSENERAVIEKAMQEFETLTCVRFV-----PRTTERDYLNIESRSGCW-SYIGRQGGRQTVSLQkQGC-MY 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71993835 425 KGVAIHETMHALGVAHQHLRNDRDQFITINWSNIDPQQYDAFVVVDSKlytSYGVKYAYDSIMHYNGYTAAQNiAIPTMN 504
Cdd:cd04283  78 KGIIQHELLHALGFYHEQTRSDRDKYVRINWENIIPDQLYNFDKQDTN---NLGTPYDYSSVMHYGRYAFSIN-GKPTIV 153

                       170       180       190
                ....*....|....*....|....*....|.
gi 71993835 505 PKTNSAVnlkVLGQRQKMGTTDIELLKKMYC 535
Cdd:cd04283 154 PIPDPNV---PIGQRQGMSNLDILRINKLYN 181
ZnMc_BMP1_TLD cd04281
Zinc-dependent metalloprotease; BMP1/TLD-like subfamily. BMP1 (Bone morphogenetic protein 1) ...
 339-534 2.05e-26

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: 106.76  E-value: 2.05e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71993835 339 KKWdPSSPIRYVLDSSLEDLDKNDVRAAIYEIEKNTCIRFKELSspPTGSHIVYYKVDsptfCGL-SYVGR-ADPANPVY 416
Cdd:cd04281   8 RIW-PGGVIPYVIDGNFTGSQRAMFKQAMRHWENFTCVTFVERT--PEENYIVFTYRP----CGCcSYVGRrGNGPQAIS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71993835 417 LSFGCDNNkGVAIHETMHALGVAHQHLRNDRDQFITINWSNIDPQQYDAFVVVDSKLYTSYGVKYAYDSIMHYNGYTAAQ 496
Cdd:cd04281  81 IGKNCDKF-GIVVHELGHVIGFWHEHTRPDRDDHVTIIRENIQPGQEYNFLKMEPEEVDSLGEPYDFDSIMHYARNTFSR 159

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 71993835 497 NIAIPTMNPKTNSAVNLKVLGQRQKMGTTDIELLKKMY 534
Cdd:cd04281 160 GMFLDTILPKRDPNGVRPEIGQRTRLSEGDIIQANKLY 197
ZnMc_meprin cd04282
Zinc-dependent metalloprotease, meprin_like subfamily. Meprins are membrane-bound or secreted ...
 346-534 1.95e-20

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: 90.22  E-value: 1.95e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71993835 346 PIRYVLDSSLEDLDKNDVRAAIYEIEKNTCIRFKELSSPPTgsHIVYYKVDSptfCgLSYVGRADPANPVYLSFGCDNnK 425
Cdd:cd04282  49 PIPYILDDSLDLNAKGVILKAFEMYRLKSCVDFKPYEGESN--YIFFFKGSG---C-WSMVGDQQGGQNLSIGAGCDY-K 121

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71993835 426 GVAIHETMHALGVAHQHLRNDRDQFITINWSNIDPQQYDAFVVVDSKLYTSYGVKYAYDSIMHYNGYTAAQNIAIPTMNp 505
Cdd:cd04282 122 ATVEHEFLHALGFYHEQSRSDRDDYVKIWWDQILSGREHNFNKYDDSFSTDLNTPYDYESVMHYSPFSFNKGASEPTIT- 200

                       170       180
                ....*....|....*....|....*....
gi 71993835 506 kTNSAVNLKVLGQRQKMGTTDIELLKKMY 534
Cdd:cd04282 201 -TKIPEFNDIIGQRLDFSDIDLERLNRMY 228
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 346-534 6.44e-10

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: 58.28  E-value: 6.44e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71993835 346 PIRYVLDSSLEDLDKNDVRAAIYEIEKNTCIRFKE--LSSPPTGSHIVYYKVDSPTFCGLSYVGRADPA------NPVYL 417
Cdd:cd04268   3 PITYYIDDSVPDKLRAAILDAIEAWNKAFAIGFKNanDVDPADIRYSVIRWIPYNDGTWSYGPSQVDPLtgeillARVYL 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71993835 418 SFGC-----DNNKGVAIHETMHALGVAHQHLRNDRDqfitinwsnidpqqydafvvvdsKLYTSYGVKYAYDSIMHYngy 492
Cdd:cd04268  83 YSSFveysgARLRNTAEHELGHALGLRHNFAASDRD-----------------------DNVDLLAEKGDTSSVMDY--- 136

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 71993835 493 tAAQNIAIPTmnpktnsavnlkVLGQRQKMGTTDIELLKKMY 534
Cdd:cd04268 137 -APSNFSIQL------------GDGQKYTIGPYDIAAIKKLY 165
ShK pfam01549
ShK domain-like; This domain of is found in several C. elegans proteins. The domain is 30 ...
 538-575 9.44e-10

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: 53.94  E-value: 9.44e-10
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 71993835   538 GCDDKNVYCGAWAlKDLCKNPGHDQYMAANCKKSCGLC 575
Cdd:pfam01549   1 SCVDPHSDCASWA-ALGCTSPFYQDFMKENCPKTCGFC 37
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 346-489 3.04e-09

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: 56.38  E-value: 3.04e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71993835 346 PIRYVLDSSLEDLDKNDVRAAIYEI--------EKNTCIRFKeLSSPPTGSHIVYYKVDSPTFC----GLSYVGRADPA- 412
Cdd:cd00203   2 VIPYVVVADDRDVEEENLSAQIQSLiliamqiwRDYLNIRFV-LVGVEIDKADIAILVTRQDFDggtgGWAYLGRVCDSl 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71993835 413 --NPVYLSFGCDNN--KGVAIHETMHALGVAHQHLRNDRDQFITINWSNidpqqydafvvvdsklytsYGVKYAYDSIMH 488
Cdd:cd00203  81 rgVGVLQDNQSGTKegAQTIAHELGHALGFYHDHDRKDRDDYPTIDDTL-------------------NAEDDDYYSVMS 141


                .
gi 71993835 489 Y 489
Cdd:cd00203 142 Y 142
ShKT smart00254
ShK toxin domain; ShK toxin domain
 539-575 1.37e-08

ShK toxin domain; ShK toxin domain


Pssm-ID: 214586 [Multi-domain]  Cd Length: 33  Bit Score: 50.46  E-value: 1.37e-08
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 71993835    539 CDDKNVYCGAWAlKDLCKNPghdQYMAANCKKSCGLC 575
Cdd:smart00254   1 CVDRHPDCAAWA-KGFCTNP---FYMKSNCPKTCGFC 33
ZnMc_MMP_like_3 cd04327
Zinc-dependent metalloprotease; MMP_like sub-family 3. A group of bacterial and fungal ...
 339-489 2.86e-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: 45.06  E-value: 2.86e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71993835 339 KKWDPSSPIRYV-LDSSLEDLdKNDVRAAIYEIEKNTCIRFKELSSPPTGSHIVYYKVDSptfcGLSYVGR---ADPANP 414
Cdd:cd04327   1 KLWRNGTVLRIAfLGGPDAFL-KDKVRAAAREWLPYANLKFKFVTDADADIRISFTPGDG----YWSYVGTdalLIGADA 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71993835 415 VYLSFGCDNNKG-------VAIHETMHALGVAHQHLRndrdQFITINWS------------NIDPQQYDAFVVVDskLYT 475
Cdd:cd04327  76 PTMNLGWFTDDTpdpefsrVVLHEFGHALGFIHEHQS----PAANIPWDkeavyayfsgppNWDRETVINHNVFA--KLD 149

                       170
                ....*....|....*..
gi 71993835 476 SYGVKYA-YD--SIMHY 489
Cdd:cd04327 150 DGDVAYSpYDpdSIMHY 166
ZnMc_serralysin_like cd04277
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
 353-500 3.98e-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: 38.55  E-value: 3.98e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71993835 353 SSLEDLDKNDVRAAIYEIEKNTCIRFKELSSPPTGS-HIVYYKVDSPTFCGLSY----------VGRA------DPANPV 415
Cdd:cd04277  29 AALSAAQQAAARDALEAWEDVADIDFVEVSDNSGADiRFGNSSDPDGNTAGYAYypgsgsgtayGGDIwfnssyDTNSDS 108

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71993835 416 YLSFGcdnnKGVAIHETMHALGVAHQHLRNDrdqfitinwSNIDPQQYDAfvvvDSKLYTsygvkyaydsIMHYNGYTAA 495
Cdd:cd04277 109 PGSYG----YQTIIHEIGHALGLEHPGDYNG---------GDPVPPTYAL----DSREYT----------VMSYNSGYGN 161


                ....*
gi 71993835 496 QNIAI 500
Cdd:cd04277 162 GASAG 166
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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