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Conserved domains on  [gi|568931271|ref|XP_006538942|]
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matrix metalloproteinase-23 isoform X1 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 88-284 1.62e-58

Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are responsible for a great deal of pericellular proteolysis of extracellular matrix and cell surface molecules, playing crucial roles in morphogenesis, cell fate specification, cell migration, tissue repair, tumorigenesis, gain or loss of tissue-specific functions, and apoptosis. In many instances, they are anchored to cell membranes via trans-membrane domains, and their activity is controlled via TIMPs (tissue inhibitors of metalloproteinases).


:

Pssm-ID: 239805 [Multi-domain]  Cd Length: 157  Bit Score: 188.18  E-value: 1.62e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931271  88 RWDHFNLTYRChldqrggwsghnsdtntdsnitaalhhrvLSFPRNLlSPEETRRGLAAAFRMWSDVSPFSFREVAPERP 167
Cdd:cd04278    1 KWSKTNLTYRI-----------------------------LNYPPDL-PRDDVRRAIARAFRVWSDVTPLTFREVTSGQE 50

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931271 168 SDLKIGFYPVNHTDclvsavHHCFDGPTGELAHAFFP--PHGGIHFDDSEYWVLGPtryswkkGVWLTNLVHVAAHEIGH 245
Cdd:cd04278   51 ADIRISFARGNHGD------GYPFDGPGGTLAHAFFPggIGGDIHFDDDEQWTLGS-------DSGGTDLFSVAAHEIGH 117

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 568931271 246 ALGLMHSQQDQALMHLNATLR-GWKALSQDELWGLHRLYG 284
Cdd:cd04278  118 ALGLGHSSDPDSIMYPYYQGPvPKFKLSQDDIRGIQALYG 157
ShKT smart00254
ShK toxin domain; ShK toxin domain
 285-319 2.30e-05

ShK toxin domain; ShK toxin domain


:

Pssm-ID: 214586 [Multi-domain]  Cd Length: 33  Bit Score: 41.21  E-value: 2.30e-05
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 568931271   285 CLDRIFVCASWArKGFCdVRQRLMKRLCPRSCDFC 319
Cdd:smart00254   1 CVDRHPDCAAWA-KGFC-TNPFYMKSNCPKTCGFC 33
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 341-403 5.33e-03

Immunoglobulin domain; This family contains immunoglobulin-like domains.


:

Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 35.62  E-value: 5.33e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568931271  341 VREGRNMTFHC---GqkilHKKGKVYWYKDQEPL--EFSYPGYLALGEAQLSII-ANAVNEGTYTCVVR 403
Cdd:pfam13927  13 VREGETVTLTCeatG----SPPPTITWYKNGEPIssGSTRSRSLSGSNSTLTISnVTRSDAGTYTCVAS 77
 
Name Accession Description Interval E-value
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 88-284 1.62e-58

Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are responsible for a great deal of pericellular proteolysis of extracellular matrix and cell surface molecules, playing crucial roles in morphogenesis, cell fate specification, cell migration, tissue repair, tumorigenesis, gain or loss of tissue-specific functions, and apoptosis. In many instances, they are anchored to cell membranes via trans-membrane domains, and their activity is controlled via TIMPs (tissue inhibitors of metalloproteinases).


Pssm-ID: 239805 [Multi-domain]  Cd Length: 157  Bit Score: 188.18  E-value: 1.62e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931271  88 RWDHFNLTYRChldqrggwsghnsdtntdsnitaalhhrvLSFPRNLlSPEETRRGLAAAFRMWSDVSPFSFREVAPERP 167
Cdd:cd04278    1 KWSKTNLTYRI-----------------------------LNYPPDL-PRDDVRRAIARAFRVWSDVTPLTFREVTSGQE 50

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931271 168 SDLKIGFYPVNHTDclvsavHHCFDGPTGELAHAFFP--PHGGIHFDDSEYWVLGPtryswkkGVWLTNLVHVAAHEIGH 245
Cdd:cd04278   51 ADIRISFARGNHGD------GYPFDGPGGTLAHAFFPggIGGDIHFDDDEQWTLGS-------DSGGTDLFSVAAHEIGH 117

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 568931271 246 ALGLMHSQQDQALMHLNATLR-GWKALSQDELWGLHRLYG 284
Cdd:cd04278  118 ALGLGHSSDPDSIMYPYYQGPvPKFKLSQDDIRGIQALYG 157
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 88-284 1.94e-40

Matrixin; The members of this family are enzymes that cleave peptides. These proteases require zinc for catalysis.


Pssm-ID: 425668 [Multi-domain]  Cd Length: 159  Bit Score: 141.22  E-value: 1.94e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931271   88 RWDHFNLTYRchldqrggwsghnsdtntdsnitaalhhrVLSFPrNLLSPEETRRGLAAAFRMWSDVSPFSFREVaPERP 167
Cdd:pfam00413   1 KWRKKNLTYR-----------------------------ILNYT-PDLPRAEVRRAIRRAFKVWSEVTPLTFTEV-STGE 49

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931271  168 SDLKIGFYPVNHTDCLVsavhhcFDGPTGELAHAFFP---PHGGIHFDDSEYWVLGPTRYSwkkGvwlTNLVHVAAHEIG 244
Cdd:pfam00413  50 ADIMIGFGRGDHGDGYP------FDGPGGVLAHAFFPgpgLGGDIHFDDDETWTVGSDPPH---G---INLFLVAAHEIG 117

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 568931271  245 HALGLMHSQQDQALMHlnATLRGWKA----LSQDELWGLHRLYG 284
Cdd:pfam00413 118 HALGLGHSSDPGAIMY--PTYSPLDSkkfrLSQDDIKGIQQLYG 159
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 85-284 1.22e-22

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: 92.80  E-value: 1.22e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931271    85 ARLRWDHFNLTYRchldqrggwsghnsdtntdsnitaalhhrvlsFPRNLLSPEEtRRGLAAAFRMWSDVSPFSFREVAP 164
Cdd:smart00235   1 GSKKWPKGTVPYV--------------------------------IDSSSLSPEE-REAIAKALAEWSDVTCIRFVERTG 47

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931271   165 ErpSDLKIGFYPVNHtdclvsavhHCFdgptgeLAHAFFPpHGGIHFDDsEYWVLGptryswkkgvwltnlVHVAAHEIG 244
Cdd:smart00235  48 T--ADIYISFGSGDS---------GCT------LSHAGRP-GGDQHLSL-GNGCIN---------------TGVAAHELG 93

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 568931271   245 HALGLMHSQQDQA---LMHLNAT--LRGWKALSQDELWGLHRLYG 284
Cdd:smart00235  94 HALGLYHEQSRSDrdnYMYINYTniDTRNFDLSEDDSLGIPYDYG 138
ShKT smart00254
ShK toxin domain; ShK toxin domain
 285-319 2.30e-05

ShK toxin domain; ShK toxin domain


Pssm-ID: 214586 [Multi-domain]  Cd Length: 33  Bit Score: 41.21  E-value: 2.30e-05
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 568931271   285 CLDRIFVCASWArKGFCdVRQRLMKRLCPRSCDFC 319
Cdd:smart00254   1 CVDRHPDCAAWA-KGFC-TNPFYMKSNCPKTCGFC 33
ShK pfam01549
ShK domain-like; This domain of is found in several C. elegans proteins. The domain is 30 ...
 284-319 6.41e-04

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: 36.99  E-value: 6.41e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 568931271  284 GCLDRIFVCASWARKGfCDVR--QRLMKRLCPRSCDFC 319
Cdd:pfam01549   1 SCVDPHSDCASWAALG-CTSPfyQDFMKENCPKTCGFC 37
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 341-403 5.33e-03

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 35.62  E-value: 5.33e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568931271  341 VREGRNMTFHC---GqkilHKKGKVYWYKDQEPL--EFSYPGYLALGEAQLSII-ANAVNEGTYTCVVR 403
Cdd:pfam13927  13 VREGETVTLTCeatG----SPPPTITWYKNGEPIssGSTRSRSLSGSNSTLTISnVTRSDAGTYTCVAS 77
 
Name Accession Description Interval E-value
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 88-284 1.62e-58

Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are responsible for a great deal of pericellular proteolysis of extracellular matrix and cell surface molecules, playing crucial roles in morphogenesis, cell fate specification, cell migration, tissue repair, tumorigenesis, gain or loss of tissue-specific functions, and apoptosis. In many instances, they are anchored to cell membranes via trans-membrane domains, and their activity is controlled via TIMPs (tissue inhibitors of metalloproteinases).


Pssm-ID: 239805 [Multi-domain]  Cd Length: 157  Bit Score: 188.18  E-value: 1.62e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931271  88 RWDHFNLTYRChldqrggwsghnsdtntdsnitaalhhrvLSFPRNLlSPEETRRGLAAAFRMWSDVSPFSFREVAPERP 167
Cdd:cd04278    1 KWSKTNLTYRI-----------------------------LNYPPDL-PRDDVRRAIARAFRVWSDVTPLTFREVTSGQE 50

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931271 168 SDLKIGFYPVNHTDclvsavHHCFDGPTGELAHAFFP--PHGGIHFDDSEYWVLGPtryswkkGVWLTNLVHVAAHEIGH 245
Cdd:cd04278   51 ADIRISFARGNHGD------GYPFDGPGGTLAHAFFPggIGGDIHFDDDEQWTLGS-------DSGGTDLFSVAAHEIGH 117

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 568931271 246 ALGLMHSQQDQALMHLNATLR-GWKALSQDELWGLHRLYG 284
Cdd:cd04278  118 ALGLGHSSDPDSIMYPYYQGPvPKFKLSQDDIRGIQALYG 157
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 88-284 1.94e-40

Matrixin; The members of this family are enzymes that cleave peptides. These proteases require zinc for catalysis.


Pssm-ID: 425668 [Multi-domain]  Cd Length: 159  Bit Score: 141.22  E-value: 1.94e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931271   88 RWDHFNLTYRchldqrggwsghnsdtntdsnitaalhhrVLSFPrNLLSPEETRRGLAAAFRMWSDVSPFSFREVaPERP 167
Cdd:pfam00413   1 KWRKKNLTYR-----------------------------ILNYT-PDLPRAEVRRAIRRAFKVWSEVTPLTFTEV-STGE 49

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931271  168 SDLKIGFYPVNHTDCLVsavhhcFDGPTGELAHAFFP---PHGGIHFDDSEYWVLGPTRYSwkkGvwlTNLVHVAAHEIG 244
Cdd:pfam00413  50 ADIMIGFGRGDHGDGYP------FDGPGGVLAHAFFPgpgLGGDIHFDDDETWTVGSDPPH---G---INLFLVAAHEIG 117

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 568931271  245 HALGLMHSQQDQALMHlnATLRGWKA----LSQDELWGLHRLYG 284
Cdd:pfam00413 118 HALGLGHSSDPGAIMY--PTYSPLDSkkfrLSQDDIKGIQQLYG 159
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 85-284 1.22e-22

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: 92.80  E-value: 1.22e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931271    85 ARLRWDHFNLTYRchldqrggwsghnsdtntdsnitaalhhrvlsFPRNLLSPEEtRRGLAAAFRMWSDVSPFSFREVAP 164
Cdd:smart00235   1 GSKKWPKGTVPYV--------------------------------IDSSSLSPEE-REAIAKALAEWSDVTCIRFVERTG 47

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931271   165 ErpSDLKIGFYPVNHtdclvsavhHCFdgptgeLAHAFFPpHGGIHFDDsEYWVLGptryswkkgvwltnlVHVAAHEIG 244
Cdd:smart00235  48 T--ADIYISFGSGDS---------GCT------LSHAGRP-GGDQHLSL-GNGCIN---------------TGVAAHELG 93

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 568931271   245 HALGLMHSQQDQA---LMHLNAT--LRGWKALSQDELWGLHRLYG 284
Cdd:smart00235  94 HALGLYHEQSRSDrdnYMYINYTniDTRNFDLSEDDSLGIPYDYG 138
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 137-254 1.38e-07

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: 50.96  E-value: 1.38e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931271 137 PEETRRGLAAAFRMWSDVSPFSFREVAPERPSDLKIGFYPVNHTDclvsavhhcfDGPTGELAHAFFPPHGGIHFDDsey 216
Cdd:cd04268   13 PDKLRAAILDAIEAWNKAFAIGFKNANDVDPADIRYSVIRWIPYN----------DGTWSYGPSQVDPLTGEILLAR--- 79

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 568931271 217 wvlgPTRYSWKKGVWLTNLVHVAAHEIGHALGLMHSQQ 254
Cdd:cd04268   80 ----VYLYSSFVEYSGARLRNTAEHELGHALGLRHNFA 113
ZnMc_serralysin_like cd04277
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
 135-255 5.37e-07

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: 49.72  E-value: 5.37e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931271 135 LSPEETRRgLAAAFRMWSDVSPFSFREVAPERPSDLKIGFYPvnhtdclvsavhhcfDGPTGELAHAFFPPHGG------ 208
Cdd:cd04277   31 LSAAQQAA-ARDALEAWEDVADIDFVEVSDNSGADIRFGNSS---------------DPDGNTAGYAYYPGSGSgtaygg 94

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 568931271 209 -IHFDDSEYwvlgpTRYSWKKGVWLtnlvHVAAHEIGHALGLMHSQQD 255
Cdd:cd04277   95 dIWFNSSYD-----TNSDSPGSYGY----QTIIHEIGHALGLEHPGDY 133
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 146-253 1.32e-05

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: 45.21  E-value: 1.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931271 146 AAFRMWSDVSPFSFREVAPER-PSDLKIGFYpvnHTDclvsavhhcFDGPTGelAHAFFP----PHGG-IHFDDSEYWvl 219
Cdd:cd00203   29 IAMQIWRDYLNIRFVLVGVEIdKADIAILVT---RQD---------FDGGTG--GWAYLGrvcdSLRGvGVLQDNQSG-- 92

                         90       100       110
                 ....*....|....*....|....*....|....
gi 568931271 220 gpTRYSWKkgvwltnlvhVAAHEIGHALGLMHSQ 253
Cdd:cd00203   93 --TKEGAQ----------TIAHELGHALGFYHDH 114
ShKT smart00254
ShK toxin domain; ShK toxin domain
 285-319 2.30e-05

ShK toxin domain; ShK toxin domain


Pssm-ID: 214586 [Multi-domain]  Cd Length: 33  Bit Score: 41.21  E-value: 2.30e-05
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 568931271   285 CLDRIFVCASWArKGFCdVRQRLMKRLCPRSCDFC 319
Cdd:smart00254   1 CVDRHPDCAAWA-KGFC-TNPFYMKSNCPKTCGFC 33
ZnMc_MMP_like_2 cd04276
Zinc-dependent metalloprotease; MMP_like sub-family 2. A group of bacterial metalloproteinase ...
 195-251 1.30e-04

Zinc-dependent metalloprotease; MMP_like sub-family 2. A group of bacterial metalloproteinase domains similar to matrix metalloproteinases and astacin.


Pssm-ID: 239803  Cd Length: 197  Bit Score: 42.70  E-value: 1.30e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 568931271 195 TGELAHAF-FPPHGGIHFDDSEYWVLGPTRYSwkkgvwltnlvHVAAHEIGHALGLMH 251
Cdd:cd04276   86 TGEILKADvILYSGFLRQDQLWYEDLLAASLR-----------YLLAHEVGHTLGLRH 132
ZnMc_MMP_like_1 cd04279
Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ...
 144-284 2.99e-04

Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and fungal metalloproteinase domains similar to matrix metalloproteinases and astacin.


Pssm-ID: 239806 [Multi-domain]  Cd Length: 156  Bit Score: 40.90  E-value: 2.99e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931271 144 LAAAFRMWSDVSPFSFREVaPERPSDLKIGFYPVNHTDCLVSAvhhcfdgptGELAHAFFPPHGG------IHFDDSEYW 217
Cdd:cd04279   26 VKQAAAEWENVGPLKFVYN-PEEDNDADIVIFFDRPPPVGGAG---------GGLARAGFPLISDgnrklfNRTDINLGP 95

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931271 218 VLGPtryswkkgvWLTNLVHVAAHEIGHALGLMHSQ-QDQALM--HLNATLRGWKALSQDELWGLHRLYG 284
Cdd:cd04279   96 GQPR---------GAENLQAIALHELGHALGLWHHSdRPEDAMypSQGQGPDGNPTLSARDVATLKRLYG 156
ShK pfam01549
ShK domain-like; This domain of is found in several C. elegans proteins. The domain is 30 ...
 284-319 6.41e-04

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: 36.99  E-value: 6.41e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 568931271  284 GCLDRIFVCASWARKGfCDVR--QRLMKRLCPRSCDFC 319
Cdd:pfam01549   1 SCVDPHSDCASWAALG-CTSPfyQDFMKENCPKTCGFC 37
DUF4953 pfam16313
Met-zincin; This is a family of uncharacterized proteins that carry the highly characteriztic ...
 238-251 1.06e-03

Met-zincin; This is a family of uncharacterized proteins that carry the highly characteriztic met-zincin mmotif HExxHxxGxxH, the extended zinc-binding domain of metallopeptidases.


Pssm-ID: 435269  Cd Length: 319  Bit Score: 40.70  E-value: 1.06e-03
                          10
                  ....*....|....
gi 568931271  238 VAAHEIGHALGLMH 251
Cdd:pfam16313  16 VSAHEVGHTLGLRH 29
ZnMc_MMP_like_3 cd04327
Zinc-dependent metalloprotease; MMP_like sub-family 3. A group of bacterial and fungal ...
 146-254 1.34e-03

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: 1.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931271 146 AAFRMWSDVSPFSFREVApERPSDLKIGFYPVNH------TDCLvsAVHHcfDGPTGELAhaffpphggihfddseyWVL 219
Cdd:cd04327   27 AAAREWLPYANLKFKFVT-DADADIRISFTPGDGywsyvgTDAL--LIGA--DAPTMNLG-----------------WFT 84

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 568931271 220 GPTRYSwkkgvwltNLVHVAAHEIGHALGLMHSQQ 254
Cdd:cd04327   85 DDTPDP--------EFSRVVLHEFGHALGFIHEHQ 111
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 341-403 5.33e-03

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 35.62  E-value: 5.33e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568931271  341 VREGRNMTFHC---GqkilHKKGKVYWYKDQEPL--EFSYPGYLALGEAQLSII-ANAVNEGTYTCVVR 403
Cdd:pfam13927  13 VREGETVTLTCeatG----SPPPTITWYKNGEPIssGSTRSRSLSGSNSTLTISnVTRSDAGTYTCVAS 77
ZnMc_astacin_like cd04280
Zinc-dependent metalloprotease, astacin_like subfamily or peptidase family M12A, a group of ...
 238-254 8.85e-03

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: 37.17  E-value: 8.85e-03
                         10
                 ....*....|....*..
gi 568931271 238 VAAHEIGHALGLMHSQQ 254
Cdd:cd04280   77 TIVHELMHALGFYHEQS 93
 
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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