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Conserved domains on  [gi|27363472|ref|NP_758960|]
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WD repeat domain phosphoinositide-interacting protein 4 isoform a [Mus musculus]

Protein Classification

WD40 repeat domain-containing protein( domain architecture ID 13234759)

WD40 repeat domain-containing protein similar to a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly

CATH:  2.130.10.10
Gene Ontology:  GO:0005515
PubMed:  10322433
SCOP:  4002744

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
167-271 1.66e-09

WD40 repeat [General function prediction only];


:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 58.77  E-value: 1.66e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27363472 167 GSLQLVDLASTKPGTssapfTINAHQSDVACVSLNQPGTVVASASQKGTlIRLFDTQSKEKLVELRRGTDPATlyCINFS 246
Cdd:COG2319 226 GTVRLWDLATGKLLR-----TLTGHSGSVRSVAFSPDGRLLASGSADGT-VRLWDLATGELLRTLTGHSGGVN--SVAFS 297
                        90       100
                ....*....|....*....|....*
gi 27363472 247 HDSSFLCASSDKGTVHIFALKDTRL 271
Cdd:COG2319 298 PDGKLLASGSDDGTVRLWDLATGKL 322
WD40 super family cl29593
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
8-264 2.44e-08

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


The actual alignment was detected with superfamily member cd00200:

Pssm-ID: 475233 [Multi-domain]  Cd Length: 289  Bit Score: 54.65  E-value: 2.44e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27363472   8 GVTSLHFNQDQS--CFCCAMETgVRIYNVEPLME----KGHLdheqvGSVGLVEMLHRSNLLALVGGGSSpkfseisVLI 81
Cdd:cd00200  11 GVTCVAFSPDGKllATGSGDGT-IKVWDLETGELlrtlKGHT-----GPVRDVAASADGTYLASGSSDKT-------IRL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27363472  82 WDDaregkdSKDKLVLEFT-FTKPVLAVRMRHDkivivlrNRIYVYSFPDSPRKLFEFDT-------RDNPKGLCDLCPS 153
Cdd:cd00200  78 WDL------ETGECVRTLTgHTSYVSSVAFSPD-------GRILSSSSRDKTIKVWDVETgkclttlRGHTDWVNSVAFS 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27363472 154 LEKQLLVFpGHKCGSLQLVDLASTKPGTssapfTINAHQSDVACVSLNQPGTVVASASQKGTlIRLFDTQSKEKLVELRR 233
Cdd:cd00200 145 PDGTFVAS-SSQDGTIKLWDLRTGKCVA-----TLTGHTGEVNSVAFSPDGEKLLSSSSDGT-IKLWDLSTGKCLGTLRG 217
                       250       260       270
                ....*....|....*....|....*....|.
gi 27363472 234 GTDPatLYCINFSHDSSFLCASSDKGTVHIF 264
Cdd:cd00200 218 HENG--VNSVAFSPDGYLLASGSEDGTIRVW 246
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
167-271 1.66e-09

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 58.77  E-value: 1.66e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27363472 167 GSLQLVDLASTKPGTssapfTINAHQSDVACVSLNQPGTVVASASQKGTlIRLFDTQSKEKLVELRRGTDPATlyCINFS 246
Cdd:COG2319 226 GTVRLWDLATGKLLR-----TLTGHSGSVRSVAFSPDGRLLASGSADGT-VRLWDLATGELLRTLTGHSGGVN--SVAFS 297
                        90       100
                ....*....|....*....|....*
gi 27363472 247 HDSSFLCASSDKGTVHIFALKDTRL 271
Cdd:COG2319 298 PDGKLLASGSDDGTVRLWDLATGKL 322
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
187-274 7.09e-09

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 56.19  E-value: 7.09e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27363472 187 TINAHQSDVACVSLNQPGTVVASASQKGTlIRLFDTQSKEKLVELRRGTDPATlyCINFSHDSSFLCASSDKGTVHIFAL 266
Cdd:cd00200  88 TLTGHTSYVSSVAFSPDGRILSSSSRDKT-IKVWDVETGKCLTTLRGHTDWVN--SVAFSPDGTFVASSSQDGTIKLWDL 164

                ....*...
gi 27363472 267 KDTRLNRR 274
Cdd:cd00200 165 RTGKCVAT 172
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
8-264 2.44e-08

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 54.65  E-value: 2.44e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27363472   8 GVTSLHFNQDQS--CFCCAMETgVRIYNVEPLME----KGHLdheqvGSVGLVEMLHRSNLLALVGGGSSpkfseisVLI 81
Cdd:cd00200  11 GVTCVAFSPDGKllATGSGDGT-IKVWDLETGELlrtlKGHT-----GPVRDVAASADGTYLASGSSDKT-------IRL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27363472  82 WDDaregkdSKDKLVLEFT-FTKPVLAVRMRHDkivivlrNRIYVYSFPDSPRKLFEFDT-------RDNPKGLCDLCPS 153
Cdd:cd00200  78 WDL------ETGECVRTLTgHTSYVSSVAFSPD-------GRILSSSSRDKTIKVWDVETgkclttlRGHTDWVNSVAFS 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27363472 154 LEKQLLVFpGHKCGSLQLVDLASTKPGTssapfTINAHQSDVACVSLNQPGTVVASASQKGTlIRLFDTQSKEKLVELRR 233
Cdd:cd00200 145 PDGTFVAS-SSQDGTIKLWDLRTGKCVA-----TLTGHTGEVNSVAFSPDGEKLLSSSSDGT-IKLWDLSTGKCLGTLRG 217
                       250       260       270
                ....*....|....*....|....*....|.
gi 27363472 234 GTDPatLYCINFSHDSSFLCASSDKGTVHIF 264
Cdd:cd00200 218 HENG--VNSVAFSPDGYLLASGSEDGTIRVW 246
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
167-271 1.66e-09

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 58.77  E-value: 1.66e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27363472 167 GSLQLVDLASTKPGTssapfTINAHQSDVACVSLNQPGTVVASASQKGTlIRLFDTQSKEKLVELRRGTDPATlyCINFS 246
Cdd:COG2319 226 GTVRLWDLATGKLLR-----TLTGHSGSVRSVAFSPDGRLLASGSADGT-VRLWDLATGELLRTLTGHSGGVN--SVAFS 297
                        90       100
                ....*....|....*....|....*
gi 27363472 247 HDSSFLCASSDKGTVHIFALKDTRL 271
Cdd:COG2319 298 PDGKLLASGSDDGTVRLWDLATGKL 322
WD40 COG2319
WD40 repeat [General function prediction only];
167-274 1.89e-09

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 58.77  E-value: 1.89e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27363472 167 GSLQLVDLASTKPgtssaPFTINAHQSDVACVSLNQPGTVVASASQKGTlIRLFDTQSKEKLVELRRGTDPAtlYCINFS 246
Cdd:COG2319 184 GTVRLWDLATGKL-----LRTLTGHTGAVRSVAFSPDGKLLASGSADGT-VRLWDLATGKLLRTLTGHSGSV--RSVAFS 255
                        90       100
                ....*....|....*....|....*...
gi 27363472 247 HDSSFLCASSDKGTVHIFALKDTRLNRR 274
Cdd:COG2319 256 PDGRLLASGSADGTVRLWDLATGELLRT 283
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
187-274 7.09e-09

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 56.19  E-value: 7.09e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27363472 187 TINAHQSDVACVSLNQPGTVVASASQKGTlIRLFDTQSKEKLVELRRGTDPATlyCINFSHDSSFLCASSDKGTVHIFAL 266
Cdd:cd00200  88 TLTGHTSYVSSVAFSPDGRILSSSSRDKT-IKVWDVETGKCLTTLRGHTDWVN--SVAFSPDGTFVASSSQDGTIKLWDL 164

                ....*...
gi 27363472 267 KDTRLNRR 274
Cdd:cd00200 165 RTGKCVAT 172
WD40 COG2319
WD40 repeat [General function prediction only];
167-271 1.81e-08

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 55.69  E-value: 1.81e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27363472 167 GSLQLVDLASTKPGTssapfTINAHQSDVACVSLNQPGTVVASASQKGTlIRLFDTQSKEKLVELRRGTDPatLYCINFS 246
Cdd:COG2319 142 GTVRLWDLATGKLLR-----TLTGHSGAVTSVAFSPDGKLLASGSDDGT-VRLWDLATGKLLRTLTGHTGA--VRSVAFS 213
                        90       100
                ....*....|....*....|....*
gi 27363472 247 HDSSFLCASSDKGTVHIFALKDTRL 271
Cdd:COG2319 214 PDGKLLASGSADGTVRLWDLATGKL 238
WD40 COG2319
WD40 repeat [General function prediction only];
167-271 2.06e-08

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 55.30  E-value: 2.06e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27363472 167 GSLQLVDLASTKPgtssaPFTINAHQSDVACVSLNQPGTVVASASQKGTlIRLFDTQSKEKLVELRRGTDPatLYCINFS 246
Cdd:COG2319 100 GTVRLWDLATGLL-----LRTLTGHTGAVRSVAFSPDGKTLASGSADGT-VRLWDLATGKLLRTLTGHSGA--VTSVAFS 171
                        90       100
                ....*....|....*....|....*
gi 27363472 247 HDSSFLCASSDKGTVHIFALKDTRL 271
Cdd:COG2319 172 PDGKLLASGSDDGTVRLWDLATGKL 196
WD40 COG2319
WD40 repeat [General function prediction only];
167-268 2.41e-08

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 55.30  E-value: 2.41e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27363472 167 GSLQLVDLASTKPgtssaPFTINAHQSDVACVSLNQPGTVVASASQKGTlIRLFDTQSKEKLVELRRGTDPatLYCINFS 246
Cdd:COG2319 310 GTVRLWDLATGKL-----LRTLTGHTGAVRSVAFSPDGKTLASGSDDGT-VRLWDLATGELLRTLTGHTGA--VTSVAFS 381
                        90       100
                ....*....|....*....|..
gi 27363472 247 HDSSFLCASSDKGTVHIFALKD 268
Cdd:COG2319 382 PDGRTLASGSADGTVRLWDLAT 403
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
8-264 2.44e-08

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 54.65  E-value: 2.44e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27363472   8 GVTSLHFNQDQS--CFCCAMETgVRIYNVEPLME----KGHLdheqvGSVGLVEMLHRSNLLALVGGGSSpkfseisVLI 81
Cdd:cd00200  11 GVTCVAFSPDGKllATGSGDGT-IKVWDLETGELlrtlKGHT-----GPVRDVAASADGTYLASGSSDKT-------IRL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27363472  82 WDDaregkdSKDKLVLEFT-FTKPVLAVRMRHDkivivlrNRIYVYSFPDSPRKLFEFDT-------RDNPKGLCDLCPS 153
Cdd:cd00200  78 WDL------ETGECVRTLTgHTSYVSSVAFSPD-------GRILSSSSRDKTIKVWDVETgkclttlRGHTDWVNSVAFS 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27363472 154 LEKQLLVFpGHKCGSLQLVDLASTKPGTssapfTINAHQSDVACVSLNQPGTVVASASQKGTlIRLFDTQSKEKLVELRR 233
Cdd:cd00200 145 PDGTFVAS-SSQDGTIKLWDLRTGKCVA-----TLTGHTGEVNSVAFSPDGEKLLSSSSDGT-IKLWDLSTGKCLGTLRG 217
                       250       260       270
                ....*....|....*....|....*....|.
gi 27363472 234 GTDPatLYCINFSHDSSFLCASSDKGTVHIF 264
Cdd:cd00200 218 HENG--VNSVAFSPDGYLLASGSEDGTIRVW 246
WD40 COG2319
WD40 repeat [General function prediction only];
167-271 2.57e-08

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 55.30  E-value: 2.57e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27363472 167 GSLQLVDLASTKPGTssapfTINAHQSDVACVSLNQPGTVVASASQKGTlIRLFDTQSKEKLVELRRGTDPatLYCINFS 246
Cdd:COG2319 268 GTVRLWDLATGELLR-----TLTGHSGGVNSVAFSPDGKLLASGSDDGT-VRLWDLATGKLLRTLTGHTGA--VRSVAFS 339
                        90       100
                ....*....|....*....|....*
gi 27363472 247 HDSSFLCASSDKGTVHIFALKDTRL 271
Cdd:COG2319 340 PDGKTLASGSDDGTVRLWDLATGEL 364
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
186-271 5.55e-08

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 53.49  E-value: 5.55e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27363472 186 FTINAHQSDVACVSLNQPGTVVASASQKGTlIRLFDTQSkEKLVELRRG-TDPatLYCINFSHDSSFLCASSDKGTVHIF 264
Cdd:cd00200 129 TTLRGHTDWVNSVAFSPDGTFVASSSQDGT-IKLWDLRT-GKCVATLTGhTGE--VNSVAFSPDGEKLLSSSSDGTIKLW 204

                ....*..
gi 27363472 265 ALKDTRL 271
Cdd:cd00200 205 DLSTGKC 211
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
3-265 2.61e-06

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 48.49  E-value: 2.61e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27363472   3 QQPLRGVTSLHFnqDQSCFCCAMETGVRIYNVEplmeKGHLDHEQVGSVGLVE--MLHRSNLLALVGGGSSpkfseiSVL 80
Cdd:cd00200  51 TGPVRDVAASAD--GTYLASGSSDKTIRLWDLE----TGECVRTLTGHTSYVSsvAFSPDGRILSSSSRDK------TIK 118
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27363472  81 IWDdareGKDSKDKLVLEfTFTKPVLAVRMRHDKIVIV--LRNR-IYVYSFPD-SPRKLFEFDTRDnpkgLCDLCPSLEK 156
Cdd:cd00200 119 VWD----VETGKCLTTLR-GHTDWVNSVAFSPDGTFVAssSQDGtIKLWDLRTgKCVATLTGHTGE----VNSVAFSPDG 189
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27363472 157 QLLVFPGHKcGSLQLVDLASTKPGTssapfTINAHQSDVACVSLNQPGTVVASASQKGTlIRLFDTQSKEKLVELRRGTD 236
Cdd:cd00200 190 EKLLSSSSD-GTIKLWDLSTGKCLG-----TLRGHENGVNSVAFSPDGYLLASGSEDGT-IRVWDLRTGECVQTLSGHTN 262
                       250       260
                ....*....|....*....|....*....
gi 27363472 237 PATlyCINFSHDSSFLCASSDKGTVHIFA 265
Cdd:cd00200 263 SVT--SLAWSPDGKRLASGSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
168-271 6.90e-06

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 47.60  E-value: 6.90e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27363472 168 SLQLVDLASTKPGTSSAPFTINAHQSDVACVSLNQPGTVVASASQKGTlIRLFDTQSKEKLVELRRGTDPATlyCINFSH 247
Cdd:COG2319  54 GAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGT-VRLWDLATGLLLRTLTGHTGAVR--SVAFSP 130
                        90       100
                ....*....|....*....|....
gi 27363472 248 DSSFLCASSDKGTVHIFALKDTRL 271
Cdd:COG2319 131 DGKTLASGSADGTVRLWDLATGKL 154
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
186-274 5.28e-05

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 44.25  E-value: 5.28e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27363472 186 FTINAHQSDVACVSLNQPGTVVASASQKGTlIRLFDTQSKEKLVELRRGTDPatLYCINFSHDSSFLCASSDKGTVHIFA 265
Cdd:cd00200   3 RTLKGHTGGVTCVAFSPDGKLLATGSGDGT-IKVWDLETGELLRTLKGHTGP--VRDVAASADGTYLASGSSDKTIRLWD 79

                ....*....
gi 27363472 266 LKDTRLNRR 274
Cdd:cd00200  80 LETGECVRT 88
 
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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