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Conserved domains on  [gi|568973058|ref|XP_006532962|]
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telomerase Cajal body protein 1 isoform X1 [Mus musculus]

Protein Classification

WD40 repeat domain-containing protein( domain architecture ID 1000017)

WD40 repeat domain-containing protein folds into a beta-propeller structure and functions as a scaffold, providing a platform for the interaction and assembly of several proteins into a signalosome; 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
SCOP:  4002744

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
WD40 super family cl29593
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
134-254 1.15e-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.


The actual alignment was detected with superfamily member cd00200:

Pssm-ID: 475233 [Multi-domain]  Cd Length: 289  Bit Score: 45.79  E-value: 1.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973058 134 FSQVPRYL-SGS-------WSEFSTRSENFLKG-------CKWAPDGSCILTNSADNVLRIYNLppelyseqeqvdyaEM 198
Cdd:cd00200   17 FSPDGKLLaTGSgdgtikvWDLETGELLRTLKGhtgpvrdVAASADGTYLASGSSDKTIRLWDL--------------ET 82
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 568973058 199 VPVLRMVEGDTIYdycWYSLMSStqPDTSYVASSSRENPIHIWDAFTGELRASFRA 254
Cdd:cd00200   83 GECVRTLTGHTSY---VSSVAFS--PDGRILSSSSRDKTIKVWDVETGKCLTTLRG 133
 
Name Accession Description Interval E-value
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
134-254 1.15e-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: 45.79  E-value: 1.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973058 134 FSQVPRYL-SGS-------WSEFSTRSENFLKG-------CKWAPDGSCILTNSADNVLRIYNLppelyseqeqvdyaEM 198
Cdd:cd00200   17 FSPDGKLLaTGSgdgtikvWDLETGELLRTLKGhtgpvrdVAASADGTYLASGSSDKTIRLWDL--------------ET 82
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 568973058 199 VPVLRMVEGDTIYdycWYSLMSStqPDTSYVASSSRENPIHIWDAFTGELRASFRA 254
Cdd:cd00200   83 GECVRTLTGHTSY---VSSVAFS--PDGRILSSSSRDKTIKVWDVETGKCLTTLRG 133
WD40 COG2319
WD40 repeat [General function prediction only];
224-253 6.56e-03

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 37.58  E-value: 6.56e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 568973058 224 PDTSYVASSSRENPIHIWDAFTGELRASFR 253
Cdd:COG2319  130 PDGKTLASGSADGTVRLWDLATGKLLRTLT 159
 
Name Accession Description Interval E-value
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
134-254 1.15e-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: 45.79  E-value: 1.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973058 134 FSQVPRYL-SGS-------WSEFSTRSENFLKG-------CKWAPDGSCILTNSADNVLRIYNLppelyseqeqvdyaEM 198
Cdd:cd00200   17 FSPDGKLLaTGSgdgtikvWDLETGELLRTLKGhtgpvrdVAASADGTYLASGSSDKTIRLWDL--------------ET 82
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 568973058 199 VPVLRMVEGDTIYdycWYSLMSStqPDTSYVASSSRENPIHIWDAFTGELRASFRA 254
Cdd:cd00200   83 GECVRTLTGHTSY---VSSVAFS--PDGRILSSSSRDKTIKVWDVETGKCLTTLRG 133
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
133-257 9.12e-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: 43.09  E-value: 9.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973058 133 SFSQVPRYLSGSWSEFSTR---------------SENFLKGCKWAPDGSCILTNSADNVLRIYNLppelySEQEQVDyae 197
Cdd:cd00200  142 AFSPDGTFVASSSQDGTIKlwdlrtgkcvatltgHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDL-----STGKCLG--- 213
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973058 198 mvpVLRmveGDTiyDYCWySLMSStqPDTSYVASSSRENPIHIWDAFTGELRASFRAYNH 257
Cdd:cd00200  214 ---TLR---GHE--NGVN-SVAFS--PDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTN 262
WD40 COG2319
WD40 repeat [General function prediction only];
224-253 6.56e-03

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 37.58  E-value: 6.56e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 568973058 224 PDTSYVASSSRENPIHIWDAFTGELRASFR 253
Cdd:COG2319  130 PDGKTLASGSADGTVRLWDLATGKLLRTLT 159
 
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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