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Conserved domains on  [gi|2000179063|gb|KAG4405043|]
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hypothetical protein JTP64_006057 [Candida tropicalis]

Protein Classification

WD40 and DUF2415 domain-containing protein( domain architecture ID 13236969)

WD40 and DUF2415 domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DUF2415 pfam10313
Uncharacterized protein domain (DUF2415); This is a short, 30 residue domain, from a family of ...
421-467 6.82e-18

Uncharacterized protein domain (DUF2415); This is a short, 30 residue domain, from a family of proteins conserved in fungi. The function is unknown. There is a characteriztic DLL sequence motif.


:

Pssm-ID: 402091  Cd Length: 43  Bit Score: 77.39  E-value: 6.82e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2000179063 421 GAFRVVKFSPENDLNDLLIISEHVGRVHLIDLRNlnydNVDDHQVVV 467
Cdd:pfam10313   1 GAFRVCKFSPESGLNDLLVISEHVGRVHLVDLRT----GFMNHQVIV 43
WD40 super family cl29593
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
331-431 1.04e-04

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: 44.63  E-value: 1.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000179063 331 NNVIKNPKSDKILAATGDSSsIFLIDPSSKnSIIKTInSGHDSGGFGVDYHANGLLFSTVFQDGICQIYDIRNLsqkliE 410
Cdd:cd00200   181 NSVAFSPDGEKLLSSSSDGT-IKLWDLSTG-KCLGTL-RGHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTG-----E 252
                          90       100
                  ....*....|....*....|.
gi 2000179063 411 IKSTRPGHQSGAFRvVKFSPE 431
Cdd:cd00200   253 CVQTLSGHTNSVTS-LAWSPD 272
 
Name Accession Description Interval E-value
DUF2415 pfam10313
Uncharacterized protein domain (DUF2415); This is a short, 30 residue domain, from a family of ...
421-467 6.82e-18

Uncharacterized protein domain (DUF2415); This is a short, 30 residue domain, from a family of proteins conserved in fungi. The function is unknown. There is a characteriztic DLL sequence motif.


Pssm-ID: 402091  Cd Length: 43  Bit Score: 77.39  E-value: 6.82e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2000179063 421 GAFRVVKFSPENDLNDLLIISEHVGRVHLIDLRNlnydNVDDHQVVV 467
Cdd:pfam10313   1 GAFRVCKFSPESGLNDLLVISEHVGRVHLVDLRT----GFMNHQVIV 43
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
331-431 1.04e-04

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: 44.63  E-value: 1.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000179063 331 NNVIKNPKSDKILAATGDSSsIFLIDPSSKnSIIKTInSGHDSGGFGVDYHANGLLFSTVFQDGICQIYDIRNLsqkliE 410
Cdd:cd00200   181 NSVAFSPDGEKLLSSSSDGT-IKLWDLSTG-KCLGTL-RGHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTG-----E 252
                          90       100
                  ....*....|....*....|.
gi 2000179063 411 IKSTRPGHQSGAFRvVKFSPE 431
Cdd:cd00200   253 CVQTLSGHTNSVTS-LAWSPD 272
WD40 COG2319
WD40 repeat [General function prediction only];
341-454 3.58e-03

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 40.28  E-value: 3.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000179063 341 KILAATGDSSSIFLIDPSSkNSIIKTINsGHDSGGFGVDYHANGLLFSTVFQDGICQIYDIRNLsqkliEIKSTRPGHQS 420
Cdd:COG2319   217 KLLASGSADGTVRLWDLAT-GKLLRTLT-GHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATG-----ELLRTLTGHSG 289
                          90       100       110
                  ....*....|....*....|....*....|....
gi 2000179063 421 GAFRVVkFSPEndlNDLLIISEHVGRVHLIDLRN 454
Cdd:COG2319   290 GVNSVA-FSPD---GKLLASGSDDGTVRLWDLAT 319
 
Name Accession Description Interval E-value
DUF2415 pfam10313
Uncharacterized protein domain (DUF2415); This is a short, 30 residue domain, from a family of ...
421-467 6.82e-18

Uncharacterized protein domain (DUF2415); This is a short, 30 residue domain, from a family of proteins conserved in fungi. The function is unknown. There is a characteriztic DLL sequence motif.


Pssm-ID: 402091  Cd Length: 43  Bit Score: 77.39  E-value: 6.82e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2000179063 421 GAFRVVKFSPENDLNDLLIISEHVGRVHLIDLRNlnydNVDDHQVVV 467
Cdd:pfam10313   1 GAFRVCKFSPESGLNDLLVISEHVGRVHLVDLRT----GFMNHQVIV 43
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
331-431 1.04e-04

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: 44.63  E-value: 1.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000179063 331 NNVIKNPKSDKILAATGDSSsIFLIDPSSKnSIIKTInSGHDSGGFGVDYHANGLLFSTVFQDGICQIYDIRNLsqkliE 410
Cdd:cd00200   181 NSVAFSPDGEKLLSSSSDGT-IKLWDLSTG-KCLGTL-RGHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTG-----E 252
                          90       100
                  ....*....|....*....|.
gi 2000179063 411 IKSTRPGHQSGAFRvVKFSPE 431
Cdd:cd00200   253 CVQTLSGHTNSVTS-LAWSPD 272
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
343-455 2.40e-04

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: 43.86  E-value: 2.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000179063 343 LAATGDSSSIFLIDpSSKNSIIKTINsGHDSGGFGVDYHANGLLFSTVFQDGICQIYDIRNLsqkliEIKSTRPGHQSGA 422
Cdd:cd00200    66 LASGSSDKTIRLWD-LETGECVRTLT-GHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETG-----KCLTTLRGHTDWV 138
                          90       100       110
                  ....*....|....*....|....*....|...
gi 2000179063 423 fRVVKFSPEndlNDLLIISEHVGRVHLIDLRNL 455
Cdd:cd00200   139 -NSVAFSPD---GTFVASSSQDGTIKLWDLRTG 167
WD40 COG2319
WD40 repeat [General function prediction only];
341-454 3.58e-03

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 40.28  E-value: 3.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000179063 341 KILAATGDSSSIFLIDPSSkNSIIKTINsGHDSGGFGVDYHANGLLFSTVFQDGICQIYDIRNLsqkliEIKSTRPGHQS 420
Cdd:COG2319   217 KLLASGSADGTVRLWDLAT-GKLLRTLT-GHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATG-----ELLRTLTGHSG 289
                          90       100       110
                  ....*....|....*....|....*....|....
gi 2000179063 421 GAFRVVkFSPEndlNDLLIISEHVGRVHLIDLRN 454
Cdd:COG2319   290 GVNSVA-FSPD---GKLLASGSDDGTVRLWDLAT 319
 
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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