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Conserved domains on  [gi|41053489|ref|NP_956995|]
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WD repeat domain 21 [Danio rerio]

Protein Classification

WD40 repeat domain-containing protein( domain architecture ID 11455410)

WD40 repeat domain-containing protein similar to 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
PubMed:  10322433|8090199
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];
276-467 1.08e-08

WD40 repeat [General function prediction only];


:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 57.23  E-value: 1.08e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053489 276 STAWSCAWCLNPQADKTFSTGLSRRVIVTDAVTGRRATYLADSDVLAQQFALRAPVLFNGCRSGeifSIDLRQRDRGRMG 355
Cdd:COG2319  37 AAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADG---TVRLWDLATGLLL 113

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053489 356 FHGWKTSrfyqeSAITSVQLLQDENYLLAADMLGKIKLWDIRVKRCVKQYEGHHNEYAYLPIHinePEGLLLAVG-QDCY 434
Cdd:COG2319 114 RTLTGHT-----GAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTSVAFS---PDGKLLASGsDDGT 185

                       170       180       190
                ....*....|....*....|....*....|...
gi 41053489 435 TRLWSLQDSRLLRTIPSPhpagKDSIPNVVFSP 467
Cdd:COG2319 186 VRLWDLATGKLLRTLTGH----TGAVRSVAFSP 214
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
276-467 1.08e-08

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 57.23  E-value: 1.08e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053489 276 STAWSCAWCLNPQADKTFSTGLSRRVIVTDAVTGRRATYLADSDVLAQQFALRAPVLFNGCRSGeifSIDLRQRDRGRMG 355
Cdd:COG2319  37 AAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADG---TVRLWDLATGLLL 113

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053489 356 FHGWKTSrfyqeSAITSVQLLQDENYLLAADMLGKIKLWDIRVKRCVKQYEGHHNEYAYLPIHinePEGLLLAVG-QDCY 434
Cdd:COG2319 114 RTLTGHT-----GAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTSVAFS---PDGKLLASGsDDGT 185

                       170       180       190
                ....*....|....*....|....*....|...
gi 41053489 435 TRLWSLQDSRLLRTIPSPhpagKDSIPNVVFSP 467
Cdd:COG2319 186 VRLWDLATGKLLRTLTGH----TGAVRSVAFSP 214
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 367-467 2.91e-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: 55.03  E-value: 2.91e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053489 367 ESAITSVQLLQDENYLLAADMLGKIKLWDIRVKRCVKQYEGHHNEYAYLPIHinePEGLLLAVG-QDCYTRLWSLQDSRL 445
Cdd:cd00200  93 TSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFS---PDGTFVASSsQDGTIKLWDLRTGKC 169

                        90       100
                ....*....|....*....|..
gi 41053489 446 LRTIPSpHpagKDSIPNVVFSP 467
Cdd:cd00200 170 VATLTG-H---TGEVNSVAFSP 187
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
276-467 1.08e-08

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 57.23  E-value: 1.08e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053489 276 STAWSCAWCLNPQADKTFSTGLSRRVIVTDAVTGRRATYLADSDVLAQQFALRAPVLFNGCRSGeifSIDLRQRDRGRMG 355
Cdd:COG2319  37 AAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADG---TVRLWDLATGLLL 113

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053489 356 FHGWKTSrfyqeSAITSVQLLQDENYLLAADMLGKIKLWDIRVKRCVKQYEGHHNEYAYLPIHinePEGLLLAVG-QDCY 434
Cdd:COG2319 114 RTLTGHT-----GAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTSVAFS---PDGKLLASGsDDGT 185

                       170       180       190
                ....*....|....*....|....*....|...
gi 41053489 435 TRLWSLQDSRLLRTIPSPhpagKDSIPNVVFSP 467
Cdd:COG2319 186 VRLWDLATGKLLRTLTGH----TGAVRSVAFSP 214
WD40 COG2319
WD40 repeat [General function prediction only];
367-467 2.22e-08

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 56.07  E-value: 2.22e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053489 367 ESAITSVQLLQDENYLLAADMLGKIKLWDIRVKRCVKQYEGHHNEYAYLPIHinePEGLLLAVG-QDCYTRLWSLQDSRL 445
Cdd:COG2319 204 TGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFS---PDGRLLASGsADGTVRLWDLATGEL 280

                        90       100
                ....*....|....*....|..
gi 41053489 446 LRTIPSPHpagkDSIPNVVFSP 467
Cdd:COG2319 281 LRTLTGHS----GGVNSVAFSP 298
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 367-467 2.91e-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: 55.03  E-value: 2.91e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053489 367 ESAITSVQLLQDENYLLAADMLGKIKLWDIRVKRCVKQYEGHHNEYAYLPIHinePEGLLLAVG-QDCYTRLWSLQDSRL 445
Cdd:cd00200  93 TSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFS---PDGTFVASSsQDGTIKLWDLRTGKC 169

                        90       100
                ....*....|....*....|..
gi 41053489 446 LRTIPSpHpagKDSIPNVVFSP 467
Cdd:cd00200 170 VATLTG-H---TGEVNSVAFSP 187
WD40 COG2319
WD40 repeat [General function prediction only];
366-467 3.55e-08

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 55.69  E-value: 3.55e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053489 366 QESAITSVQLLQDENYLLAADMLGKIKLWDIRVKRCVKQYEGHHNEYAYLPIHinePEGLLLAVG-QDCYTRLWSLQDSR 444
Cdd:COG2319 287 HSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFS---PDGKTLASGsDDGTVRLWDLATGE 363

                        90       100
                ....*....|....*....|...
gi 41053489 445 LLRTIpsphPAGKDSIPNVVFSP 467
Cdd:COG2319 364 LLRTL----TGHTGAVTSVAFSP 382
WD40 COG2319
WD40 repeat [General function prediction only];
367-467 9.27e-08

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 54.15  E-value: 9.27e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053489 367 ESAITSVQLLQDENYLLAADMLGKIKLWDIRVKRCVKQYEGHHNEyaylpihINE----PEGLLLAVG-QDCYTRLWSLQ 441
Cdd:COG2319 162 SGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGA-------VRSvafsPDGKLLASGsADGTVRLWDLA 234

                        90       100
                ....*....|....*....|....*.
gi 41053489 442 DSRLLRTIPSPHpagkDSIPNVVFSP 467
Cdd:COG2319 235 TGKLLRTLTGHS----GSVRSVAFSP 256
WD40 COG2319
WD40 repeat [General function prediction only];
304-467 2.34e-07

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 52.99  E-value: 2.34e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053489 304 TDAVTGRRATYLADSDVLAQQFALRAPVLFNGCRSGEIFSIDLRQRDRGRMGFHGWKTSRFYQESAITSVQLLQDENYLL 383
Cdd:COG2319  15 DLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLA 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053489 384 AADMLGKIKLWDIRVKRCVKQYEGHHNEYAYLPIHinePEGLLLAVG-QDCYTRLWSLQDSRLLRTIPSPHpagkDSIPN 462
Cdd:COG2319  95 SASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFS---PDGKTLASGsADGTVRLWDLATGKLLRTLTGHS----GAVTS 167


                ....*
gi 41053489 463 VVFSP 467
Cdd:COG2319 168 VAFSP 172
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 367-449 1.38e-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: 50.03  E-value: 1.38e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053489 367 ESAITSVQLLQDENYLLAADMLGKIKLWDIRVKRCVKQYEGHH---NEYAYLPIHinepeGLLLAVGQDCYTRLWSLQDS 443
Cdd:cd00200   9 TGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTgpvRDVAASADG-----TYLASGSSDKTIRLWDLETG 83


                ....*.
gi 41053489 444 RLLRTI 449
Cdd:cd00200  84 ECVRTL 89
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 367-467 4.87e-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: 4.87e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053489 367 ESAITSVQLLQDENYLLAADMLGKIKLWDIRVKRCVKQYEGH-HNEYAylpIHINEPEGLLLAVGQDCYTRLWSLQDSRL 445
Cdd:cd00200  51 TGPVRDVAASADGTYLASGSSDKTIRLWDLETGECVRTLTGHtSYVSS---VAFSPDGRILSSSSRDKTIKVWDVETGKC 127

                        90       100
                ....*....|....*....|..
gi 41053489 446 LRTIPSpHpagKDSIPNVVFSP 467
Cdd:cd00200 128 LTTLRG-H---TDWVNSVAFSP 145
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 277-439 1.05e-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: 47.33  E-value: 1.05e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053489 277 TAWSCAWCLNPqaDKTFSTGLS--RRVIVTDAVTGR-RATYLA-DSDVLAQQFALRAPVLFNGCRSGEIFSIDLRQRDrg 352
Cdd:cd00200 135 TDWVNSVAFSP--DGTFVASSSqdGTIKLWDLRTGKcVATLTGhTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGK-- 210

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053489 353 rmgfhgWKTSRFYQESAITSVQLLQDENYLLAADMLGKIKLWDIRVKRCVKQYEGHHNEyaylpihIN----EPEGLLLA 428
Cdd:cd00200 211 ------CLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNS-------VTslawSPDGKRLA 277

                       170
                ....*....|..
gi 41053489 429 VG-QDCYTRLWS 439
Cdd:cd00200 278 SGsADGTIRIWD 289
 
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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