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Conserved domains on  [gi|1207153564|ref|XP_021324054|]
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WD repeat domain 21 isoform X1 [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];
276-465 8.97e-09

WD40 repeat [General function prediction only];


:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 57.61  E-value: 8.97e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153564 276 STAWSCAWCLNPQADKTFSTGLSRRVIVTDAVTGRRATYLADSDVLAQQFALRAPVLFNGCRSGeifSIDLRQRDRGRSH 355
Cdd:COG2319    37 AAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADG---TVRLWDLATGLLL 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153564 356 GWKTSrfyQESAITSVQLLQDENYLLAADMLGKIKLWDIRVKRCVKQYEGHHNEYAYLPIHinePEGLLLAVG-QDCYTR 434
Cdd:COG2319   114 RTLTG---HTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTSVAFS---PDGKLLASGsDDGTVR 187

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1207153564 435 LWSLQDSRLLRTIPSPhpagKDSIPNVVFSP 465
Cdd:COG2319   188 LWDLATGKLLRTLTGH----TGAVRSVAFSP 214
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
276-465 8.97e-09

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 57.61  E-value: 8.97e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153564 276 STAWSCAWCLNPQADKTFSTGLSRRVIVTDAVTGRRATYLADSDVLAQQFALRAPVLFNGCRSGeifSIDLRQRDRGRSH 355
Cdd:COG2319    37 AAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADG---TVRLWDLATGLLL 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153564 356 GWKTSrfyQESAITSVQLLQDENYLLAADMLGKIKLWDIRVKRCVKQYEGHHNEYAYLPIHinePEGLLLAVG-QDCYTR 434
Cdd:COG2319   114 RTLTG---HTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTSVAFS---PDGKLLASGsDDGTVR 187

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1207153564 435 LWSLQDSRLLRTIPSPhpagKDSIPNVVFSP 465
Cdd:COG2319   188 LWDLATGKLLRTLTGH----TGAVRSVAFSP 214
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 365-465 3.20e-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: 3.20e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153564 365 ESAITSVQLLQDENYLLAADMLGKIKLWDIRVKRCVKQYEGHHNEYAYLPIHinePEGLLLAVG-QDCYTRLWSLQDSRL 443
Cdd:cd00200    93 TSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFS---PDGTFVASSsQDGTIKLWDLRTGKC 169

                          90       100
                  ....*....|....*....|..
gi 1207153564 444 LRTIPSpHpagKDSIPNVVFSP 465
Cdd:cd00200   170 VATLTG-H---TGEVNSVAFSP 187
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
276-465 8.97e-09

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 57.61  E-value: 8.97e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153564 276 STAWSCAWCLNPQADKTFSTGLSRRVIVTDAVTGRRATYLADSDVLAQQFALRAPVLFNGCRSGeifSIDLRQRDRGRSH 355
Cdd:COG2319    37 AAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADG---TVRLWDLATGLLL 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153564 356 GWKTSrfyQESAITSVQLLQDENYLLAADMLGKIKLWDIRVKRCVKQYEGHHNEYAYLPIHinePEGLLLAVG-QDCYTR 434
Cdd:COG2319   114 RTLTG---HTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTSVAFS---PDGKLLASGsDDGTVR 187

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1207153564 435 LWSLQDSRLLRTIPSPhpagKDSIPNVVFSP 465
Cdd:COG2319   188 LWDLATGKLLRTLTGH----TGAVRSVAFSP 214
WD40 COG2319
WD40 repeat [General function prediction only];
365-465 2.21e-08

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 56.07  E-value: 2.21e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153564 365 ESAITSVQLLQDENYLLAADMLGKIKLWDIRVKRCVKQYEGHHNEYAYLPIHinePEGLLLAVG-QDCYTRLWSLQDSRL 443
Cdd:COG2319   204 TGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFS---PDGRLLASGsADGTVRLWDLATGEL 280

                          90       100
                  ....*....|....*....|..
gi 1207153564 444 LRTIPSPHpagkDSIPNVVFSP 465
Cdd:COG2319   281 LRTLTGHS----GGVNSVAFSP 298
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 365-465 3.20e-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: 3.20e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153564 365 ESAITSVQLLQDENYLLAADMLGKIKLWDIRVKRCVKQYEGHHNEYAYLPIHinePEGLLLAVG-QDCYTRLWSLQDSRL 443
Cdd:cd00200    93 TSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFS---PDGTFVASSsQDGTIKLWDLRTGKC 169

                          90       100
                  ....*....|....*....|..
gi 1207153564 444 LRTIPSpHpagKDSIPNVVFSP 465
Cdd:cd00200   170 VATLTG-H---TGEVNSVAFSP 187
WD40 COG2319
WD40 repeat [General function prediction only];
364-465 3.52e-08

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 55.69  E-value: 3.52e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153564 364 QESAITSVQLLQDENYLLAADMLGKIKLWDIRVKRCVKQYEGHHNEYAYLPIHinePEGLLLAVG-QDCYTRLWSLQDSR 442
Cdd:COG2319   287 HSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFS---PDGKTLASGsDDGTVRLWDLATGE 363

                          90       100
                  ....*....|....*....|...
gi 1207153564 443 LLRTIpsphPAGKDSIPNVVFSP 465
Cdd:COG2319   364 LLRTL----TGHTGAVTSVAFSP 382
WD40 COG2319
WD40 repeat [General function prediction only];
365-465 9.21e-08

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 54.15  E-value: 9.21e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153564 365 ESAITSVQLLQDENYLLAADMLGKIKLWDIRVKRCVKQYEGHHNEyaylpihINE----PEGLLLAVG-QDCYTRLWSLQ 439
Cdd:COG2319   162 SGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGA-------VRSvafsPDGKLLASGsADGTVRLWDLA 234

                          90       100
                  ....*....|....*....|....*.
gi 1207153564 440 DSRLLRTIPSPHpagkDSIPNVVFSP 465
Cdd:COG2319   235 TGKLLRTLTGHS----GSVRSVAFSP 256
WD40 COG2319
WD40 repeat [General function prediction only];
294-465 2.72e-07

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 52.61  E-value: 2.72e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153564 294 STGLSRRVIVTDAVTGRRATYLADSDVLAQQFALRAPVLFNGCRSGEIFSIDLRQRDRGRSHGWKTSRFYQESAITSVQL 373
Cdd:COG2319     7 AALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAF 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153564 374 LQDENYLLAADMLGKIKLWDIRVKRCVKQYEGHHNEYAYLPIHinePEGLLLAVG-QDCYTRLWSLQDSRLLRTIPSPHp 452
Cdd:COG2319    87 SPDGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFS---PDGKTLASGsADGTVRLWDLATGKLLRTLTGHS- 162

                         170
                  ....*....|...
gi 1207153564 453 agkDSIPNVVFSP 465
Cdd:COG2319   163 ---GAVTSVAFSP 172
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 365-447 1.52e-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: 1.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153564 365 ESAITSVQLLQDENYLLAADMLGKIKLWDIRVKRCVKQYEGHH---NEYAYLPIHinepeGLLLAVGQDCYTRLWSLQDS 441
Cdd:cd00200     9 TGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTgpvRDVAASADG-----TYLASGSSDKTIRLWDLETG 83


                  ....*.
gi 1207153564 442 RLLRTI 447
Cdd:cd00200    84 ECVRTL 89
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 365-465 5.54e-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: 48.10  E-value: 5.54e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153564 365 ESAITSVQLLQDENYLLAADMLGKIKLWDIRVKRCVKQYEGH-HNEYAylpIHINEPEGLLLAVGQDCYTRLWSLQDSRL 443
Cdd:cd00200    51 TGPVRDVAASADGTYLASGSSDKTIRLWDLETGECVRTLTGHtSYVSS---VAFSPDGRILSSSSRDKTIKVWDVETGKC 127

                          90       100
                  ....*....|....*....|..
gi 1207153564 444 LRTIPSpHpagKDSIPNVVFSP 465
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 ...
 277-437 6.75e-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: 47.71  E-value: 6.75e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153564 277 TAWSCAWCLNPqaDKTFSTGLS--RRVIVTDAVTGR-RATYLA-DSDVLAQQFALRAPVLFNGCRSGEIFSIDLRQRDrg 352
Cdd:cd00200   135 TDWVNSVAFSP--DGTFVASSSqdGTIKLWDLRTGKcVATLTGhTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGK-- 210

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153564 353 rshgWKTSRFYQESAITSVQLLQDENYLLAADMLGKIKLWDIRVKRCVKQYEGHHNEyaylpihIN----EPEGLLLAVG 428
Cdd:cd00200   211 ----CLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNS-------VTslawSPDGKRLASG 279

                         170
                  ....*....|
gi 1207153564 429 -QDCYTRLWS 437
Cdd:cd00200   280 sADGTIRIWD 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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