NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|966949332|ref|XP_014996634|]
View 

serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B beta isoform isoform X8 [Macaca mulatta]

Protein Classification

CDC55 family protein( domain architecture ID 706555)

CDC55 family protein is a WD40-repeat containing protein similar to Homo sapiens serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B

Gene Ontology:  GO:0019888|GO:0000159
PubMed:  1849734

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
CDC55 super family cl27186
Serine/threonine protein phosphatase 2A, regulatory subunit [Signal transduction mechanisms];
13-427 7.55e-165

Serine/threonine protein phosphatase 2A, regulatory subunit [Signal transduction mechanisms];


The actual alignment was detected with superfamily member COG5170:

Pssm-ID: 227498 [Multi-domain]  Cd Length: 460  Bit Score: 471.44  E-value: 7.55e-165
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966949332  13 ADIISTVEFNHTGELLATGDKGGRVVIFQREQEsknqvhRRGEYNVYSTFQSHEPEFDYLKSLEIEEKINKIRWLPQQNA 92
Cdd:COG5170   26 ADKITAVEFDETGLYLATGDKGGRVVLFEREKS------YGCEYKFFTEFQSHELEFDYLKSLEIEEKINAIEWFDDTGR 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966949332  93 AYFLLSTNDKTVKLWKVSERD-KRPEGYNLKDEEGRLRDPATITT--LRVPVLRPMDLMVEATPRRVFANAHTYHINSIS 169
Cdd:COG5170  100 NHFLLSTNDKTIKLWKIYEKNlKVVAENNLSDSFHSPMGGPLTSTkeLLLPRLSEHDEIIAAKPCRVYANAHPYHINSIS 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966949332 170 VNSDYETYMSADDLRINLWNFEITNQSFNIVDIKPANMEELTEVITAAEFHPHHCNTFVYSSSKGTIRLCDMRASALCDR 249
Cdd:COG5170  180 FNSDKETLLSADDLRINLWNLEIIDGSFNIVDIKPHNMEELTEVITSAEFHPEMCNVFMYSSSKGEIKLNDLRQSALCDN 259
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966949332 250 HTKFFEEPEDPSNRSFFSEIISSISDVKFSHSGRYIMTRDYLTVKVWDLNMENRPIETYQVHDYLRSKLCSLYENDCIFD 329
Cdd:COG5170  260 SKKLFELTIDGVDVDFFEEIVSSISDFKFSDNGRYILSRDYLTVKIWDVNMAKNPIKTIPMHCDLMDELNDVYENDAIFD 339
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966949332 330 KFECVWNGSDSVIMTGSYNNFFRMFDRNTKRD------VTL-EASRENSKPRAILK--PRKVCVGGKRRKDEISV----- 395
Cdd:COG5170  340 KFEISFSGDDKHVLSGSYSNNFGIYPTDSSGFkdvghvVNLaDGSAEDFKVKCETNnvEKKDKLKNNDWRSVSSSadgfv 419
                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 966949332 396 ------DSLDFSKKILHTAWHPSENIIAVAATNNLYIF 427
Cdd:COG5170  420 vacedpDNLDLLKKILHRSWHPFEDSVAIAATNNLFVF 457
 
Name Accession Description Interval E-value
CDC55 COG5170
Serine/threonine protein phosphatase 2A, regulatory subunit [Signal transduction mechanisms];
13-427 7.55e-165

Serine/threonine protein phosphatase 2A, regulatory subunit [Signal transduction mechanisms];


Pssm-ID: 227498 [Multi-domain]  Cd Length: 460  Bit Score: 471.44  E-value: 7.55e-165
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966949332  13 ADIISTVEFNHTGELLATGDKGGRVVIFQREQEsknqvhRRGEYNVYSTFQSHEPEFDYLKSLEIEEKINKIRWLPQQNA 92
Cdd:COG5170   26 ADKITAVEFDETGLYLATGDKGGRVVLFEREKS------YGCEYKFFTEFQSHELEFDYLKSLEIEEKINAIEWFDDTGR 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966949332  93 AYFLLSTNDKTVKLWKVSERD-KRPEGYNLKDEEGRLRDPATITT--LRVPVLRPMDLMVEATPRRVFANAHTYHINSIS 169
Cdd:COG5170  100 NHFLLSTNDKTIKLWKIYEKNlKVVAENNLSDSFHSPMGGPLTSTkeLLLPRLSEHDEIIAAKPCRVYANAHPYHINSIS 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966949332 170 VNSDYETYMSADDLRINLWNFEITNQSFNIVDIKPANMEELTEVITAAEFHPHHCNTFVYSSSKGTIRLCDMRASALCDR 249
Cdd:COG5170  180 FNSDKETLLSADDLRINLWNLEIIDGSFNIVDIKPHNMEELTEVITSAEFHPEMCNVFMYSSSKGEIKLNDLRQSALCDN 259
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966949332 250 HTKFFEEPEDPSNRSFFSEIISSISDVKFSHSGRYIMTRDYLTVKVWDLNMENRPIETYQVHDYLRSKLCSLYENDCIFD 329
Cdd:COG5170  260 SKKLFELTIDGVDVDFFEEIVSSISDFKFSDNGRYILSRDYLTVKIWDVNMAKNPIKTIPMHCDLMDELNDVYENDAIFD 339
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966949332 330 KFECVWNGSDSVIMTGSYNNFFRMFDRNTKRD------VTL-EASRENSKPRAILK--PRKVCVGGKRRKDEISV----- 395
Cdd:COG5170  340 KFEISFSGDDKHVLSGSYSNNFGIYPTDSSGFkdvghvVNLaDGSAEDFKVKCETNnvEKKDKLKNNDWRSVSSSadgfv 419
                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 966949332 396 ------DSLDFSKKILHTAWHPSENIIAVAATNNLYIF 427
Cdd:COG5170  420 vacedpDNLDLLKKILHRSWHPFEDSVAIAATNNLFVF 457
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
179-423 2.15e-03

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: 39.63  E-value: 2.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966949332 179 SADDLRINLWNFEiTNQSFNIvdikpanMEELTEVITAAEFHPHhcNTFVYSSSK-GTIRLCDMrasalcdrhtkffeep 257
Cdd:cd00200   69 GSSDKTIRLWDLE-TGECVRT-------LTGHTSYVSSVAFSPD--GRILSSSSRdKTIKVWDV---------------- 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966949332 258 EDPSNRSFFSEIISSISDVKFSHSGRYIMTRDY-LTVKVWDLNmENRPIETYQVH-DYLRSklcslyendcifdkfeCVW 335
Cdd:cd00200  123 ETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQdGTIKLWDLR-TGKCVATLTGHtGEVNS----------------VAF 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966949332 336 NGSDSVIMTGSYNNFFRMFDRNTKRDV-TLEASRENSKPRAILKPRKVCVGGKRRKDeISVDSLDfSKKILHT------- 407
Cdd:cd00200  186 SPDGEKLLSSSSDGTIKLWDLSTGKCLgTLRGHENGVNSVAFSPDGYLLASGSEDGT-IRVWDLR-TGECVQTlsghtns 263
                        250       260
                 ....*....|....*....|
gi 966949332 408 ----AWHPSENIIAVAATNN 423
Cdd:cd00200  264 vtslAWSPDGKRLASGSADG 283
 
Name Accession Description Interval E-value
CDC55 COG5170
Serine/threonine protein phosphatase 2A, regulatory subunit [Signal transduction mechanisms];
13-427 7.55e-165

Serine/threonine protein phosphatase 2A, regulatory subunit [Signal transduction mechanisms];


Pssm-ID: 227498 [Multi-domain]  Cd Length: 460  Bit Score: 471.44  E-value: 7.55e-165
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966949332  13 ADIISTVEFNHTGELLATGDKGGRVVIFQREQEsknqvhRRGEYNVYSTFQSHEPEFDYLKSLEIEEKINKIRWLPQQNA 92
Cdd:COG5170   26 ADKITAVEFDETGLYLATGDKGGRVVLFEREKS------YGCEYKFFTEFQSHELEFDYLKSLEIEEKINAIEWFDDTGR 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966949332  93 AYFLLSTNDKTVKLWKVSERD-KRPEGYNLKDEEGRLRDPATITT--LRVPVLRPMDLMVEATPRRVFANAHTYHINSIS 169
Cdd:COG5170  100 NHFLLSTNDKTIKLWKIYEKNlKVVAENNLSDSFHSPMGGPLTSTkeLLLPRLSEHDEIIAAKPCRVYANAHPYHINSIS 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966949332 170 VNSDYETYMSADDLRINLWNFEITNQSFNIVDIKPANMEELTEVITAAEFHPHHCNTFVYSSSKGTIRLCDMRASALCDR 249
Cdd:COG5170  180 FNSDKETLLSADDLRINLWNLEIIDGSFNIVDIKPHNMEELTEVITSAEFHPEMCNVFMYSSSKGEIKLNDLRQSALCDN 259
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966949332 250 HTKFFEEPEDPSNRSFFSEIISSISDVKFSHSGRYIMTRDYLTVKVWDLNMENRPIETYQVHDYLRSKLCSLYENDCIFD 329
Cdd:COG5170  260 SKKLFELTIDGVDVDFFEEIVSSISDFKFSDNGRYILSRDYLTVKIWDVNMAKNPIKTIPMHCDLMDELNDVYENDAIFD 339
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966949332 330 KFECVWNGSDSVIMTGSYNNFFRMFDRNTKRD------VTL-EASRENSKPRAILK--PRKVCVGGKRRKDEISV----- 395
Cdd:COG5170  340 KFEISFSGDDKHVLSGSYSNNFGIYPTDSSGFkdvghvVNLaDGSAEDFKVKCETNnvEKKDKLKNNDWRSVSSSadgfv 419
                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 966949332 396 ------DSLDFSKKILHTAWHPSENIIAVAATNNLYIF 427
Cdd:COG5170  420 vacedpDNLDLLKKILHRSWHPFEDSVAIAATNNLFVF 457
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
179-423 2.15e-03

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: 39.63  E-value: 2.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966949332 179 SADDLRINLWNFEiTNQSFNIvdikpanMEELTEVITAAEFHPHhcNTFVYSSSK-GTIRLCDMrasalcdrhtkffeep 257
Cdd:cd00200   69 GSSDKTIRLWDLE-TGECVRT-------LTGHTSYVSSVAFSPD--GRILSSSSRdKTIKVWDV---------------- 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966949332 258 EDPSNRSFFSEIISSISDVKFSHSGRYIMTRDY-LTVKVWDLNmENRPIETYQVH-DYLRSklcslyendcifdkfeCVW 335
Cdd:cd00200  123 ETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQdGTIKLWDLR-TGKCVATLTGHtGEVNS----------------VAF 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966949332 336 NGSDSVIMTGSYNNFFRMFDRNTKRDV-TLEASRENSKPRAILKPRKVCVGGKRRKDeISVDSLDfSKKILHT------- 407
Cdd:cd00200  186 SPDGEKLLSSSSDGTIKLWDLSTGKCLgTLRGHENGVNSVAFSPDGYLLASGSEDGT-IRVWDLR-TGECVQTlsghtns 263
                        250       260
                 ....*....|....*....|
gi 966949332 408 ----AWHPSENIIAVAATNN 423
Cdd:cd00200  264 vtslAWSPDGKRLASGSADG 283
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH