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Conserved domains on  [gi|1825761149|ref|NP_858061|]
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serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B beta isoform isoform e [Homo sapiens]

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

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List of domain hits

Name Accession Description Interval E-value
CDC55 super family cl27186
Serine/threonine protein phosphatase 2A, regulatory subunit [Signal transduction mechanisms];
22-438 1.93e-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: 473.75  E-value: 1.93e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825761149  22 TEADIISTVEFNHTGELLATGDKGGRVVIFQREQEsknqvhRRGEYNVYSTFQSHEPEFDYLKSLEIEEKINKIRWLPQQ 101
Cdd:COG5170    24 TEADKITAVEFDETGLYLATGDKGGRVVLFEREKS------YGCEYKFFTEFQSHELEFDYLKSLEIEEKINAIEWFDDT 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825761149 102 NAAYFLLSTNDKTVKLWKVSERD-KRPEGYNLKDEEGRLRDPATITT--LRVPVLRPMDLMVEATPRRVFANAHTYHINS 178
Cdd:COG5170    98 GRNHFLLSTNDKTIKLWKIYEKNlKVVAENNLSDSFHSPMGGPLTSTkeLLLPRLSEHDEIIAAKPCRVYANAHPYHINS 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825761149 179 ISVNSDYETYMSADDLRINLWNFEITNQSFNIVDIKPANMEELTEVITAAEFHPHHCNTFVYSSSKGTIRLCDMRASALC 258
Cdd:COG5170   178 ISFNSDKETLLSADDLRINLWNLEIIDGSFNIVDIKPHNMEELTEVITSAEFHPEMCNVFMYSSSKGEIKLNDLRQSALC 257
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825761149 259 DRHTKFFEEPEDPSNRSFFSEIISSISDVKFSHSGRYIMTRDYLTVKVWDLNMENRPIETYQVHDYLRSKLCSLYENDCI 338
Cdd:COG5170   258 DNSKKLFELTIDGVDVDFFEEIVSSISDFKFSDNGRYILSRDYLTVKIWDVNMAKNPIKTIPMHCDLMDELNDVYENDAI 337
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825761149 339 FDKFECVWNGSDSVIMTGSYNNFFRMFDRNTKRD------VTL-EASRENSKPRAILK--PRKVCVGGKRRKDEISV--- 406
Cdd:COG5170   338 FDKFEISFSGDDKHVLSGSYSNNFGIYPTDSSGFkdvghvVNLaDGSAEDFKVKCETNnvEKKDKLKNNDWRSVSSSadg 417
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|
gi 1825761149 407 --------DSLDFSKKILHTAWHPSENIIAVAATNNLYIF 438
Cdd:COG5170   418 fvvacedpDNLDLLKKILHRSWHPFEDSVAIAATNNLFVF 457
 
Name Accession Description Interval E-value
CDC55 COG5170
Serine/threonine protein phosphatase 2A, regulatory subunit [Signal transduction mechanisms];
22-438 1.93e-165

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


Pssm-ID: 227498 [Multi-domain]  Cd Length: 460  Bit Score: 473.75  E-value: 1.93e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825761149  22 TEADIISTVEFNHTGELLATGDKGGRVVIFQREQEsknqvhRRGEYNVYSTFQSHEPEFDYLKSLEIEEKINKIRWLPQQ 101
Cdd:COG5170    24 TEADKITAVEFDETGLYLATGDKGGRVVLFEREKS------YGCEYKFFTEFQSHELEFDYLKSLEIEEKINAIEWFDDT 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825761149 102 NAAYFLLSTNDKTVKLWKVSERD-KRPEGYNLKDEEGRLRDPATITT--LRVPVLRPMDLMVEATPRRVFANAHTYHINS 178
Cdd:COG5170    98 GRNHFLLSTNDKTIKLWKIYEKNlKVVAENNLSDSFHSPMGGPLTSTkeLLLPRLSEHDEIIAAKPCRVYANAHPYHINS 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825761149 179 ISVNSDYETYMSADDLRINLWNFEITNQSFNIVDIKPANMEELTEVITAAEFHPHHCNTFVYSSSKGTIRLCDMRASALC 258
Cdd:COG5170   178 ISFNSDKETLLSADDLRINLWNLEIIDGSFNIVDIKPHNMEELTEVITSAEFHPEMCNVFMYSSSKGEIKLNDLRQSALC 257
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825761149 259 DRHTKFFEEPEDPSNRSFFSEIISSISDVKFSHSGRYIMTRDYLTVKVWDLNMENRPIETYQVHDYLRSKLCSLYENDCI 338
Cdd:COG5170   258 DNSKKLFELTIDGVDVDFFEEIVSSISDFKFSDNGRYILSRDYLTVKIWDVNMAKNPIKTIPMHCDLMDELNDVYENDAI 337
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825761149 339 FDKFECVWNGSDSVIMTGSYNNFFRMFDRNTKRD------VTL-EASRENSKPRAILK--PRKVCVGGKRRKDEISV--- 406
Cdd:COG5170   338 FDKFEISFSGDDKHVLSGSYSNNFGIYPTDSSGFkdvghvVNLaDGSAEDFKVKCETNnvEKKDKLKNNDWRSVSSSadg 417
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|
gi 1825761149 407 --------DSLDFSKKILHTAWHPSENIIAVAATNNLYIF 438
Cdd:COG5170   418 fvvacedpDNLDLLKKILHRSWHPFEDSVAIAATNNLFVF 457
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
190-434 3.57e-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: 39.24  E-value: 3.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825761149 190 SADDLRINLWNFEiTNQSFNIvdikpanMEELTEVITAAEFHPHhcNTFVYSSSK-GTIRLCDMrasalcdrhtkffeep 268
Cdd:cd00200    69 GSSDKTIRLWDLE-TGECVRT-------LTGHTSYVSSVAFSPD--GRILSSSSRdKTIKVWDV---------------- 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825761149 269 EDPSNRSFFSEIISSISDVKFSHSGRYIMTRDY-LTVKVWDLNmENRPIETYQVH-DYLRSklcslyendcifdkfeCVW 346
Cdd:cd00200   123 ETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQdGTIKLWDLR-TGKCVATLTGHtGEVNS----------------VAF 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825761149 347 NGSDSVIMTGSYNNFFRMFDRNTKRDV-TLEASRENSKPRAILKPRKVCVGGKRRKDeISVDSLDfSKKILHT------- 418
Cdd:cd00200   186 SPDGEKLLSSSSDGTIKLWDLSTGKCLgTLRGHENGVNSVAFSPDGYLLASGSEDGT-IRVWDLR-TGECVQTlsghtns 263
                         250       260
                  ....*....|....*....|
gi 1825761149 419 ----AWHPSENIIAVAATNN 434
Cdd:cd00200   264 vtslAWSPDGKRLASGSADG 283
 
Name Accession Description Interval E-value
CDC55 COG5170
Serine/threonine protein phosphatase 2A, regulatory subunit [Signal transduction mechanisms];
22-438 1.93e-165

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


Pssm-ID: 227498 [Multi-domain]  Cd Length: 460  Bit Score: 473.75  E-value: 1.93e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825761149  22 TEADIISTVEFNHTGELLATGDKGGRVVIFQREQEsknqvhRRGEYNVYSTFQSHEPEFDYLKSLEIEEKINKIRWLPQQ 101
Cdd:COG5170    24 TEADKITAVEFDETGLYLATGDKGGRVVLFEREKS------YGCEYKFFTEFQSHELEFDYLKSLEIEEKINAIEWFDDT 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825761149 102 NAAYFLLSTNDKTVKLWKVSERD-KRPEGYNLKDEEGRLRDPATITT--LRVPVLRPMDLMVEATPRRVFANAHTYHINS 178
Cdd:COG5170    98 GRNHFLLSTNDKTIKLWKIYEKNlKVVAENNLSDSFHSPMGGPLTSTkeLLLPRLSEHDEIIAAKPCRVYANAHPYHINS 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825761149 179 ISVNSDYETYMSADDLRINLWNFEITNQSFNIVDIKPANMEELTEVITAAEFHPHHCNTFVYSSSKGTIRLCDMRASALC 258
Cdd:COG5170   178 ISFNSDKETLLSADDLRINLWNLEIIDGSFNIVDIKPHNMEELTEVITSAEFHPEMCNVFMYSSSKGEIKLNDLRQSALC 257
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825761149 259 DRHTKFFEEPEDPSNRSFFSEIISSISDVKFSHSGRYIMTRDYLTVKVWDLNMENRPIETYQVHDYLRSKLCSLYENDCI 338
Cdd:COG5170   258 DNSKKLFELTIDGVDVDFFEEIVSSISDFKFSDNGRYILSRDYLTVKIWDVNMAKNPIKTIPMHCDLMDELNDVYENDAI 337
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825761149 339 FDKFECVWNGSDSVIMTGSYNNFFRMFDRNTKRD------VTL-EASRENSKPRAILK--PRKVCVGGKRRKDEISV--- 406
Cdd:COG5170   338 FDKFEISFSGDDKHVLSGSYSNNFGIYPTDSSGFkdvghvVNLaDGSAEDFKVKCETNnvEKKDKLKNNDWRSVSSSadg 417
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|
gi 1825761149 407 --------DSLDFSKKILHTAWHPSENIIAVAATNNLYIF 438
Cdd:COG5170   418 fvvacedpDNLDLLKKILHRSWHPFEDSVAIAATNNLFVF 457
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
190-434 3.57e-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: 39.24  E-value: 3.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825761149 190 SADDLRINLWNFEiTNQSFNIvdikpanMEELTEVITAAEFHPHhcNTFVYSSSK-GTIRLCDMrasalcdrhtkffeep 268
Cdd:cd00200    69 GSSDKTIRLWDLE-TGECVRT-------LTGHTSYVSSVAFSPD--GRILSSSSRdKTIKVWDV---------------- 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825761149 269 EDPSNRSFFSEIISSISDVKFSHSGRYIMTRDY-LTVKVWDLNmENRPIETYQVH-DYLRSklcslyendcifdkfeCVW 346
Cdd:cd00200   123 ETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQdGTIKLWDLR-TGKCVATLTGHtGEVNS----------------VAF 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825761149 347 NGSDSVIMTGSYNNFFRMFDRNTKRDV-TLEASRENSKPRAILKPRKVCVGGKRRKDeISVDSLDfSKKILHT------- 418
Cdd:cd00200   186 SPDGEKLLSSSSDGTIKLWDLSTGKCLgTLRGHENGVNSVAFSPDGYLLASGSEDGT-IRVWDLR-TGECVQTlsghtns 263
                         250       260
                  ....*....|....*....|
gi 1825761149 419 ----AWHPSENIIAVAATNN 434
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.
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