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Conserved domains on  [gi|332801069|ref|NP_001193923|]
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protein phosphatase 2, regulatory subunit B, gamma isoform c [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];
17-431 3.42e-161

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: 462.58  E-value: 3.42e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801069  17 ADIISTVEFNHTGELLATGDKGGRVVIFQREpesknapHSQG-EYDVYSTFQSHEPEFDYLKSLEIEEKINKIKWLPQQN 95
Cdd:COG5170   26 ADKITAVEFDETGLYLATGDKGGRVVLFERE-------KSYGcEYKFFTEFQSHELEFDYLKSLEIEEKINAIEWFDDTG 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801069  96 AAHSLLSTNDKTIKLWKITERDKRPEGYNLKDEE---GKLKDLSTVTSLQVPVLKPMDLMVEVSPRRIFANGHTYHINSI 172
Cdd:COG5170   99 RNHFLLSTNDKTIKLWKIYEKNLKVVAENNLSDSfhsPMGGPLTSTKELLLPRLSEHDEIIAAKPCRVYANAHPYHINSI 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801069 173 SVNSDCETYMSADDLRINLWHLAITDRSFNIVDIKPANMEDLTEVITASEFHPHHCNLFVYSSSKGSLRLCDMRAAALCD 252
Cdd:COG5170  179 SFNSDKETLLSADDLRINLWNLEIIDGSFNIVDIKPHNMEELTEVITSAEFHPEMCNVFMYSSSKGEIKLNDLRQSALCD 258
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801069 253 KHSKLFEEPEDPSNRSFFSEIISSVSDVKFSHSGRYMLTRDYLTVKVWDLNMEARPIETYQVHDYLRSKLCSLYENDCIF 332
Cdd:COG5170  259 NSKKLFELTIDGVDVDFFEEIVSSISDFKFSDNGRYILSRDYLTVKIWDVNMAKNPIKTIPMHCDLMDELNDVYENDAIF 338
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801069 333 DKFECAWNGSDSVIMTGAYNNFFRMFDRNTKRD------VTL-----EASRESSKPRAVLKPRRVCVGGKRRRDDIS--- 398
Cdd:COG5170  339 DKFEISFSGDDKHVLSGSYSNNFGIYPTDSSGFkdvghvVNLadgsaEDFKVKCETNNVEKKDKLKNNDWRSVSSSAdgf 418
                        410       420       430
                 ....*....|....*....|....*....|....*....
gi 332801069 399 ------VDSLDFTKKILHTAWHPAENIIAIAATNNLYIF 431
Cdd:COG5170  419 vvacedPDNLDLLKKILHRSWHPFEDSVAIAATNNLFVF 457
 
Name Accession Description Interval E-value
CDC55 COG5170
Serine/threonine protein phosphatase 2A, regulatory subunit [Signal transduction mechanisms];
17-431 3.42e-161

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


Pssm-ID: 227498 [Multi-domain]  Cd Length: 460  Bit Score: 462.58  E-value: 3.42e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801069  17 ADIISTVEFNHTGELLATGDKGGRVVIFQREpesknapHSQG-EYDVYSTFQSHEPEFDYLKSLEIEEKINKIKWLPQQN 95
Cdd:COG5170   26 ADKITAVEFDETGLYLATGDKGGRVVLFERE-------KSYGcEYKFFTEFQSHELEFDYLKSLEIEEKINAIEWFDDTG 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801069  96 AAHSLLSTNDKTIKLWKITERDKRPEGYNLKDEE---GKLKDLSTVTSLQVPVLKPMDLMVEVSPRRIFANGHTYHINSI 172
Cdd:COG5170   99 RNHFLLSTNDKTIKLWKIYEKNLKVVAENNLSDSfhsPMGGPLTSTKELLLPRLSEHDEIIAAKPCRVYANAHPYHINSI 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801069 173 SVNSDCETYMSADDLRINLWHLAITDRSFNIVDIKPANMEDLTEVITASEFHPHHCNLFVYSSSKGSLRLCDMRAAALCD 252
Cdd:COG5170  179 SFNSDKETLLSADDLRINLWNLEIIDGSFNIVDIKPHNMEELTEVITSAEFHPEMCNVFMYSSSKGEIKLNDLRQSALCD 258
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801069 253 KHSKLFEEPEDPSNRSFFSEIISSVSDVKFSHSGRYMLTRDYLTVKVWDLNMEARPIETYQVHDYLRSKLCSLYENDCIF 332
Cdd:COG5170  259 NSKKLFELTIDGVDVDFFEEIVSSISDFKFSDNGRYILSRDYLTVKIWDVNMAKNPIKTIPMHCDLMDELNDVYENDAIF 338
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801069 333 DKFECAWNGSDSVIMTGAYNNFFRMFDRNTKRD------VTL-----EASRESSKPRAVLKPRRVCVGGKRRRDDIS--- 398
Cdd:COG5170  339 DKFEISFSGDDKHVLSGSYSNNFGIYPTDSSGFkdvghvVNLadgsaEDFKVKCETNNVEKKDKLKNNDWRSVSSSAdgf 418
                        410       420       430
                 ....*....|....*....|....*....|....*....
gi 332801069 399 ------VDSLDFTKKILHTAWHPAENIIAIAATNNLYIF 431
Cdd:COG5170  419 vvacedPDNLDLLKKILHRSWHPFEDSVAIAATNNLFVF 457
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
18-359 8.12e-07

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: 50.41  E-value: 8.12e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801069  18 DIISTVEFNHTGELLATGDKGGRVVIFQREPEsknaphsqgeyDVYSTFQSHEpefdylksleieEKINKIKWLPQQNaa 97
Cdd:cd00200   10 GGVTCVAFSPDGKLLATGSGDGTIKVWDLETG-----------ELLRTLKGHT------------GPVRDVAASADGT-- 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801069  98 hSLLST-NDKTIKLWKIterdkrpegynlkdeeGKLKDLSTVTslqvpvlkpmdlmvevsprrifanGHTYHINSISVNS 176
Cdd:cd00200   65 -YLASGsSDKTIRLWDL----------------ETGECVRTLT------------------------GHTSYVSSVAFSP 103
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801069 177 DCeTYMSA--DDLRINLWHLAITDRSFNIVDIkpanmedlTEVITASEFHPhhCNLFVYSSSK-GSLRLCDMRAAalcdK 253
Cdd:cd00200  104 DG-RILSSssRDKTIKVWDVETGKCLTTLRGH--------TDWVNSVAFSP--DGTFVASSSQdGTIKLWDLRTG----K 168
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801069 254 HSKLFEEPEDPsnrsffseiissVSDVKFSHSGRYMLT--RDYlTVKVWDLNMEaRPIETYQVHDY--------LRSKLC 323
Cdd:cd00200  169 CVATLTGHTGE------------VNSVAFSPDGEKLLSssSDG-TIKLWDLSTG-KCLGTLRGHENgvnsvafsPDGYLL 234
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 332801069 324 SLYEND---CIFD--KFEC--------------AWNGSDSVIMTGAYNNFFRMFD 359
Cdd:cd00200  235 ASGSEDgtiRVWDlrTGECvqtlsghtnsvtslAWSPDGKRLASGSADGTIRIWD 289
 
Name Accession Description Interval E-value
CDC55 COG5170
Serine/threonine protein phosphatase 2A, regulatory subunit [Signal transduction mechanisms];
17-431 3.42e-161

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


Pssm-ID: 227498 [Multi-domain]  Cd Length: 460  Bit Score: 462.58  E-value: 3.42e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801069  17 ADIISTVEFNHTGELLATGDKGGRVVIFQREpesknapHSQG-EYDVYSTFQSHEPEFDYLKSLEIEEKINKIKWLPQQN 95
Cdd:COG5170   26 ADKITAVEFDETGLYLATGDKGGRVVLFERE-------KSYGcEYKFFTEFQSHELEFDYLKSLEIEEKINAIEWFDDTG 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801069  96 AAHSLLSTNDKTIKLWKITERDKRPEGYNLKDEE---GKLKDLSTVTSLQVPVLKPMDLMVEVSPRRIFANGHTYHINSI 172
Cdd:COG5170   99 RNHFLLSTNDKTIKLWKIYEKNLKVVAENNLSDSfhsPMGGPLTSTKELLLPRLSEHDEIIAAKPCRVYANAHPYHINSI 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801069 173 SVNSDCETYMSADDLRINLWHLAITDRSFNIVDIKPANMEDLTEVITASEFHPHHCNLFVYSSSKGSLRLCDMRAAALCD 252
Cdd:COG5170  179 SFNSDKETLLSADDLRINLWNLEIIDGSFNIVDIKPHNMEELTEVITSAEFHPEMCNVFMYSSSKGEIKLNDLRQSALCD 258
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801069 253 KHSKLFEEPEDPSNRSFFSEIISSVSDVKFSHSGRYMLTRDYLTVKVWDLNMEARPIETYQVHDYLRSKLCSLYENDCIF 332
Cdd:COG5170  259 NSKKLFELTIDGVDVDFFEEIVSSISDFKFSDNGRYILSRDYLTVKIWDVNMAKNPIKTIPMHCDLMDELNDVYENDAIF 338
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801069 333 DKFECAWNGSDSVIMTGAYNNFFRMFDRNTKRD------VTL-----EASRESSKPRAVLKPRRVCVGGKRRRDDIS--- 398
Cdd:COG5170  339 DKFEISFSGDDKHVLSGSYSNNFGIYPTDSSGFkdvghvVNLadgsaEDFKVKCETNNVEKKDKLKNNDWRSVSSSAdgf 418
                        410       420       430
                 ....*....|....*....|....*....|....*....
gi 332801069 399 ------VDSLDFTKKILHTAWHPAENIIAIAATNNLYIF 431
Cdd:COG5170  419 vvacedPDNLDLLKKILHRSWHPFEDSVAIAATNNLFVF 457
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
18-359 8.12e-07

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: 50.41  E-value: 8.12e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801069  18 DIISTVEFNHTGELLATGDKGGRVVIFQREPEsknaphsqgeyDVYSTFQSHEpefdylksleieEKINKIKWLPQQNaa 97
Cdd:cd00200   10 GGVTCVAFSPDGKLLATGSGDGTIKVWDLETG-----------ELLRTLKGHT------------GPVRDVAASADGT-- 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801069  98 hSLLST-NDKTIKLWKIterdkrpegynlkdeeGKLKDLSTVTslqvpvlkpmdlmvevsprrifanGHTYHINSISVNS 176
Cdd:cd00200   65 -YLASGsSDKTIRLWDL----------------ETGECVRTLT------------------------GHTSYVSSVAFSP 103
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801069 177 DCeTYMSA--DDLRINLWHLAITDRSFNIVDIkpanmedlTEVITASEFHPhhCNLFVYSSSK-GSLRLCDMRAAalcdK 253
Cdd:cd00200  104 DG-RILSSssRDKTIKVWDVETGKCLTTLRGH--------TDWVNSVAFSP--DGTFVASSSQdGTIKLWDLRTG----K 168
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801069 254 HSKLFEEPEDPsnrsffseiissVSDVKFSHSGRYMLT--RDYlTVKVWDLNMEaRPIETYQVHDY--------LRSKLC 323
Cdd:cd00200  169 CVATLTGHTGE------------VNSVAFSPDGEKLLSssSDG-TIKLWDLSTG-KCLGTLRGHENgvnsvafsPDGYLL 234
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 332801069 324 SLYEND---CIFD--KFEC--------------AWNGSDSVIMTGAYNNFFRMFD 359
Cdd:cd00200  235 ASGSEDgtiRVWDlrTGECvqtlsghtnsvtslAWSPDGKRLASGSADGTIRIWD 289
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
105-374 9.50e-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: 46.94  E-value: 9.50e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801069 105 DKTIKLWKITERDKRpegYNLKDEEGKLKDLSTVTSLQVPVLKPMDLMVEV------SPRRIFAnGHTYHINSISVNSDC 178
Cdd:cd00200   30 DGTIKVWDLETGELL---RTLKGHTGPVRDVAASADGTYLASGSSDKTIRLwdletgECVRTLT-GHTSYVSSVAFSPDG 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801069 179 eTYMSA--DDLRINLWHLAITDRSFNIVDIkpanmedlTEVITASEFHPhhCNLFVYSSSK-GSLRLCDMRAAalcdKHS 255
Cdd:cd00200  106 -RILSSssRDKTIKVWDVETGKCLTTLRGH--------TDWVNSVAFSP--DGTFVASSSQdGTIKLWDLRTG----KCV 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332801069 256 KLFEEPEDPsnrsffseiissVSDVKFSHSGRYMLT--RDYlTVKVWDLNMEaRPIETYQVHDylrSKLCSlyendcifd 333
Cdd:cd00200  171 ATLTGHTGE------------VNSVAFSPDGEKLLSssSDG-TIKLWDLSTG-KCLGTLRGHE---NGVNS--------- 224
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 332801069 334 kfeCAWNGSDSVIMTGAYNNFFRMFDRNTKRDV-TLEASRES 374
Cdd:cd00200  225 ---VAFSPDGYLLASGSEDGTIRVWDLRTGECVqTLSGHTNS 263
 
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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