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Conserved domains on  [gi|1039779212|ref|XP_017177839|]
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serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B delta isoform isoform X1 [Mus musculus]

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];
2-283 4.88e-115

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: 338.93  E-value: 4.88e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779212   2 DLMVEASPRRIFANAHTYHINSISVNSDHETYLSADDLRINLWHLEITDRSFNIVDIKPANMEELTEVITAAEFHPHQCN 81
Cdd:COG5170   156 DEIIAAKPCRVYANAHPYHINSISFNSDKETLLSADDLRINLWNLEIIDGSFNIVDIKPHNMEELTEVITSAEFHPEMCN 235
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779212  82 VFVYSSSKGTIRLCDMRSSALCDRHAKFFEEPEDPSSRSFFSEIISSISDVKFSHSGRYMMTRDYLSVKVWDLNMEGRPV 161
Cdd:COG5170   236 VFMYSSSKGEIKLNDLRQSALCDNSKKLFELTIDGVDVDFFEEIVSSISDFKFSDNGRYILSRDYLTVKIWDVNMAKNPI 315
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779212 162 ETHQVHEYLRSKLCSLYENDCIFDKFECCWNGSDSAIMTGSYNNFFRMFDRNTRRD------VTL-EASRENSKPRASL- 233
Cdd:COG5170   316 KTIPMHCDLMDELNDVYENDAIFDKFEISFSGDDKHVLSGSYSNNFGIYPTDSSGFkdvghvVNLaDGSAEDFKVKCETn 395
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039779212 234 ---KPRKVCTGGKRKKDEIS---------VDSLDFNKKILHTAWHPMESIIAVAATNNLYIF 283
Cdd:COG5170   396 nveKKDKLKNNDWRSVSSSAdgfvvacedPDNLDLLKKILHRSWHPFEDSVAIAATNNLFVF 457
 
Name Accession Description Interval E-value
CDC55 COG5170
Serine/threonine protein phosphatase 2A, regulatory subunit [Signal transduction mechanisms];
2-283 4.88e-115

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


Pssm-ID: 227498 [Multi-domain]  Cd Length: 460  Bit Score: 338.93  E-value: 4.88e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779212   2 DLMVEASPRRIFANAHTYHINSISVNSDHETYLSADDLRINLWHLEITDRSFNIVDIKPANMEELTEVITAAEFHPHQCN 81
Cdd:COG5170   156 DEIIAAKPCRVYANAHPYHINSISFNSDKETLLSADDLRINLWNLEIIDGSFNIVDIKPHNMEELTEVITSAEFHPEMCN 235
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779212  82 VFVYSSSKGTIRLCDMRSSALCDRHAKFFEEPEDPSSRSFFSEIISSISDVKFSHSGRYMMTRDYLSVKVWDLNMEGRPV 161
Cdd:COG5170   236 VFMYSSSKGEIKLNDLRQSALCDNSKKLFELTIDGVDVDFFEEIVSSISDFKFSDNGRYILSRDYLTVKIWDVNMAKNPI 315
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779212 162 ETHQVHEYLRSKLCSLYENDCIFDKFECCWNGSDSAIMTGSYNNFFRMFDRNTRRD------VTL-EASRENSKPRASL- 233
Cdd:COG5170   316 KTIPMHCDLMDELNDVYENDAIFDKFEISFSGDDKHVLSGSYSNNFGIYPTDSSGFkdvghvVNLaDGSAEDFKVKCETn 395
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039779212 234 ---KPRKVCTGGKRKKDEIS---------VDSLDFNKKILHTAWHPMESIIAVAATNNLYIF 283
Cdd:COG5170   396 nveKKDKLKNNDWRSVSSSAdgfvvacedPDNLDLLKKILHRSWHPFEDSVAIAATNNLFVF 457
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
17-211 6.47e-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: 43.48  E-value: 6.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779212  17 HTYHINSISVNSDHeTYLSA--DDLRINLWHLEITDRSFNIVDIkpanmeelTEVITAAEFHPhqCNVFVYSSSK-GTIR 93
Cdd:cd00200    92 HTSYVSSVAFSPDG-RILSSssRDKTIKVWDVETGKCLTTLRGH--------TDWVNSVAFSP--DGTFVASSSQdGTIK 160
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779212  94 LCDMRSSalcdRHAKFFEEPEDPssrsffseiissISDVKFSHSGRYMMT--RDYlSVKVWDLNMeGRPVETHQVHEY-- 169
Cdd:cd00200   161 LWDLRTG----KCVATLTGHTGE------------VNSVAFSPDGEKLLSssSDG-TIKLWDLST-GKCLGTLRGHENgv 222
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039779212 170 ------LRSKLCSLYEND---CIFD--KFEC--------------CWNGSDSAIMTGSYNNFFRMFD 211
Cdd:cd00200   223 nsvafsPDGYLLASGSEDgtiRVWDlrTGECvqtlsghtnsvtslAWSPDGKRLASGSADGTIRIWD 289
 
Name Accession Description Interval E-value
CDC55 COG5170
Serine/threonine protein phosphatase 2A, regulatory subunit [Signal transduction mechanisms];
2-283 4.88e-115

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


Pssm-ID: 227498 [Multi-domain]  Cd Length: 460  Bit Score: 338.93  E-value: 4.88e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779212   2 DLMVEASPRRIFANAHTYHINSISVNSDHETYLSADDLRINLWHLEITDRSFNIVDIKPANMEELTEVITAAEFHPHQCN 81
Cdd:COG5170   156 DEIIAAKPCRVYANAHPYHINSISFNSDKETLLSADDLRINLWNLEIIDGSFNIVDIKPHNMEELTEVITSAEFHPEMCN 235
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779212  82 VFVYSSSKGTIRLCDMRSSALCDRHAKFFEEPEDPSSRSFFSEIISSISDVKFSHSGRYMMTRDYLSVKVWDLNMEGRPV 161
Cdd:COG5170   236 VFMYSSSKGEIKLNDLRQSALCDNSKKLFELTIDGVDVDFFEEIVSSISDFKFSDNGRYILSRDYLTVKIWDVNMAKNPI 315
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779212 162 ETHQVHEYLRSKLCSLYENDCIFDKFECCWNGSDSAIMTGSYNNFFRMFDRNTRRD------VTL-EASRENSKPRASL- 233
Cdd:COG5170   316 KTIPMHCDLMDELNDVYENDAIFDKFEISFSGDDKHVLSGSYSNNFGIYPTDSSGFkdvghvVNLaDGSAEDFKVKCETn 395
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039779212 234 ---KPRKVCTGGKRKKDEIS---------VDSLDFNKKILHTAWHPMESIIAVAATNNLYIF 283
Cdd:COG5170   396 nveKKDKLKNNDWRSVSSSAdgfvvacedPDNLDLLKKILHRSWHPFEDSVAIAATNNLFVF 457
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
17-211 6.47e-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: 43.48  E-value: 6.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779212  17 HTYHINSISVNSDHeTYLSA--DDLRINLWHLEITDRSFNIVDIkpanmeelTEVITAAEFHPhqCNVFVYSSSK-GTIR 93
Cdd:cd00200    92 HTSYVSSVAFSPDG-RILSSssRDKTIKVWDVETGKCLTTLRGH--------TDWVNSVAFSP--DGTFVASSSQdGTIK 160
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779212  94 LCDMRSSalcdRHAKFFEEPEDPssrsffseiissISDVKFSHSGRYMMT--RDYlSVKVWDLNMeGRPVETHQVHEY-- 169
Cdd:cd00200   161 LWDLRTG----KCVATLTGHTGE------------VNSVAFSPDGEKLLSssSDG-TIKLWDLST-GKCLGTLRGHENgv 222
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039779212 170 ------LRSKLCSLYEND---CIFD--KFEC--------------CWNGSDSAIMTGSYNNFFRMFD 211
Cdd:cd00200   223 nsvafsPDGYLLASGSEDgtiRVWDlrTGECvqtlsghtnsvtslAWSPDGKRLASGSADGTIRIWD 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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