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Conserved domains on  [gi|29558099|ref|NP_808908|]
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protein phosphatase 1B isoform 3 [Homo sapiens]

Protein Classification

PP2C_C domain-containing protein( domain architecture ID 10544878)

PP2C_C domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PP2C_C pfam07830
Protein serine/threonine phosphatase 2C, C-terminal domain; Protein phosphatase 2C (PP2C) is ...
 2-81 2.89e-40

Protein serine/threonine phosphatase 2C, C-terminal domain; Protein phosphatase 2C (PP2C) is involved in regulating cellular responses to stress in various eukaryotes. It consists of two domains: an N-terminal catalytic domain and a C-terminal domain characteriztic of mammalian PP2Cs. This domain consists of three antiparallel alpha helices, one of which packs against two corresponding alpha-helices of the N-terminal domain. The C-terminal domain does not seem to play a role in catalysis, but it may provide protein substrate specificity due to the cleft that is created between it and the catalytic domain.


:

Pssm-ID: 429684  Cd Length: 79  Bit Score: 131.48  E-value: 2.89e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29558099     2 SIVLVCFSNAPKVSDEAVKKDSELDKHLESRVEEIMEKSgEEGMPDLAHVMRILSAENIPNLPPGGGLAGKRNVIEAVYS 81
Cdd:pfam07830   1 SIVLVCFPGAPKVSEEAVKKEAELDKKLEKRVKEIIEQS-DGEEPDLLYVLRVLASEDIPGLPPGGGLASKRSVIEAVYK 79
 
Name Accession Description Interval E-value
PP2C_C pfam07830
Protein serine/threonine phosphatase 2C, C-terminal domain; Protein phosphatase 2C (PP2C) is ...
 2-81 2.89e-40

Protein serine/threonine phosphatase 2C, C-terminal domain; Protein phosphatase 2C (PP2C) is involved in regulating cellular responses to stress in various eukaryotes. It consists of two domains: an N-terminal catalytic domain and a C-terminal domain characteriztic of mammalian PP2Cs. This domain consists of three antiparallel alpha helices, one of which packs against two corresponding alpha-helices of the N-terminal domain. The C-terminal domain does not seem to play a role in catalysis, but it may provide protein substrate specificity due to the cleft that is created between it and the catalytic domain.


Pssm-ID: 429684  Cd Length: 79  Bit Score: 131.48  E-value: 2.89e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29558099     2 SIVLVCFSNAPKVSDEAVKKDSELDKHLESRVEEIMEKSgEEGMPDLAHVMRILSAENIPNLPPGGGLAGKRNVIEAVYS 81
Cdd:pfam07830   1 SIVLVCFPGAPKVSEEAVKKEAELDKKLEKRVKEIIEQS-DGEEPDLLYVLRVLASEDIPGLPPGGGLASKRSVIEAVYK 79
 
Name Accession Description Interval E-value
PP2C_C pfam07830
Protein serine/threonine phosphatase 2C, C-terminal domain; Protein phosphatase 2C (PP2C) is ...
 2-81 2.89e-40

Protein serine/threonine phosphatase 2C, C-terminal domain; Protein phosphatase 2C (PP2C) is involved in regulating cellular responses to stress in various eukaryotes. It consists of two domains: an N-terminal catalytic domain and a C-terminal domain characteriztic of mammalian PP2Cs. This domain consists of three antiparallel alpha helices, one of which packs against two corresponding alpha-helices of the N-terminal domain. The C-terminal domain does not seem to play a role in catalysis, but it may provide protein substrate specificity due to the cleft that is created between it and the catalytic domain.


Pssm-ID: 429684  Cd Length: 79  Bit Score: 131.48  E-value: 2.89e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29558099     2 SIVLVCFSNAPKVSDEAVKKDSELDKHLESRVEEIMEKSgEEGMPDLAHVMRILSAENIPNLPPGGGLAGKRNVIEAVYS 81
Cdd:pfam07830   1 SIVLVCFPGAPKVSEEAVKKEAELDKKLEKRVKEIIEQS-DGEEPDLLYVLRVLASEDIPGLPPGGGLASKRSVIEAVYK 79
 
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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