Difference between revisions of "Phosphatase Subfamily FCP1"
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[[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Fold_HAD|Fold HAD]]: [[Phosphatase_Superfamily_HAD|Superfamily HAD]]: [[Phosphatase_Family_FCP|Family FCP]]: [[Phosphatase_Subfamily_FCP1|Subfamily FCP1]] | [[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Fold_HAD|Fold HAD]]: [[Phosphatase_Superfamily_HAD|Superfamily HAD]]: [[Phosphatase_Family_FCP|Family FCP]]: [[Phosphatase_Subfamily_FCP1|Subfamily FCP1]] | ||
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===Domain Structure=== | ===Domain Structure=== | ||
| − | In additional to the catalytic domain, it has a breast cancer protein-related carboxy-terminal (BRCT) domain and a C-terminal region (FCP1_C) that binds regulatory TFIIF. | + | In additional to the catalytic domain, it has a breast cancer protein-related carboxy-terminal (BRCT) domain and a C-terminal region (FCP1_C) that binds regulatory TFIIF. Profile models for this domain fail to find it in nematodes or insects, but HHsearch or multiple alignments with Drosophila and C. elegans proteins show several subregions aligned with human and other FCP1, indicating that the domain is conserved in these species. |
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===Functions=== | ===Functions=== | ||
FCP1 preferentially hydrolyzes Ser2 in CTD repeats in budding yeast <cite> Kamenski04 </cite> and fission yeast <cite> Schwer15 </cite>. | FCP1 preferentially hydrolyzes Ser2 in CTD repeats in budding yeast <cite> Kamenski04 </cite> and fission yeast <cite> Schwer15 </cite>. | ||
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See [[CTD_Phosphorylation|Phosphorylation of RNA polymerase II C-terminal domain]]. | See [[CTD_Phosphorylation|Phosphorylation of RNA polymerase II C-terminal domain]]. | ||
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#Schwer15 pmid=25883047 | #Schwer15 pmid=25883047 | ||
</biblio> | </biblio> | ||
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Latest revision as of 21:45, 3 April 2017
Phosphatase Classification: Fold HAD: Superfamily HAD: Family FCP: Subfamily FCP1
F-cell production 1 (FCP1) also called TFIIF-stimulated CTD phosphatase 1 (CTDP1), prefers to dephosphorylate pSer2 of heptapeptide repeats at CTD of RNA polymerase II. The molecular function is mainly studied in yeast [1].
Evolution
FCP1 is conserved from yeast to human, usually one copy per genome.
Domain Structure
In additional to the catalytic domain, it has a breast cancer protein-related carboxy-terminal (BRCT) domain and a C-terminal region (FCP1_C) that binds regulatory TFIIF. Profile models for this domain fail to find it in nematodes or insects, but HHsearch or multiple alignments with Drosophila and C. elegans proteins show several subregions aligned with human and other FCP1, indicating that the domain is conserved in these species.
Functions
FCP1 preferentially hydrolyzes Ser2 in CTD repeats in budding yeast [1] and fission yeast [2].
See Phosphorylation of RNA polymerase II C-terminal domain.
References
- Kamenski T, Heilmeier S, Meinhart A, and Cramer P. Structure and mechanism of RNA polymerase II CTD phosphatases. Mol Cell. 2004 Aug 13;15(3):399-407. DOI:10.1016/j.molcel.2004.06.035 |
- Schwer B, Ghosh A, Sanchez AM, Lima CD, and Shuman S. Genetic and structural analysis of the essential fission yeast RNA polymerase II CTD phosphatase Fcp1. RNA. 2015 Jun;21(6):1135-46. DOI:10.1261/rna.050286.115 |
- Hsin JP, Xiang K, and Manley JL. Function and control of RNA polymerase II C-terminal domain phosphorylation in vertebrate transcription and RNA processing. Mol Cell Biol. 2014 Jul;34(13):2488-98. DOI:10.1128/MCB.00181-14 |
