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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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. | ||
| − | The FCP1_C | + | The FCP1_C domain is found widely in deuterosomes (from sea urchin to chordates). It is absent from most proteostomes, except some individual organisms. It is present in basal eumetazoan Nematostella. It is probably FCP1_C domain was gained in eumetazoa, but was lost in multiple independent events. See technical notes. |
===Functions=== | ===Functions=== | ||
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=== Links === | === Links === | ||
[http://www.ncbi.nlm.nih.gov/gene/2221 Human FCP1] from NCBI Gene | [http://www.ncbi.nlm.nih.gov/gene/2221 Human FCP1] from NCBI Gene | ||
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| + | === Technical notes === | ||
| + | ==== FCP1_C domain ==== | ||
| + | In order to find FCP1_C domain phylogenetic distribution among FCP1, we obtained the FCP1 from our [http://resdev.gene.com/gOrtholog/view/cluster/MC0001572/overview internal orthology database], which contains 227 from 183 eukaryotic genomes. We then searched the FCP1_C domain by Pfam web server. | ||
Revision as of 18:33, 26 June 2015
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.
The FCP1_C domain is found widely in deuterosomes (from sea urchin to chordates). It is absent from most proteostomes, except some individual organisms. It is present in basal eumetazoan Nematostella. It is probably FCP1_C domain was gained in eumetazoa, but was lost in multiple independent events. See technical notes.
Functions
FCP1 preferentially hydrolyzes Ser2 in CTD repeats in budding yeast [1] and fission yeast [2].
Substrates and Related Kinases
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 |
Links
Human FCP1 from NCBI Gene
Technical notes
FCP1_C domain
In order to find FCP1_C domain phylogenetic distribution among FCP1, we obtained the FCP1 from our internal orthology database, which contains 227 from 183 eukaryotic genomes. We then searched the FCP1_C domain by Pfam web server.
