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Q9P376

- FCP1_SCHPO

UniProt

Q9P376 - FCP1_SCHPO

Protein

RNA polymerase II subunit A C-terminal domain phosphatase

Gene

fcp1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 94 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
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    Functioni

    Processively dephosphorylates 'Ser-2' and 'Ser-5' of the heptad repeats YSPTSPS in the C-terminal domain of the largest RNA polymerase II subunit. This promotes the activity of RNA polymerase II.1 Publication

    Catalytic activityi

    [a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.1 Publication

    Cofactori

    Magnesium or manganese or cobalt.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei170 – 17011 Publication
    Active sitei172 – 17211 Publication

    GO - Molecular functioni

    1. CTD phosphatase activity Source: PomBase
    2. metal ion binding Source: UniProtKB-KW
    3. protein binding Source: PomBase

    GO - Biological processi

    1. cellular protein complex assembly Source: PomBase
    2. cellular response to nitrogen starvation Source: PomBase
    3. negative regulation of G0 to G1 transition Source: PomBase
    4. protein dephosphorylation Source: PomBase
    5. regulation of mitotic cytokinesis Source: PomBase
    6. regulation of transcription from RNA polymerase II promoter Source: PomBase

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Keywords - Ligandi

    Cobalt, Magnesium, Manganese, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_215564. RNA Polymerase II Pre-transcription Events.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    RNA polymerase II subunit A C-terminal domain phosphatase (EC:3.1.3.16)
    Alternative name(s):
    CTD phosphatase fcp1
    Gene namesi
    Name:fcp1
    ORF Names:SPAC19B12.05c
    OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
    Taxonomic identifieri284812 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
    ProteomesiUP000002485: Chromosome I

    Organism-specific databases

    PomBaseiSPAC19B12.05c.

    Subcellular locationi

    Nucleus Curated

    GO - Cellular componenti

    1. nucleus Source: PomBase

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi170 – 1701D → A, N or E: No activity. 1 Publication
    Mutagenesisi172 – 1721D → A, N or E: No activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 723723RNA polymerase II subunit A C-terminal domain phosphatasePRO_0000212567Add
    BLAST

    Proteomic databases

    MaxQBiQ9P376.

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Protein-protein interaction databases

    BioGridi278698. 14 interactions.
    MINTiMINT-1213896.
    STRINGi4896.SPAC19B12.05c-1.

    Structurei

    Secondary structure

    1
    723
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi151 – 16212
    Beta strandi165 – 1695
    Turni172 – 1743
    Beta strandi175 – 1795
    Helixi183 – 1886
    Turni194 – 1963
    Helixi197 – 1993
    Beta strandi203 – 2097
    Turni210 – 2134
    Beta strandi214 – 2229
    Helixi226 – 2349
    Beta strandi237 – 2426
    Helixi247 – 25711
    Beta strandi263 – 2664
    Turni271 – 2733
    Helixi282 – 2843
    Beta strandi293 – 2986
    Helixi301 – 3033
    Beta strandi309 – 3113
    Helixi399 – 4024
    Helixi403 – 41513
    Helixi417 – 42711
    Helixi434 – 4363
    Helixi445 – 47026
    Turni471 – 4733
    Helixi479 – 4879
    Beta strandi495 – 5028
    Turni508 – 5103
    Helixi512 – 5198
    Beta strandi526 – 5305
    Beta strandi533 – 5375
    Helixi543 – 5508
    Beta strandi551 – 5533
    Beta strandi556 – 5583
    Helixi559 – 5679
    Helixi574 – 5774
    Beta strandi578 – 5803

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3EF0X-ray2.10A149-329[»]
    A394-580[»]
    3EF1X-ray2.15A140-580[»]
    ProteinModelPortaliQ9P376.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9P376.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini160 – 341182FCP1 homologyPROSITE-ProRule annotationAdd
    BLAST
    Domaini486 – 57994BRCTPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 BRCT domain.PROSITE-ProRule annotation
    Contains 1 FCP1 homology domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG5190.
    HOGENOMiHOG000197682.
    KOiK15732.
    OMAiPDKKLFG.
    OrthoDBiEOG7TXKSN.
    PhylomeDBiQ9P376.

    Family and domain databases

    Gene3Di3.40.50.1000. 2 hits.
    3.40.50.10190. 1 hit.
    InterProiIPR001357. BRCT_dom.
    IPR011947. FCP1_euk.
    IPR023214. HAD-like_dom.
    IPR004274. NIF.
    [Graphical view]
    PfamiPF03031. NIF. 1 hit.
    PF12738. PTCB-BRCT. 1 hit.
    [Graphical view]
    SMARTiSM00292. BRCT. 1 hit.
    SM00577. CPDc. 1 hit.
    [Graphical view]
    SUPFAMiSSF52113. SSF52113. 1 hit.
    SSF56784. SSF56784. 1 hit.
    TIGRFAMsiTIGR02250. FCP1_euk. 1 hit.
    PROSITEiPS50172. BRCT. 1 hit.
    PS50969. FCP1. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9P376-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSKRLTPIHL PNSLNYPIEI ASCLVPQGSY VKKGTPLLLY RFFTKVKEDQ    50
    EDGSEVYVDR EFVEQFECPV EGELVEWAVK KEESIENFSK IVAKLHEPCT 100
    HEVNYGGLCA ICGKNITSQD YMGYSDMARA NISMTHNTGD LTVSLEEASR 150
    LESENVKRLR QEKRLSLIVD LDQTIIHATV DPTVGEWMSD PGNVNYDVLR 200
    DVRSFNLQEG PSGYTSCYYI KFRPGLAQFL QKISELYELH IYTMGTKAYA 250
    KEVAKIIDPT GKLFQDRVLS RDDSGSLAQK SLRRLFPCDT SMVVVIDDRG 300
    DVWDWNPNLI KVVPYEFFVG IGDINSNFLA KSTPLPEQEQ LIPLEIPKDE 350
    PDSVDEINEE NEETPEYDSS NSSYAQDSST IPEKTLLKDT FLQNREALEE 400
    QNKERVTALE LQKSERPLAK QQNALLEDEG KPTPSHTLLH NRDHELERLE 450
    KVLKDIHAVY YEEENDISSR SGNHKHANVG LIIPKMKQKV LKGCRLLFSG 500
    VIPLGVDVLS SDIAKWAMSF GAEVVLDFSV PPTHLIAAKI RTEKVKKAVS 550
    MGNIKVVKLN WLTESLSQWK RLPESDYLLY PSYDLPDRNL SEHSYSSSSD 600
    DEQRISELND RELDEIDWQA ADQDVENALK DLSDDNDFDT GSISASQSQP 650
    EALEVNTPIK RKADLIQPSY NYDGEKRRKE NDNHEGYDLL PNSSTKGEES 700
    AENENELDDL ADIMEAELSK DTA 723
    Length:723
    Mass (Da):81,965
    Last modified:October 1, 2000 - v1
    Checksum:iA127A06CD2FD3435
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CU329670 Genomic DNA. Translation: CAC00553.1.
    RefSeqiNP_594768.1. NM_001020195.2.

    Genome annotation databases

    EnsemblFungiiSPAC19B12.05c.1; SPAC19B12.05c.1:pep; SPAC19B12.05c.
    GeneIDi2542225.
    KEGGispo:SPAC19B12.05c.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CU329670 Genomic DNA. Translation: CAC00553.1 .
    RefSeqi NP_594768.1. NM_001020195.2.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3EF0 X-ray 2.10 A 149-329 [» ]
    A 394-580 [» ]
    3EF1 X-ray 2.15 A 140-580 [» ]
    ProteinModelPortali Q9P376.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 278698. 14 interactions.
    MINTi MINT-1213896.
    STRINGi 4896.SPAC19B12.05c-1.

    Proteomic databases

    MaxQBi Q9P376.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii SPAC19B12.05c.1 ; SPAC19B12.05c.1:pep ; SPAC19B12.05c .
    GeneIDi 2542225.
    KEGGi spo:SPAC19B12.05c.

    Organism-specific databases

    PomBasei SPAC19B12.05c.

    Phylogenomic databases

    eggNOGi COG5190.
    HOGENOMi HOG000197682.
    KOi K15732.
    OMAi PDKKLFG.
    OrthoDBi EOG7TXKSN.
    PhylomeDBi Q9P376.

    Enzyme and pathway databases

    Reactomei REACT_215564. RNA Polymerase II Pre-transcription Events.

    Miscellaneous databases

    EvolutionaryTracei Q9P376.
    NextBioi 20803293.
    PROi Q9P376.

    Family and domain databases

    Gene3Di 3.40.50.1000. 2 hits.
    3.40.50.10190. 1 hit.
    InterProi IPR001357. BRCT_dom.
    IPR011947. FCP1_euk.
    IPR023214. HAD-like_dom.
    IPR004274. NIF.
    [Graphical view ]
    Pfami PF03031. NIF. 1 hit.
    PF12738. PTCB-BRCT. 1 hit.
    [Graphical view ]
    SMARTi SM00292. BRCT. 1 hit.
    SM00577. CPDc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52113. SSF52113. 1 hit.
    SSF56784. SSF56784. 1 hit.
    TIGRFAMsi TIGR02250. FCP1_euk. 1 hit.
    PROSITEi PS50172. BRCT. 1 hit.
    PS50969. FCP1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The genome sequence of Schizosaccharomyces pombe."
      Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
      , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
      Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 972 / ATCC 24843.
    2. "Characterization of the CTD phosphatase Fcp1 from fission yeast. Preferential dephosphorylation of serine 2 versus serine 5."
      Hausmann S., Shuman S.
      J. Biol. Chem. 277:21213-21220(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, COFACTOR, SUBUNIT, CATALYTIC ACTIVITY, ACTIVE SITE, MUTAGENESIS OF ASP-170 AND ASP-172.

    Entry informationi

    Entry nameiFCP1_SCHPO
    AccessioniPrimary (citable) accession number: Q9P376
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 6, 2002
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 94 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. Schizosaccharomyces pombe
      Schizosaccharomyces pombe: entries and gene names
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3