ID   FCP1_ENCCU              Reviewed;         411 AA.
AC   Q8SV03;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=RNA polymerase II subunit A C-terminal domain phosphatase;
DE            EC=3.1.3.16;
DE   AltName: Full=CTD phosphatase FCP1;
GN   Name=FCP1; OrderedLocusNames=ECU07_0890;
OS   Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC   Encephalitozoon.
OX   NCBI_TaxID=284813;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GB-M1;
RX   PubMed=11719806; DOI=10.1038/35106579;
RA   Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA   Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA   Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA   Vivares C.P.;
RT   "Genome sequence and gene compaction of the eukaryote parasite
RT   Encephalitozoon cuniculi.";
RL   Nature 414:450-453(2001).
RN   [2]
RP   FUNCTION, AND SUBUNIT.
RX   PubMed=15170348; DOI=10.1021/bi0499617;
RA   Hausmann S., Schwer B., Shuman S.;
RT   "An Encephalitozoon cuniculi ortholog of the RNA polymerase II carboxyl-
RT   terminal domain (CTD) serine phosphatase Fcp1.";
RL   Biochemistry 43:7111-7120(2004).
CC   -!- FUNCTION: Processively dephosphorylates 'Ser-2' and 'Ser-5' of the
CC       heptad repeats YSPTSPS in the C-terminal domain of the largest RNA
CC       polymerase II subunit (RPB1). This promotes the activity of RNA
CC       polymerase II. {ECO:0000269|PubMed:15170348}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:83421; EC=3.1.3.16;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC         COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:61977; EC=3.1.3.16;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000250};
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:15170348}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
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DR   EMBL; AL590447; CAD25621.1; -; Genomic_DNA.
DR   RefSeq; NP_586017.1; NM_001041639.1.
DR   AlphaFoldDB; Q8SV03; -.
DR   SMR; Q8SV03; -.
DR   STRING; 284813.Q8SV03; -.
DR   GeneID; 859447; -.
DR   KEGG; ecu:ECU07_0890; -.
DR   VEuPathDB; MicrosporidiaDB:ECU07_0890; -.
DR   HOGENOM; CLU_007683_2_0_1; -.
DR   InParanoid; Q8SV03; -.
DR   OrthoDB; 683531at2759; -.
DR   Proteomes; UP000000819; Chromosome VII.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008420; F:RNA polymerase II CTD heptapeptide repeat phosphatase activity; IEA:InterPro.
DR   GO; GO:0070940; P:dephosphorylation of RNA polymerase II C-terminal domain; IEA:InterPro.
DR   Gene3D; 3.40.50.1000; -; 1.
DR   Gene3D; 3.40.50.10190; -; 1.
DR   InterPro; IPR001357; BRCT_dom.
DR   InterPro; IPR036420; BRCT_dom_sf.
DR   InterPro; IPR039189; Fcp1.
DR   InterPro; IPR004274; FCP1_dom.
DR   InterPro; IPR011947; FCP1_euk.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR023214; HAD_sf.
DR   PANTHER; PTHR23081; PTHR23081; 1.
DR   Pfam; PF16589; BRCT_2; 1.
DR   Pfam; PF03031; NIF; 1.
DR   SMART; SM00577; CPDc; 1.
DR   SUPFAM; SSF52113; SSF52113; 1.
DR   SUPFAM; SSF56784; SSF56784; 1.
DR   TIGRFAMs; TIGR02250; FCP1_euk; 1.
DR   PROSITE; PS50172; BRCT; 1.
DR   PROSITE; PS50969; FCP1; 1.
PE   1: Evidence at protein level;
KW   Cobalt; Hydrolase; Magnesium; Manganese; Metal-binding; Nucleus;
KW   Protein phosphatase; Reference proteome.
FT   CHAIN           1..411
FT                   /note="RNA polymerase II subunit A C-terminal domain
FT                   phosphatase"
FT                   /id="PRO_0000212566"
FT   DOMAIN          56..212
FT                   /note="FCP1 homology"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00336"
FT   DOMAIN          309..393
FT                   /note="BRCT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT   ACT_SITE        66
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        68
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   411 AA;  47791 MW;  030806FD1C2C6221 CRC64;
     MGGCNHPIRL GTLCGVCGME IQEESHLFCA LYNTDNVKIT HEEAVAIHKE KMEALEMQMK
     LILVLDLDQT VLHTTYGTSS LEGTVKFVID RCRYCVKLRP NLDYMLRRIS KLYEIHVYTM
     GTRAYAERIV EIIDPSGKYF DDRIITRDEN QGVLVKRLSR LFPHDHRNIV ILDDRPDVWD
     YCENLVLIRP FWYFNRVDIN DPLRLKRKIE KEAGENKALE EFVSKRKKIE DIRNPEIASR
     LDDMVLESSC GSEGVEDDSR STEEKEVSEV QSVASGDSEL LKVAGFLRKV HRKYFASKQR
     NVKRILRKIR RRVFGGDRFF VAEIANRAWL VKTIEMYGGI VGIPESGVDF VVSSCEREAE
     YLAQKFECLA VSPKWIADCV YSLKRVEYGK YVVCDHRTKD EYEEELERLF T