(data stored in ACNUC6288 zone)

SWISSPROT: Q6BMS0_DEBHA

ID   Q6BMS0_DEBHA            Unreviewed;       795 AA.
AC   Q6BMS0;
DT   16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT   04-NOV-2008, sequence version 2.
DT   11-DEC-2019, entry version 90.
DE   RecName: Full=RNA polymerase II subunit A C-terminal domain phosphatase {ECO:0000256|RuleBase:RU366066};
DE            EC=3.1.3.16 {ECO:0000256|RuleBase:RU366066};
GN   OrderedLocusNames=DEHA2F03102g {ECO:0000313|EMBL:CAG88814.2};
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 /
OS   IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592 {ECO:0000313|EMBL:CAG88814.2, ECO:0000313|Proteomes:UP000000599};
RN   [1] {ECO:0000313|EMBL:CAG88814.2, ECO:0000313|Proteomes:UP000000599}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968
RC   {ECO:0000313|Proteomes:UP000000599};
RX   PubMed=15229592; DOI=10.1038/nature02579;
RG   Genolevures;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.F., Straub M.L.,
RA   Suleau A., Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E.,
RA   Wirth B., Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   Wincker P., Souciet J.L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: This promotes the activity of RNA polymerase II.
CC       {ECO:0000256|RuleBase:RU366066}.
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         Evidence={ECO:0000256|RuleBase:RU366066};
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         Evidence={ECO:0000256|RuleBase:RU366066};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU366066}.
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DR   EMBL; CR382138; CAG88814.2; -; Genomic_DNA.
DR   RefSeq; XP_460501.2; XM_460501.1.
DR   STRING; 4959.XP_460501.2; -.
DR   EnsemblFungi; CAG88814; CAG88814; DEHA2F03102g.
DR   GeneID; 2903902; -.
DR   KEGG; dha:DEHA2F03102g; -.
DR   HOGENOM; HOG000197682; -.
DR   InParanoid; Q6BMS0; -.
DR   KO; K15732; -.
DR   OMA; NYAHMIA; -.
DR   OrthoDB; 683531at2759; -.
DR   Proteomes; UP000000599; Chromosome F.
DR   GO; GO:0005634; C:nucleus; IEA:InterPro.
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; PF00533; BRCT; 1.
DR   Pfam; PF03031; NIF; 1.
DR   SMART; SM00292; BRCT; 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   4: Predicted;
DR   PRODOM; Q6BMS0.
DR   SWISS-2DPAGE; Q6BMS0.
KW   Hydrolase {ECO:0000256|RuleBase:RU366066};
KW   Nucleus {ECO:0000256|RuleBase:RU366066};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000599}.
FT   DOMAIN          161..348
FT                   /note="FCP1 homology"
FT                   /evidence="ECO:0000259|PROSITE:PS50969"
FT   DOMAIN          529..631
FT                   /note="BRCT"
FT                   /evidence="ECO:0000259|PROSITE:PS50172"
FT   REGION          363..411
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          451..485
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          694..730
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          757..777
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        368..394
FT                   /note="Acidic"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        469..485
FT                   /note="Acidic"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        694..719
FT                   /note="Acidic"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   795 AA;  90095 MW;  CB66AEAC857D5AC4 CRC64;
     MAELTSITLP QSVPFPVTIS SILCRQGETV PKHQTLFKYK YWDYQDDPNS KEETPPKIRV
     ERIGTYESPI EGEVNSINVC LSDEIAHSGV ELCFIKEPCA HAVQYGGLCA LCGKAVEDEK
     DYSGYNYEDR ATISMSHDNT GLKISLDEAT KIEHNTTDRL SREKKLILVV DLDQTVIHAT
     VDPTVGEWQS DPSNPNYPAV KNVRSFCLEE DPIAPPGWTG PKLPPSKCWY YVKLRPGLEE
     FLRSASDLYE MHIYTMATRN YALAIAKIID PEGEYFGDRI LSRDESGSLT HKNLKRLFPV
     DQSMVVIIDD RGDVWQWENN LIKVVPYDFF VGIGDINSSF LPKKFGQLTG PTKKRKSIAK
     LEALENEKNS TDDEESEANE NDKEASEEDD NPSQENDTPS SSPVDRILEM GGGEDNASLL
     MEQSISRNMS LEQQQHDRPL AKLQHDLDKI HEHDSHSPSG SSSPEESDGD KKEEEDEEED
     NLLYDDDNEL YSLKKALVRI HSEYYKILAA NKIKSPHLKP DLTHIIPFLK SKCLEGITIL
     FSGILPLGIN LDTADIVIWC KQFGVKVVNE VYPEVTHVVC RDPNANSFKS GPTFKVRVAK
     KILPNVKIVN PDWLFACLSA WGKVDETDYL VESEEDNWYL EDKDLKKYQK GLESQKQKQI
     NTIESRPRFD SIGSVEEYDL DNANQEVDDF LAGISEDDNS EKDDDDNDND DDNNDNEDTD
     NDKAEVSKPF DSFIKDAYKV NKKRSLEADE DIILQQEVTS KKQKTQQAEP ESEVDLDELE
     KELLDGFDDM EEANV
//

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