ID G3ARZ1_SPAPN Unreviewed; 770 AA.
AC G3ARZ1;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 61.
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 ORFNames=SPAPADRAFT_140004 {ECO:0000313|EMBL:EGW31840.1};
OS Spathaspora passalidarum (strain NRRL Y-27907 / 11-Y1).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Spathaspora.
OX NCBI_TaxID=619300 {ECO:0000313|Proteomes:UP000000709};
RN [1] {ECO:0000313|EMBL:EGW31840.1, ECO:0000313|Proteomes:UP000000709}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL Y-27907 / 11-Y1 {ECO:0000313|Proteomes:UP000000709};
RX PubMed=21788494; DOI=10.1073/pnas.1103039108;
RA Wohlbach D.J., Kuo A., Sato T.K., Potts K.M., Salamov A.A., LaButti K.M.,
RA Sun H., Clum A., Pangilinan J.L., Lindquist E.A., Lucas S., Lapidus A.,
RA Jin M., Gunawan C., Balan V., Dale B.E., Jeffries T.W., Zinkel R.,
RA Barry K.W., Grigoriev I.V., Gasch A.P.;
RT "Comparative genomics of xylose-fermenting fungi for enhanced biofuel
RT production.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:13212-13217(2011).
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|ARBA:ARBA00001512,
CC 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|ARBA:ARBA00001482,
CC ECO:0000256|RuleBase:RU366066};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|RuleBase:RU366066}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GL996503; EGW31840.1; -; Genomic_DNA.
DR RefSeq; XP_007376618.1; XM_007376556.1.
DR AlphaFoldDB; G3ARZ1; -.
DR STRING; 619300.G3ARZ1; -.
DR GeneID; 18870262; -.
DR KEGG; spaa:SPAPADRAFT_140004; -.
DR eggNOG; KOG0323; Eukaryota.
DR HOGENOM; CLU_007683_0_0_1; -.
DR InParanoid; G3ARZ1; -.
DR OMA; DQTVIHC; -.
DR OrthoDB; 73422at2759; -.
DR Proteomes; UP000000709; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:UniProtKB-UniRule.
DR CDD; cd17729; BRCT_CTDP1; 1.
DR CDD; cd07521; HAD_FCP1-like; 1.
DR Gene3D; 3.40.50.10190; BRCT domain; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR Gene3D; 1.10.287.10; S15/NS1, RNA-binding; 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 NCBIfam; TIGR02250; FCP1_euk; 1.
DR PANTHER; PTHR23081; RNA POLYMERASE II CTD PHOSPHATASE; 1.
DR PANTHER; PTHR23081:SF36; RNA POLYMERASE II SUBUNIT A C-TERMINAL DOMAIN PHOSPHATASE; 1.
DR Pfam; PF00533; BRCT; 1.
DR Pfam; PF03031; NIF; 1.
DR SMART; SM00577; CPDc; 1.
DR SUPFAM; SSF52113; BRCT domain; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR PROSITE; PS50172; BRCT; 1.
DR PROSITE; PS50969; FCP1; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU366066};
KW Nucleus {ECO:0000256|RuleBase:RU366066};
KW Reference proteome {ECO:0000313|Proteomes:UP000000709}.
FT DOMAIN 168..355
FT /note="FCP1 homology"
FT /evidence="ECO:0000259|PROSITE:PS50969"
FT DOMAIN 517..617
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 354..402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 455..475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 681..752
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 681..704
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 720..746
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 770 AA; 87217 MW; 6BF28ED6A2F17D36 CRC64;
MSEFNESSSP LTPIRLPTSA PFPVIISSIL INEGDSVEKH KTIFKYKYWD YQDDPKSTEE
PPKKVRVERI GTFESPVTGE IDKININILD TVTDSSVEIC TIKEPCTHTV QYGGLCALCG
KSLEDERDYS GYNYEDRATI SMAHDNTGLR ISLDEATKIE QSTTDRLTEE KKLILVVDLD
QTVIHATVDP TVGEWQSDPS NPNYPAVKDV KSFCLEEDPI TPPNWTGPKL APTKCWYYVK
VRPGLAEFLE QVSNKYEMHI YTMATRNYAL AIANIIDPEG KYFGDRILSR DESGSLTHKN
LKRLFPVDQS MVVIIDDRGD VWQWESNLIK VVPYDFFVGI GDINSSFLPK KNGQITGPTK
KRKSIAKLEA QQAGPVASET EEDVLSEVDY SENNTPATTT PLTSSPVERI LELGGGEDNA
NLLLEQSISR NQSIEQQQHD RPLAKLQHDL EALHQQHHHE ENNINEVEDE ESEDENLLYD
DDNELNSLNK VLANIHDAYY KQANSSKPDL TEIIPSLKSK CLEGITLLFS GIIPLGVPLD
SADIVIWAKQ FGVKVVNEVY PEVTHVICRD ITPESGPTFK ARAAHHLYPD TIKIVNPDWL
FACLSTWSRV DETEYLLSTT NAKTWLVNNK DVEKYQKMLE ENRERELNLM DMSRFDDIES
FEEYDLDEAN QEVDDFLAGL SEDEDDGEGF NDQEEDEEKA DSEEPEVNES NGSGHDTFIQ
EAYSKKRALG DDEPTPIKKL KQDISPEDDL EELEQELEQE LLEGFDDLEE
//
