ID A0A1Y2LN79_EPING Unreviewed; 803 AA.
AC A0A1Y2LN79;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=B5807_11097 {ECO:0000313|EMBL:OSS44348.1};
OS Epicoccum nigrum (Soil fungus) (Epicoccum purpurascens).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Didymellaceae; Epicoccum.
OX NCBI_TaxID=105696 {ECO:0000313|EMBL:OSS44348.1, ECO:0000313|Proteomes:UP000193240};
RN [1] {ECO:0000313|EMBL:OSS44348.1, ECO:0000313|Proteomes:UP000193240}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ICMP 19927 {ECO:0000313|EMBL:OSS44348.1,
RC ECO:0000313|Proteomes:UP000193240};
RA Fokin M., Fleetwood D., Weir B.S., Villas-Boas S.G.;
RT "Genome sequence of the saprophytic ascomycete Epicoccum nigrum ICMP 19927
RT strain isolated from New Zealand.";
RL Genome Announc. 0:0-0(2017).
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}.
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DR EMBL; KZ107858; OSS44348.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2LN79; -.
DR STRING; 105696.A0A1Y2LN79; -.
DR InParanoid; A0A1Y2LN79; -.
DR OMA; DQTVIHC; -.
DR OrthoDB; 73422at2759; -.
DR Proteomes; UP000193240; 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; SM00292; BRCT; 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:UP000193240}.
FT DOMAIN 156..333
FT /note="FCP1 homology"
FT /evidence="ECO:0000259|PROSITE:PS50969"
FT DOMAIN 519..613
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 353..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 414..455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 615..641
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 667..783
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 417..431
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 669..688
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 709..723
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 737..752
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 803 AA; 89514 MW; ACEF8F30EFFFC7C5 CRC64;
MKITSPPSLH YPVTVFELLK KPNDDVKRSE RLFTYSYKSM VTETDRNDIE HRVSRTFTTH
FHASTEGTIS RWHIKAGTVL TRPGTDIIEI EEPCTHEIQF GGLCADCGQD MTKVDHLTEV
RDTDRATVNM THDNVALLIS HDEALRGEEE TKRRLLGSSK LTLIVDLDQT VIHTTCERTI
AEWKADPENP NHDAVKDVEG FQLDDDNVSN VAANWYYVKM RPGLKDFFDR VSTKYEMHVY
TMATRAYAQA VCRIIDPERK YFGDRILSRD ENYTDKLKSL QRLFYHNTSM VVIIDDRADV
WQYSPHLIRV PVFNFFPGAG DINASFLPKQ QELVTQSKPI AAPVKKIADD SATTADADKA
APTTAVESAS GVGEALEQQL LSMASPETID EQTKEQEKVI IAQQTERPLL QQQLMQDKAD
EEAEAEAEAK ASEEPVATNG NSEHSEPPKH RHSILHDDDR GLDVIEQNLN RVHSAFYEQY
RTSKAVRPAG RVAALKGERS PKKRPSDSIP DVAELMPAIK EQVLRDTVVV FSGIIPLGVD
VQTSDFALWI KSFGAEVSTS VNRRTTHVIA NPDRKTTKVK RAARYDNVKI VNPEWMFQSC
SRWERVDETP YLIEVDPAER GTSPLEDDSL NASDEDEVDD VADDPVALNL TADNWESVDD
ELAEFMQGDD DTDSEHPSES DSERSDDSTA STSSRGQKKR KRTNGNTTDG SEADESDTSV
TSTSRLQRRK KRTMERVTSL TTVLTAEKSS GLPTPEATGP EALPAGEAKE GPEDNGVAPD
LAEDNDAALE AELLAGFDSS DGE
//
