ID A0A367XZ03_9ASCO Unreviewed; 816 AA.
AC A0A367XZ03;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
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 Name=FCP1_1 {ECO:0000313|EMBL:RCK58042.1};
GN ORFNames=Cantr_06061 {ECO:0000313|EMBL:RCK58042.1};
OS Candida viswanathii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=5486 {ECO:0000313|EMBL:RCK58042.1, ECO:0000313|Proteomes:UP000253472};
RN [1] {ECO:0000313|EMBL:RCK58042.1, ECO:0000313|Proteomes:UP000253472}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 20962 {ECO:0000313|EMBL:RCK58042.1,
RC ECO:0000313|Proteomes:UP000253472};
RA Ahn J.;
RT "Whole genome sequencing of Candida tropicalis (genome annotated by CSBL at
RT Korea University).";
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RCK58042.1}.
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DR EMBL; QLNQ01000028; RCK58042.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A367XZ03; -.
DR STRING; 5486.A0A367XZ03; -.
DR Proteomes; UP000253472; 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; 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:UP000253472}.
FT DOMAIN 161..348
FT /note="FCP1 homology"
FT /evidence="ECO:0000259|PROSITE:PS50969"
FT DOMAIN 535..635
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 370..420
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 468..495
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 692..797
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 370..393
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 468..482
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 692..710
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 782..797
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 816 AA; 91433 MW; A9F78DA30092D9EC CRC64;
MSESTPIKLP SSAPFPVVVS AILCKPGETV SKHKTIFNYK YWDYQDDPSS TADPPKKIRV
ERLGTFESPI EGQIDKINIS PQDEITHNGI ELMFIKEACP HTVQYGGLCA LCGKSLEEEK
DYSGYNYEDR ATIEMSHDST GLKISYDEAA KIEHSTTDRL IEEKRLILVV DLDQTVIHAT
VDPTVGEWQL DPSNPNYGAV KDVKSFCLEE EPIVPPGWTG PKLAPTKCTY YVKLRPGLLE
FLKRMSEKYE MHIYTMATRN YALAIAKIID PDGKYFGDRI LSRDESGSLT HKNLKRLFPV
DQSMVAIIDD RGDVWQWESN LIKVVPYDFF VGIGDINSSF LPKKNGQLTG PTKKRKTIAK
LEAAAELSKE GEIIDEQGEI ESVTPETERE GEESGSGGSS SIGGSDDDDD AHSDVSTSSP
VERILELGGG EGNTTLLLDQ SLARNQSIEQ QQQDRPLAKL QHDLEQLHEH RHDGTDSKSE
SGASEDESDD DDNLLLDDDN ELVALDKVLV NIHSEYYKRY SKENKPDLTE IIPNMKSRVL
EGITVLFSGI IPLGINLDSA DIVIWCKQFG VKVVNEVYPD VTHVICRDVS EDVGPTFKAR
VARKLYPDTV KIVNPDWLFA CLSNWTIVDE KEYLVSTDNP KLWKVQDPEV DKYKRLVEEK
SNMAEATHID SIESFDEYDL DEANQEVDDF LAGLSDDDDD DEDDDENENA AAANDLGSPN
GVNYAEDDED NGNKVEDDEE KEEEASTTNG HDSFIKNLYS NKKRPLELDE DEDEGDDADA
ESNGESASKK QKVEMDEEFL DDLEKELLDG FDDLEE
//
