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Database: UniProt
Entry: A0A0R3WFU9_TAEAS
LinkDB: A0A0R3WFU9_TAEAS
Original site: A0A0R3WFU9_TAEAS 
ID   A0A0R3WFU9_TAEAS        Unreviewed;       694 AA.
AC   A0A0R3WFU9;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 31.
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=TASK_LOCUS9743 {ECO:0000313|EMBL:VDK45224.1};
OS   Taenia asiatica (Asian tapeworm).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC   Eucestoda; Cyclophyllidea; Taeniidae; Taenia.
OX   NCBI_TaxID=60517 {ECO:0000313|Proteomes:UP000046400, ECO:0000313|WBParaSite:TASK_0000974201-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:TASK_0000974201-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDK45224.1, ECO:0000313|Proteomes:UP000282613}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Pathogen Informatics;
RL   Submitted (NOV-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}.
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DR   EMBL; UYRS01019424; VDK45224.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0R3WFU9; -.
DR   STRING; 60517.A0A0R3WFU9; -.
DR   WBParaSite; TASK_0000974201-mRNA-1; TASK_0000974201-mRNA-1; TASK_0000974201.
DR   Proteomes; UP000046400; Unplaced.
DR   Proteomes; UP000282613; 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   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:UP000282613}.
FT   DOMAIN          114..278
FT                   /note="FCP1 homology"
FT                   /evidence="ECO:0000259|PROSITE:PS50969"
FT   DOMAIN          576..634
FT                   /note="BRCT"
FT                   /evidence="ECO:0000259|PROSITE:PS50172"
FT   REGION          267..438
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        285..315
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        324..370
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        371..401
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   694 AA;  77885 MW;  DC5757A078AD9167 CRC64;
     MNVPDQIVKV PEHCESVKVV KVKVKKRQAV TPSTVVCTLE VPGHPKMNIN GPGYGKVTML
     CQEGCTLGPK EGGVCGERIA AASASIPMVH MIPDLHVSES VAAEIALKDE ESLLTARKLA
     LLIDLDQTVL HTTTTPHAFR YKNVHRFNLA GCEMMYHTRF RPHLGKFLRR MVKRFQMHIC
     TFGNRAYAHQ LASILDPKRK YFCQRILSRD ECFNPVTKSA NLRALFPRGV HLVCIIDDRG
     DVWDWSPNLI QVQPYRFFPE VGDINGPPGR PLSMMPMPDF RAFNPPSPTG TSTSTDTSNS
     SDEEGPSSSN MSKPGALETD LRPPNETIDQ SLGHLISPSK SVEETVPSRS SSEPSSPTGE
     SLVSMGQDTP LKSKESKEPS KRTNDEVETK SSIESPRPVE EEGVNSKFLG ENAPTKDKVE
     EVPDYPPLCE SPPPPPLSPT QSIFEMSEEA LDAFDSDYLL RLEEILTEIH RRYYHAYDKY
     MAEVKQRKAN NIPVEEGSRL SGIPHVANVM SQMRARVLGP NTHITLSGLT PRNRPACDSL
     AGQIALGLGA TLHNRLRLPK QPLAMRSRVT GHRAFTTHLV ACRQNTEKVI AARNFQTQCA
     TNPSQPSLLH IVSPRWLWAS HFRWQRLPES QFPLDHDYSV HAFDPDANSP AAFHGRSRYH
     HQHHRRCHHQ HRFPLQHPHR FMRDDTEVVM EVAK
//
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