ID A0A0N5D776_THECL Unreviewed; 589 AA.
AC A0A0N5D776;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
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=TCLT_LOCUS8901 {ECO:0000313|EMBL:VDN06490.1};
OS Thelazia callipaeda (Oriental eyeworm) (Parasitic nematode).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Thelazioidea; Thelaziidae; Thelazia.
OX NCBI_TaxID=103827 {ECO:0000313|Proteomes:UP000046394, ECO:0000313|WBParaSite:TCLT_0000891201-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:TCLT_0000891201-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDN06490.1, ECO:0000313|Proteomes:UP000276776}
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; UYYF01004699; VDN06490.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N5D776; -.
DR STRING; 103827.A0A0N5D776; -.
DR WBParaSite; TCLT_0000891201-mRNA-1; TCLT_0000891201-mRNA-1; TCLT_0000891201.
DR OMA; RVEDQHR; -.
DR Proteomes; UP000046394; Unplaced.
DR Proteomes; UP000276776; 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:UP000276776}.
FT DOMAIN 141..302
FT /note="FCP1 homology"
FT /evidence="ECO:0000259|PROSITE:PS50969"
FT DOMAIN 369..462
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 530..576
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 589 AA; 66634 MW; 8FC5907F6F1CB0FC CRC64;
MGSRADLLFE DDEGELINWK ITDGAFVTVD SVLFVYSVKS GEKKPLKTSL SGVVTIDTTI
TEGKILKKGM VVASIRPCKH AIVIKDMCAS CGKDLRGRPG FSGDVSEVST ANVSMIHHVP
ELIVSDELAW KIGSRDRELL LKARKLVLLV DLDQTLIHTT NHACKPKNEM DILHYKLKGI
DFYTKVRPYT RDFLENMAEL YEMHIISYGE RQYAHRIAEI LDPDKKYFGH RILSRDELFC
AMYKTKNMQA LFPCGDHMIV MIDDRPDVWQ YSDALVQVKP YRFFKEVGDI NNSRYPENEV
SAPTIHAEQD SDSEVDETLE YVAAVLTKLH SAFYELFDDA KIDRFPVCLL SIALFYCHFK
DLKGIISYLR KQVLKNCSIV ISGIVPVGVD VKKTEVYRLC VQFGASVTNN LCESTTHLIA
ARLGTAKVYE AQKRKNIFIV NIKWLFTCVE RWEKVDEKDF ELLSFETPSA EKLQRNVIIT
NELSRLPTFG KKTLSQMTGE VDEALSEEEL DNNKEGTEIK SSDILFSIEG KKRRSENTET
ENSASSSKKL AVEDLGDNGS ETSSLSVKSE TDDDVDDMAA AVEEQFFAM
//
