ID T1HI84_RHOPR Unreviewed; 581 AA.
AC T1HI84;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 55.
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};
OS Rhodnius prolixus (Triatomid bug).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Paraneoptera; Hemiptera; Heteroptera; Panheteroptera;
OC Cimicomorpha; Reduviidae; Triatominae; Rhodnius.
OX NCBI_TaxID=13249 {ECO:0000313|EnsemblMetazoa:RPRC003757-PA, ECO:0000313|Proteomes:UP000015103};
RN [1] {ECO:0000313|Proteomes:UP000015103}
RP NUCLEOTIDE SEQUENCE.
RA Wilson R.K., Warren W., Dotson E., Oliveira P.L.;
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:RPRC003757-PA}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (MAY-2015) to UniProtKB.
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; ACPB03000895; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; T1HI84; -.
DR STRING; 13249.T1HI84; -.
DR EnsemblMetazoa; RPRC003757-RA; RPRC003757-PA; RPRC003757.
DR VEuPathDB; VectorBase:RPRC003757; -.
DR eggNOG; KOG0323; Eukaryota.
DR HOGENOM; CLU_007683_1_0_1; -.
DR InParanoid; T1HI84; -.
DR OMA; DQTVIHC; -.
DR OrthoDB; 73422at2759; -.
DR Proteomes; UP000015103; 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; 2.40.50.100; -; 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 InterPro; IPR011053; Single_hybrid_motif.
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 SUPFAM; SSF51230; Single hybrid motif; 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:UP000015103}.
SQ SEQUENCE 581 AA; 66480 MW; 78B1221EACEBFFC2 CRC64;
MSDTRNIFLT LRKSVKLTKW KVEEGTIIYD GRVLLLYEET DSGKSAKLKS KNVGSVSKLL
VKEGDVVNPG DALLEIAAGC SHPTVINDLC AECGADLQRE GETQSRATVP MVHSIPQLKV
SQEQAQKLGH KDTERLLRDR KLVLLVDLDQ TLIHTTHDNI PNNLKDVHHF QLPGSPNPWY
HTRLRPGTDR FLLNMSRFYE LHICTFGVRP YAHTVAAILD KDRRLFSNRI LSRDEFFDPN
SKLHNLQALF PCGDELVCII DDREDVWDNS PNLIQVKPYH FFAVTADIND ILSRINRIKD
NSYLAPGNFE FTHSIFIFIY REPFSGFFKL EDNRKPLKIL DFRYILSNKT FLEQFYGLIE
TKSTENKKYK NHTNHCGDKR FIVYPFRVKE NKLREHPNEK GPHNAETDEE NGKGEMKVVE
EDSEDNKSEE DSDLIDFEDE DDYLLHLEDI LIRLHRRFYS IYDKKEEGIA DVKWVIEQER
SAVLRGCTLV LSGLVPLYQD GVVSPEPVAP AAKIAAKLGA KLAQDLTSET THLVAANRCT
AKVHQAKKMP HIKVVNPHWL AACAHRWEKV EEALFEVGTG G
//
