ID B0WCB3_CULQU Unreviewed; 764 AA.
AC B0WCB3;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 88.
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=6036281 {ECO:0000313|EnsemblMetazoa:CPIJ004583-PA};
GN ORFNames=CpipJ_CPIJ004583 {ECO:0000313|EMBL:EDS43358.1};
OS Culex quinquefasciatus (Southern house mosquito) (Culex pungens).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Culicinae; Culicini; Culex; Culex.
OX NCBI_TaxID=7176;
RN [1] {ECO:0000313|EMBL:EDS43358.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JHB {ECO:0000313|EMBL:EDS43358.1};
RG The Broad Institute Genome Sequencing Platform;
RA Atkinson P.W., Hemingway J., Christensen B.M., Higgs S., Kodira C.,
RA Hannick L., Megy K., O'Leary S., Pearson M., Haas B.J., Mauceli E.,
RA Wortman J.R., Lee N.H., Guigo R., Stanke M., Alvarado L., Amedeo P.,
RA Antoine C.H., Arensburger P., Bidwell S.L., Crawford M., Camaro F.,
RA Devon K., Engels R., Hammond M., Howarth C., Koehrsen M., Lawson D.,
RA Montgomery P., Nene V., Nusbaum C., Puiu D., Romero-Severson J.,
RA Severson D.W., Shumway M., Sisk P., Stolte C., Zeng Q., Eisenstadt E.,
RA Fraser-Liggett C., Strausberg R., Galagan J., Birren B., Collins F.H.;
RT "Annotation of Culex pipiens quinquefasciatus.";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:CPIJ004583-PA}
RP IDENTIFICATION.
RC STRAIN=JHB {ECO:0000313|EnsemblMetazoa:CPIJ004583-PA};
RG EnsemblMetazoa;
RL Submitted (FEB-2021) 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; DS231886; EDS43358.1; -; Genomic_DNA.
DR RefSeq; XP_001846347.1; XM_001846295.1.
DR AlphaFoldDB; B0WCB3; -.
DR STRING; 7176.B0WCB3; -.
DR EnsemblMetazoa; CPIJ004583-RA; CPIJ004583-PA; CPIJ004583.
DR GeneID; 6036281; -.
DR KEGG; cqu:CpipJ_CPIJ004583; -.
DR VEuPathDB; VectorBase:CPIJ004583; -.
DR VEuPathDB; VectorBase:CQUJHB010478; -.
DR eggNOG; KOG0323; Eukaryota.
DR HOGENOM; CLU_007683_1_0_1; -.
DR InParanoid; B0WCB3; -.
DR OMA; DQTVIHC; -.
DR OrthoDB; 73422at2759; -.
DR Proteomes; UP000002320; 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:UP000002320}.
FT DOMAIN 140..305
FT /note="FCP1 homology"
FT /evidence="ECO:0000259|PROSITE:PS50969"
FT DOMAIN 465..557
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 317..421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 564..598
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 620..748
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 317..419
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 620..639
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 640..664
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 693..710
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 764 AA; 85876 MW; 74A9C54B0348A95D CRC64;
MAENQNIICA PPDCAIKINK WKVREGFSVT GGNIILFYEC PGGPEKDIRR LKATKAGVVK
KRLAKEGEIV ERGKPLLELQ QCSHTTVIKD MCADCGADLR QDEQAGGSEA SVPMIHSVPE
LKVTEKLAKK LGQADTERLL RDRKLVLLVD LDQTLIHTTN DNVPNNLKDV YHFQLYGPNS
PWYHTRLRPG ALQFLAKMDP FYELHICTFG ARNYAHMIAQ FLDEKGRYFS HRILSRDECF
NATSKTDNLK ALFPCGDSMV CIIDDREDVW NMAANLIQVK PYHFFQHTGD INAPPGMSKN
ELDGKGVDFK DLIGQAHKEK KDKEGSRPPT PKIETEEVTK PVEDSSKLEE KEPPAVKAED
EKETGVTEGK EEEKPPETKQ ADDGGTKEDK KPSDSTDGKK EDATEEMVVV KKPDSDSGEN
LIEIEDPDDY LLYLEHILQK IHEMFYKEYD STKQISDLKR LIPQVKSQVL VGHKLVFSGL
VPNSMKLHQS KAFQVARSLG ATVTQSFEPD TTHLVAVNGT SKVHHARKNP KIKIVTPEWL
WTCAERWEHV EELLFPLRQS KPVKMNRQPP PHCHSPEHVV NYGEGKSGSS KKSDNVPPKF
IDTINPLLSF SNDDLDAMND DFDEFFESDD SSSDDEPVDI ENPPMDKKLR KRQRKEKEKP
QNIFQKREGG GGSGGAICDV DPDEESTSKT LIRYTDQEDN SQTNLSSDED ESPSAKFRRG
GELPSDLDMG SNSEGSDDPI DDVDDGDWNM MGAALEREFL GLDD
//
