ID A0A182N813_9DIPT Unreviewed; 843 AA.
AC A0A182N813;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
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 Anopheles dirus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=7168 {ECO:0000313|EnsemblMetazoa:ADIR003787-PA, ECO:0000313|Proteomes:UP000075884};
RN [1] {ECO:0000313|Proteomes:UP000075884}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WRAIR2 {ECO:0000313|Proteomes:UP000075884};
RG The Broad Institute Genomics Platform;
RA Neafsey D.E., Walton C., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Anopheles dirus WRAIR2.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:ADIR003787-PA}
RP IDENTIFICATION.
RC STRAIN=WRAIR2 {ECO:0000313|EnsemblMetazoa:ADIR003787-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) 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 AlphaFoldDB; A0A182N813; -.
DR STRING; 7168.A0A182N813; -.
DR EnsemblMetazoa; ADIR003787-RA; ADIR003787-PA; ADIR003787.
DR VEuPathDB; VectorBase:ADIR003787; -.
DR OrthoDB; 73422at2759; -.
DR Proteomes; UP000075884; 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 CDD; cd06849; lipoyl_domain; 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}.
FT DOMAIN 141..306
FT /note="FCP1 homology"
FT /evidence="ECO:0000259|PROSITE:PS50969"
FT DOMAIN 548..641
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 318..504
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 698..828
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 318..364
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..478
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 479..493
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 698..713
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 717..775
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 788..804
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 843 AA; 95048 MW; AA03D1C82184BA7E CRC64;
MADPNQNIIC APDDWAIKIN KWKVREGFPV TSGSIILFYE LLDGSDKEVK RLKATKSGVV
KKRLAREGAT VAKGKPVLEL GQCSHTTVIK DMCADCGADL RQDEPSSCSK ASVPMIHSVP
ELKVTETLAK KLGQADTERL LSDRKLVLLV DLDQTLIHTT NDNVPNNLKD VYHFQLYGPN
SPWYHTRLRP GALAFLAKMH PYYELHICTF GARNYAHMIA QFLDKDGNFF SHRILSRDEC
FNATSKTDNL KALFPCGDSM VCIIDDREDV WNMASNLIQV KPYHFFRHTG DINAPPGMSK
NELDGKGVDF KELMKDQSLK EKKAKDAEED GGRPPTPKIH AQDASTEKKK CEKSMPKHAL
DDEVVEEEES TSEEKVADDE KKMENAEKVE ENSTADAKED SCLKVEKEDV KVEEKEAQSE
DKTVAEDTEK QENETEKEEV KGQNTPPEEQ KTGDEKSAEP ATVGAERGKE KETSNETDAP
SESEGSATVT DKPSTDDTAE EKELLEVEDP DDYLLYLEHI LLKIHEMFYA EYDRSKAISD
LKQLIPQVKA RVLVGTRLCF SGLIPNTVKL EQSKAYLIAR SLGAVVTQNL EPTTTHLVAV
TIGTSKVNNA RKNAKIKIVT PEWLWSCAER WEHVEERLYP LKASNPAKMR QPPPHCHSPE
HVVNYGAMAK SREEPKFMDT VNPLLSFSND DLDAMNNDFD DFFESDSSSS DDEPVDIENP
PMEKALRKRR RVVEKESNRG RHNIFRKRAE EEEEQQRRAE ETRRILKHDA EPENNDENSQ
TNASSEDDDE SPSTKFRRGE DLPSDLELGS NSEGSDEPID DVDDGDWNMM GAALEREFLG
LDD
//
