ID A0A182WAA4_9DIPT Unreviewed; 1219 AA.
AC A0A182WAA4;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
OS Anopheles minimus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=112268 {ECO:0000313|EnsemblMetazoa:AMIN007282-PA, ECO:0000313|Proteomes:UP000075920};
RN [1] {ECO:0000313|Proteomes:UP000075920}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MINIMUS1 {ECO:0000313|Proteomes:UP000075920};
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 minimus MINIMUS1.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:AMIN007282-PA}
RP IDENTIFICATION.
RC STRAIN=MINIMUS1 {ECO:0000313|EnsemblMetazoa:AMIN007282-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
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 -!- 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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR AlphaFoldDB; A0A182WAA4; -.
DR STRING; 112268.A0A182WAA4; -.
DR EnsemblMetazoa; AMIN007282-RA; AMIN007282-PA; AMIN007282.
DR VEuPathDB; VectorBase:AMIN007282; -.
DR OrthoDB; 73422at2759; -.
DR Proteomes; UP000075920; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0008420; F:RNA polymerase II CTD heptapeptide repeat phosphatase activity; IEA:InterPro.
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}.
FT DOMAIN 538..703
FT /note="FCP1 homology"
FT /evidence="ECO:0000259|PROSITE:PS50969"
FT DOMAIN 927..1020
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 716..815
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 846..875
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1077..1203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 739..815
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1077..1095
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1096..1151
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1164..1178
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1219 AA; 138912 MW; 09674A70A353CC41 CRC64;
MRKYQQLALV LLSITCVVIL LVYKSENNRL KYVLEVVNIF GRNDAASLIR IDNSSRLHSS
PYDFDSPLPA WQRLGDGFYV YSAFWQKNEL AAGGTVISIA VGLEHAAVNF KCQIQHGTGD
VATGKLHFVR LEHPTGSVKA PNGEVFVVYK LLCKVARDFG QPTEIIFTDT TQSSKRYVPL
RVLESRSVQQ RMTMTACVDM SDYLELEEEF RMPASVLQYF LHHQIVGVED FIVYNSNALN
GATKSLLYSH GIKINLLPYN FPFGLADKQQ NRLLIEMDCL MRNYNAAKLT FIGAINEYLY
PCSRLRVNNK FLKYAWKVSS DVSRFAIASR SVCIDKRKKI FSDNLLYDVD AHLNAPTERP
FHVYKPQDYN RTAGTPDFVK TLDVDRSMIF VHRYGGKCSS KTNLQDWTSS MQPEFLHKWK
VREGFSVTSG SIILFYEQLD GCDKEVKRLK ATQSGVVKKR LAREGATVAK GKPVLELGQC
SHMTVIKDMC ADCGADLRQD EASSCSKASV PMIHSVPELK VTETLAKKLG QADTDRLLSD
RKLVLLVDLD QTLIHTTNDN VPNNLKDVYH FQLYGPNSPW YHTRLRPGAL EFLAKMHPYY
ELHICTFGAR NYAHMIAQFL DKDGNFFSHR ILSRDECFNA TSKTDNLKAL FPCGDSMVCI
IDDREDVWNM AANLIQVKPY HFFQHTGDIN APPGMSKNEL DGKGVDFKEL MNQSLKEKKT
KEASDGDRPP TPKIQTQEAG KQKCEKSMPE HVLDDDRVED EPTTVETANQ EKTSKDEKMR
PEAEIVETCV TTNKEKEEEE KKESDKTENK DELLSQKELV QNAGERITHF EEPKELWTEN
ETKDTAAEID KQEEPPGDTE SLVDWSAKEE DKSAPDYKQG KDLMEVEDPD DYLLYLEHIL
LKIHKTFYEE YDKTQTILDL KQLIPKVKAR VLVGMRLCFS GLIPNNVKLE QSKAYLIARS
LGAVVTQNLE PTTTHLVAVT IGTSKVNNAR KNAKIKIVTP EWLWSCAERW EHVEELLYPL
KASNPAKMRQ PPPHCHSPEH AVNYGAITKS REEPKFMDTV NPLLSFSNDD LDAMNNDFDD
FFESDDSSSD DEPVDIENPP MEKALRKRKR VEEIETNRGR HNIFRKRTEE EEDAQKEEKR
RILKYDNPEH NDENSQTNAS SEDEDESPSA KFRRGENLPS DLDMGSNSEG SNEPIDDIDD
GDWNMMGAAL EREFLGLDD
//
