(data stored in ACNUC27125 zone)

SWISSPROT: E9BIR7_LEIDB

ID   E9BIR7_LEIDB            Unreviewed;       480 AA.
AC   E9BIR7;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   11-DEC-2019, entry version 42.
DE   RecName: Full=Serine/threonine-protein phosphatase {ECO:0000256|RuleBase:RU004273};
DE            EC=3.1.3.16 {ECO:0000256|RuleBase:RU004273};
GN   ORFNames=LDBPK_262560 {ECO:0000313|EMBL:CBZ35143.1};
OS   Leishmania donovani (strain BPK282A1).
OC   Eukaryota; Euglenozoa; Kinetoplastida; Trypanosomatidae; Leishmaniinae;
OC   Leishmania.
OX   NCBI_TaxID=981087 {ECO:0000313|EMBL:CBZ35143.1, ECO:0000313|Proteomes:UP000008980};
RN   [1] {ECO:0000313|EMBL:CBZ35143.1, ECO:0000313|Proteomes:UP000008980}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BPK282A1 {ECO:0000313|EMBL:CBZ35143.1,
RC   ECO:0000313|Proteomes:UP000008980};
RX   PubMed=22038251; DOI=10.1101/gr.123430.111;
RA   Downing T., Imamura H., Decuypere S., Clark T.G., Coombs G.H., Cotton J.A.,
RA   Hilley J.D., de Doncker S., Maes I., Mottram J.C., Quail M.A., Rijal S.,
RA   Sanders M., Schonian G., Stark O., Sundar S., Vanaerschot M.,
RA   Hertz-Fowler C., Dujardin J.C., Berriman M.;
RT   "Whole genome sequencing of multiple Leishmania donovani clinical isolates
RT   provides insights into population structure and mechanisms of drug
RT   resistance.";
RL   Genome Res. 21:2143-2156(2011).
RN   [2] {ECO:0000313|Proteomes:UP000008980}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BPK282A1 {ECO:0000313|Proteomes:UP000008980};
RA   Downing T., Imamura H., Sanders M., Decuypere S., Hertz-Fowler C.,
RA   Clark T.G., Rijal S., Sundar S., Quail M.A., De Doncker S., Maes I.,
RA   Vanaerschot M., Stark O., Schonian G., Dujardin J.C., Berriman M.;
RT   "Whole genome sequencing of Leishmania donovani clinical lines reveals
RT   dynamic variation related to drug resistance.";
RL   Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
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|RuleBase:RU004273};
CC   -!- SIMILARITY: Belongs to the PPP phosphatase family.
CC       {ECO:0000256|RuleBase:RU004273}.
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DR   EMBL; FR799613; CBZ35143.1; -; Genomic_DNA.
DR   RefSeq; XP_003861840.1; XM_003861792.1.
DR   EnsemblProtists; CBZ35143; CBZ35143; LDBPK_262560.
DR   GeneDB; LdBPK_262560.1.1:pep; -.
DR   GeneID; 13389088; -.
DR   KEGG; ldo:LDBPK_262560; -.
DR   EuPathDB; TriTrypDB:LdBPK_262560.1; -.
DR   HOGENOM; HOG000172699; -.
DR   KO; K04348; -.
DR   OMA; LWSLKIW; -.
DR   Proteomes; UP000008980; Chromosome 26.
DR   GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:UniProtKB-EC.
DR   CDD; cd07416; MPP_PP2B; 1.
DR   Gene3D; 3.60.21.10; -; 1.
DR   InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   InterPro; IPR041751; MPP_PP2B.
DR   InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR   Pfam; PF00149; Metallophos; 1.
DR   PRINTS; PR00114; STPHPHTASE.
DR   SMART; SM00156; PP2Ac; 1.
DR   PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
PE   3: Inferred from homology;
DR   PRODOM; E9BIR7.
DR   SWISS-2DPAGE; E9BIR7.
KW   Hydrolase {ECO:0000256|RuleBase:RU004273}.
FT   DOMAIN          137..142
FT                   /note="SER_THR_PHOSPHATASE"
FT                   /evidence="ECO:0000259|PROSITE:PS00125"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   480 AA;  53175 MW;  E9CBC2029F9ECFA0 CRC64;
     MLLTDRGNPS VPPPNWEPLS SSALFDESGK ARPDVVREHL TKEGLLQEAD ALTIITQCAL
     IWKDEPNVLR LDGPVVIAGD IHGQFFDLLN LLSIGGDPSQ QKYIFLGDYV DRGCFGMEVI
     LLLMCYKICY PETMIMLRGN HESRHLTTYF NFKREVLYKY SIAVYNAIMS AFDCLPLACI
     LNDRFLCVHG GLSPELKRIS DIGAIHRFRE PPSSGPMCDL LWADPLDEKE EDPAAAPLFV
     PNTTRGCSYV YSNAAACNFL EENGLITIIR GHEAQDEGYH LYKKTNKGFP AVICIFSAPN
     YCDTYDNRAA VVMLNRNIMS IRQFNSSPHP YYLPNFMNAF TWSLPFVEEK LLDIGTNVLH
     PIDGSEDHLL LDGAEATTAA PTPGANTESR DGNVLEQRGE KIREKILAMG RLSRMFHTLC
     EGGESRLPPK GLAGGILPQG GLPCGPDSVQ AAGRGLQQSK EMDSANGRWQ DCLIEGDLEP
//

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