(data stored in ACNUC27125 zone)

SWISSPROT: B9W6M3_CANDC

ID   B9W6M3_CANDC            Unreviewed;       607 AA.
AC   B9W6M3;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   11-DEC-2019, entry version 63.
DE   RecName: Full=Serine/threonine-protein phosphatase {ECO:0000256|RuleBase:RU004273};
DE            EC=3.1.3.16 {ECO:0000256|RuleBase:RU004273};
GN   Name=CNA1 {ECO:0000313|CGD:CAL0000166815};
GN   OrderedLocusNames=Cd36_00650 {ECO:0000313|CGD:CAL0000166815};
GN   ORFNames=CD36_00650 {ECO:0000313|EMBL:CAX44328.1};
OS   Candida dubliniensis (strain CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 /
OS   NRRL Y-17841) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=573826 {ECO:0000313|EMBL:CAX44328.1, ECO:0000313|Proteomes:UP000002605};
RN   [1] {ECO:0000313|EMBL:CAX44328.1, ECO:0000313|Proteomes:UP000002605}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 / NRRL Y-17841
RC   {ECO:0000313|Proteomes:UP000002605};
RX   PubMed=19745113; DOI=10.1101/gr.097501.109;
RA   Jackson A.P., Gamble J.A., Yeomans T., Moran G.P., Saunders D., Harris D.,
RA   Aslett M., Barrell J.F., Butler G., Citiulo F., Coleman D.C.,
RA   de Groot P.W.J., Goodwin T.J., Quail M.A., McQuillan J., Munro C.A.,
RA   Pain A., Poulter R.T., Rajandream M.A., Renauld H., Spiering M.J.,
RA   Tivey A., Gow N.A.R., Barrell B., Sullivan D.J., Berriman M.;
RT   "Comparative genomics of the fungal pathogens Candida dubliniensis and
RT   Candida albicans.";
RL   Genome Res. 19:2231-2244(2009).
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; FM992688; CAX44328.1; -; Genomic_DNA.
DR   RefSeq; XP_002416744.1; XM_002416699.1.
DR   STRING; 42374.XP_002416744.1; -.
DR   ChEMBL; CHEMBL1293271; -.
DR   EnsemblFungi; CAX44328; CAX44328; CD36_00650.
DR   GeneID; 8045551; -.
DR   KEGG; cdu:CD36_00650; -.
DR   CGD; CAL0000166815; CNA1.
DR   eggNOG; ENOG410IQC1; Eukaryota.
DR   eggNOG; ENOG41115W3; LUCA.
DR   HOGENOM; HOG000172699; -.
DR   KO; K04348; -.
DR   OrthoDB; 463522at2759; -.
DR   Proteomes; UP000002605; Chromosome 1.
DR   GO; GO:0005623; C:cell; IEA:GOC.
DR   GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030003; P:cellular cation homeostasis; IMP:CGD.
DR   GO; GO:0035690; P:cellular response to drug; IMP:CGD.
DR   GO; GO:0036170; P:filamentous growth of a population of unicellular organisms in response to starvation; IMP:CGD.
DR   GO; GO:0031505; P:fungal-type cell wall organization; IMP:CGD.
DR   GO; GO:0009405; P:pathogenesis; IMP:CGD.
DR   GO; GO:1900233; P:positive regulation of single-species biofilm formation on inanimate substrate; IMP:CGD.
DR   CDD; cd07416; MPP_PP2B; 1.
DR   InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
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; B9W6M3.
DR   SWISS-2DPAGE; B9W6M3.
KW   Hydrolase {ECO:0000256|RuleBase:RU004273, ECO:0000313|EMBL:CAX44328.1}.
FT   DOMAIN          196..201
FT                   /note="SER_THR_PHOSPHATASE"
FT                   /evidence="ECO:0000259|PROSITE:PS00125"
FT   REGION          442..467
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   607 AA;  69556 MW;  7EF1F8A2D352E17C CRC64;
     MSGNTVQRNT EQINNALNAI QHRRTTTGND LNHTNQRIIS QNSINDKDYT IYITDDGEKY
     STVERAVKSV DPPVTFKPKD EQVFLSNGKP NHQFLKQHFI HEGRLHEHQA IQILKQATHL
     LSKESNLLNV PAPVTICGDV HGQYYDLMKL FEVGGDPATT KYLFLGDYVD RGSFSIECLL
     YLYSLKINYP DTFWMLRGNH ECRHLTEYFT FKNECLHKYS EQLYEECLVS FNALPLAAIM
     NEQFFCVHGG LSPQLTSLDS LRKLHRFREP PTKGLMCDLL WADPIEEYDE DNIDQEYVTN
     VVRGCSFAFT YKAACKFLDK TKLLSVIRAH EAQNAGYRMY KRTKTMGFPS LLTMFSAPNY
     LDSYNNKAAV LKYENNVMNI RQFNASPHPY WLPHFMDVFT WSLPFVGEKV TDMLVSILNV
     CTEEELDEDL PFSESEIGVA TKTTKTTTPV SPVSPKAHPP STRITSPYKS TKLVESDNNP
     NTNNDDSEMT LEEKKQALRN KIIAIGKMSR MFQVLREEQE NVAHLKELNR GSLPKGSLLH
     GVDGLKNTIN SFEEAKAADR INEALPPSPE DIQRLKQEKN TRIRQQIENQ EMSGPVFQRL
     IRRLSQS
//

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