(data stored in ACNUC27125 zone)

SWISSPROT: Q6C5D3_YARLI

ID   Q6C5D3_YARLI            Unreviewed;       549 AA.
AC   Q6C5D3;
DT   16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT   16-AUG-2004, sequence version 1.
DT   11-DEC-2019, entry version 96.
DE   RecName: Full=Serine/threonine-protein phosphatase {ECO:0000256|RuleBase:RU004273};
DE            EC=3.1.3.16 {ECO:0000256|RuleBase:RU004273};
GN   ORFNames=YALI0_E19008g {ECO:0000313|EMBL:CAG79724.1};
OS   Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Dipodascaceae; Yarrowia.
OX   NCBI_TaxID=284591 {ECO:0000313|EMBL:CAG79724.1, ECO:0000313|Proteomes:UP000001300};
RN   [1] {ECO:0000313|EMBL:CAG79724.1, ECO:0000313|Proteomes:UP000001300}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 122 / E 150 {ECO:0000313|Proteomes:UP000001300};
RX   PubMed=15229592; DOI=10.1038/nature02579;
RG   Genolevures;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.F., Straub M.L.,
RA   Suleau A., Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E.,
RA   Wirth B., Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   Wincker P., Souciet J.L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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; CR382131; CAG79724.1; -; Genomic_DNA.
DR   RefSeq; XP_504129.1; XM_504129.1.
DR   EnsemblFungi; CAG79724; CAG79724; YALI0_E19008g.
DR   GeneID; 2911741; -.
DR   KEGG; yli:YALI0E19008g; -.
DR   HOGENOM; HOG000172699; -.
DR   InParanoid; Q6C5D3; -.
DR   KO; K04348; -.
DR   OMA; LWSLKIW; -.
DR   Proteomes; UP000001300; Chromosome E.
DR   GO; GO:0005955; C:calcineurin complex; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005516; F:calmodulin binding; IBA:GO_Central.
DR   GO; GO:0033192; F:calmodulin-dependent protein phosphatase activity; IBA:GO_Central.
DR   GO; GO:0097720; P:calcineurin-mediated signaling; IBA:GO_Central.
DR   GO; GO:0031505; P:fungal-type cell wall organization; IBA:GO_Central.
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; Q6C5D3.
DR   SWISS-2DPAGE; Q6C5D3.
KW   Hydrolase {ECO:0000256|RuleBase:RU004273};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001300}.
FT   DOMAIN          173..178
FT                   /note="SER_THR_PHOSPHATASE"
FT                   /evidence="ECO:0000259|PROSITE:PS00125"
FT   REGION          406..429
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          501..549
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        513..549
FT                   /note="Polyampholyte"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   549 AA;  61875 MW;  BC496CBD38EFE37D CRC64;
     MDNTQLSNAV KAFQNRKPLP KIDFTQHTME DGSVVSTVDR PIKSVPAPAT NKPSDDDVFD
     RATGKPNLEF LKDHFYREGR LSNEQAIRIV EAGSRILEQE PTLLEVDAPI TICGDVHGQF
     YDLLKLFEVG GTPGPSTRYL FLGDYVDRGY FSVECVLYLW SLKIHYPDSI YLLRGNHECR
     HLTEYFTFKL ECVHKYGVDL YEACLASFCT LPLAAIMNRQ FLCVHGGLSP ELHTLDDLRR
     IDRFREPPTH GIMCDLLWAD PCEDFGAEKG NEHFVHNSVR GCSFFYSYHA ACAFLEANGL
     LSIIRAHEAQ DAGYRMYRKT KSTGFPSVMT IFSAPNYLDA YNNKAAVLKY ENNVMNIRQF
     NSSPHPYWLP NFMNVFTWSM PFVGEKITEM LITMLNICTK EELEDDDSVS GISEATEPKP
     AASVATGDSD APSAISFDQR RALRNKILAI GRVSRLFNVL RQESESVSEL KAVSGGKLPQ
     GTLMLGGQGI RDAITSFEEA RSADLSNERL PPTSEEQAKE KQQQQEGFKK AMGEHDEKIQ
     RLARRLSRG
//

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