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Database: UniProt
Entry: Q6FVU1_CANGA
LinkDB: Q6FVU1_CANGA
Original site: Q6FVU1_CANGA 
ID   Q6FVU1_CANGA            Unreviewed;       447 AA.
AC   Q6FVU1;
DT   19-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   19-JUL-2004, sequence version 1.
DT   24-JAN-2024, entry version 90.
DE   SubName: Full=Candida glabrata strain CBS138 chromosome D complete sequence {ECO:0000313|EMBL:CAG58564.1};
GN   OrderedLocusNames=CAGL0D05610g {ECO:0000313|CGD:CAL0128163,
GN   ECO:0000313|EMBL:CAG58564.1};
OS   Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 /
OS   NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces.
OX   NCBI_TaxID=284593 {ECO:0000313|EMBL:CAG58564.1, ECO:0000313|Proteomes:UP000002428};
RN   [1] {ECO:0000313|EMBL:CAG58564.1, ECO:0000313|Proteomes:UP000002428}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65
RC   {ECO:0000313|Proteomes:UP000002428};
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).
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DR   EMBL; CR380950; CAG58564.1; -; Genomic_DNA.
DR   RefSeq; XP_445653.1; XM_445653.1.
DR   AlphaFoldDB; Q6FVU1; -.
DR   STRING; 284593.Q6FVU1; -.
DR   EnsemblFungi; CAGL0D05610g-T; CAGL0D05610g-T-p1; CAGL0D05610g.
DR   GeneID; 2887089; -.
DR   KEGG; cgr:CAGL0D05610g; -.
DR   CGD; CAL0128163; CAGL0D05610g.
DR   VEuPathDB; FungiDB:CAGL0D05610g; -.
DR   eggNOG; KOG1605; Eukaryota.
DR   HOGENOM; CLU_020262_1_2_1; -.
DR   InParanoid; Q6FVU1; -.
DR   Proteomes; UP000002428; Chromosome D.
DR   GO; GO:0016791; F:phosphatase activity; IEA:InterPro.
DR   GO; GO:1904262; P:negative regulation of TORC1 signaling; IEA:EnsemblFungi.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:EnsemblFungi.
DR   GO; GO:0009651; P:response to salt stress; IEA:EnsemblFungi.
DR   CDD; cd07521; HAD_FCP1-like; 1.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR   InterPro; IPR011948; Dullard_phosphatase.
DR   InterPro; IPR004274; FCP1_dom.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR023214; HAD_sf.
DR   NCBIfam; TIGR02251; HIF-SF_euk; 1.
DR   PANTHER; PTHR12210; DULLARD PROTEIN PHOSPHATASE; 1.
DR   PANTHER; PTHR12210:SF171; PHOSPHATASE HERZOG; 1.
DR   Pfam; PF03031; NIF; 1.
DR   SMART; SM00577; CPDc; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
DR   PROSITE; PS50969; FCP1; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000002428}.
FT   DOMAIN          273..431
FT                   /note="FCP1 homology"
FT                   /evidence="ECO:0000259|PROSITE:PS50969"
FT   REGION          12..234
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        23..57
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        58..72
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        73..142
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        154..182
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        183..200
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        207..227
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   447 AA;  50518 MW;  B8AE15A5894FC79C CRC64;
     MDIISSFFCC ADEQVQESGQ RKTMNTERTE SKPSNRRDLP RNNGDSRQVR SAELYKEENT
     DTTVSSGSTP KLRDSDSNKK KGDRSRDNAH MDRKHANNKS HINDADAAEN SQKRHSTRRS
     QVNGKTHDKK RLADSDNKKG DDDVDEITEE EVPVPVNKNS SKKSTSNNSN NVKPSGSDLE
     KSNSNMDGEK YKKLSTEEEE ELANQLEYGT KLSQVNSVGS DNSEENYDSV PTYDEEDLDE
     VEEEEEYIDL TVLQPGQYHA PGLDTLLSPK GDAFKHKKCL VLDLDETLVH SSFKYLHTAD
     FVLPVDIDDQ IHNVYVIKRP GVDEFLQRVG ELYEVVVFTA SVSRYGDPLL DVLDKSNNIH
     HRLFRDACYT YEGNYIKNLS QIGRPLSEII ILDNSPPSYI FHPQHAIPIS SWFSDSHDNE
     LLDILPLLED LAKPSLPDIG KVLDVTI
//
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