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Database: UniProt/TrEMBL
Entry: A5DRG1_PICGU
LinkDB: A5DRG1_PICGU
Original site: A5DRG1_PICGU 
ID   A5DRG1_PICGU            Unreviewed;       518 AA.
AC   A5DRG1;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2008, sequence version 2.
DT   03-APR-2013, entry version 39.
DE   SubName: Full=Putative uncharacterized protein;
GN   ORFNames=PGUG_05862;
OS   Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM
OS   1539 / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX   NCBI_TaxID=294746;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL
RC   Y-324;
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA   Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L.,
RA   Agrafioti I., Arnaud M.B., Bates S., Brown A.J.P., Brunke S.,
RA   Costanzo M.C., Fitzpatrick D.A., de Groot P.W.J., Harris D.,
RA   Hoyer L.L., Hube B., Klis F.M., Kodira C., Lennard N., Logue M.E.,
RA   Martin R., Neiman A.M., Nikolaou E., Quail M.A., Quinn J.,
RA   Santos M.C., Schmitzberger F.F., Sherlock G., Shah P.,
RA   Silverstein K.A.T., Skrzypek M.S., Soll D., Staggs R., Stansfield I.,
RA   Stumpf M.P.H., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA   Berriman M., Heitman J., Gow N.A.R., Lorenz M.C., Birren B.W.,
RA   Kellis M., Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(2009).
CC   -!- SIMILARITY: Belongs to the GHMP kinase family.
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DR   EMBL; CH408162; EDK41764.2; -; Genomic_DNA.
DR   RefSeq; XP_001482099.1; XM_001482049.1.
DR   ProteinModelPortal; A5DRG1; -.
DR   STRING; 4929.A5DRG1; -.
DR   GeneID; 5123864; -.
DR   KEGG; pgu:PGUG_05862; -.
DR   KO; K00849; -.
DR   OrthoDB; EOG4GTPNF; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004335; F:galactokinase activity; IEA:InterPro.
DR   GO; GO:0006012; P:galactose metabolic process; IEA:InterPro.
DR   Gene3D; 3.30.230.10; -; 1.
DR   InterPro; IPR000705; Galactokinase.
DR   InterPro; IPR019539; GalKase_gal-bd.
DR   InterPro; IPR013750; GHMP_kinase_C_dom.
DR   InterPro; IPR006204; GHMP_kinase_N_dom.
DR   InterPro; IPR006203; GHMP_knse_ATP-bd_CS.
DR   InterPro; IPR006206; Mevalonate/galactokinase.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR   Pfam; PF10509; GalKase_gal_bdg; 1.
DR   Pfam; PF08544; GHMP_kinases_C; 1.
DR   Pfam; PF00288; GHMP_kinases_N; 1.
DR   PIRSF; PIRSF000530; Galactokinase; 1.
DR   PRINTS; PR00473; GALCTOKINASE.
DR   PRINTS; PR00959; MEVGALKINASE.
DR   SUPFAM; SSF54211; Ribosomal_S5_D2-typ_fold; 1.
DR   TIGRFAMs; TIGR00131; gal_kin; 1.
DR   PROSITE; PS00627; GHMP_KINASES_ATP; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Kinase; Nucleotide-binding;
KW   Transferase.
SQ   SEQUENCE   518 AA;  57252 MW;  E859490CAC7F2D0E CRC64;
     MPLVSTVKDF SFYSDSEKQK KRYGSVVETF TKTFHQKPDF LVRAPGRVNL MGDHIDYCHF
     SVLPMAIEVD VITAVSKSDD NSVTIANTDE KFTTQTFDLP SDGSLVTIDK NQHSWGNYFK
     CGLLVAHKYI TETYPEKTGS GKKPLKGLHA LFDGTVPTGG GLSSSAAFCI AATLAVLKAN
     DISDITKEDL TRITVVCEHY VGLSNGGMDQ CASIYGEPSK VLLISFKPKL ETTPFELPKT
     KPEAVFLISN SLVTSNKTET APTNYNLRVV EVAVAADLLA HKLGLKTDQD SNLNTATLRG
     AFDAYFTQKL GEPHWDGKDI NMGIERLTRI LEYIETVFSD EEKKGFTTEE AAKAAGKSKD
     EFSSTYLSAF PVRYDLLKIY QRTKHVFSDS LRVLQCIKVA RDFKGDSEDY LQQFGKLMNE
     SQVSCNILNN ASPPKCEELC RIARENGAYG SRITGAAFGG SIVHLTTVDR LQKLIDVLTT
     EYYKKTYPNI TETELNEAIV VSKPAEGACV VDILDKIE
//
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