ID   PHO85_YARLI             Reviewed;         294 AA.
AC   Q6C7U8;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   27-MAR-2024, entry version 113.
DE   RecName: Full=Negative regulator of the PHO system;
DE            EC=2.7.11.22;
DE   AltName: Full=Serine/threonine-protein kinase PHO85;
GN   Name=PHO85; OrderedLocusNames=YALI0D25190g;
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 122 / E 150;
RX   PubMed=15229592; DOI=10.1038/nature02579;
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.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: When phosphate concentrations are high it phosphorylates the
CC       PHO4 transcription factor thus establishing repression. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.22;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.22;
CC   -!- SUBUNIT: Interacts with a number of cyclins. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC       protein kinase family. CDC2/CDKX subfamily. {ECO:0000305}.
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DR   EMBL; CR382130; CAG81468.1; -; Genomic_DNA.
DR   RefSeq; XP_503264.1; XM_503264.1.
DR   AlphaFoldDB; Q6C7U8; -.
DR   SMR; Q6C7U8; -.
DR   STRING; 284591.Q6C7U8; -.
DR   EnsemblFungi; CAG81468; CAG81468; YALI0_D25190g.
DR   GeneID; 2910782; -.
DR   KEGG; yli:YALI0D25190g; -.
DR   VEuPathDB; FungiDB:YALI0_D25190g; -.
DR   HOGENOM; CLU_000288_181_1_1; -.
DR   InParanoid; Q6C7U8; -.
DR   OMA; WPGISQY; -.
DR   OrthoDB; 244018at2759; -.
DR   Proteomes; UP000001300; Chromosome D.
DR   GO; GO:0005935; C:cellular bud neck; IEA:EnsemblFungi.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:1990860; C:Pho85-Pho80 CDK-cyclin complex; IEA:EnsemblFungi.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; IBA:GO_Central.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0006974; P:DNA damage response; IEA:EnsemblFungi.
DR   GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IEA:EnsemblFungi.
DR   GO; GO:0055088; P:lipid homeostasis; IEA:EnsemblFungi.
DR   GO; GO:0050849; P:negative regulation of calcium-mediated signaling; IEA:EnsemblFungi.
DR   GO; GO:0045719; P:negative regulation of glycogen biosynthetic process; IEA:EnsemblFungi.
DR   GO; GO:0016242; P:negative regulation of macroautophagy; IEA:EnsemblFungi.
DR   GO; GO:0045936; P:negative regulation of phosphate metabolic process; IEA:EnsemblFungi.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:EnsemblFungi.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0016239; P:positive regulation of macroautophagy; IEA:EnsemblFungi.
DR   GO; GO:0071073; P:positive regulation of phospholipid biosynthetic process; IEA:EnsemblFungi.
DR   GO; GO:1901987; P:regulation of cell cycle phase transition; IEA:EnsemblFungi.
DR   GO; GO:0051302; P:regulation of cell division; IEA:EnsemblFungi.
DR   GO; GO:0032878; P:regulation of establishment or maintenance of cell polarity; IEA:EnsemblFungi.
DR   GO; GO:0046822; P:regulation of nucleocytoplasmic transport; IEA:EnsemblFungi.
DR   GO; GO:0032880; P:regulation of protein localization; IEA:EnsemblFungi.
DR   GO; GO:0031647; P:regulation of protein stability; IEA:EnsemblFungi.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR24056; CELL DIVISION PROTEIN KINASE; 1.
DR   PANTHER; PTHR24056:SF46; CYCLIN-DEPENDENT KINASE 5; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Kinase; Nucleotide-binding; Reference proteome;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..294
FT                   /note="Negative regulator of the PHO system"
FT                   /id="PRO_0000086520"
FT   DOMAIN          7..289
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   ACT_SITE        130
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         13..21
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         36
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   294 AA;  33671 MW;  5764A684447E6C79 CRC64;
     MNTSSQFQQL EKLGEGTYAT VYKGRNRTTG QLVALKEINL DSEEGTPSTA IREISLMKEL
     KHENIVTLYD VIHTENKLNL VFEYMDKDLK KFMDTNGNKG ALETKQVKWF MYQLLRGILF
     CHDNRVLHRD LKPQNLLINA KGQLKLADFG LARAFGIPVN TFSNEVVTLW YRAPDVLLGS
     RTYSTSIDIW SAGCIMAEMF TGRPLFPGSS NDDQLQHIFK LMGTPNESTW PNISSLPNYR
     SNFQVYAPQD LRVIIPQIDN VALDLLLSLL QLKPENRITA RQSLEHPWFA EYHQ
//