ID   PHO85_CANAX             Reviewed;         326 AA.
AC   Q9HGY5;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Negative regulator of the PHO system;
DE            EC=2.7.11.22;
DE   AltName: Full=CaPHO85;
DE   AltName: Full=Serine/threonine-protein kinase PHO85;
GN   Name=PHO85;
OS   Candida albicans (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=5476;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10923026;
RX   DOI=10.1002/1097-0061(200008)16:11<1045::aid-yea595>3.0.co;2-l;
RA   Miyakawa Y.;
RT   "Identification of a Candida albicans homologue of the PHO85 gene, a
RT   negative regulator of the PHO system in Saccharomyces cerevisiae.";
RL   Yeast 16:1045-1051(2000).
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; AB033276; BAB12209.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9HGY5; -.
DR   SMR; Q9HGY5; -.
DR   VEuPathDB; FungiDB:C1_04520C_A; -.
DR   VEuPathDB; FungiDB:CAWG_00942; -.
DR   GO; GO:0042764; C:ascospore-type prospore; IEA:EnsemblFungi.
DR   GO; GO:0005634; C:nucleus; IEA:EnsemblFungi.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   GO; GO:0000083; P:regulation of transcription involved in G1/S transition of mitotic cell cycle; IEA:EnsemblFungi.
DR   GO; GO:0007089; P:traversing start control point of mitotic cell cycle; IEA:EnsemblFungi.
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   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 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; Serine/threonine-protein kinase;
KW   Transferase.
FT   CHAIN           1..326
FT                   /note="Negative regulator of the PHO system"
FT                   /id="PRO_0000086516"
FT   DOMAIN          8..290
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          300..326
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        301..326
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        131
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         14..22
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         37
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   326 AA;  37371 MW;  DE0FB9D13D1FF4A9 CRC64;
     MTGSSSQFQQ LEKLGEGTYA TVYKGRNRAT GALVALKEIS LDSEEGTPST AIREISLMKE
     LDHENIVTLY DVIHTENKLT LVFEYMDKDL KKYMEVHGQQ SALDLKVVKS FMFQLLKGIM
     FCHDNRVLHR DLKPQNLLIN NKGELKLGDF GLARAFGIPF NTFSNEVVTL WYRAPDVLLG
     SRAYTTSIDI WSAGCIFAEM CTGKPLFPGT ANEDQLIKIF RLMGTPNERT WPGISQYTNY
     KNNWQIFVPQ DLRLIVPNLD SMGLNLLQSL LQMRPESRIT ARQALQHPWF HEITMPNAVP
     QHLSDPYQQQ QQQQQHPHQP IIDQQY