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 27-MAR-2024, entry version 91.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB033276; BAB12209.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9HGY5; -.
DR SMR; Q9HGY5; -.
DR EnsemblFungi; C1_04520C_A-T; C1_04520C_A-T-p1; C1_04520C_A.
DR VEuPathDB; FungiDB:C1_04520C_A; -.
DR VEuPathDB; FungiDB:CAWG_00942; -.
DR GO; GO:0005935; C:cellular bud neck; IEA:EnsemblFungi.
DR GO; GO:0005634; C:nucleus; IEA:EnsemblFungi.
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; IEA:UniProtKB-EC.
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; 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
//
