PHO85_KLULA
ID PHO85_KLULA Reviewed; 304 AA.
AC Q92241; Q6CR43;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2004, sequence version 2.
DT 03-AUG-2022, entry version 135.
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=KLLA0D11990g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 76492 / CBS 2359/152 / CLIB 210;
RA Uccelletti D., Morlupi A., Palleschi C.;
RT "The PHO85 gene of K.lactis.";
RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
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; X95418; CAA64698.1; -; Genomic_DNA.
DR EMBL; CR382124; CAH00692.1; -; Genomic_DNA.
DR RefSeq; XP_453596.1; XM_453596.1.
DR AlphaFoldDB; Q92241; -.
DR SMR; Q92241; -.
DR STRING; 28985.XP_453596.1; -.
DR EnsemblFungi; CAH00692; CAH00692; KLLA0_D11990g.
DR GeneID; 2893430; -.
DR KEGG; kla:KLLA0_D11990g; -.
DR eggNOG; KOG0594; Eukaryota.
DR HOGENOM; CLU_000288_181_1_1; -.
DR InParanoid; Q92241; -.
DR OMA; QHPWFND; -.
DR Proteomes; UP000000598; Chromosome D.
DR GO; GO:0042764; C:ascospore-type prospore; IEA:EnsemblFungi.
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:cellular response to DNA damage stimulus; 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:0043433; P:negative regulation of DNA-binding transcription factor activity; 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:0016239; P:positive regulation of macroautophagy; IEA:EnsemblFungi.
DR GO; GO:0071073; P:positive regulation of phospholipid biosynthetic process; IEA:EnsemblFungi.
DR GO; GO:0006468; P:protein phosphorylation; 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 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; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..304
FT /note="Negative regulator of the PHO system"
FT /id="PRO_0000086519"
FT DOMAIN 7..297
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 133
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"
FT CONFLICT 101
FT /note="S -> P (in Ref. 1; CAA64698)"
FT /evidence="ECO:0000305"
FT CONFLICT 189
FT /note="S -> L (in Ref. 1; CAA64698)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 304 AA; 34658 MW; CC1BD5B7A9997BC7 CRC64;
MVAPSQFKQL EKVGNGTYAT VYKGLNKTTG VYVALKEVKL DSEEGTPSTA IREISLMKEL
KHDNIVRLFD VIHTENKLTL VFEFMDNDLK KFMDNRNKGN SHKGLEMDLV KYFQWQLLQG
VAFCHENRIL HRDLKPQNLL INNRGQLKLG DFGLARAFGI PVNTFSSEVV TLWYRAPDVL
MGSRNYCTSI DIWSCGCILA EMIMGKPLFP GSNDEEQLKL IFDTMGTPVE QTWPQVTQLA
KYNPLLPPHM PRDLKQLLQN NTEEVLDDNV VDLLHGLLQL NPDARLSAKD ALNHPWFAEY
NHAN
