PHO85_ASHGO
ID PHO85_ASHGO Reviewed; 301 AA.
AC Q751E8;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2013, sequence version 2.
DT 03-AUG-2022, entry version 108.
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=AGL242C;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 6.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
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; AE016820; AAS54249.2; -; Genomic_DNA.
DR RefSeq; NP_986425.2; NM_211487.2.
DR AlphaFoldDB; Q751E8; -.
DR SMR; Q751E8; -.
DR STRING; 33169.AAS54249; -.
DR PRIDE; Q751E8; -.
DR EnsemblFungi; AAS54249; AAS54249; AGOS_AGL242C.
DR GeneID; 4622718; -.
DR KEGG; ago:AGOS_AGL242C; -.
DR eggNOG; KOG0594; Eukaryota.
DR HOGENOM; CLU_000288_181_1_1; -.
DR InParanoid; Q751E8; -.
DR OMA; QHPWFND; -.
DR Proteomes; UP000000591; Chromosome VII.
DR GO; GO:0042764; C:ascospore-type prospore; IEA:EnsemblFungi.
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: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; IBA:GO_Central.
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; IBA:GO_Central.
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..301
FT /note="Negative regulator of the PHO system"
FT /id="PRO_0000086515"
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"
SQ SEQUENCE 301 AA; 34366 MW; 576D8B7FE50C8619 CRC64;
MTSTSQFKQL ERLGNGTYAT VYKGLNKTTG LYVALKEVKL DSEEGTPSTA IREISLMKEL
KHENIVRLYD VIHTENKLTL VFEFMDNDLK KFMDSRLDRE MPRGLELSLV KYFQWQLLQG
VAFCHENRIL HRDLKPQNLL INNKGQLKLG DFGLARAFGI PVNTFSSEVV TLWYRAPDVL
MGSRTYCTSI DIWSCGCILA EMIMGKALFP GTNDDEQLKL IFETMGTPTE QTWVGVSQLP
KYNPQIPLYP NKDIKQLLQA TTKEQISDVL VNLIQGLLQL NPSMRLSAQQ ALSHPLFEEY
H
