(data stored in ACNUC7421 zone)

SWISSPROT: 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   11-DEC-2019, entry version 98.
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}.
DR   EMBL; AE016820; AAS54249.2; -; Genomic_DNA.
DR   RefSeq; NP_986425.2; NM_211487.2.
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   HOGENOM; HOG000233024; -.
DR   InParanoid; Q751E8; -.
DR   KO; K06655; -.
DR   OMA; FEFMDKD; -.
DR   Proteomes; UP000000591; Chromosome VII.
DR   GO; GO:0042764; C:ascospore-type prospore; 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:0006974; P:cellular response to DNA damage stimulus; 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:0032878; P:regulation of establishment or maintenance of cell polarity; 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;
DR   PRODOM; Q751E8.
DR   SWISS-2DPAGE; Q751E8.
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   NP_BIND         13..21
FT                   /note="ATP"
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         36
FT                   /note="ATP"
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
//

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