GON7_YEAST
ID GON7_YEAST Reviewed; 123 AA.
AC P46984; D6VW06;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=EKC/KEOPS complex subunit GON7;
DE AltName: Full=Low-dye-binding protein 6;
DE AltName: Full=Polarized growth chromatin-associated controller 2;
GN Name=GON7; Synonyms=LDB6, PCC2; OrderedLocusNames=YJL184W; ORFNames=J0420;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP INDUCTION.
RX PubMed=10681550; DOI=10.1074/jbc.275.8.5668;
RA Garay-Arroyo A., Colmenero-Flores J.M., Garciarrubio A., Covarrubias A.A.;
RT "Highly hydrophilic proteins in prokaryotes and eukaryotes are common
RT during conditions of water deficit.";
RL J. Biol. Chem. 275:5668-5674(2000).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=14690591; DOI=10.1016/s1097-2765(03)00476-3;
RA Hazbun T.R., Malmstroem L., Anderson S., Graczyk B.J., Fox B., Riffle M.,
RA Sundin B.A., Aranda J.D., McDonald W.H., Chiu C.-H., Snydsman B.E.,
RA Bradley P., Muller E.G.D., Fields S., Baker D., Yates J.R. III, Davis T.N.;
RT "Assigning function to yeast proteins by integration of technologies.";
RL Mol. Cell 12:1353-1365(2003).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [7]
RP IDENTIFICATION IN THE EKC/KEOPS COMPLEX, FUNCTION OF THE EKC/KEOPS COMPLEX,
RP SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16874308; DOI=10.1038/sj.emboj.7601235;
RA Kisseleva-Romanova E., Lopreiato R., Baudin-Baillieu A., Rousselle J.-C.,
RA Ilan L., Hofmann K., Namane A., Mann C., Libri D.;
RT "Yeast homolog of a cancer-testis antigen defines a new transcription
RT complex.";
RL EMBO J. 25:3576-3585(2006).
RN [8]
RP FUNCTION, AND IDENTIFICATION IN THE EKC/KEOPS COMPLEX.
RX PubMed=16564010; DOI=10.1016/j.cell.2005.12.044;
RA Downey M., Houlsworth R., Maringele L., Rollie A., Brehme M., Galicia S.,
RA Guillard S., Partington M., Zubko M.K., Krogan N.J., Emili A.,
RA Greenblatt J.F., Harrington L., Lydall D., Durocher D.;
RT "A genome-wide screen identifies the evolutionarily conserved KEOPS complex
RT as a telomere regulator.";
RL Cell 124:1155-1168(2006).
RN [9]
RP FUNCTION IN T(6)A37 FORMATION.
RX PubMed=21183954; DOI=10.1038/emboj.2010.343;
RA Srinivasan M., Mehta P., Yu Y., Prugar E., Koonin E.V., Karzai A.W.,
RA Sternglanz R.;
RT "The highly conserved KEOPS/EKC complex is essential for a universal tRNA
RT modification, t6A.";
RL EMBO J. 30:873-881(2011).
RN [10]
RP FUNCTION IN T(6)A37 FORMATION.
RX PubMed=21459853; DOI=10.1093/nar/gkr178;
RA Daugeron M.C., Lenstra T.L., Frizzarin M., El Yacoubi B., Liu X.,
RA Baudin-Baillieu A., Lijnzaad P., Decourty L., Saveanu C., Jacquier A.,
RA Holstege F.C., de Crecy-Lagard V., van Tilbeurgh H., Libri D.;
RT "Gcn4 misregulation reveals a direct role for the evolutionary conserved
RT EKC/KEOPS in the t6A modification of tRNAs.";
RL Nucleic Acids Res. 39:6148-6160(2011).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [12]
RP FUNCTION IN T(6)A TRNA MODIFICATION.
RX PubMed=23258706; DOI=10.1093/nar/gks1287;
RA Perrochia L., Crozat E., Hecker A., Zhang W., Bareille J., Collinet B.,
RA van Tilbeurgh H., Forterre P., Basta T.;
RT "In vitro biosynthesis of a universal t6A tRNA modification in Archaea and
RT Eukarya.";
RL Nucleic Acids Res. 41:1953-1964(2013).
RN [13]
RP FUNCTION IN THE EKC/KEOPS COMPLEX.
RX PubMed=23620299; DOI=10.1093/nar/gkt322;
RA Wan L.C., Mao D.Y., Neculai D., Strecker J., Chiovitti D., Kurinov I.,
RA Poda G., Thevakumaran N., Yuan F., Szilard R.K., Lissina E., Nislow C.,
RA Caudy A.A., Durocher D., Sicheri F.;
RT "Reconstitution and characterization of eukaryotic N6-
RT threonylcarbamoylation of tRNA using a minimal enzyme system.";
RL Nucleic Acids Res. 41:6332-6346(2013).
CC -!- FUNCTION: Component of the EKC/KEOPS complex that is required for the
CC formation of a threonylcarbamoyl group on adenosine at position 37
CC (t(6)A37) in tRNAs that read codons beginning with adenine. The complex
CC is probably involved in the transfer of the threonylcarbamoyl moiety of
CC threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. GON7 likely
CC plays a supporting role to the catalytic subunit KAE1 in the complex.
CC The EKC/KEOPS complex also promotes both telomere uncapping and
CC telomere elongation. The complex is required for efficient recruitment
CC of transcriptional coactivators. {ECO:0000269|PubMed:16564010,
CC ECO:0000269|PubMed:16874308, ECO:0000269|PubMed:21183954,
CC ECO:0000269|PubMed:21459853, ECO:0000269|PubMed:23258706,
CC ECO:0000269|PubMed:23620299}.
CC -!- SUBUNIT: Component of the EKC/KEOPS complex composed of at least BUD32,
CC CGI121, GON7, KAE1 and PCC1; the whole complex dimerizes.
CC {ECO:0000269|PubMed:16564010, ECO:0000269|PubMed:16874308}.
CC -!- INTERACTION:
CC P46984; P53323: BUD32; NbExp=6; IntAct=EBI-26178, EBI-3809;
CC P46984; P36132: KAE1; NbExp=8; IntAct=EBI-26178, EBI-26411;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16874308}.
CC Chromosome, telomere {ECO:0000305|PubMed:16874308}.
CC -!- INDUCTION: Accumulates in response to hyperosmostic conditions.
CC {ECO:0000269|PubMed:10681550}.
CC -!- MISCELLANEOUS: Present with 2180 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the GON7 family. {ECO:0000305}.
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DR EMBL; Z49459; CAA89479.1; -; Genomic_DNA.
DR EMBL; AY558252; AAS56578.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08622.1; -; Genomic_DNA.
DR PIR; S56967; S56967.
DR RefSeq; NP_012351.1; NM_001181617.1.
DR PDB; 4WX8; X-ray; 2.99 A; D/E/F=1-123.
DR PDB; 4WXA; X-ray; 2.44 A; D/E/F=1-123.
DR PDBsum; 4WX8; -.
DR PDBsum; 4WXA; -.
DR AlphaFoldDB; P46984; -.
DR SMR; P46984; -.
DR BioGRID; 33578; 38.
DR ComplexPortal; CPX-995; KEOPS complex.
DR DIP; DIP-1474N; -.
DR IntAct; P46984; 11.
DR MINT; P46984; -.
DR STRING; 4932.YJL184W; -.
DR iPTMnet; P46984; -.
DR MaxQB; P46984; -.
DR PaxDb; P46984; -.
DR PRIDE; P46984; -.
DR EnsemblFungi; YJL184W_mRNA; YJL184W; YJL184W.
DR GeneID; 853255; -.
DR KEGG; sce:YJL184W; -.
DR SGD; S000003720; GON7.
DR VEuPathDB; FungiDB:YJL184W; -.
DR eggNOG; ENOG502S429; Eukaryota.
DR HOGENOM; CLU_151420_1_0_1; -.
DR InParanoid; P46984; -.
DR OMA; QINVYLT; -.
DR BioCyc; YEAST:G3O-31618-MON; -.
DR PRO; PR:P46984; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P46984; protein.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0000408; C:EKC/KEOPS complex; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0031490; F:chromatin DNA binding; IDA:SGD.
DR GO; GO:0000032; P:cell wall mannoprotein biosynthetic process; IMP:SGD.
DR GO; GO:1990145; P:maintenance of translational fidelity; IC:ComplexPortal.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IPI:SGD.
DR GO; GO:0000723; P:telomere maintenance; IMP:SGD.
DR GO; GO:0000722; P:telomere maintenance via recombination; IGI:SGD.
DR GO; GO:0002949; P:tRNA threonylcarbamoyladenosine modification; IC:ComplexPortal.
DR DisProt; DP00958; -.
DR InterPro; IPR014849; EKC/KEOPS_Gon7.
DR Pfam; PF08738; Gon7; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Chromosome; Nucleus; Reference proteome; Telomere;
KW Transcription; Transcription regulation; tRNA processing.
FT CHAIN 1..123
FT /note="EKC/KEOPS complex subunit GON7"
FT /id="PRO_0000203021"
FT REGION 1..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..58
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 6..10
FT /evidence="ECO:0007829|PDB:4WXA"
FT TURN 11..13
FT /evidence="ECO:0007829|PDB:4WXA"
FT STRAND 14..18
FT /evidence="ECO:0007829|PDB:4WXA"
FT HELIX 66..94
FT /evidence="ECO:0007829|PDB:4WXA"
FT HELIX 99..111
FT /evidence="ECO:0007829|PDB:4WXA"
SQ SEQUENCE 123 AA; 13605 MW; 437EAF6CF1332CC8 CRC64;
MKLPVAQYSA PDGVEKSFAP IRDDPRYMTT EGRTTGPSDH VLNAGQIDRD KPSEPERTKD
GSQLTYLGQL RTQLTGLQDD INEFLTGRME LAKNKKKAGA DEKRIQEEIN QLLDGGDGDE
DAV
