CG121_YEAST
ID CG121_YEAST Reviewed; 181 AA.
AC Q03705; A2TBM6; D6VZD9; Q6Q5A2;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=EKC/KEOPS complex subunit CGI121;
DE AltName: Full=CGI-121 homolog;
GN Name=CGI121; OrderedLocusNames=YML036W;
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=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(1997).
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 [MRNA] OF 1-179.
RC STRAIN=ATCC 201390 / BY4743;
RX PubMed=17244705; DOI=10.1073/pnas.0610354104;
RA Juneau K., Palm C., Miranda M., Davis R.W.;
RT "High-density yeast-tiling array reveals previously undiscovered introns
RT and extensive regulation of meiotic splicing.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1522-1527(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-154.
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 [5]
RP IDENTIFICATION IN THE EKC/KEOPS COMPLEX, FUNCTION OF THE EKC/KEOPS COMPLEX,
RP 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 [6]
RP IDENTIFICATION OF INTRON.
RX PubMed=17101987; DOI=10.1073/pnas.0605645103;
RA Miura F., Kawaguchi N., Sese J., Toyoda A., Hattori M., Morishita S.,
RA Ito T.;
RT "A large-scale full-length cDNA analysis to explore the budding yeast
RT transcriptome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:17846-17851(2006).
RN [7]
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 [8]
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 [9]
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 [10]
RP FUNCTION IN T(6)A37 FORMATION.
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 [11]
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. CGI121 acts as
CC an allosteric effector that regulates the t(6)A activity of the
CC complex. The EKC/KEOPS complex also promotes both telomere uncapping
CC and telomere elongation. The complex is required for efficient
CC recruitment of transcriptional coactivators. CGI121 is not required for
CC tRNA modification. {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 Q03705; P53323: BUD32; NbExp=9; IntAct=EBI-912262, EBI-3809;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Chromosome, telomere
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the CGI121/TPRKB family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAS56559.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAA86619.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; Z46659; CAA86619.1; ALT_SEQ; Genomic_DNA.
DR EMBL; EF123129; ABM97473.1; -; mRNA.
DR EMBL; AY558233; AAS56559.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BK006946; DAA09863.1; -; Genomic_DNA.
DR PIR; S49743; S49743.
DR RefSeq; NP_013676.2; NM_001182394.1.
DR PDB; 4WW5; X-ray; 2.00 A; B=1-181.
DR PDB; 4WW7; X-ray; 1.67 A; B=1-181.
DR PDB; 4WW9; X-ray; 1.95 A; B=1-181.
DR PDB; 4WWA; X-ray; 2.95 A; B=1-181.
DR PDB; 4XAH; X-ray; 2.50 A; A/B=1-181.
DR PDBsum; 4WW5; -.
DR PDBsum; 4WW7; -.
DR PDBsum; 4WW9; -.
DR PDBsum; 4WWA; -.
DR PDBsum; 4XAH; -.
DR AlphaFoldDB; Q03705; -.
DR SMR; Q03705; -.
DR BioGRID; 35134; 101.
DR ComplexPortal; CPX-995; KEOPS complex.
DR DIP; DIP-6420N; -.
DR IntAct; Q03705; 7.
DR MINT; Q03705; -.
DR STRING; 4932.YML036W; -.
DR MaxQB; Q03705; -.
DR PaxDb; Q03705; -.
DR PRIDE; Q03705; -.
DR EnsemblFungi; YML036W_mRNA; YML036W; YML036W.
DR GeneID; 854972; -.
DR KEGG; sce:YML036W; -.
DR SGD; S000004500; CGI121.
DR VEuPathDB; FungiDB:YML036W; -.
DR eggNOG; KOG4066; Eukaryota.
DR GeneTree; ENSGT00390000012942; -.
DR HOGENOM; CLU_065847_1_1_1; -.
DR InParanoid; Q03705; -.
DR OMA; HNVHSEI; -.
DR BioCyc; YEAST:G3O-32635-MON; -.
DR PRO; PR:Q03705; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; Q03705; protein.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0000408; C:EKC/KEOPS complex; IDA:SGD.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0006310; P:DNA recombination; 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; IMP:SGD.
DR GO; GO:0002949; P:tRNA threonylcarbamoyladenosine modification; IBA:GO_Central.
DR Gene3D; 3.30.2380.10; -; 1.
DR InterPro; IPR013926; CGI121/TPRKB.
DR InterPro; IPR036504; CGI121/TPRKB_sf.
DR PANTHER; PTHR15840; PTHR15840; 1.
DR Pfam; PF08617; CGI-121; 1.
DR SUPFAM; SSF143870; SSF143870; 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..181
FT /note="EKC/KEOPS complex subunit CGI121"
FT /id="PRO_0000203259"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:4WW7"
FT STRAND 9..21
FT /evidence="ECO:0007829|PDB:4WW7"
FT HELIX 25..30
FT /evidence="ECO:0007829|PDB:4WW7"
FT TURN 31..34
FT /evidence="ECO:0007829|PDB:4WW5"
FT TURN 36..38
FT /evidence="ECO:0007829|PDB:4XAH"
FT STRAND 40..42
FT /evidence="ECO:0007829|PDB:4WW7"
FT HELIX 44..46
FT /evidence="ECO:0007829|PDB:4WW7"
FT HELIX 50..66
FT /evidence="ECO:0007829|PDB:4WW7"
FT STRAND 71..73
FT /evidence="ECO:0007829|PDB:4WW7"
FT HELIX 74..82
FT /evidence="ECO:0007829|PDB:4WW7"
FT STRAND 83..85
FT /evidence="ECO:0007829|PDB:4WW7"
FT HELIX 88..95
FT /evidence="ECO:0007829|PDB:4WW7"
FT STRAND 104..110
FT /evidence="ECO:0007829|PDB:4WW7"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:4WW9"
FT HELIX 118..128
FT /evidence="ECO:0007829|PDB:4WW7"
FT STRAND 131..134
FT /evidence="ECO:0007829|PDB:4WW7"
FT HELIX 138..144
FT /evidence="ECO:0007829|PDB:4WW7"
FT HELIX 147..153
FT /evidence="ECO:0007829|PDB:4WW7"
FT HELIX 165..178
FT /evidence="ECO:0007829|PDB:4WW7"
SQ SEQUENCE 181 AA; 20662 MW; B0B697F8AB578ED4 CRC64;
MVVSIIPQFP DIKVSLALFE QVKNAKEIRS KMSELSTSFA FIDPRLVCSG EQMYSAIYKT
LIEVKYNKMR TRNLNSECVL CLSPTSNISD AFLKFGIKDD SSQLICLKFH TNTDDVDKEQ
LRTIMTSIVK GQEIEFNDDN LSRFYDEALI RKIYKLSDDF KPQDVNGLSR ALVDAIQLRG
V
