KAE1_YEAST
ID KAE1_YEAST Reviewed; 386 AA.
AC P36132; D6VXA1;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 2.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=tRNA N6-adenosine threonylcarbamoyltransferase {ECO:0000255|HAMAP-Rule:MF_03180};
DE EC=2.3.1.234 {ECO:0000255|HAMAP-Rule:MF_03180};
DE AltName: Full=Kinase-associated endopeptidase 1;
DE AltName: Full=N6-L-threonylcarbamoyladenine synthase;
DE Short=t(6)A synthase;
DE AltName: Full=t(6)A37 threonylcarbamoyladenosine biosynthesis protein KAE1 {ECO:0000255|HAMAP-Rule:MF_03180};
DE AltName: Full=tRNA threonylcarbamoyladenosine biosynthesis protein KAE1 {ECO:0000255|HAMAP-Rule:MF_03180};
GN Name=KAE1 {ECO:0000255|HAMAP-Rule:MF_03180}; OrderedLocusNames=YKR038C;
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=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
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 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 [4]
RP IDENTIFICATION OF PROBABLE INITIATION SITE.
RX PubMed=12748633; DOI=10.1038/nature01644;
RA Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.;
RT "Sequencing and comparison of yeast species to identify genes and
RT regulatory elements.";
RL Nature 423:241-254(2003).
RN [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(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 INTERACTION WITH BUD32.
RX PubMed=14519092; DOI=10.1042/bj20030638;
RA Lopreiato R., Facchin S., Sartori G., Arrigoni G., Casonato S., Ruzzene M.,
RA Pinna L.A., Carignani G.;
RT "Analysis of the interaction between piD261/Bud32, an evolutionarily
RT conserved protein kinase of Saccharomyces cerevisiae, and the Grx4
RT glutaredoxin.";
RL Biochem. J. 377:395-405(2004).
RN [8]
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 [9]
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 [10]
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 [11]
RP FUNCTION IN T(6)A37 FORMATION.
RX PubMed=21285948; DOI=10.1038/emboj.2010.363;
RA El Yacoubi B., Hatin I., Deutsch C., Kahveci T., Rousset J.P.,
RA Iwata-Reuyl D., Murzin A.G., de Crecy-Lagard V.;
RT "A role for the universal Kae1/Qri7/YgjD (COG0533) family in tRNA
RT modification.";
RL EMBO J. 30:882-893(2011).
RN [12]
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 [13]
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 [14]
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. KAE1 likely
CC plays a direct catalytic role in this reaction, but requires other
CC protein(s) of the complex to fulfill this activity. The EKC/KEOPS
CC complex also promotes both telomere uncapping and telomere elongation.
CC The complex is required for efficient recruitment of transcriptional
CC coactivators. {ECO:0000255|HAMAP-Rule:MF_03180,
CC ECO:0000269|PubMed:16564010, ECO:0000269|PubMed:16874308,
CC ECO:0000269|PubMed:21183954, ECO:0000269|PubMed:21285948,
CC ECO:0000269|PubMed:21459853, ECO:0000269|PubMed:23258706,
CC ECO:0000269|PubMed:23620299}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine(37) in tRNA + L-threonylcarbamoyladenylate = AMP +
CC H(+) + N(6)-L-threonylcarbamoyladenosine(37) in tRNA;
CC Xref=Rhea:RHEA:37059, Rhea:RHEA-COMP:10162, Rhea:RHEA-COMP:10163,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:73682, ChEBI:CHEBI:74411,
CC ChEBI:CHEBI:74418, ChEBI:CHEBI:456215; EC=2.3.1.234;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03180};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03180};
CC Note=Binds 1 divalent metal cation per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_03180};
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:0000255|HAMAP-Rule:MF_03180, ECO:0000269|PubMed:16564010,
CC ECO:0000269|PubMed:16874308}.
CC -!- INTERACTION:
CC P36132; P53323: BUD32; NbExp=21; IntAct=EBI-26411, EBI-3809;
CC P36132; P46984: GON7; NbExp=8; IntAct=EBI-26411, EBI-26178;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03180,
CC ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03180,
CC ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16874308}.
CC -!- MISCELLANEOUS: Present with 1270 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the KAE1 / TsaD family. {ECO:0000255|HAMAP-
CC Rule:MF_03180}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA82112.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; Z28263; CAA82112.1; ALT_INIT; Genomic_DNA.
DR EMBL; BK006944; DAA09191.1; -; Genomic_DNA.
DR PIR; S38110; S38110.
DR RefSeq; NP_012964.2; NM_001179828.1.
DR AlphaFoldDB; P36132; -.
DR SMR; P36132; -.
DR BioGRID; 34169; 118.
DR ComplexPortal; CPX-995; KEOPS complex.
DR DIP; DIP-6421N; -.
DR IntAct; P36132; 4.
DR MINT; P36132; -.
DR STRING; 4932.YKR038C; -.
DR iPTMnet; P36132; -.
DR MaxQB; P36132; -.
DR PaxDb; P36132; -.
DR PRIDE; P36132; -.
DR EnsemblFungi; YKR038C_mRNA; YKR038C; YKR038C.
DR GeneID; 853910; -.
DR KEGG; sce:YKR038C; -.
DR SGD; S000001746; KAE1.
DR VEuPathDB; FungiDB:YKR038C; -.
DR eggNOG; KOG2708; Eukaryota.
DR GeneTree; ENSGT00940000153744; -.
DR HOGENOM; CLU_023208_2_2_1; -.
DR InParanoid; P36132; -.
DR OMA; MRIMCEE; -.
DR BioCyc; YEAST:G3O-32010-MON; -.
DR BRENDA; 2.3.1.234; 984.
DR PRO; PR:P36132; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P36132; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0000408; C:EKC/KEOPS complex; IDA:SGD.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0031490; F:chromatin DNA binding; IDA:SGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061711; F:N(6)-L-threonylcarbamoyladenine synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0051276; P:chromosome organization; 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; IPI:SGD.
DR GO; GO:0000722; P:telomere maintenance via recombination; IMP:SGD.
DR GO; GO:0006400; P:tRNA modification; IDA:SGD.
DR GO; GO:0070525; P:tRNA threonylcarbamoyladenosine metabolic process; IMP:SGD.
DR GO; GO:0002949; P:tRNA threonylcarbamoyladenosine modification; IC:ComplexPortal.
DR HAMAP; MF_01446; Kae1; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR000905; Gcp-like_dom.
DR InterPro; IPR017861; KAE1/TsaD.
DR InterPro; IPR034680; Kae1_archaea_euk.
DR InterPro; IPR017860; Peptidase_M22_CS.
DR PANTHER; PTHR11735; PTHR11735; 1.
DR PANTHER; PTHR11735:SF14; PTHR11735:SF14; 1.
DR Pfam; PF00814; TsaD; 1.
DR PRINTS; PR00789; OSIALOPTASE.
DR SUPFAM; SSF53067; SSF53067; 1.
DR TIGRFAMs; TIGR00329; gcp_kae1; 1.
DR PROSITE; PS01016; GLYCOPROTEASE; 1.
PE 1: Evidence at protein level;
KW Activator; Acyltransferase; Cytoplasm; Metal-binding; Nucleus;
KW Reference proteome; Transcription; Transcription regulation; Transferase;
KW tRNA processing.
FT CHAIN 1..386
FT /note="tRNA N6-adenosine threonylcarbamoyltransferase"
FT /id="PRO_0000096989"
FT BINDING 141
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03180"
FT BINDING 145
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03180"
FT BINDING 162..166
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03180"
FT BINDING 162
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03180"
FT BINDING 194
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03180"
FT BINDING 209
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03180"
FT BINDING 213
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03180"
FT BINDING 315
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03180"
FT BINDING 344
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03180"
SQ SEQUENCE 386 AA; 42748 MW; 76A73F2E9E26CF4C CRC64;
MVNLNTIPPK NGRDYYIALG LEGSANKLGV GIVKHPLLPK HANSDLSYDC EAEMLSNIRD
TYVTPPGEGF LPRDTARHHR NWCIRLIKQA LAEADIKSPT LDIDVICFTK GPGMGAPLHS
VVIAARTCSL LWDVPLVGVN HCIGHIEMGR EITKAQNPVV LYVSGGNTQV IAYSEKRYRI
FGETLDIAIG NCLDRFARTL KIPNEPSPGY NIEQLAKKAP HKENLVELPY TVKGMDLSMS
GILASIDLLA KDLFKGNKKN KILFDKTTGE QKVTVEDLCY SLQENLFAML VEITERAMAH
VNSNQVLIVG GVGCNVRLQE MMAQMCKDRA NGQVHATDNR FCIDNGVMIA QAGLLEYRMG
GIVKDFSETV VTQKFRTDEV YAAWRD
