KAE1_COCIM
ID KAE1_COCIM Reviewed; 371 AA.
AC Q1E406; J3KMC5;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 99.
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=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}; ORFNames=CIMG_02707;
OS Coccidioides immitis (strain RS) (Valley fever fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX NCBI_TaxID=246410;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RS;
RX PubMed=19717792; DOI=10.1101/gr.087551.108;
RA Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA Henn M.R., Birren B.W., Taylor J.W.;
RT "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT and their relatives.";
RL Genome Res. 19:1722-1731(2009).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=RS;
RX PubMed=20516208; DOI=10.1101/gr.103911.109;
RA Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA Taylor J.W., Rounsley S.D.;
RT "Population genomic sequencing of Coccidioides fungi reveals recent
RT hybridization and transposon control.";
RL Genome Res. 20:938-946(2010).
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 -!- 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}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03180}.
CC Nucleus {ECO:0000255|HAMAP-Rule:MF_03180}.
CC -!- SIMILARITY: Belongs to the KAE1 / TsaD family. {ECO:0000255|HAMAP-
CC Rule:MF_03180}.
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DR EMBL; GG704911; EAS37353.3; -; Genomic_DNA.
DR RefSeq; XP_001248936.1; XM_001248935.2.
DR AlphaFoldDB; Q1E406; -.
DR SMR; Q1E406; -.
DR STRING; 246410.Q1E406; -.
DR PRIDE; Q1E406; -.
DR EnsemblFungi; EAS37353; EAS37353; CIMG_02707.
DR GeneID; 4567634; -.
DR KEGG; cim:CIMG_02707; -.
DR VEuPathDB; FungiDB:CIMG_02707; -.
DR InParanoid; Q1E406; -.
DR OMA; MRIMCEE; -.
DR OrthoDB; 829465at2759; -.
DR Proteomes; UP000001261; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000408; C:EKC/KEOPS complex; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0002949; P:tRNA threonylcarbamoyladenosine modification; IEA:UniProtKB-UniRule.
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 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.
PE 3: Inferred from homology;
KW Activator; Acyltransferase; Cytoplasm; Metal-binding; Nucleus;
KW Reference proteome; Transcription; Transcription regulation; Transferase;
KW tRNA processing.
FT CHAIN 1..371
FT /note="tRNA N6-adenosine threonylcarbamoyltransferase"
FT /id="PRO_0000278932"
FT BINDING 114
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03180"
FT BINDING 118
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03180"
FT BINDING 135..139
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03180"
FT BINDING 135
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03180"
FT BINDING 167
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03180"
FT BINDING 182
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03180"
FT BINDING 186
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03180"
FT BINDING 301
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03180"
FT BINDING 329
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03180"
SQ SEQUENCE 371 AA; 40282 MW; AD564EF0AE9182FA CRC64;
MIAIGLEGSA NKLGVGIILH PDNGGEPRVL ANIRHTYVSP PGEGFLPKDT AKHHRKWVVS
LVKAALKEAE IGVSDVDCIC YTKGPGMGPP LQSVALAART LSLLWGKQLV GVNHCVGHIE
MGRYITGAQN PIVLYVSGGN TQVIAYSSQR YRIFGETLDI AVGNCLDRFA RTLHISNDPA
PGYNIEQLAK KGKRLVELPY TVKGMDCSFS GILAAIDALA AAYGLSGDQQ AKENIGLTED
ALKLKVDSVD KYNNEGGIPT REDLCFSLQE TVFSMLVEIT ERAMAHVGSR EVLIVGGVGC
NERLQEMMGI MARDRGGNVF ATDERFCIDN GIMIAQAGIL AYKTGFTTKL EDSTCTQRFR
TDEVFVQWRD D
