ID   KAE1B_THEVO             Reviewed;         527 AA.
AC   Q978W6;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   27-MAR-2024, entry version 144.
DE   RecName: Full=Probable bifunctional tRNA threonylcarbamoyladenosine biosynthesis protein {ECO:0000255|HAMAP-Rule:MF_01447};
DE   Includes:
DE     RecName: Full=tRNA N6-adenosine threonylcarbamoyltransferase {ECO:0000255|HAMAP-Rule:MF_01447};
DE              EC=2.3.1.234 {ECO:0000255|HAMAP-Rule:MF_01447};
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_01447};
DE     AltName: Full=tRNA threonylcarbamoyladenosine biosynthesis protein Kae1 {ECO:0000255|HAMAP-Rule:MF_01447};
DE   Includes:
DE     RecName: Full=Serine/threonine-protein kinase Bud32 {ECO:0000255|HAMAP-Rule:MF_01447};
DE              EC=2.7.11.1 {ECO:0000255|HAMAP-Rule:MF_01447};
GN   OrderedLocusNames=TV1299; ORFNames=TVG1340828;
OS   Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC
OS   15438 / GSS1).
OC   Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC   Thermoplasmataceae; Thermoplasma.
OX   NCBI_TaxID=273116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1;
RX   PubMed=11121031; DOI=10.1073/pnas.97.26.14257;
RA   Kawashima T., Amano N., Koike H., Makino S., Higuchi S., Kawashima-Ohya Y.,
RA   Watanabe K., Yamazaki M., Kanehori K., Kawamoto T., Nunoshiba T.,
RA   Yamamoto Y., Aramaki H., Makino K., Suzuki M.;
RT   "Archaeal adaptation to higher temperatures revealed by genomic sequence of
RT   Thermoplasma volcanium.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:14257-14262(2000).
CC   -!- FUNCTION: Required for the formation of a threonylcarbamoyl group on
CC       adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning
CC       with adenine. Is a component of the KEOPS complex that is probably
CC       involved in the transfer of the threonylcarbamoyl moiety of
CC       threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. The Kae1 domain
CC       likely plays a direct catalytic role in this reaction. The Bud32 domain
CC       probably displays kinase activity that regulates Kae1 function.
CC       {ECO:0000255|HAMAP-Rule:MF_01447}.
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=2.7.11.1;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01447};
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=2.7.11.1; Evidence={ECO:0000255|HAMAP-Rule:MF_01447};
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_01447};
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01447};
CC       Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01447};
CC   -!- SUBUNIT: Component of the KEOPS complex that consists of Kae1, Bud32,
CC       Cgi121 and Pcc1; the whole complex dimerizes. {ECO:0000255|HAMAP-
CC       Rule:MF_01447}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01447}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the KAE1 / TsaD
CC       family. {ECO:0000255|HAMAP-Rule:MF_01447}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the protein kinase
CC       superfamily. Tyr protein kinase family. BUD32 subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01447}.
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DR   EMBL; BA000011; BAB60441.1; -; Genomic_DNA.
DR   RefSeq; WP_010917534.1; NC_002689.2.
DR   AlphaFoldDB; Q978W6; -.
DR   SMR; Q978W6; -.
DR   STRING; 273116.gene:9382106; -.
DR   PaxDb; 273116-14325538; -.
DR   DNASU; 1441416; -.
DR   GeneID; 1441416; -.
DR   KEGG; tvo:TVG1340828; -.
DR   eggNOG; arCOG01183; Archaea.
DR   eggNOG; arCOG01185; Archaea.
DR   HOGENOM; CLU_023208_2_2_2; -.
DR   OrthoDB; 6818at2157; -.
DR   PhylomeDB; Q978W6; -.
DR   Proteomes; UP000001017; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000408; C:EKC/KEOPS complex; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0061711; F:N(6)-L-threonylcarbamoyladenine synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0002949; P:tRNA threonylcarbamoyladenosine modification; IEA:InterPro.
DR   Gene3D; 3.30.420.40; -; 2.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   HAMAP; MF_01446; Kae1; 1.
DR   HAMAP; MF_01447; Kae1_Bud32_arch; 1.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR022495; Bud32.
DR   InterPro; IPR000905; Gcp-like_dom.
DR   InterPro; IPR017861; KAE1/TsaD.
DR   InterPro; IPR034680; Kae1_archaea_euk.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR017860; Peptidase_M22_CS.
DR   InterPro; IPR009220; tRNA_threonyl_synthase/kinase.
DR   InterPro; IPR008266; Tyr_kinase_AS.
DR   NCBIfam; TIGR03724; arch_bud32; 1.
DR   NCBIfam; TIGR03722; arch_KAE1; 1.
DR   NCBIfam; TIGR00329; gcp_kae1; 1.
DR   PANTHER; PTHR11735; TRNA N6-ADENOSINE THREONYLCARBAMOYLTRANSFERASE; 1.
DR   PANTHER; PTHR11735:SF14; TRNA N6-ADENOSINE THREONYLCARBAMOYLTRANSFERASE; 1.
DR   Pfam; PF00814; TsaD; 1.
DR   PIRSF; PIRSF036401; Gcp_STYKS; 1.
DR   PRINTS; PR00789; OSIALOPTASE.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS01016; GLYCOPROTEASE; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; ATP-binding; Cytoplasm; Iron; Kinase; Metal-binding;
KW   Multifunctional enzyme; Nucleotide-binding;
KW   Serine/threonine-protein kinase; Transferase; tRNA processing.
FT   CHAIN           1..527
FT                   /note="Probable bifunctional tRNA
FT                   threonylcarbamoyladenosine biosynthesis protein"
FT                   /id="PRO_0000303662"
FT   DOMAIN          330..527
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01447"
FT   REGION          1..324
FT                   /note="Kae1"
FT   ACT_SITE        445
FT                   /note="Proton acceptor; for kinase activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01447"
FT   BINDING         107
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01447"
FT   BINDING         111
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01447"
FT   BINDING         128..132
FT                   /ligand="L-threonylcarbamoyladenylate"
FT                   /ligand_id="ChEBI:CHEBI:73682"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01447"
FT   BINDING         128
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01447"
FT   BINDING         160
FT                   /ligand="L-threonylcarbamoyladenylate"
FT                   /ligand_id="ChEBI:CHEBI:73682"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01447"
FT   BINDING         173
FT                   /ligand="L-threonylcarbamoyladenylate"
FT                   /ligand_id="ChEBI:CHEBI:73682"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01447"
FT   BINDING         177
FT                   /ligand="L-threonylcarbamoyladenylate"
FT                   /ligand_id="ChEBI:CHEBI:73682"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01447"
FT   BINDING         257
FT                   /ligand="L-threonylcarbamoyladenylate"
FT                   /ligand_id="ChEBI:CHEBI:73682"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01447"
FT   BINDING         285
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01447"
FT   BINDING         333..341
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01447"
FT   BINDING         354
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01447"
SQ   SEQUENCE   527 AA;  58291 MW;  E66A4EF292645941 CRC64;
     MIVLGLEGTA HTISCGILDE NSIMANVSSM YKPKTGGIHP TQAAAHHVDK VSEVIAKAIE
     IAGIKPSDID LVAFSMGPGL GPSLRVTSTA ARTLAVTLKR PIIGVNHPLG HIEIGKRLSG
     AQDPVMLYVS GGNTQVIAHL NGRYRVLGET LDIGIGNMID KFARYAGIPF PGGPEIEKLA
     KDGRKLLTLP YSVKGMDTSF SGILTSALEY LKKGEPVEDI SFSIQETAFS MLVEVLERAL
     YVSGKDEVLM AGGVALNNRL REMVSEMGRE VDATTYMTDK NYCMDNGAMI AQAGLLMYKS
     GIRMNIEDTS INPRYRIDEV DAPWVIEKNV KYRDAGAESR IVNTDFYGRS AVKKIRIAKG
     YRLKELDERI RGERMKNEFT VIRRMRDAGI CVPIVYDYDP FEKTLTLSQI QGELLRDVIR
     ARPNVMGNVG HDVAVMHKNK ISHGDLTVNN IIVSDRICFI DASMGKVNAE LEDLAVDVYT
     LEDSINSLSE NGKTLMKEFK MSYRANFPQA NDVLNIVEDI RRRHRYV
//