ID   KAE1B_PICTO             Reviewed;         529 AA.
AC   Q6L243;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 134.
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=PTO0374;
OS   Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC
OS   100828 / KAW 2/3).
OC   Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC   Picrophilaceae; Picrophilus.
OX   NCBI_TaxID=1122961;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828 / KAW 2/3;
RX   PubMed=15184674; DOI=10.1073/pnas.0401356101;
RA   Fuetterer O., Angelov A., Liesegang H., Gottschalk G., Schleper C.,
RA   Schepers B., Dock C., Antranikian G., Liebl W.;
RT   "Genome sequence of Picrophilus torridus and its implications for life
RT   around pH 0.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9091-9096(2004).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE017261; AAT42959.1; -; Genomic_DNA.
DR   RefSeq; WP_011177175.1; NC_005877.1.
DR   AlphaFoldDB; Q6L243; -.
DR   SMR; Q6L243; -.
DR   STRING; 263820.PTO0374; -.
DR   PaxDb; 263820-PTO0374; -.
DR   GeneID; 2845198; -.
DR   KEGG; pto:PTO0374; -.
DR   PATRIC; fig|263820.9.peg.398; -.
DR   eggNOG; arCOG01183; Archaea.
DR   eggNOG; arCOG01185; Archaea.
DR   HOGENOM; CLU_023208_2_2_2; -.
DR   InParanoid; Q6L243; -.
DR   OrthoDB; 6818at2157; -.
DR   Proteomes; UP000000438; 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; 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; PF01163; RIO1; 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; 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..529
FT                   /note="Probable bifunctional tRNA
FT                   threonylcarbamoyladenosine biosynthesis protein"
FT                   /id="PRO_0000303660"
FT   DOMAIN          331..529
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01447"
FT   REGION          1..324
FT                   /note="Kae1"
FT   ACT_SITE        447
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         335..342
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01447"
FT   BINDING         355
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01447"
SQ   SEQUENCE   529 AA;  60103 MW;  230A4D3F0DA22B02 CRC64;
     MIVLGLEGTA HTISAGIVDE KSILSNVSST YVPEHGGIHP REAAVHHADK IYDVIKRSFD
     NAGLKPEDLD LIAFSMGPGL GPCLRVVSTA ARALSIKYSK PLLGVNHPLG HVEIGRKLSG
     ARDPIMLYIS GGNTQVIAHL NGRYRVLGET MDIGLGNMLD KFARDLGIPF PGGPVIERMA
     LDGKDLLELP YSVKGMDTSF SGIYTAAKRY LSLGKNKNDI CYSLQETSFS MVVEVLERAM
     YYTNKNEILL AGGVARNDRL RSMVNDMARD SGYKAYLTDK EYCMDNGAMI AQAGMLMYMH
     GARQDIMETR INQRFRIDEV PAPWIKDENS ISFKDKGAES IITNGEFYGR SVVFKKRPEK
     SYRDKRLDLK IRLERMKNEF YIMYYLHKTG NAPIVYDFDR FDMVLTIERI NGLTMNDYFK
     SKYDENVIRM IADAVAKMHG LRISHGDLTP NNIIISDKIY FIDTSMGHLR CSDEDIADDL
     FLLYESMKSL YVNGHEMIKH FENEYSKNVE DYNYYKELIK KIESRRRYV
//