KAE1B_PICTO
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 03-AUG-2022, entry version 125.
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).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Picrophilaceae; Picrophilus.
OX NCBI_TaxID=263820;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828;
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;
CC Evidence={ECO:0000255|HAMAP-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; AE017261; AAT42959.1; -; Genomic_DNA.
DR RefSeq; WP_011177175.1; NC_005877.1.
DR AlphaFoldDB; Q6L243; -.
DR SMR; Q6L243; -.
DR STRING; 263820.PTO0374; -.
DR PRIDE; Q6L243; -.
DR EnsemblBacteria; AAT42959; AAT42959; 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 OMA; GETMDTG; -.
DR OrthoDB; 9881at2157; -.
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:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0002949; P:tRNA threonylcarbamoyladenosine modification; IEA:InterPro.
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; IPR022449; Kae1_arc.
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 PANTHER; PTHR11735; PTHR11735; 1.
DR PANTHER; PTHR11735:SF14; PTHR11735:SF14; 1.
DR Pfam; PF00814; TsaD; 1.
DR PIRSF; PIRSF036401; Gcp_STYKS; 1.
DR PRINTS; PR00789; OSIALOPTASE.
DR SUPFAM; SSF53067; SSF53067; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR TIGRFAMs; TIGR03724; arch_bud32; 1.
DR TIGRFAMs; TIGR03722; arch_KAE1; 1.
DR TIGRFAMs; TIGR00329; gcp_kae1; 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; Reference proteome;
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
