ID   KAE1B_NATPD             Reviewed;         533 AA.
AC   Q3IMN2;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   27-MAR-2024, entry version 114.
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=NP_5070A;
OS   Natronomonas pharaonis (strain ATCC 35678 / DSM 2160 / CIP 103997 / JCM
OS   8858 / NBRC 14720 / NCIMB 2260 / Gabara) (Halobacterium pharaonis).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Haloarculaceae; Natronomonas.
OX   NCBI_TaxID=348780;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 /
RC   NCIMB 2260 / Gabara;
RX   PubMed=16169924; DOI=10.1101/gr.3952905;
RA   Falb M., Pfeiffer F., Palm P., Rodewald K., Hickmann V., Tittor J.,
RA   Oesterhelt D.;
RT   "Living with two extremes: conclusions from the genome sequence of
RT   Natronomonas pharaonis.";
RL   Genome Res. 15:1336-1343(2005).
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; CR936257; CAI50626.1; -; Genomic_DNA.
DR   RefSeq; WP_011324236.1; NC_007426.1.
DR   AlphaFoldDB; Q3IMN2; -.
DR   SMR; Q3IMN2; -.
DR   STRING; 348780.NP_5070A; -.
DR   EnsemblBacteria; CAI50626; CAI50626; NP_5070A.
DR   GeneID; 3702246; -.
DR   KEGG; nph:NP_5070A; -.
DR   eggNOG; arCOG01185; Archaea.
DR   HOGENOM; CLU_023208_2_2_2; -.
DR   OrthoDB; 6818at2157; -.
DR   Proteomes; UP000002698; 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-UniRule.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
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:0004712; F:protein serine/threonine/tyrosine kinase activity; IEA:UniProtKB-UniRule.
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:UniProtKB-UniRule.
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; IPR002575; Aminoglycoside_PTrfase.
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   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; PF01636; APH; 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.
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..533
FT                   /note="Probable bifunctional tRNA
FT                   threonylcarbamoyladenosine biosynthesis protein"
FT                   /id="PRO_0000303659"
FT   DOMAIN          338..533
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01447"
FT   REGION          1..329
FT                   /note="Kae1"
FT   ACT_SITE        452
FT                   /note="Proton acceptor; for kinase activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01447"
FT   BINDING         113
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01447"
FT   BINDING         117
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01447"
FT   BINDING         134..138
FT                   /ligand="L-threonylcarbamoyladenylate"
FT                   /ligand_id="ChEBI:CHEBI:73682"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01447"
FT   BINDING         166
FT                   /ligand="L-threonylcarbamoyladenylate"
FT                   /ligand_id="ChEBI:CHEBI:73682"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01447"
FT   BINDING         179
FT                   /ligand="L-threonylcarbamoyladenylate"
FT                   /ligand_id="ChEBI:CHEBI:73682"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01447"
FT   BINDING         183
FT                   /ligand="L-threonylcarbamoyladenylate"
FT                   /ligand_id="ChEBI:CHEBI:73682"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01447"
FT   BINDING         262
FT                   /ligand="L-threonylcarbamoyladenylate"
FT                   /ligand_id="ChEBI:CHEBI:73682"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01447"
FT   BINDING         290
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01447"
FT   BINDING         345..352
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01447"
FT   BINDING         363
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01447"
SQ   SEQUENCE   533 AA;  57263 MW;  03E030815ECABE24 CRC64;
     MTRVLGIEGT AWCASAAVFD AETDAVFIDS DAYVPESGGI HPREAAEHMR EAVPSVVEAA
     LDHVESNWGD PADAIDAVAF SRGPGLGPCL RIAGTAARSL AGTLSCPLVG VNHMVAHLEI
     GRHRSGFESP VCLNASGANA HVLGYHNGRY RVLGETMDTG VGNAIDKFTR HVGWSHPGGP
     KVESHAEDGD YVELPYVVKG MDFSFSGIMS AAKQAYDDGT PVADVCCGLQ ETIFAMLAEV
     SERALSLTGA DELVVGGGVA QNSRLQEMLT QMCENRGAAI YVPEPRFLRD NAGMIAVLGA
     KMYEAGDIIS IPESGVRPDF RPDEVPVSWR DDEAVARPVP TDERRQGAEA VVDIDADGGR
     VTKRRLEKAY RHPVLDSRLR SQRTRSEARL TSEARRQGVP TPVVYDVDPD AGRLVFQYVG
     DADLKTALSE SAVRDVGRHL AACHAAGFVH GDPTPRNVRV GEDRAFLIDF GLGYYTDAVE
     DYAMDLHVFE GALGGTADDP TAQITAFEDA YRSAGDGAVV DHLREIETRG RYQ
//