ID   KAE1B_HALMA             Reviewed;         548 AA.
AC   P36174; Q5UZK8;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 2.
DT   27-MAR-2024, entry version 147.
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=rrnAC2490;
OS   Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM
OS   B-1809) (Halobacterium marismortui).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Haloarculaceae; Haloarcula.
OX   NCBI_TaxID=272569;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX   PubMed=15520287; DOI=10.1101/gr.2700304;
RA   Baliga N.S., Bonneau R., Facciotti M.T., Pan M., Glusman G., Deutsch E.W.,
RA   Shannon P., Chiu Y., Weng R.S., Gan R.R., Hung P., Date S.V., Marcotte E.,
RA   Hood L., Ng W.V.;
RT   "Genome sequence of Haloarcula marismortui: a halophilic archaeon from the
RT   Dead Sea.";
RL   Genome Res. 14:2221-2234(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-226.
RX   PubMed=1468549; DOI=10.1016/0014-5793(92)81473-y;
RA   Arndt E., Steffens C.;
RT   "Nucleotide sequence of the genes for ribosomal proteins HS15 and HSH from
RT   Haloarcula marismortui: an archaeon-specific gene cluster.";
RL   FEBS Lett. 314:211-214(1992).
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; AY596297; AAV47295.1; -; Genomic_DNA.
DR   EMBL; X70117; CAA49709.1; -; Genomic_DNA.
DR   PIR; S27037; S27037.
DR   RefSeq; WP_011224258.1; NZ_CP039138.1.
DR   AlphaFoldDB; P36174; -.
DR   SMR; P36174; -.
DR   STRING; 272569.rrnAC2490; -.
DR   PaxDb; 272569-rrnAC2490; -.
DR   EnsemblBacteria; AAV47295; AAV47295; rrnAC2490.
DR   GeneID; 40153386; -.
DR   KEGG; hma:rrnAC2490; -.
DR   PATRIC; fig|272569.17.peg.3100; -.
DR   eggNOG; arCOG01185; Archaea.
DR   HOGENOM; CLU_023208_2_2_2; -.
DR   Proteomes; UP000001169; Chromosome I.
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; 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; IPR000719; Prot_kinase_dom.
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; 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; PS50011; PROTEIN_KINASE_DOM; 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..548
FT                   /note="Probable bifunctional tRNA
FT                   threonylcarbamoyladenosine biosynthesis protein"
FT                   /id="PRO_0000096977"
FT   DOMAIN          349..548
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01447"
FT   REGION          1..338
FT                   /note="Kae1"
FT   REGION          390..413
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        460
FT                   /note="Proton acceptor; for kinase activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01447"
FT   BINDING         122
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01447"
FT   BINDING         126
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01447"
FT   BINDING         143..147
FT                   /ligand="L-threonylcarbamoyladenylate"
FT                   /ligand_id="ChEBI:CHEBI:73682"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01447"
FT   BINDING         175
FT                   /ligand="L-threonylcarbamoyladenylate"
FT                   /ligand_id="ChEBI:CHEBI:73682"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01447"
FT   BINDING         188
FT                   /ligand="L-threonylcarbamoyladenylate"
FT                   /ligand_id="ChEBI:CHEBI:73682"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01447"
FT   BINDING         192
FT                   /ligand="L-threonylcarbamoyladenylate"
FT                   /ligand_id="ChEBI:CHEBI:73682"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01447"
FT   BINDING         271
FT                   /ligand="L-threonylcarbamoyladenylate"
FT                   /ligand_id="ChEBI:CHEBI:73682"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01447"
FT   BINDING         299
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01447"
FT   BINDING         355..362
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01447"
FT   BINDING         371
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01447"
SQ   SEQUENCE   548 AA;  59796 MW;  A708A918A7FEB672 CRC64;
     MRILGIEGTA WAASASVFET PDPARVTDDD HVFIETDAYA PDSGGIHPRE AAEHMGEAIP
     TVVETAIEHT HGRAGRDGDD SAPIDAVAFA RGPGLGPCLR IVATAARAVA QRFDVPLVGV
     NHMVAHLEVG RHRSGFDSPV CLNASGANAH ILGYRNGRYR VLGETMDTGV GNAIDKFTRH
     IGWSHPGGPK VEQHARDGEY HELPYVVKGM DFSFSGIMSA AKQAVDDGVP VENVCRGMEE
     TIFAMLTEVS ERALSLTGAD ELVLGGGVGQ NARLQRMLGE MCEQREAEFY APENRFLRDN
     AGMIAMLGAK MYAAGDTIAI EDSRIDSNFR PDEVAVTWRG PEESVDSYRM GGDEVQGAEA
     TVHFDGDRVI KVRVPRSYRH PTLDERLRTE RTRQEARLTS EARRNGVPTP LVRDVDPQES
     RIVFQRVGDT DLREGLSEGR VADVGRWLAR IHDAGFVHGD PTTRNVRVGG RDEQADRTTL
     IDFGLGYYTQ EAEDHAMDLH VLAQSLAGTA DDPETLLSAA EDAYRTESDH ADAVFASLDD
     IEGRGRYQ
//