ID   B9LSM0_HALLT            Unreviewed;       571 AA.
AC   B9LSM0;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   04-NOV-2026, entry version 107.
DE   RecName: Full=Probable bifunctional tRNA threonylcarbamoyladenosine biosynthesis protein {ECO:0000256|HAMAP-Rule:MF_01447};
DE   Includes:
DE     RecName: Full=tRNA N6-adenosine threonylcarbamoyltransferase {ECO:0000256|HAMAP-Rule:MF_01447};
DE              EC=2.3.1.234 {ECO:0000256|HAMAP-Rule:MF_01447};
DE     AltName: Full=tRNA threonylcarbamoyladenosine biosynthesis protein Kae1 {ECO:0000256|HAMAP-Rule:MF_01447};
DE     AltName: Full=t(6)A37 threonylcarbamoyladenosine biosynthesis protein Kae1 {ECO:0000256|HAMAP-Rule:MF_01447};
DE   Includes:
DE     RecName: Full=Serine/threonine-protein kinase Bud32 {ECO:0000256|HAMAP-Rule:MF_01447};
DE              EC=2.7.11.1 {ECO:0000256|HAMAP-Rule:MF_01447};
GN   OrderedLocusNames=Hlac_2392 {ECO:0000313|EMBL:ACM57967.1};
OS   Halorubrum lacusprofundi (strain ATCC 49239 / DSM 5036 / JCM 8891 / ACAM
OS   34).
OC   Archaea; Methanobacteriati; Methanobacteriota; Stenosarchaea group;
OC   Halobacteria; Halobacteriales; Haloferacaceae; Halorubrum.
OX   NCBI_TaxID=416348 {ECO:0000313|EMBL:ACM57967.1, ECO:0000313|Proteomes:UP000000740};
RN   [1] {ECO:0000313|EMBL:ACM57967.1, ECO:0000313|Proteomes:UP000000740}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49239 / DSM 5036 / JCM 8891 / ACAM 34
RC   {ECO:0000313|Proteomes:UP000000740};
RX   PubMed=27617060; DOI=10.1186/s40793-016-0194-2;
RA   Anderson I.J., DasSarma P., Lucas S., Copeland A., Lapidus A.,
RA   Del Rio T.G., Tice H., Dalin E., Bruce D.C., Goodwin L., Pitluck S.,
RA   Sims D., Brettin T.S., Detter J.C., Han C.S., Larimer F., Hauser L.,
RA   Land M., Ivanova N., Richardson P., Cavicchioli R., DasSarma S.,
RA   Woese C.R., Kyrpides N.C.;
RT   "Complete genome sequence of the Antarctic Halorubrum lacusprofundi type
RT   strain ACAM 34.";
RL   Stand. Genomic Sci. 11:70-70(2016).
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:0000256|HAMAP-Rule:MF_01447}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP +
CC         H(+); 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:0000256|ARBA:ARBA00048679, ECO:0000256|HAMAP-
CC         Rule:MF_01447};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] +
CC         ADP + H(+); Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC         COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00047899, ECO:0000256|HAMAP-
CC         Rule:MF_01447};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-threonylcarbamoyladenylate + adenosine(37) in tRNA = N(6)-L-
CC         threonylcarbamoyladenosine(37) in tRNA + AMP + H(+);
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:0000256|ARBA:ARBA00048117, ECO:0000256|HAMAP-
CC         Rule:MF_01447};
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01447};
CC       Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000256|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:0000256|HAMAP-
CC       Rule:MF_01447}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01447}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. BUD32 family.
CC       {ECO:0000256|ARBA:ARBA00010630}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the protein kinase
CC       superfamily. Tyr protein kinase family. BUD32 subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_01447}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the KAE1 / TsaD
CC       family. {ECO:0000256|HAMAP-Rule:MF_01447}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_01447}.
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DR   EMBL; CP001365; ACM57967.1; -; Genomic_DNA.
DR   RefSeq; WP_015911087.1; NC_012029.1.
DR   GeneID; 7400510; -.
DR   KEGG; hla:Hlac_2392; -.
DR   eggNOG; arCOG01185; Archaea.
DR   HOGENOM; CLU_023208_2_2_2; -.
DR   OMA; AAEHMHD; -.
DR   Gene3D; 3.30.420.40; -; 2.
DR   Gene3D; 3.30.200.20; Phosphorylase Kinase, domain 1; 1.
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   PANTHER; PTHR11735; TRNA N6-ADENOSINE THREONYLCARBAMOYLTRANSFERASE; 1.
DR   PANTHER; PTHR11735:SF14; TRNA N6-ADENOSINE THREONYLCARBAMOYLTRANSFERASE; 1.
DR   Pfam; PF00814; TsaD; 1.
DR   PRINTS; PR00789; OSIALOPTASE.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   NCBIfam; TIGR03724; arch_bud32; 1.
DR   NCBIfam; TIGR03722; arch_KAE1; 1.
DR   NCBIfam; TIGR00329; gcp_kae1; 1.
DR   NCBIfam; NF007174; PRK09605.1; 1.
DR   PROSITE; PS01016; GLYCOPROTEASE; 1.
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:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0061711; F:tRNA N(6)-L-threonylcarbamoyladenine synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0002949; P:tRNA threonylcarbamoyladenosine modification; IEA:UniProtKB-UniRule.
DR   Proteomes; UP000000740; Chromosome 1.
DR   AlphaFoldDB; B9LSM0; -.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315, ECO:0000256|HAMAP-
KW   Rule:MF_01447};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_01447};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01447};
KW   Hydrolase {ECO:0000313|EMBL:ACM57967.1};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_01447};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_01447};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_01447};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268, ECO:0000256|HAMAP-
KW   Rule:MF_01447};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_01447}; Reference proteome {ECO:0000313|Proteomes:UP000000740};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW   ECO:0000256|HAMAP-Rule:MF_01447};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_01447};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW   Rule:MF_01447}.
FT   DOMAIN          27..301
FT                   /note="Gcp-like"
FT                   /evidence="ECO:0000259|Pfam:PF00814"
FT   REGION          1..334
FT                   /note="Kae1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01447"
FT   REGION          318..359
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        347..359
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        471
FT                   /note="Proton acceptor; for kinase activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01447"
FT   BINDING         110
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01447"
FT   BINDING         114
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01447"
FT   BINDING         131..135
FT                   /ligand="L-threonylcarbamoyladenylate"
FT                   /ligand_id="ChEBI:CHEBI:73682"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01447"
FT   BINDING         163
FT                   /ligand="L-threonylcarbamoyladenylate"
FT                   /ligand_id="ChEBI:CHEBI:73682"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01447"
FT   BINDING         176
FT                   /ligand="L-threonylcarbamoyladenylate"
FT                   /ligand_id="ChEBI:CHEBI:73682"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01447"
FT   BINDING         180
FT                   /ligand="L-threonylcarbamoyladenylate"
FT                   /ligand_id="ChEBI:CHEBI:73682"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01447"
FT   BINDING         267
FT                   /ligand="L-threonylcarbamoyladenylate"
FT                   /ligand_id="ChEBI:CHEBI:73682"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01447"
FT   BINDING         295
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01447"
FT   BINDING         355..363
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01447"
FT   BINDING         380
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01447"
SQ   SEQUENCE   571 AA;  60894 MW;  1C521D374E76AAC1 CRC64;
     MRVLGIEGTA WCASAALYDA ETDSVLIESN PYEPDSGGIH PREAAEHMSE AIPEVVDAVL
     TTAEAEHGPD AIDAVAFSRG PGLGPCLRIV GTAARSLAGT LDVPLVGVNH MVAHLEIGRH
     QSGFENPVCL NTSGANAHLL GYHDGRYRVL GETMDAGVGN AIDKFTRHVG WDHPGGPKVE
     AAARRYAEGN DGPEDLLDLP YVVKGMDFSF SGISSAANDA YDDGVPVEEI CFSLQEHVFA
     MLTEVSERAL SLTGADELVL GGGVAQNDRL REMLASMCAA RGARFHAPDS RFLRDNAGMI
     AVLGAKMAQA GDTVPISESA IDPNFRPDQV PVTWRSGESV ARGRAPGSDD KTDADRRGAE
     ATVEIVPSGE PDAADRRVIK RRVPKEYRHP GLDRTLRRDR TVAEARLTSE ARQAGVTTPL
     VYDADVPNAT LTLQYVGDRD LAAALDGGTE RVAAVGRYLA RLHDAGIVHG DPTTRNVRVG
     VGDSDTQTGD GEANGTTAVD DRTALIDFGL AYHTGHVEDH AMDLHVFEGS VRATAIDPDP
     LIEAFEDGYA TVGDDDVLDR LRDVEGRGRY R
//