ID KAE1B_HALWD Reviewed; 533 AA. AC Q18KI0; DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot. DT 25-JUL-2006, sequence version 1. DT 02-OCT-2024, entry version 112. 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=HQ_1341A; OS Haloquadratum walsbyi (strain DSM 16790 / HBSQ001). OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales; OC Haloferacaceae; Haloquadratum. OX NCBI_TaxID=362976; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 16790 / HBSQ001; RX PubMed=16820047; DOI=10.1186/1471-2164-7-169; RA Bolhuis H., Palm P., Wende A., Falb M., Rampp M., Rodriguez-Valera F., RA Pfeiffer F., Oesterhelt D.; RT "The genome of the square archaeon Haloquadratum walsbyi: life at the RT limits of water activity."; RL BMC Genomics 7:169-169(2006). 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}. 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; AM180088; CAJ51469.1; -; Genomic_DNA. DR RefSeq; WP_011570626.1; NC_008212.1. DR AlphaFoldDB; Q18KI0; -. DR SMR; Q18KI0; -. DR STRING; 362976.HQ_1341A; -. DR GeneID; 4194019; -. DR KEGG; hwa:HQ_1341A; -. DR eggNOG; arCOG01185; Archaea. DR HOGENOM; CLU_023208_2_2_2; -. DR Proteomes; UP000001975; 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: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; 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; 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..533 FT /note="Probable bifunctional tRNA FT threonylcarbamoyladenosine biosynthesis protein" FT /id="PRO_0000303649" FT DOMAIN 339..533 FT /note="Protein kinase" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01447" FT REGION 1..328 FT /note="Kae1" FT ACT_SITE 452 FT /note="Proton acceptor; for kinase activity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01447" FT BINDING 112 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01447" FT BINDING 116 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01447" FT BINDING 133..137 FT /ligand="L-threonylcarbamoyladenylate" FT /ligand_id="ChEBI:CHEBI:73682" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01447" FT BINDING 165 FT /ligand="L-threonylcarbamoyladenylate" FT /ligand_id="ChEBI:CHEBI:73682" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01447" FT BINDING 178 FT /ligand="L-threonylcarbamoyladenylate" FT /ligand_id="ChEBI:CHEBI:73682" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01447" FT BINDING 182 FT /ligand="L-threonylcarbamoyladenylate" FT /ligand_id="ChEBI:CHEBI:73682" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01447" FT BINDING 261 FT /ligand="L-threonylcarbamoyladenylate" FT /ligand_id="ChEBI:CHEBI:73682" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01447" FT BINDING 289 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01447" FT BINDING 347..354 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; 57542 MW; A504147E944A27A2 CRC64; MRILGIEGTA WAASAALYNT HDETIVIESD PYQPDSGGLH PREAAEHMST ALPEVISTIL ERAVSSGNTD AIGIDAIAFS RGPGLGPCLR VVGTAARTLT QALSVPLIGV NHMIAHLEIG RHQSGFTTPV CLNASGANAH LLGYHRRQYQ VLGETMDTGV GNAIDKFTRH LGWNHPGGPK VEAAATDGSY HDLPYVVKGM DFSFSGIMSA AKDAVDNEVP VVDVCTGLQE TIFAMLTEVA ERALSLTGSN ELVLGGGVGQ NDRLREMLST MCTARGASFY APESRFLRDN AGMIAVLGAA MYEAGQTISV NDSAVDPTFR PDAVTVTWRD DETSVTRTPA TLDKTPVRGA EAIVRRINDH VVKRRVEKSY RHPKLDRRLR AERTRAEARL TSAARRLGVP TPLIFDADPE TGTLVFEYVG ETDLAADLTV SRCHAVGQHL GRIHNAGFVH GDPTTRNVRV DSAQNYLIDF GLGYHTDHVE DHAMDLHVFI QSVTGTASDP APLITAFESG YAETGISTVQ SRLRDIESRG RYH //