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 14-MAY-2014, entry version 63. DE RecName: Full=Probable bifunctional tRNA threonylcarbamoyladenosine biosynthesis protein; DE Includes: DE RecName: Full=tRNA N6-adenosine threonylcarbamoyltransferase; DE EC=2.6.99.4; DE AltName: Full=N6-L-threonylcarbamoyladenine synthase; DE Short=t(6)A synthase; DE AltName: Full=t(6)A37 threonylcarbamoyladenosine biosynthesis protein Kae1; DE AltName: Full=tRNA threonylcarbamoyladenosine biosynthesis protein Kae1; DE Includes: DE RecName: Full=Serine/threonine-protein kinase Bud32; DE EC=2.7.11.1; GN OrderedLocusNames=HQ_1341A; OS Haloquadratum walsbyi (strain DSM 16790 / HBSQ001). OC Archaea; Euryarchaeota; Halobacteria; Halobacteriales; OC Halobacteriaceae; 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 CC on adenosine at position 37 (t(6)A37) in tRNAs that read codons CC beginning with adenine. Is a component of the KEOPS complex that CC is probably involved in the transfer of the threonylcarbamoyl CC moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. CC The Kae1 domain likely plays a direct catalytic role in this CC reaction. The Bud32 domain probably displays kinase activity that CC regulates Kae1 function (By similarity). CC -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein. CC -!- CATALYTIC ACTIVITY: L-threonylcarbamoyladenylate + adenine(37) in CC tRNA = AMP + N(6)-L-threonylcarbamoyladenine(37) in tRNA. CC -!- COFACTOR: Binds 1 Fe(2+) ion per subunit (By similarity). CC -!- SUBUNIT: Component of the KEOPS complex that consists of Kae1, CC Bud32, Cgi121 and Pcc1; the whole complex dimerizes (By CC similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: In the N-terminal section; belongs to the KAE1 / TsaD CC family. CC -!- SIMILARITY: In the C-terminal section; belongs to the protein CC kinase superfamily. Tyr protein kinase family. BUD32 subfamily. CC -!- SIMILARITY: Contains 1 protein kinase domain. 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; YP_657116.1; NC_008212.1. DR ProteinModelPortal; Q18KI0; -. DR STRING; 362976.HQ1341A; -. DR EnsemblBacteria; CAJ51469; CAJ51469; HQ_1341A. DR GeneID; 4194019; -. DR KEGG; hwa:HQ1341A; -. DR eggNOG; COG0533; -. DR HOGENOM; HOG000109569; -. DR KO; K15904; -. DR OMA; RDNAGMI; -. DR BioCyc; HWAL362976:GJSR-360-MONOMER; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. 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-HAMAP. DR GO; GO:0016747; F:transferase activity, transferring acyl groups other than amino-acyl groups; IEA:UniProtKB-HAMAP. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0070526; P:threonylcarbamoyladenosine biosynthetic process; IEA:UniProtKB-HAMAP. DR HAMAP; MF_01447; Kae1_Bud32_arch; 1. DR InterPro; IPR022495; Bud32. DR InterPro; IPR000905; Gcp-like_dom. DR InterPro; IPR022449; Kae1. DR InterPro; IPR017861; KAE1/YgjD. DR InterPro; IPR011009; Kinase-like_dom. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR009220; tRNA_threonyl_synthase/kinase. DR PANTHER; PTHR11735:SF6; PTHR11735:SF6; 1. DR Pfam; PF00814; Peptidase_M22; 1. DR PIRSF; PIRSF036401; Gcp_STYKS; 1. DR PRINTS; PR00789; OSIALOPTASE. 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; PS50011; PROTEIN_KINASE_DOM; 1. PE 3: Inferred from homology; KW Acyltransferase; ATP-binding; Complete proteome; Cytoplasm; Iron; KW Kinase; Metal-binding; Multifunctional enzyme; Nucleotide-binding; KW Serine/threonine-protein kinase; Transferase; tRNA processing. FT CHAIN 1 533 Probable bifunctional tRNA FT threonylcarbamoyladenosine biosynthesis FT protein. FT /FTId=PRO_0000303649. FT DOMAIN 339 533 Protein kinase. FT NP_BIND 347 354 ATP (By similarity). FT REGION 1 328 Kae1. FT REGION 133 137 Threonylcarbamoyl-AMP binding (By FT similarity). FT ACT_SITE 452 452 Proton acceptor; for kinase activity (By FT similarity). FT METAL 112 112 Iron (By similarity). FT METAL 116 116 Iron (By similarity). FT METAL 289 289 Iron (By similarity). FT BINDING 165 165 Threonylcarbamoyl-AMP (By similarity). FT BINDING 178 178 Threonylcarbamoyl-AMP; via amide nitrogen FT (By similarity). FT BINDING 182 182 Threonylcarbamoyl-AMP (By similarity). FT BINDING 261 261 Threonylcarbamoyl-AMP (By similarity). FT BINDING 363 363 ATP (By similarity). 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 //