KAE1B_METJA
ID KAE1B_METJA Reviewed; 535 AA.
AC Q58530;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 03-AUG-2022, entry version 156.
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=MJ1130;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (3.05 ANGSTROMS) IN COMPLEX WITH AN ATP ANALOG.
RX PubMed=19172740; DOI=10.1038/emboj.2008.157;
RA Hecker A., Lopreiato R., Graille M., Collinet B., Forterre P., Libri D.,
RA van Tilbeurgh H.;
RT "Structure of the archaeal Kae1/Bud32 fusion protein MJ1130: a model for
RT the eukaryotic EKC/KEOPS subcomplex.";
RL EMBO J. 27:2340-2351(2008).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.67 ANGSTROMS) IN COMPLEXES WITH MAGNESIUM AND
RP CGI121, FUNCTION, SUBUNIT, AND ACTIVITY REGULATION.
RX PubMed=18951093; DOI=10.1016/j.molcel.2008.10.002;
RA Mao D.Y., Neculai D., Downey M., Orlicky S., Haffani Y.Z., Ceccarelli D.F.,
RA Ho J.S., Szilard R.K., Zhang W., Ho C.S., Wan L., Fares C., Rumpel S.,
RA Kurinov I., Arrowsmith C.H., Durocher D., Sicheri F.;
RT "Atomic structure of the KEOPS complex: an ancient protein kinase-
RT containing molecular machine.";
RL Mol. Cell 32:259-275(2008).
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 (By similarity).
CC The Bud32 domain probably displays kinase activity that regulates Kae1
CC function. In vitro, exhibits low ATPase activity, but does not bind DNA
CC and does not have endonuclease activity. {ECO:0000255|HAMAP-
CC Rule:MF_01447, ECO:0000269|PubMed:18951093}.
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 -!- ACTIVITY REGULATION: Activity provided by the Kae1 region seems to be
CC regulated via phosphorylation by the protein kinase Bud32, which is
CC itself activated by Cgi121. {ECO:0000269|PubMed:18951093}.
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, ECO:0000269|PubMed:18951093,
CC ECO:0000269|PubMed:19172740}.
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; L77117; AAB99132.1; -; Genomic_DNA.
DR RefSeq; WP_010870641.1; NC_000909.1.
DR PDB; 2VWB; X-ray; 3.05 A; A/B=1-535.
DR PDB; 3EN9; X-ray; 2.67 A; A/B=1-535.
DR PDB; 3ENH; X-ray; 3.60 A; A/B=1-535.
DR PDB; 5JMV; X-ray; 3.39 A; A/B/C=1-335.
DR PDBsum; 2VWB; -.
DR PDBsum; 3EN9; -.
DR PDBsum; 3ENH; -.
DR PDBsum; 5JMV; -.
DR AlphaFoldDB; Q58530; -.
DR SMR; Q58530; -.
DR STRING; 243232.MJ_1130; -.
DR EnsemblBacteria; AAB99132; AAB99132; MJ_1130.
DR GeneID; 1452026; -.
DR KEGG; mja:MJ_1130; -.
DR eggNOG; arCOG01183; Archaea.
DR eggNOG; arCOG01185; Archaea.
DR HOGENOM; CLU_023208_2_2_2; -.
DR InParanoid; Q58530; -.
DR OMA; GETMDTG; -.
DR OrthoDB; 9881at2157; -.
DR PhylomeDB; Q58530; -.
DR EvolutionaryTrace; Q58530; -.
DR Proteomes; UP000000805; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0000408; C:EKC/KEOPS complex; IBA:GO_Central.
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:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0002949; P:tRNA threonylcarbamoyladenosine modification; IEA:UniProtKB-UniRule.
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; IPR022449; Kae1_arc.
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 InterPro; IPR008266; Tyr_kinase_AS.
DR PANTHER; PTHR11735; PTHR11735; 1.
DR PANTHER; PTHR11735:SF14; PTHR11735:SF14; 1.
DR Pfam; PF00814; TsaD; 1.
DR PIRSF; PIRSF036401; Gcp_STYKS; 1.
DR PRINTS; PR00789; OSIALOPTASE.
DR SUPFAM; SSF53067; SSF53067; 1.
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; PS01016; GLYCOPROTEASE; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; ATP-binding; Cytoplasm; Iron; Kinase;
KW Metal-binding; Multifunctional enzyme; Nucleotide-binding;
KW Reference proteome; Serine/threonine-protein kinase; Transferase;
KW tRNA processing.
FT CHAIN 1..535
FT /note="Probable bifunctional tRNA
FT threonylcarbamoyladenosine biosynthesis protein"
FT /id="PRO_0000096979"
FT DOMAIN 333..535
FT /note="Protein kinase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01447"
FT REGION 1..323
FT /note="Kae1"
FT ACT_SITE 451
FT /note="Proton acceptor; for kinase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01447"
FT BINDING 106
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000305"
FT BINDING 110
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000305"
FT BINDING 127..131
FT /ligand="L-threonylcarbamoyladenylate"
FT /ligand_id="ChEBI:CHEBI:73682"
FT /evidence="ECO:0000305"
FT BINDING 127
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000305"
FT BINDING 159
FT /ligand="L-threonylcarbamoyladenylate"
FT /ligand_id="ChEBI:CHEBI:73682"
FT /evidence="ECO:0000305"
FT BINDING 172
FT /ligand="L-threonylcarbamoyladenylate"
FT /ligand_id="ChEBI:CHEBI:73682"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01447"
FT BINDING 176
FT /ligand="L-threonylcarbamoyladenylate"
FT /ligand_id="ChEBI:CHEBI:73682"
FT /evidence="ECO:0000305"
FT BINDING 256
FT /ligand="L-threonylcarbamoyladenylate"
FT /ligand_id="ChEBI:CHEBI:73682"
FT /evidence="ECO:0000305"
FT BINDING 284
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000305"
FT BINDING 339..347
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01447"
FT BINDING 360
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01447"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:3EN9"
FT STRAND 9..19
FT /evidence="ECO:0007829|PDB:3EN9"
FT STRAND 20..22
FT /evidence="ECO:0007829|PDB:5JMV"
FT STRAND 24..31
FT /evidence="ECO:0007829|PDB:3EN9"
FT STRAND 37..40
FT /evidence="ECO:0007829|PDB:3EN9"
FT HELIX 44..62
FT /evidence="ECO:0007829|PDB:3EN9"
FT HELIX 65..67
FT /evidence="ECO:0007829|PDB:3EN9"
FT STRAND 70..78
FT /evidence="ECO:0007829|PDB:3EN9"
FT HELIX 80..97
FT /evidence="ECO:0007829|PDB:3EN9"
FT STRAND 101..105
FT /evidence="ECO:0007829|PDB:3EN9"
FT HELIX 106..117
FT /evidence="ECO:0007829|PDB:3EN9"
FT STRAND 124..128
FT /evidence="ECO:0007829|PDB:3EN9"
FT STRAND 133..139
FT /evidence="ECO:0007829|PDB:3EN9"
FT STRAND 142..152
FT /evidence="ECO:0007829|PDB:3EN9"
FT HELIX 154..164
FT /evidence="ECO:0007829|PDB:3EN9"
FT HELIX 172..180
FT /evidence="ECO:0007829|PDB:3EN9"
FT HELIX 200..211
FT /evidence="ECO:0007829|PDB:3EN9"
FT HELIX 216..242
FT /evidence="ECO:0007829|PDB:3EN9"
FT STRAND 245..251
FT /evidence="ECO:0007829|PDB:3EN9"
FT HELIX 252..255
FT /evidence="ECO:0007829|PDB:3EN9"
FT HELIX 257..269
FT /evidence="ECO:0007829|PDB:3EN9"
FT STRAND 273..275
FT /evidence="ECO:0007829|PDB:3EN9"
FT HELIX 279..282
FT /evidence="ECO:0007829|PDB:3EN9"
FT HELIX 286..298
FT /evidence="ECO:0007829|PDB:3EN9"
FT HELIX 305..307
FT /evidence="ECO:0007829|PDB:3EN9"
FT HELIX 316..318
FT /evidence="ECO:0007829|PDB:5JMV"
FT STRAND 345..351
FT /evidence="ECO:0007829|PDB:3EN9"
FT STRAND 356..362
FT /evidence="ECO:0007829|PDB:3EN9"
FT HELIX 370..390
FT /evidence="ECO:0007829|PDB:3EN9"
FT HELIX 391..394
FT /evidence="ECO:0007829|PDB:3EN9"
FT STRAND 401..405
FT /evidence="ECO:0007829|PDB:3EN9"
FT TURN 406..409
FT /evidence="ECO:0007829|PDB:3EN9"
FT STRAND 410..414
FT /evidence="ECO:0007829|PDB:3EN9"
FT STRAND 418..420
FT /evidence="ECO:0007829|PDB:3EN9"
FT HELIX 421..424
FT /evidence="ECO:0007829|PDB:3EN9"
FT HELIX 430..444
FT /evidence="ECO:0007829|PDB:3EN9"
FT STRAND 456..465
FT /evidence="ECO:0007829|PDB:3EN9"
FT HELIX 477..494
FT /evidence="ECO:0007829|PDB:3EN9"
FT HELIX 496..498
FT /evidence="ECO:0007829|PDB:3EN9"
FT HELIX 499..513
FT /evidence="ECO:0007829|PDB:3EN9"
FT HELIX 517..528
FT /evidence="ECO:0007829|PDB:3EN9"
SQ SEQUENCE 535 AA; 60570 MW; B18EEFACE8E5A99F CRC64;
MICLGLEGTA EKTGVGIVTS DGEVLFNKTI MYKPPKQGIN PREAADHHAE TFPKLIKEAF
EVVDKNEIDL IAFSQGPGLG PSLRVTATVA RTLSLTLKKP IIGVNHCIAH IEIGKLTTEA
EDPLTLYVSG GNTQVIAYVS KKYRVFGETL DIAVGNCLDQ FARYVNLPHP GGPYIEELAR
KGKKLVDLPY TVKGMDIAFS GLLTAAMRAY DAGERLEDIC YSLQEYAFSM LTEITERALA
HTNKGEVMLV GGVAANNRLR EMLKAMCEGQ NVDFYVPPKE FCGDNGAMIA WLGLLMHKNG
RWMSLDETKI IPNYRTDMVE VNWIKEIKGK KRKIPEHLIG KGAEADIKRD SYLDFDVIIK
ERVKKGYRDE RLDENIRKSR TAREARYLAL VKDFGIPAPY IFDVDLDNKR IMMSYINGKL
AKDVIEDNLD IAYKIGEIVG KLHKNDVIHN DLTTSNFIFD KDLYIIDFGL GKISNLDEDK
AVDLIVFKKA VLSTHHEKFD EIWERFLEGY KSVYDRWEII LELMKDVERR ARYVE
