KAE1B_THEAC
ID KAE1B_THEAC Reviewed; 529 AA.
AC Q9HLA5;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 131.
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=Ta0324;
OS Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC
OS 15155 / AMRC-C165).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Thermoplasmataceae; Thermoplasma.
OX NCBI_TaxID=273075;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX PubMed=11029001; DOI=10.1038/35035069;
RA Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C.,
RA Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.;
RT "The genome sequence of the thermoacidophilic scavenger Thermoplasma
RT acidophilum.";
RL Nature 407:508-513(2000).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (3.02 ANGSTROMS) OF 1-329.
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. 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}.
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DR EMBL; AL445064; CAC11469.1; -; Genomic_DNA.
DR RefSeq; WP_010900753.1; NC_002578.1.
DR PDB; 3ENO; X-ray; 3.02 A; A/B=1-329.
DR PDBsum; 3ENO; -.
DR AlphaFoldDB; Q9HLA5; -.
DR SMR; Q9HLA5; -.
DR STRING; 273075.Ta0324; -.
DR EnsemblBacteria; CAC11469; CAC11469; CAC11469.
DR GeneID; 1455944; -.
DR KEGG; tac:Ta0324; -.
DR eggNOG; arCOG01183; Archaea.
DR eggNOG; arCOG01185; Archaea.
DR HOGENOM; CLU_023208_2_2_2; -.
DR OMA; GETMDTG; -.
DR OrthoDB; 9881at2157; -.
DR EvolutionaryTrace; Q9HLA5; -.
DR Proteomes; UP000001024; 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-KW.
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: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:InterPro.
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; IPR009220; tRNA_threonyl_synthase/kinase.
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.
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..529
FT /note="Probable bifunctional tRNA
FT threonylcarbamoyladenosine biosynthesis protein"
FT /id="PRO_0000303661"
FT DOMAIN 329..529
FT /note="Protein kinase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01447"
FT REGION 1..324
FT /note="Kae1"
FT ACT_SITE 447
FT /note="Proton acceptor; for kinase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01447"
FT BINDING 107
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01447"
FT BINDING 111
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01447"
FT BINDING 128..132
FT /ligand="L-threonylcarbamoyladenylate"
FT /ligand_id="ChEBI:CHEBI:73682"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01447"
FT BINDING 128
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01447"
FT BINDING 160
FT /ligand="L-threonylcarbamoyladenylate"
FT /ligand_id="ChEBI:CHEBI:73682"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01447"
FT BINDING 173
FT /ligand="L-threonylcarbamoyladenylate"
FT /ligand_id="ChEBI:CHEBI:73682"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01447"
FT BINDING 177
FT /ligand="L-threonylcarbamoyladenylate"
FT /ligand_id="ChEBI:CHEBI:73682"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01447"
FT BINDING 257
FT /ligand="L-threonylcarbamoyladenylate"
FT /ligand_id="ChEBI:CHEBI:73682"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01447"
FT BINDING 285
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01447"
FT BINDING 335..342
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01447"
FT BINDING 355
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:3ENO"
FT STRAND 9..21
FT /evidence="ECO:0007829|PDB:3ENO"
FT STRAND 25..30
FT /evidence="ECO:0007829|PDB:3ENO"
FT HELIX 40..62
FT /evidence="ECO:0007829|PDB:3ENO"
FT HELIX 66..68
FT /evidence="ECO:0007829|PDB:3ENO"
FT STRAND 71..75
FT /evidence="ECO:0007829|PDB:3ENO"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:3ENO"
FT HELIX 81..98
FT /evidence="ECO:0007829|PDB:3ENO"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:3ENO"
FT HELIX 107..119
FT /evidence="ECO:0007829|PDB:3ENO"
FT STRAND 125..132
FT /evidence="ECO:0007829|PDB:3ENO"
FT STRAND 134..139
FT /evidence="ECO:0007829|PDB:3ENO"
FT STRAND 141..152
FT /evidence="ECO:0007829|PDB:3ENO"
FT HELIX 155..163
FT /evidence="ECO:0007829|PDB:3ENO"
FT TURN 164..167
FT /evidence="ECO:0007829|PDB:3ENO"
FT HELIX 172..177
FT /evidence="ECO:0007829|PDB:3ENO"
FT HELIX 178..182
FT /evidence="ECO:0007829|PDB:3ENO"
FT HELIX 201..212
FT /evidence="ECO:0007829|PDB:3ENO"
FT HELIX 217..243
FT /evidence="ECO:0007829|PDB:3ENO"
FT STRAND 246..253
FT /evidence="ECO:0007829|PDB:3ENO"
FT HELIX 254..256
FT /evidence="ECO:0007829|PDB:3ENO"
FT HELIX 258..271
FT /evidence="ECO:0007829|PDB:3ENO"
FT STRAND 273..275
FT /evidence="ECO:0007829|PDB:3ENO"
FT TURN 280..283
FT /evidence="ECO:0007829|PDB:3ENO"
FT HELIX 288..299
FT /evidence="ECO:0007829|PDB:3ENO"
FT HELIX 306..308
FT /evidence="ECO:0007829|PDB:3ENO"
FT HELIX 317..319
FT /evidence="ECO:0007829|PDB:3ENO"
SQ SEQUENCE 529 AA; 58202 MW; 9C878F334EE056D3 CRC64;
MIVLGLEGTA HTISCGIIDE SRILAMESSM YRPKTGGIRP LDAAVHHSEV IDTVISRALE
KAKISIHDID LIGFSMGPGL APSLRVTATA ARTISVLTGK PIIGVNHPLG HIEIGRRVTG
AIDPVMLYVS GGNTQVIAHV NGRYRVLGET LDIGIGNMID KFAREAGIPF PGGPEIEKLA
MKGTKLLDLP YSVKGMDTAF SGILTAALQY LKTGQAIEDI SYSIQETAFA MLVEVLERAL
YVSGKDEILM AGGVALNRRL RDMVTNMARE AGIRSYLTDR EYCMDNGIMI AQAALLMYKS
GVRMSVEETA VNPRFRIDEV DAPWITDASR KDYGKAGAES RIEEVSFHGR PAIRKVRISK
SYRNSDLDKK IRYERMRNEF TILRKLKEAG VNSPVVYDFD PFSMSITMQK IPGRMMSAEL
NEGRTDFLNE LGIMIAKMHR AGIAHGDLTV NNIIVNDSVF IIDPSMGKVN AEIEDMAVDI
YALEDSIKGL GLDSGSVIGQ MLKSYRNNFN LADDVLETVS AIRRRHRYV
