AC   MF_01447;
DC   Protein; auto
TR   HAMAP; MF_01447; -; 1; level=0
XX
Names: Kae1_Bud32_arch
XX
ID   KAE1B
DE   RecName: Full=Probable bifunctional tRNA threonylcarbamoyladenosine biosynthesis protein;
DE   Includes:
DE     RecName: Full=tRNA N6-adenosine threonylcarbamoyltransferase;
DE              EC=2.3.1.234;
DE     AltName: Full=tRNA threonylcarbamoyladenosine biosynthesis protein Kae1;
DE     AltName: Full=t(6)A37 threonylcarbamoyladenosine biosynthesis protein Kae1;
DE   Includes:
DE     RecName: Full=Serine/threonine-protein kinase Bud32;
DE              EC=2.7.11.1;
XX
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   -!- 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   -!- 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   -!- 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;
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC       Note=Binds 1 Fe(2+) ion per subunit.;
CC   -!- SUBUNIT: Component of the KEOPS complex that consists of Kae1, Bud32,
CC       Cgi121 and Pcc1; the whole complex dimerizes.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
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 kinase
CC       superfamily. Tyr protein kinase family. BUD32 subfamily.
XX
DR   PROSITE; PS01016; GLYCOPROTEASE; 1; trigger=no
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1; trigger=no
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1; trigger=no
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1; trigger=no
DR   Pfam; PF00814; Peptidase_M22; 1; trigger=no
DR   Pfam; PF00069; Pkinase; 1; trigger=no
DR   Pfam; PF01163; RIO1; 1; trigger=no
DR   PRINTS; PR00789; OSIALOPTASE; 1; trigger=no
DR   NCBIfam; TIGR03724; Arch_bud32; 1; trigger=no
DR   NCBIfam; TIGR03722; Arch_KAE1; 1; trigger=no
DR   NCBIfam; TIGR00329; Gcp_kae1; 1; trigger=no
DR   PIRSF; PIRSF036401; Gcp_STYKS; 1; trigger=no
XX
KW   Acyltransferase
KW   ATP-binding
KW   Cytoplasm
KW   Kinase
KW   Nucleotide-binding
KW   Serine/threonine-protein kinase
KW   Transferase
KW   tRNA processing
KW   Iron
KW   Metal-binding
KW   Multifunctional enzyme
XX
GO   GO:0005506; F:iron ion binding
GO   GO:0005524; F:ATP binding
GO   GO:0004712; F:protein serine/threonine/tyrosine kinase activity
GO   GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups
GO   GO:0002949; P:tRNA threonylcarbamoyladenosine modification
GO   GO:0005737; C:cytoplasm
XX
FT   From: KAE1B_METJA (Q58530)
FT   DOMAIN          333..Cter
FT                   /note="Protein kinase"
FT   BINDING         339..347
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   REGION          Nter..323
FT                   /note="Kae1"
FT   ACT_SITE        451
FT                   /note="Proton acceptor; for kinase activity"
FT   Condition: D
FT   BINDING         127..131
FT                   /ligand="L-threonylcarbamoyladenylate"
FT                   /ligand_id="ChEBI:CHEBI:73682"
FT   Condition: x-x-S-G-[GA]
FT   BINDING         106
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT   Condition: H
FT   BINDING         110
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT   Condition: H
FT   BINDING         127
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT   Optional; Condition: Y
FT   BINDING         284
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT   Condition: D
FT   BINDING         159
FT                   /ligand="L-threonylcarbamoyladenylate"
FT                   /ligand_id="ChEBI:CHEBI:73682"
FT   Condition: D
FT   BINDING         172
FT                   /ligand="L-threonylcarbamoyladenylate"
FT                   /ligand_id="ChEBI:CHEBI:73682"
FT   Condition: G
FT   BINDING         176
FT                   /ligand="L-threonylcarbamoyladenylate"
FT                   /ligand_id="ChEBI:CHEBI:73682"
FT   Condition: E
FT   BINDING         256
FT                   /ligand="L-threonylcarbamoyladenylate"
FT                   /ligand_id="ChEBI:CHEBI:73682"
FT   Condition: N
FT   BINDING         360
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: K
XX
Size: 520-548;
Related: MF_01446;
Template: Q58530; P36132;
Scope:
 Archaea; Euryarchaeota
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: None
Comments: None
XX
# Revision 1.23 2023/06/01
//