AC   MF_00252;
DC   Protein; auto
TR   HAMAP; MF_00252; -; 1; level=0
XX
Names: Lys_tRNA_synth_class2
XX
ID   SYK
DE   RecName: Full=Lysine--tRNA ligase;
DE            EC=6.1.1.6;
DE   AltName: Full=Lysyl-tRNA synthetase;
DE            Short=LysRS;
GN   Name=lysS;
XX
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-lysine + tRNA(Lys) = AMP + diphosphate + L-lysyl-
CC         tRNA(Lys); Xref=Rhea:RHEA:20792, Rhea:RHEA-COMP:9696, Rhea:RHEA-
CC         COMP:9697, ChEBI:CHEBI:30616, ChEBI:CHEBI:32551, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:78442, ChEBI:CHEBI:78529, ChEBI:CHEBI:456215; EC=6.1.1.6;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC       Note=Binds 3 Mg(2+) ions per subunit.;
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
XX
DR   Pfam; PF00152; tRNA-synt_2; 1; trigger=no
DR   PRINTS; PR00982; TRNASYNTHLYS; 1; trigger=no
DR   NCBIfam; TIGR00499; LysS_bact; 1; trigger=no
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1; trigger=no
XX
case <FT:4> or <FT:5>
KW   Acetylation
end case
KW   Aminoacyl-tRNA synthetase
KW   ATP-binding
KW   Cytoplasm
KW   Ligase
KW   Magnesium
KW   Metal-binding
KW   Nucleotide-binding
KW   Protein biosynthesis
XX
GO   GO:0005524; F:ATP binding
GO   GO:0004824; F:lysine-tRNA ligase activity
GO   GO:0000287; F:magnesium ion binding
GO   GO:0006430; P:lysyl-tRNA aminoacylation
GO   GO:0005737; C:cytoplasm
XX
FT   From: SYK2_ECOLI (P0A8N5)
FT   BINDING         415
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT   Condition: [ED]
FT   BINDING         422
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT   Condition: E
FT   BINDING         422
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT   Condition: E
case <OC:Escherichia> or <OC:Shigella>
FT   MOD_RES         114
FT                   /note="N6-acetyllysine"
FT   Condition: K
FT   MOD_RES         156
FT                   /note="N6-acetyllysine"
FT   Condition: K
end case
XX
Size: 485-597;
Related: None;
Template: P0A8N3; P0A8N5;
Scope:
 Bacteria
 Archaea
Fusion:
 Nter: <Unknown>
 Cter: None
Duplicate: in ECOLI, ECOL6, ECO57, MYCPU, MYCTU
Plasmid: None
Comments: Lysyl-tRNA synthesis is catalyzed by two unrelated families of tRNA
 synthetase; class-I or class-II. Usually only one or the other is
 present, however Methanosarcina seem to have both.
 Weird insertion in AQUAE.
 Unknown C-terminal domain in SYK2_MYCTU.
XX
# Revision 1.36 2023/06/01
//