AC   MF_00098;
DC   Protein; auto
TR   HAMAP; MF_00098; -; 1; level=0
XX
Names: Met_tRNA_synth_type1
XX
ID   SYM
DE   RecName: Full=Methionine--tRNA ligase;
DE            EC=6.1.1.10;
DE   AltName: Full=Methionyl-tRNA synthetase;
DE            Short=MetRS;
GN   Name=metG;
XX
CC   -!- FUNCTION: Catalyzes the attachment of L-methionine to tRNA(Met). Is
CC       required not only for elongation of protein synthesis but also for the
CC       initiation of all mRNA translation through initiator tRNA(fMet)
CC       aminoacylation.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=tRNA(Met) + L-methionine + ATP = L-methionyl-tRNA(Met) + AMP +
CC         diphosphate; Xref=Rhea:RHEA:13481, Rhea:RHEA-COMP:9667, Rhea:RHEA-
CC         COMP:9698, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57844,
CC         ChEBI:CHEBI:78442, ChEBI:CHEBI:78530, ChEBI:CHEBI:456215;
CC         EC=6.1.1.10;
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13482;
case <FTGroup:1>
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC       Note=Binds 1 zinc ion per subunit.;
end case
case <Feature:PS50886>
CC   -!- SUBUNIT: Homodimer.
end case
case not <Feature:PS50886> and <OC:Bacteria>
CC   -!- SUBUNIT: Monomer.
end case
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       MetG type 1 subfamily.
XX
DR   Pfam; PF00133; tRNA-synt_1; 1; trigger=no
DR   PRINTS; PR01041; TRNASYNTHMET; 1; trigger=no
DR   NCBIfam; TIGR00398; MetG; 1; trigger=no
DR   NCBIfam; TIGR00399; MetG_C_term; 1; trigger=no
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1; trigger=no
DR   PROSITE; PS50886; TRBD; 0-1; trigger=yes
XX
KW   Cytoplasm
KW   Aminoacyl-tRNA synthetase
KW   Protein biosynthesis
KW   Ligase
KW   ATP-binding
KW   Nucleotide-binding
case <Feature:PS50886>
KW   RNA-binding
KW   tRNA-binding
end case
case <FTGroup:1>
KW   Metal-binding
KW   Zinc
end case
XX
GO   GO:0005524; F:ATP binding
GO   GO:0004825; F:methionine-tRNA ligase activity
GO   GO:0006431; P:methionyl-tRNA aminoacylation
GO   GO:0005737; C:cytoplasm
XX
FT   From: SYM_ECOLI (P00959)
FT   MOTIF           15..25
FT                   /note="'HIGH' region"
FT   Condition: [PYA]-[YT]-x(5)-H-[LIVFA]-G-[HNST]
FT   MOTIF           333..337
FT                   /note="'KMSKS' region"
FT   Condition: [KTQ]-[LIMF]-[SG]-[KTS]-[ST]
FT   BINDING         146
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT   Group: 1; Condition: C
FT   BINDING         149
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT   Group: 1; Condition: C
FT   BINDING         159
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT   Group: 1; Condition: C
FT   BINDING         162
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT   Group: 1; Condition: C
FT   BINDING         336
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: [KST]
XX
Size: 536-734;
Related: MF_01228;
Template: P00959;
Scope:
 Bacteria
 Archaea
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: in ACAM1
Comments: It is possible that several species such as ARCFU, METAC, METMA, METKA, METTH,
 METJA and TREPA bind a second zinc ion, as their sequences contain a second
 zinc finger motif corresponding to that of metG subfamily 2
XX
# Version: 29
# Last updated date: 2025-07-03
# Created date: 2005-02-28
//