ID   SYM_RICBR               Reviewed;         509 AA.
AC   Q1RJZ5;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   27-MAR-2024, entry version 103.
DE   RecName: Full=Methionine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_01228};
DE            EC=6.1.1.10 {ECO:0000255|HAMAP-Rule:MF_01228};
DE   AltName: Full=Methionyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_01228};
DE            Short=MetRS {ECO:0000255|HAMAP-Rule:MF_01228};
GN   Name=metG {ECO:0000255|HAMAP-Rule:MF_01228};
GN   OrderedLocusNames=RBE_0238;
OS   Rickettsia bellii (strain RML369-C).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; belli group.
OX   NCBI_TaxID=336407;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RML369-C;
RX   PubMed=16703114; DOI=10.1371/journal.pgen.0020076;
RA   Ogata H., La Scola B., Audic S., Renesto P., Blanc G., Robert C.,
RA   Fournier P.-E., Claverie J.-M., Raoult D.;
RT   "Genome sequence of Rickettsia bellii illuminates the role of amoebae in
RT   gene exchanges between intracellular pathogens.";
RL   PLoS Genet. 2:733-744(2006).
CC   -!- FUNCTION: Is required not only for elongation of protein synthesis but
CC       also for the initiation of all mRNA translation through initiator
CC       tRNA(fMet) aminoacylation. {ECO:0000255|HAMAP-Rule:MF_01228}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-methionine + tRNA(Met) = AMP + diphosphate + L-
CC         methionyl-tRNA(Met); Xref=Rhea:RHEA:13481, Rhea:RHEA-COMP:9667,
CC         Rhea:RHEA-COMP:9698, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:57844, ChEBI:CHEBI:78442, ChEBI:CHEBI:78530,
CC         ChEBI:CHEBI:456215; EC=6.1.1.10; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01228};
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01228}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01228}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       MetG type 2B subfamily. {ECO:0000255|HAMAP-Rule:MF_01228}.
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DR   EMBL; CP000087; ABE04319.1; -; Genomic_DNA.
DR   RefSeq; WP_011476932.1; NC_007940.1.
DR   AlphaFoldDB; Q1RJZ5; -.
DR   SMR; Q1RJZ5; -.
DR   KEGG; rbe:RBE_0238; -.
DR   eggNOG; COG0143; Bacteria.
DR   HOGENOM; CLU_009710_9_2_5; -.
DR   OrthoDB; 9810191at2; -.
DR   Proteomes; UP000001951; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004825; F:methionine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006431; P:methionyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   CDD; cd07957; Anticodon_Ia_Met; 1.
DR   CDD; cd00814; MetRS_core; 1.
DR   Gene3D; 2.170.220.10; -; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   HAMAP; MF_01228; Met_tRNA_synth_type2; 1.
DR   InterPro; IPR041872; Anticodon_Met.
DR   InterPro; IPR014758; Met-tRNA_synth.
DR   InterPro; IPR023457; Met-tRNA_synth_2.
DR   InterPro; IPR015413; Methionyl/Leucyl_tRNA_Synth.
DR   InterPro; IPR033911; MetRS_core.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR   NCBIfam; TIGR00398; metG; 1.
DR   PANTHER; PTHR43326:SF1; METHIONINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43326; METHIONYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF19303; Anticodon_3; 1.
DR   Pfam; PF09334; tRNA-synt_1g; 2.
DR   PRINTS; PR01041; TRNASYNTHMET.
DR   SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..509
FT                   /note="Methionine--tRNA ligase"
FT                   /id="PRO_0000272401"
FT   MOTIF           12..22
FT                   /note="'HIGH' region"
FT   MOTIF           295..299
FT                   /note="'KMSKS' region"
FT   BINDING         298
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01228"
SQ   SEQUENCE   509 AA;  58359 MW;  FFA102B509977D69 CRC64;
     MNNTYYITTP IYYVNDVPHI GHAYTSVASD VIARFMRLSG HEVMFLTGTD EHGQKVEKAA
     IDKNIDPQKF TDQTSQSFRH LMTAMHISND DFIRTTEERH KKAVAIFWQK LLDNGSIYEG
     FYEGWYAVRD EAFYDESELT ADKLAPTGAA VEWVKEPSYF FNLSKWQDKL LEFYEANPDF
     IRPISRRNEV ISFVKSGLKD LSVSRTTFNW GIKVPNDNKH VIYVWLDALA NYISALGYPD
     QNSNYGKFWP ANLQVVGKDI LRFHAVYWPA FLMAAEIPLP KTIMAHGWWT NEGQKISKSL
     GNTIDPIKLI EEFGVDQVRY FLMREITFGA DGNFARSNLI TRINSELSNK IGNLLQRTTS
     FVYKNNDGKV PAITQDAINK IYELPLLKTA INSAKQNILL MEKTEINKIL DNIINLAEEA
     NIYIDSEAPW NLKKTDPEKM LEVLYALLET LRYIAVMLQA FMPSSAGKML DQLGVNTEER
     LFKHLSLEFA LTSASDILEP VIVFPRFEE
//