ID   SYM_RICFE               Reviewed;         512 AA.
AC   Q4UMX2;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   27-MAR-2024, entry version 110.
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=RF_0235;
OS   Rickettsia felis (strain ATCC VR-1525 / URRWXCal2) (Rickettsia azadi).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=315456;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-1525 / URRWXCal2;
RX   PubMed=15984913; DOI=10.1371/journal.pbio.0030248;
RA   Ogata H., Renesto P., Audic S., Robert C., Blanc G., Fournier P.-E.,
RA   Parinello H., Claverie J.-M., Raoult D.;
RT   "The genome sequence of Rickettsia felis identifies the first putative
RT   conjugative plasmid in an obligate intracellular parasite.";
RL   PLoS Biol. 3:1-12(2005).
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; CP000053; AAY61086.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q4UMX2; -.
DR   SMR; Q4UMX2; -.
DR   STRING; 315456.RF_0235; -.
DR   KEGG; rfe:RF_0235; -.
DR   eggNOG; COG0143; Bacteria.
DR   HOGENOM; CLU_009710_9_2_5; -.
DR   OrthoDB; 9810191at2; -.
DR   Proteomes; UP000008548; 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.
FT   CHAIN           1..512
FT                   /note="Methionine--tRNA ligase"
FT                   /id="PRO_0000272402"
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   512 AA;  58800 MW;  1F892EDF5ACAA1D8 CRC64;
     MKNTYYITTP IYYVNDVPHI GHAYTSVASD VIARFIRLCG FDVMFLTGTD EHGQKVEKAA
     INKNIDPQKF TDHTSESFRH LMNVMNISND DFIRTTESRH KEAVAIFWQK LLDNGTIYEG
     FYEGWYAVRD EAFFDESELT SDGLAPTGAP VEWVKEPSYF FNLSKWQDKL LEFYEANPDF
     IRPISRRNEV ISFVKSGLKD LSVSRTTFNW GIKVPNNEKH VIYVWLDALA SYISALGYPD
     KQSNYGKFWP ADLHVVGKDI LRFHAVYWPA FLMAAEIPLP KTIMAHGWWT NEGQKISKSL
     GNTIDPIKLI DEFGVDQVRY FLMREVTFGA DGNFARSNLV TRINSELSNK IGNLLQRTTA
     FVYKNNDGKV PLLMQGIIDK IYELPILKTA SKFAEQNILL MEKTEINKVL ENIINLSEEA
     NIYIDSEAPW NLKKTDPEKM SEVLYTLLEV LRYIAIMLQP FIPSSANKML DQLGVNKEER
     LFKHLIRDYA LRAGSSILEP AIIFPRFEGD VV
//