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Database: UniProt
Entry: SYM_RICCN
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ID   SYM_RICCN               Reviewed;         508 AA.
AC   Q92GS6;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   27-MAR-2024, entry version 121.
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}; Synonyms=metS;
GN   OrderedLocusNames=RC1046;
OS   Rickettsia conorii (strain ATCC VR-613 / Malish 7).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=272944;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-613 / Malish 7;
RX   PubMed=11557893; DOI=10.1126/science.1061471;
RA   Ogata H., Audic S., Renesto-Audiffren P., Fournier P.-E., Barbe V.,
RA   Samson D., Roux V., Cossart P., Weissenbach J., Claverie J.-M., Raoult D.;
RT   "Mechanisms of evolution in Rickettsia conorii and R. prowazekii.";
RL   Science 293:2093-2098(2001).
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; AE006914; AAL03584.1; -; Genomic_DNA.
DR   PIR; F97830; F97830.
DR   RefSeq; WP_010977624.1; NC_003103.1.
DR   AlphaFoldDB; Q92GS6; -.
DR   SMR; Q92GS6; -.
DR   GeneID; 928195; -.
DR   KEGG; rco:RC1046; -.
DR   PATRIC; fig|272944.4.peg.1197; -.
DR   HOGENOM; CLU_009710_9_4_5; -.
DR   Proteomes; UP000000816; 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..508
FT                   /note="Methionine--tRNA ligase"
FT                   /id="PRO_0000139237"
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   508 AA;  58648 MW;  28BA91436B04995D CRC64;
     MNNTYYITTP IYYVNDIPHI GHAYTSVASD VIARFMRLRG FDVMFLTGTD EHGQKVEKAA
     INKNIDPQKF TDQTSESFRH LMTAMHISND DFIRTTEHRH KKAVAVFWQK LLDNGTIYEG
     FYEGWYAVRD EAFFDESELT RDGLAPTGAP VEWVKEPSYF FNLSKWQDKL LEFYEANPDF
     IRPISRRNEV ISFVKSGLKD LSVSRTTFNW GIKVPNNEKH VIYVWLDALA NYISALGYLD
     EQSNYNKFWP ADLHVVGKDI LRFHAVYWPA FLMAAEVPLP KTIMAHGWWT NEGQKISKSL
     GNTIDPIKLI DEFGVDQVRY FLMREVTFGA DGNFARSNLI TRINSELSNK IGNLLQRTTS
     FVYKNNDAKV PLLTQGVIDK IYELPILKTA SKFVEQNILL MDKTEINKIL ENIINLAEEA
     NIYIDSEAPW NLKKTDPDKM LEVLYALLEV LRYIAIMLLP FIPSSANKML DQLGVNKEER
     LFKHLIRDYT LTAGSNILEP TIIFPKFE
//
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