ID   SYM_BUCAP               Reviewed;         545 AA.
AC   Q9ZHD7;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2002, sequence version 2.
DT   03-AUG-2022, entry version 137.
DE   RecName: Full=Methionine--tRNA ligase;
DE            EC=6.1.1.10;
DE   AltName: Full=Methionyl-tRNA synthetase;
DE            Short=MetRS;
GN   Name=metG; OrderedLocusNames=BUsg_102;
OS   Buchnera aphidicola subsp. Schizaphis graminum (strain Sg).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=198804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sg;
RX   PubMed=12089438; DOI=10.1126/science.1071278;
RA   Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA   Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT   "50 million years of genomic stasis in endosymbiotic bacteria.";
RL   Science 296:2376-2379(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-234.
RX   PubMed=9767718; DOI=10.1007/s002849900392;
RA   Clark M.A., Baumann L., Baumann P.;
RT   "Buchnera aphidicola (Aphid endosymbiont) contains genes encoding enzymes
RT   of histidine biosynthesis.";
RL   Curr. Microbiol. 37:356-358(1998).
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:0000250}.
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;
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       MetG type 1 subfamily. {ECO:0000305}.
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DR   EMBL; AE013218; AAM67672.1; -; Genomic_DNA.
DR   EMBL; AF067228; AAC97364.1; -; Genomic_DNA.
DR   RefSeq; WP_011053638.1; NC_004061.1.
DR   AlphaFoldDB; Q9ZHD7; -.
DR   SMR; Q9ZHD7; -.
DR   STRING; 198804.BUsg_102; -.
DR   PRIDE; Q9ZHD7; -.
DR   EnsemblBacteria; AAM67672; AAM67672; BUsg_102.
DR   KEGG; bas:BUsg_102; -.
DR   eggNOG; COG0143; Bacteria.
DR   HOGENOM; CLU_009710_7_0_6; -.
DR   OMA; SDMHGTP; -.
DR   OrthoDB; 761140at2; -.
DR   Proteomes; UP000000416; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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   Gene3D; 2.20.28.20; -; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   HAMAP; MF_00098; Met_tRNA_synth_type1; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR041872; Anticodon_Met.
DR   InterPro; IPR023458; Met-tRNA_ligase_1.
DR   InterPro; IPR014758; Met-tRNA_synth.
DR   InterPro; IPR015413; Methionyl/Leucyl_tRNA_Synth.
DR   InterPro; IPR033911; MetRS_core.
DR   InterPro; IPR029038; MetRS_Zn.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR   PANTHER; PTHR45765; PTHR45765; 1.
DR   Pfam; PF19303; Anticodon_3; 1.
DR   Pfam; PF09334; tRNA-synt_1g; 1.
DR   PRINTS; PR01041; TRNASYNTHMET.
DR   SUPFAM; SSF47323; SSF47323; 1.
DR   SUPFAM; SSF57770; SSF57770; 1.
DR   TIGRFAMs; TIGR00398; metG; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; Metal-binding;
KW   Nucleotide-binding; Protein biosynthesis; Zinc.
FT   CHAIN           1..545
FT                   /note="Methionine--tRNA ligase"
FT                   /id="PRO_0000139112"
FT   MOTIF           15..25
FT                   /note="'HIGH' region"
FT   MOTIF           332..336
FT                   /note="'KMSKS' region"
FT   BINDING         146
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         149
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         159
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         162
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         335
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   545 AA;  63822 MW;  77F79377EF21492A CRC64;
     MSNKFKKILV TCALPYANGP IHIGHMLEHI QADIWVRYQR MRNNEVWFIS SDDAHGTAIM
     LKSEKLGITP IKLIKKIKEE HIIDFSNFNI SHDNYHSTHC VENLFLLRKI FLSLSEQKLI
     NEKKIFQFYD NTKKMFLPDR FIKGTCPFCS SKNQNGDNCE ICGSIYEPTD LVNPISVISN
     SVPILKNTTH LYFNLPLFTN MLNKWIHSGI LEKSVAKKTE EWLKSGLKEW GISRDAPYFG
     FKIPKFDKKY FYVWLDAPVG YISAFKNFCT KNKKVDFNEF WKKESKCELY HFIGKDIIYF
     HTLFWPAILE ASSYRKPNGI FVHGHLTING LKLSKSRGFL IKASDWIKCF DSDSLRYYYA
     SKLSNNINDI EINLEDFIQK INSDIVNKLV NLASRNASFI HKYFDGYLAD SLGDCNLYQD
     FIDISKKIAN FFENRQFSSV IRECMKLLDL ANQYINQREP WKIKQDNFNK LHTICTVGIN
     LFRLVVIFLK PIIPDLAKKT EYFLISDLTW KGIDKPLLSH KIKKFKKLYN RINHDKILQL
     SLLCK