ID   SYM_OCEIH               Reviewed;         673 AA.
AC   P59079;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2002, sequence version 1.
DT   03-AUG-2022, entry version 128.
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=OB0046;
OS   Oceanobacillus iheyensis (strain DSM 14371 / CIP 107618 / JCM 11309 / KCTC
OS   3954 / HTE831).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Oceanobacillus.
OX   NCBI_TaxID=221109;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14371 / CIP 107618 / JCM 11309 / KCTC 3954 / HTE831;
RX   PubMed=12235376; DOI=10.1093/nar/gkf526;
RA   Takami H., Takaki Y., Uchiyama I.;
RT   "Genome sequence of Oceanobacillus iheyensis isolated from the Iheya Ridge
RT   and its unexpected adaptive capabilities to extreme environments.";
RL   Nucleic Acids Res. 30:3927-3935(2002).
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   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       MetG type 2B subfamily. {ECO:0000305}.
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DR   EMBL; BA000028; BAC12002.1; -; Genomic_DNA.
DR   RefSeq; WP_011064448.1; NC_004193.1.
DR   AlphaFoldDB; P59079; -.
DR   SMR; P59079; -.
DR   STRING; 221109.22775724; -.
DR   EnsemblBacteria; BAC12002; BAC12002; BAC12002.
DR   KEGG; oih:OB0046; -.
DR   eggNOG; COG0073; Bacteria.
DR   eggNOG; COG0143; Bacteria.
DR   HOGENOM; CLU_009710_9_4_9; -.
DR   OMA; SDMHGTP; -.
DR   OrthoDB; 761140at2; -.
DR   PhylomeDB; P59079; -.
DR   Proteomes; UP000000822; 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:0000049; F:tRNA binding; IEA:UniProtKB-KW.
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   CDD; cd02800; tRNA_bind_EcMetRS_like; 1.
DR   Gene3D; 2.40.50.140; -; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   HAMAP; MF_01228; Met_tRNA_synth_type2; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR041872; Anticodon_Met.
DR   InterPro; IPR004495; Met-tRNA-synth_bsu_C.
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; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR002547; tRNA-bd_dom.
DR   InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR   PANTHER; PTHR43326; PTHR43326; 1.
DR   Pfam; PF19303; Anticodon_3; 1.
DR   Pfam; PF09334; tRNA-synt_1g; 1.
DR   Pfam; PF01588; tRNA_bind; 1.
DR   PRINTS; PR01041; TRNASYNTHMET.
DR   SUPFAM; SSF47323; SSF47323; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   TIGRFAMs; TIGR00398; metG; 1.
DR   TIGRFAMs; TIGR00399; metG_C_term; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
DR   PROSITE; PS50886; TRBD; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome; RNA-binding;
KW   tRNA-binding.
FT   CHAIN           1..673
FT                   /note="Methionine--tRNA ligase"
FT                   /id="PRO_0000139234"
FT   DOMAIN          571..673
FT                   /note="tRNA-binding"
FT   MOTIF           14..24
FT                   /note="'HIGH' region"
FT   MOTIF           310..314
FT                   /note="'KMSKS' region"
FT   BINDING         313
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   673 AA;  76611 MW;  D6EE8F706BD9BCAD CRC64;
     MARENAFYIT TPIYYPSGKL HIGNAYTTIA CDVMARYKRM RGFDVFYLTG SDEHGQKIEQ
     KAKEMNISPK AYVDDMAEGM KKLWNTLEIS NDKFIRTTEE QHKKVVADIF ERFLEQGDIY
     LDEYEGWYSV PDETFYTETQ LEDVERDDDG NVIGGKSPDS GHPVELIKEE SYFFRMSKYA
     DRLLKFYEDN PEFIQPESRK NEMINNFIKP GLEDLAVSRT TFSWGVQVPS NPKHVVYVWI
     DALTNYITAL GYGSEDTSLY DKFWPADVHM VGKEIVRFHT IYWPIMLMAL DLPLPKKVFA
     HGWLLMKDGK MSKSKGNVVY PEMLVERYGL DALRYYLMRE VAFGSDGVFT PEDFISRVNY
     DLANDLGNLL NRTVAMINKY FDGKVPEFKG EVTSFDGELQ TTANNAVKEY EKHMEGMQFS
     DALKQVWILI SRANKYIDET EPWIVAKDEG RRNELASVMV HLAESLHAAA LMLQPFLTHA
     PKKIAEQLGL GEEYGLDWGT IGFGNFPENT TVVKKGTPIF PRLDLDEEAA YIRDQMANGA
     NAASSEDETG DWDPNETDLV SEKEKQIKYD VFDKVELKVA EVKDCSKVEG ADKLLKFRLD
     AGDNGDRQIL SGIAEYYSEP EQLIGKKVVI VANLKPRKMR GEISQGMILS AEYDGKLQIV
     EAPSEAPNGS SIS