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Database: UniProt
Entry: Q81W03
LinkDB: Q81W03
Original site: Q81W03 
ID   SYM1_BACAN              Reviewed;         660 AA.
AC   Q81W03; Q6I506; Q6KYQ0;
DT   31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 143.
DE   RecName: Full=Methionine--tRNA ligase 1 {ECO:0000255|HAMAP-Rule:MF_01228};
DE            EC=6.1.1.10 {ECO:0000255|HAMAP-Rule:MF_01228};
DE   AltName: Full=Methionyl-tRNA synthetase 1 {ECO:0000255|HAMAP-Rule:MF_01228};
DE            Short=MetRS 1 {ECO:0000255|HAMAP-Rule:MF_01228};
GN   Name=metG1 {ECO:0000255|HAMAP-Rule:MF_01228}; Synonyms=metG, metS;
GN   OrderedLocusNames=BA_0036, GBAA_0036, BAS0037;
OS   Bacillus anthracis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=1392;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ames / isolate Porton;
RX   PubMed=12721629; DOI=10.1038/nature01586;
RA   Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T.,
RA   Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R.,
RA   Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M.,
RA   Kolonay J.F., Beanan M.J., Dodson R.J., Brinkac L.M., Gwinn M.L.,
RA   DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C.,
RA   Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y.,
RA   Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M.,
RA   Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E.,
RA   White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M.,
RA   Hanna P.C., Kolstoe A.-B., Fraser C.M.;
RT   "The genome sequence of Bacillus anthracis Ames and comparison to closely
RT   related bacteria.";
RL   Nature 423:81-86(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ames ancestor;
RX   PubMed=18952800; DOI=10.1128/jb.01347-08;
RA   Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D.,
RA   Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A.;
RT   "The complete genome sequence of Bacillus anthracis Ames 'Ancestor'.";
RL   J. Bacteriol. 191:445-446(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sterne;
RA   Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K.,
RA   Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R.,
RA   Richardson P., Rubin E., Tice H.;
RT   "Complete genome sequence of Bacillus anthracis Sterne.";
RL   Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
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: Homodimer. {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; AE016879; AAP24091.1; -; Genomic_DNA.
DR   EMBL; AE017334; AAT29115.2; -; Genomic_DNA.
DR   EMBL; AE017225; AAT52375.1; -; Genomic_DNA.
DR   RefSeq; NP_842605.1; NC_003997.3.
DR   RefSeq; WP_000134128.1; NZ_CP116895.1.
DR   RefSeq; YP_026324.1; NC_005945.1.
DR   AlphaFoldDB; Q81W03; -.
DR   SMR; Q81W03; -.
DR   IntAct; Q81W03; 5.
DR   STRING; 261594.GBAA_0036; -.
DR   DNASU; 1084885; -.
DR   KEGG; ban:BA_0036; -.
DR   KEGG; bar:GBAA_0036; -.
DR   KEGG; bat:BAS0037; -.
DR   PATRIC; fig|198094.11.peg.34; -.
DR   eggNOG; COG0073; Bacteria.
DR   eggNOG; COG0143; Bacteria.
DR   HOGENOM; CLU_009710_9_4_9; -.
DR   OMA; NMFLPDR; -.
DR   Proteomes; UP000000427; Chromosome.
DR   Proteomes; UP000000594; 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; 2.170.220.10; -; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 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   NCBIfam; TIGR00398; metG; 1.
DR   NCBIfam; TIGR00399; metG_C_term; 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; 1.
DR   Pfam; PF01588; tRNA_bind; 1.
DR   PRINTS; PR01041; TRNASYNTHMET.
DR   SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 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..660
FT                   /note="Methionine--tRNA ligase 1"
FT                   /id="PRO_0000139207"
FT   DOMAIN          560..660
FT                   /note="tRNA-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01228"
FT   MOTIF           15..25
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:0000255|HAMAP-Rule:MF_01228"
SQ   SEQUENCE   660 AA;  75125 MW;  5E9FB2B16EA70131 CRC64;
     MTEENKSFYI TTPIYYPSGK LHIGHAYTTV AGDAMARYKC MQGYNVHYLT GTDEHGQKIQ
     KKAEELNVTP QAYVDNIVAG IKELWEKMDI SYDDFIRTTE DRHKDVVEKI FKQLVDQGDI
     YLDEYEGWYS VQDETFYTEH QLVDPIMEGD KVVGGKSPDS GHDVELVREE SYFFRMGKYV
     DRLLKFYEDN PHFIQPESRK NEMINNFIKP GLEDLAVSRT SFDWGVRVPG NPKHVIYVWV
     DALSNYITAL GYGTENEEMY KKFWPADVHL VGKEIVRFHT IYWPIILMAL DLPLPKKVFA
     HGWILMKDGK MSKSKGNVVD PVILIDRYGL DALRYYLLRE VPFGSDGVFT PEGFVERINF
     DLANDLGNLL NRTVAMIDKY FNGEIPAFKA NVTEFDETLV TFAKDTLKKV EEAMENMEFS
     VALSSIWQLV SRTNKYIDET QPWVLAKDED DREKLASVMA HLAEVLRQTG IMLMPFLTVA
     PSKMFAQLGL TDEAHTSWGS LSTIGCIPAG TKVEKGQPIF PRLEMDVEVA YIKEQMKASA
     PKVEEKKEEE PKAEEITIDD FFKVELRVAE VLSAEPVKKA DKLLKIQLDL GTEKRQVVSG
     IAKFYSPEDL KGKKVICVTN LKPVKLRGEL SQGMILAGEE NGVLSLASID QNIPNGTKIK
//
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