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Database: UniProt
Entry: A0A1J4WG98_9BACT
LinkDB: A0A1J4WG98_9BACT
Original site: A0A1J4WG98_9BACT 
ID   A0A1J4WG98_9BACT        Unreviewed;       476 AA.
AC   A0A1J4WG98;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=Methionine--tRNA ligase {ECO:0000256|ARBA:ARBA00018753};
DE            EC=6.1.1.10 {ECO:0000256|ARBA:ARBA00012838};
DE   AltName: Full=Methionyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00030904};
GN   ORFNames=AUJ31_02265 {ECO:0000313|EMBL:OIO46241.1};
OS   Parcubacteria group bacterium CG1_02_39_15.
OC   Bacteria.
OX   NCBI_TaxID=1805304 {ECO:0000313|EMBL:OIO46241.1, ECO:0000313|Proteomes:UP000181921};
RN   [1] {ECO:0000313|EMBL:OIO46241.1, ECO:0000313|Proteomes:UP000181921}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CG1_02_39_15 {ECO:0000313|EMBL:OIO46241.1};
RX   PubMed=27112493;
RA   Probst A.J., Castelle C.J., Singh A., Brown C.T., Anantharaman K.,
RA   Sharon I., Hug L.A., Burstein D., Emerson J.B., Thomas B.C., Banfield J.F.;
RT   "Genomic resolution of a cold subsurface aquifer community provides
RT   metabolic insights for novel microbes adapted to high CO concentrations.";
RL   Environ. Microbiol. 0:0-0(2016).
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:0000256|ARBA:ARBA00003314}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000256|RuleBase:RU363039}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OIO46241.1}.
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DR   EMBL; MNWE01000034; OIO46241.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1J4WG98; -.
DR   STRING; 1805304.AUJ31_02265; -.
DR   Proteomes; UP000181921; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004825; F:methionine-tRNA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006431; P:methionyl-tRNA aminoacylation; IEA:InterPro.
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   InterPro; IPR041872; Anticodon_Met.
DR   InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd.
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; PF08264; Anticodon_1; 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 {ECO:0000256|ARBA:ARBA00023146,
KW   ECO:0000256|RuleBase:RU363039};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU363039};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU363039};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU363039};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW   ECO:0000256|RuleBase:RU363039}.
FT   DOMAIN          5..145
FT                   /note="Methionyl/Leucyl tRNA synthetase"
FT                   /evidence="ECO:0000259|Pfam:PF09334"
FT   DOMAIN          149..359
FT                   /note="Methionyl/Leucyl tRNA synthetase"
FT                   /evidence="ECO:0000259|Pfam:PF09334"
FT   DOMAIN          383..465
FT                   /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT                   anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF08264"
SQ   SEQUENCE   476 AA;  55615 MW;  B4158F8E15C7A28C CRC64;
     MKKFYITTTL PYVNAEAHLG FTLEIVQADV IARYFRQQGY EVFFNTGVDE HGLKVFRKTQ
     KEDLEPQVYC DIYAKRYKAL KQVLNLSYNS FIRTTDPHHI KAAQEFWRRC DKNRDIYKKN
     YKVKYCVGCE LEKTESELVR GKCPIHPEQE PEIIEEENYF FRYAKYQDKL LELYQKNPQF
     VLPESRLNEI KKFTERGLKD FSISRLKEKM SWGIPVPGDD KHVIAVWFDA LVNYISCLGW
     PDDPKRFNDF WPGLQVAGKD NLRQQSSMWQ SMLISAGLPT SKQVFIHGFV TSGGQKMSKS
     LGNVIDPFEL VKKYGTDPVR YFLLREIPPA EDGDFTYEKF EQRYNSDLAK GLGNLVARVI
     TMAKNYKIPT LAKATAGKQN PKIKKETDKA QKDYKKALKE FKFNEALIAI WGLISFCDKY
     IEKERPWENK NQKVINDLLF AISNIAQLLQ PFLPETSEKI FGQLKTRKSR PLFPRI
//
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