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Database: UniProt
Entry: A0A1J4X2Y2_9BACT
LinkDB: A0A1J4X2Y2_9BACT
Original site: A0A1J4X2Y2_9BACT 
ID   A0A1J4X2Y2_9BACT        Unreviewed;       505 AA.
AC   A0A1J4X2Y2;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 26.
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=AUJ11_00260 {ECO:0000313|EMBL:OIO52839.1};
OS   Parcubacteria group bacterium CG1_02_44_65.
OC   Bacteria.
OX   NCBI_TaxID=1805311 {ECO:0000313|EMBL:OIO52839.1, ECO:0000313|Proteomes:UP000182601};
RN   [1] {ECO:0000313|EMBL:OIO52839.1, ECO:0000313|Proteomes:UP000182601}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CG1_02_44_65 {ECO:0000313|EMBL:OIO52839.1};
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:OIO52839.1}.
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DR   EMBL; MNWL01000008; OIO52839.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1J4X2Y2; -.
DR   Proteomes; UP000182601; 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; IPR002300; aa-tRNA-synth_Ia.
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; PF00133; tRNA-synt_1; 1.
DR   Pfam; PF09334; tRNA-synt_1g; 1.
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          3..80
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          138..359
FT                   /note="Methionyl/Leucyl tRNA synthetase"
FT                   /evidence="ECO:0000259|Pfam:PF09334"
FT   DOMAIN          393..480
FT                   /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT                   anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF08264"
SQ   SEQUENCE   505 AA;  58207 MW;  BE856D8F3EFE8E7D CRC64;
     MAKKFYITTT APYVNADPHI GFALEIIQAD AVARYHRLLG EEVIFGCGTD EHGLKIYRKA
     LEEKLSPQKY CDQSVTAWNK LKQVLNLSYT HFIRTTERRH LEAAQALWQR CQDNGDIYKK
     TYKSKYCVGC ELEKTDSELE QGRCPIHPNL EIELINEENY FFRFSKYQKP LLDFYAQNPD
     FVVPRYRFNE IIEFVKNGLE DFSVSRLKSK MPWGVDIPGD PNHVMYVWFD ALVFYISTLG
     WPKIADFAGF WPGIQVAGKD NLRQQSAIWQ AMLMSASLPN TRQILIHGFI QSGGQKMSKS
     LGNVIDPIFL SQKYGADALR YYLLAKIHPF NDSDFTIQLF EEAYNSDLAN GLGNLTSRII
     TMCQKFTGGV VPPKIELKNH PLRKLEIAVW KMLEQKMPTF EFHLVLESIW NFIHALDKYI
     DETKPWVLAK QGKQKQIDEI IFVLLDCLKD LAWLIAAFLP EAAQKITTAL NLKDLLAKDP
     IYKDNWASLK PGTKIKPIKS LFPRI
//
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