ID A0A1F8F1J6_9BACT Unreviewed; 496 AA.
AC A0A1F8F1J6;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-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=A3B86_00165 {ECO:0000313|EMBL:OGN07007.1};
OS Candidatus Yanofskybacteria bacterium RIFCSPHIGHO2_02_FULL_38_22b.
OC Bacteria; Candidatus Yanofskybacteria.
OX NCBI_TaxID=1802673 {ECO:0000313|EMBL:OGN07007.1, ECO:0000313|Proteomes:UP000176834};
RN [1] {ECO:0000313|EMBL:OGN07007.1, ECO:0000313|Proteomes:UP000176834}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(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:OGN07007.1}.
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DR EMBL; MGJN01000011; OGN07007.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F8F1J6; -.
DR Proteomes; UP000176834; 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; 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:SF2; METHIONINE--TRNA LIGASE; 1.
DR PANTHER; PTHR43326; METHIONYL-TRNA SYNTHETASE; 1.
DR Pfam; PF19303; Anticodon_3; 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 136..359
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 377..482
FT /note="Methionyl-tRNA synthetase anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF19303"
SQ SEQUENCE 496 AA; 56915 MW; E51926B48CB71AF2 CRC64;
MSKFYITTAI LYTNGPPHIG FALELLLADV LARYHRLRGD ETFFLTGTDE HGSTVAKAAA
KHNIELQKFV DGLAEQAKDL TQKLNISNDD FIRTSDKERH WPSAVKLWNI LAEKGDLYKK
KYKGLYCIGH ESFIKKTDLV NGLCPLHQIE PEAIEEENWF FKLSNYKKEI KKRVESDEIK
IVPTSRKNEI LNVIEDAEDI SVSRPTSALK WGIPVPNDPD QVIWVWLDAL PNYISALGYV
KDDARFNKFW PADVHLVGKD IVRFHALIWP AILLSTGLEL PKSIYVHGFI NVDGQKMSKT
IGNVVNPFKV IEKHGTDIVR YFLLREIPSG EDGDFSDKKL EERYNGDLAN GLGNLVQRTV
TLIDSKLNGE LIYTYDQVDR EVIEKTEQIF KEYVKNIDNF VLHEALAKVW ELISYGDKYL
DEKAPWKAIK HDEAEFLSIM NNTFYILYNI AWMLMPFMPE TANKIFETMG ADTEAKSLDN
YKFLVKKSAG LFPRLP
//
