ID A0A1F6BS65_9BACT Unreviewed; 474 AA.
AC A0A1F6BS65;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
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=A2118_03275 {ECO:0000313|EMBL:OGG39799.1};
OS Candidatus Kaiserbacteria bacterium GWA2_50_9.
OC Bacteria; Candidatus Kaiserbacteria.
OX NCBI_TaxID=1798474 {ECO:0000313|EMBL:OGG39799.1, ECO:0000313|Proteomes:UP000179014};
RN [1] {ECO:0000313|EMBL:OGG39799.1, ECO:0000313|Proteomes:UP000179014}
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:OGG39799.1}.
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DR EMBL; MFKN01000041; OGG39799.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F6BS65; -.
DR STRING; 1798474.A2118_03275; -.
DR Proteomes; UP000179014; 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; cd00814; MetRS_core; 1.
DR Gene3D; 2.170.220.10; -; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
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; 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 155..363
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
SQ SEQUENCE 474 AA; 53922 MW; C6A621C6EDD41940 CRC64;
MSARYLTTTL PYVNADPHIG FALEVVQADV LARSWRLAGD EVFFSMGTDE HGQKILESAQ
RAGQEPKAYV DHYAAEFQKL KKALDLSNDT FIRTTDLMHI AAAQEMWRLC DAKGDIYKKA
YTGLYCVGCE AFKTEKETAD GKCPLHPNAA LKEVSEENYF FKFSKYEKKL LEYLEEPGVI
VPEWRRIEAI NFAKGGLEDF SISRERLRLS WGIPVPDDDS QVMYVWFDAL TNYISTLGWP
ADEKGNFTKF WGKGKTLQMA GKDQLRFQSL VWQAMLLSAG IKNTDQIFYH GFITSGGQKM
SKSLGNVINP LELVEKYGTD SVRYILLRHV SPTEDSGLTL EAIHDHYTAH LTNGLGNLVA
RVMKLAEQYL QGPISTGTVG YSKEYTDTIS NFQFNRAADL IWEHIQKLDN KIAEEKPFSV
IRENEEEGKR MINECVRELF WIATMLTPLM PETSQKIIDA IAINKKPENL FPRI
//