ID A0A0G1X2G4_9BACT Unreviewed; 479 AA.
AC A0A0G1X2G4;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 30.
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=UY68_C0005G0019 {ECO:0000313|EMBL:KKW25161.1};
OS Parcubacteria group bacterium GW2011_GWF2_52_12.
OC Bacteria.
OX NCBI_TaxID=1618976 {ECO:0000313|EMBL:KKW25161.1, ECO:0000313|Proteomes:UP000034153};
RN [1] {ECO:0000313|EMBL:KKW25161.1, ECO:0000313|Proteomes:UP000034153}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
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:KKW25161.1}.
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DR EMBL; LCQX01000005; KKW25161.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1X2G4; -.
DR PATRIC; fig|1618976.3.peg.271; -.
DR Proteomes; UP000034153; 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; 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 138..366
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
SQ SEQUENCE 479 AA; 54634 MW; C5F6ED9A055A0379 CRC64;
MKERIYITTT LPYVNADPHI GFALEAVQAD ACARWHRGSG REVFFNTGTD EHGQKIWKKA
QELGKDPQEY SNEAVIHFEA LKGKLNLSYD NFIRTTGHAH VAAAQEFWRR CDKSGDIYKK
KYQLKYCVGC ELEKSASELV GGRCPIHPHM ELELIDEENY FFKFSKYQDQ LLELYKNDDF
VLPESRRNEV RNFASQGLND FSISRLAEKM PWGIAVPGEE AILPAGRQVM YVWFDALVNY
VSAIGWPERM EEFEKWWPVI QFAGKDNTRQ QAAMWQAMLL SAGLSPSRQI VIHGFITSGG
AKMSKSAGNV IDPIAIVDEY GTDALRYYLL SAVSPFEDSD FTMEKFKESY NGNLANGLGN
LVSRIMKMSE VYQVSSQLTE VRLQSIPPEY QCAMESYRYN DAMDVIWENI RDADLRITET
EPFKLVKTDV EAGKKIITEL VHALAEIAYL LTPFMPSTAE AIQNAIKENR LPSPLFVRK
//
