ID A0A0G1FA96_9BACT Unreviewed; 255 AA.
AC A0A0G1FA96;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=methionine--tRNA ligase {ECO:0000256|ARBA:ARBA00012838};
DE EC=6.1.1.10 {ECO:0000256|ARBA:ARBA00012838};
GN ORFNames=UV60_C0033G0003 {ECO:0000313|EMBL:KKS83773.1};
OS Parcubacteria group bacterium GW2011_GWA2_43_11.
OC Bacteria.
OX NCBI_TaxID=1618825 {ECO:0000313|EMBL:KKS83773.1, ECO:0000313|Proteomes:UP000034714};
RN [1] {ECO:0000313|EMBL:KKS83773.1, ECO:0000313|Proteomes:UP000034714}
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 -!- 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:KKS83773.1}.
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DR EMBL; LCFC01000033; KKS83773.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1FA96; -.
DR STRING; 1618825.UV60_C0033G0003; -.
DR PATRIC; fig|1618825.3.peg.908; -.
DR Proteomes; UP000034714; 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 Gene3D; 3.40.50.620; HUPs; 1.
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 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 1..141
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
SQ SEQUENCE 255 AA; 29273 MW; C4F03A7C04C96193 CRC64;
MYVWFDALSN YINALDYVHD GQAFQDFWLN ANERIHCIGK GINRFHTIYW PAMLLSAGIP
LPHTVFVHGY FTVDGQKMSK SIGNVIDPID LVEKYGTDAV RYYFLRHQHP FEDGDFTMEK
FHTAYTANLV NGLGNLVSRV MKLAETYLDV PVQRPEAVGF SEEYTKALEA FEFSTAMDSV
WSRVGRADAR MTEEEPFKVI KTNPEEGKRI IAELVLELYH IARMLHPSMP ATSKLIKETI
LANKKPETMF PRIDL
//
