ID A0A0G1ZUI9_9BACT Unreviewed; 248 AA.
AC A0A0G1ZUI9;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=Methionyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00030904};
GN ORFNames=UY76_C0045G0007 {ECO:0000313|EMBL:KKW32007.1};
OS Candidatus Uhrbacteria bacterium GW2011_GWA2_52_8d.
OC Bacteria; Candidatus Uhrbacteria.
OX NCBI_TaxID=1618979 {ECO:0000313|EMBL:KKW32007.1, ECO:0000313|Proteomes:UP000034054};
RN [1] {ECO:0000313|EMBL:KKW32007.1, ECO:0000313|Proteomes:UP000034054}
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 -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-methionine + tRNA(Met) = AMP + diphosphate + L-
CC methionyl-tRNA(Met); Xref=Rhea:RHEA:13481, Rhea:RHEA-COMP:9667,
CC Rhea:RHEA-COMP:9698, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:57844, ChEBI:CHEBI:78442, ChEBI:CHEBI:78530,
CC ChEBI:CHEBI:456215; EC=6.1.1.10;
CC Evidence={ECO:0000256|ARBA:ARBA00001234};
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC MetG type 1 subfamily. {ECO:0000256|ARBA:ARBA00008258}.
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:KKW32007.1}.
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DR EMBL; LCRH01000045; KKW32007.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1ZUI9; -.
DR Proteomes; UP000034054; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004825; F:methionine-tRNA ligase activity; IEA:InterPro.
DR GO; GO:0006418; P:tRNA aminoacylation for protein translation; IEA:InterPro.
DR CDD; cd07957; Anticodon_Ia_Met; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR InterPro; IPR041872; Anticodon_Met.
DR InterPro; IPR023458; Met-tRNA_ligase_1.
DR InterPro; IPR015413; Methionyl/Leucyl_tRNA_Synth.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR PANTHER; PTHR45765; METHIONINE--TRNA LIGASE; 1.
DR PANTHER; PTHR45765:SF1; METHIONINE--TRNA LIGASE, CYTOPLASMIC; 1.
DR Pfam; PF19303; Anticodon_3; 1.
DR Pfam; PF09334; tRNA-synt_1g; 1.
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 4..87
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 98..207
FT /note="Methionyl-tRNA synthetase anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF19303"
SQ SEQUENCE 248 AA; 27811 MW; 8DD5D5370E36DC7A CRC64;
MCHGLALPWH IVSSEYLVFE DRKLSTSKGW VLWADDVLDR YDPDLIRYFL IANGPEKADT
NFTWERFVQL GNAELADNYG NLVQRVLAFV VRRFDGQVPS QGSLDDIDRE LLSLAADTFV
QVGVLIEATE LRKAVETVME LVKASNQYLH NRAPWVQIKI DSGRAGTTLA VAMQVIAGLS
ILTEPFMPFQ AARVRQMLAY GDLHTWVLPQ PIEAGITLGE VAPLFGKLDP SVVDEERARL
ESQLADKR
//
