ID A0A0G0GZJ0_9BACT Unreviewed; 456 AA.
AC A0A0G0GZJ0;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 13-SEP-2023, entry version 28.
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=US50_C0014G0004 {ECO:0000313|EMBL:KKQ35457.1};
OS Candidatus Nomurabacteria bacterium GW2011_GWB1_37_5.
OC Bacteria; Candidatus Nomurabacteria.
OX NCBI_TaxID=1618742 {ECO:0000313|EMBL:KKQ35457.1, ECO:0000313|Proteomes:UP000033876};
RN [1] {ECO:0000313|EMBL:KKQ35457.1, ECO:0000313|Proteomes:UP000033876}
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:KKQ35457.1}.
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DR EMBL; LBTF01000014; KKQ35457.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0GZJ0; -.
DR PATRIC; fig|1618742.3.peg.303; -.
DR Proteomes; UP000033876; 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 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:SF1; METHIONINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43326; METHIONYL-TRNA SYNTHETASE; 1.
DR Pfam; PF19303; Anticodon_3; 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 1..127
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 135..343
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 355..444
FT /note="Methionyl-tRNA synthetase anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF19303"
SQ SEQUENCE 456 AA; 52482 MW; 083A81E19701DB5A CRC64;
MGHALEFVRA DIIARYKRMT DLDVFFNTGA DEHGMKIYRE AGKQGKDPQA YADFYAERMK
GLIGLLGLSE FNFVRTTDAD HVKAAQEFWK KCDENGYIYK KSYKAKYCVG CEAEKTDSEL
VNAKCPDHPN LEIEFIEEEN YFFKFSLFQE KLLELYREVP DFVIPDFRYN EIKAFVARGL
EDFSISRLKS KMPWGIEVPG DPLHIMYVWF DALVNYISAV GWPSDMKKFN DWWPVTQYCG
KDNLRYQSAI WQAMLMAAGL PPSKQIIING FITGAGGIKM SKTLGNVVDP REIINEYGAE
ALRFYLAREI NQFEDSPFTK DGFKESYNAN LANGLGNLIS RIMKMAESNL DGPVADLTHH
MPDIYSEALE AFDIKKAAEY VWKEISVLDS YIQEKEPFKL VKEDKEKAKE IIIYLVKGLN
QIAYLLQPIL PTTSAEIFRL IKENKSPEKP LFLRKI
//
