ID A0A0G1W2N0_9BACT Unreviewed; 491 AA.
AC A0A0G1W2N0;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 31.
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=UY50_C0001G0013 {ECO:0000313|EMBL:KKW13021.1};
OS Parcubacteria group bacterium GW2011_GWA2_49_9.
OC Bacteria.
OX NCBI_TaxID=1618852 {ECO:0000313|EMBL:KKW13021.1, ECO:0000313|Proteomes:UP000034328};
RN [1] {ECO:0000313|EMBL:KKW13021.1, ECO:0000313|Proteomes:UP000034328}
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:KKW13021.1}.
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DR EMBL; LCQF01000001; KKW13021.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1W2N0; -.
DR STRING; 1618852.UY50_C0001G0013; -.
DR PATRIC; fig|1618852.3.peg.13; -.
DR Proteomes; UP000034328; 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 137..378
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
SQ SEQUENCE 491 AA; 55937 MW; 0B784591FB2EE7B5 CRC64;
MSKPFYITTT LPYVNADPHI GFAFELISAD IVARHRQLAG DEVFFNTGTD EHGTKVWEKA
KEAGKGTQAY TDEYAEKFKE LREPLGLLPT INFIRTTDPH HVAAAQEFWK CCLASGDIYK
KHYRVRYCVG CELEKTDSEL VDGRCGVHPN QELQTREEEN YFFRLSKYQD ALLALYDANP
DFVVPRFRLN EIRSLIQEKG LEDFSISRLK TKMPWGVPVP SDADHVMYVW FDALVNYISA
IGWPRKANPN SPRGEPDDSS FRKWWIESGG VVQFAGKDQV RQQSVMWQAM LMSAKLPPSR
QIVIHGFITS GGEKMSKSLG NVIDPLELVR EYGTDALRFY LARHVHPFED SDFTLEKFKE
AYNADLANGI GNLTSRIMKM AETNLEQPVE VGGKFYPTLD YSREFESFDI QKAATIISTY
ITGIDQIIQT HQPFKLVKED KVGGLKLIAD LVKMLYIVAD KVQVFMPKTS EKIKGLIMAN
KMPSVPLFPR K
//
