ID A0A0G0MAB3_9BACT Unreviewed; 464 AA.
AC A0A0G0MAB3;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 13-SEP-2023, entry version 32.
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=UT23_C0014G0016 {ECO:0000313|EMBL:KKQ97280.1};
OS Candidatus Woesebacteria bacterium GW2011_GWA1_39_12.
OC Bacteria; Candidatus Woesebacteria.
OX NCBI_TaxID=1618549 {ECO:0000313|EMBL:KKQ97280.1, ECO:0000313|Proteomes:UP000034325};
RN [1] {ECO:0000313|EMBL:KKQ97280.1, ECO:0000313|Proteomes:UP000034325}
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:KKQ97280.1}.
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DR EMBL; LBWA01000014; KKQ97280.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0MAB3; -.
DR PATRIC; fig|1618549.4.peg.1147; -.
DR Proteomes; UP000034325; 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; 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 6..146
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 156..352
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
SQ SEQUENCE 464 AA; 53424 MW; AD19819E77A27360 CRC64;
MNKKFFITTA IDYTNDAVHI GHSYQKILAD AIARYHRLLG EETYFLTGTD EHGQKVEKSA
IEKGVEPKKF VDEIAAEDKA EWDALNISYD RFIRTTDPDH IKFAQEFYLK AKTSGDIYLG
KYEGLYCEGC EAYYEESELV DGKCPFHPNR ELIKISEENY FFRLSKYQNF LQKYIEGHPE
FVIPETKRRE ILSFIKNGLR DFSVSRQSVS WGIPVPDDPK HTIYVWFDAL INYLTYGVEK
KSWPADLHVL GKDNQRFHAI YWPAMLKSAG YELPKTILVH DFISLNGQKI SKSLGNVIKP
SELTKDFGVD GVRYYFLRFG PSTNDVDISL EKLKTIFNSD LANGLGNLVA RVAGLSERSE
FTTSKPKKLS FSKEVVKAIE KYEVDKALEL IWGEIKKADV FINERGVWNL KGKQKEAALT
YLINRIRQVA SDLKPFLPET AEKIEKQFKG PKIKSEKPLF PRLD
//
