ID A0A0G0NGM2_9BACT Unreviewed; 492 AA.
AC A0A0G0NGM2;
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=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=US98_C0044G0002 {ECO:0000313|EMBL:KKQ76241.1};
OS Parcubacteria group bacterium GW2011_GWC1_38_6.
OC Bacteria.
OX NCBI_TaxID=1618898 {ECO:0000313|EMBL:KKQ76241.1, ECO:0000313|Proteomes:UP000034446};
RN [1] {ECO:0000313|EMBL:KKQ76241.1, ECO:0000313|Proteomes:UP000034446}
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:KKQ76241.1}.
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DR EMBL; LBVB01000044; KKQ76241.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0NGM2; -.
DR PATRIC; fig|1618898.3.peg.479; -.
DR Proteomes; UP000034446; 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 CDD; cd00814; MetRS_core; 1.
DR Gene3D; 2.170.220.10; -; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR InterPro; IPR041872; Anticodon_Met.
DR InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd.
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; PF08264; Anticodon_1; 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 148..375
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 399..482
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
SQ SEQUENCE 492 AA; 56947 MW; 3740AD93451B29F4 CRC64;
MKKNFYFSKK NKVFERPAKG FYLTTSIAYT NAPPHLGFAL ELIQTDVVAR YNRILGKKVF
FLTGTDEHGV KVAKAAAKYG KTPKEFVDTI SDKFKSLKPL LNISNNDFIR TTDQKKHWPV
VKKIWLKLQK NGDIYKKKYQ GLYCSGCEAF ITQKDLKDGK CVLHQKEPEK VEEENYFFRL
SKYTKKIKDL IAKDKLKIIP SSKKKEMLTF LENGLEDISF SRPRKDLKWG IPVPGDDTQT
IYVWADALTN YISAIGYGTA KFKQWWPADI HFVGKDILKF HSLIWPGILL SLKLPLPKTI
FVHGFINVDG QKMSKSLGNV INPLELVKKY GVDPVRYFLL RELPPTEDGD FTYEKFEERY
NADLAKGLGN LVSRTISLSS KLSIKPKTTI SNPKLKMIIN KINKNYKKSI EEFRFNNALA
EIWELVGFCD RYIDTKKPWQ ESKEQKEIIG NLLFAISEIA KLLEPFLPET TEKTTKQLRN
NKYYSLFPRI VR
//
