ID   A0A0G0BAI3_9BACT        Unreviewed;       478 AA.
AC   A0A0G0BAI3;
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=UR64_C0008G0002 {ECO:0000313|EMBL:KKP66364.1};
OS   Candidatus Nomurabacteria bacterium GW2011_GWE1_35_16.
OC   Bacteria; Candidatus Nomurabacteria.
OX   NCBI_TaxID=1618761 {ECO:0000313|EMBL:KKP66364.1, ECO:0000313|Proteomes:UP000034952};
RN   [1] {ECO:0000313|EMBL:KKP66364.1, ECO:0000313|Proteomes:UP000034952}
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:KKP66364.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LBPY01000008; KKP66364.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G0BAI3; -.
DR   PATRIC; fig|1618761.3.peg.403; -.
DR   Proteomes; UP000034952; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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; IPR001412; aa-tRNA-synth_I_CS.
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.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 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   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
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..145
FT                   /note="Methionyl/Leucyl tRNA synthetase"
FT                   /evidence="ECO:0000259|Pfam:PF09334"
FT   DOMAIN          154..365
FT                   /note="Methionyl/Leucyl tRNA synthetase"
FT                   /evidence="ECO:0000259|Pfam:PF09334"
SQ   SEQUENCE   478 AA;  55355 MW;  B2F0CC7DA022F74A CRC64;
     MNKTFYLTTT LPYVNAPLHM GHALEFVRAD TIVRYKKLLG YDVYFNTGTD EHGLKIFEKA
     KEQGISAQVF VDQGFETFKE QLKMFGVVDD IHFIRTTDEN HEKAAQEFWK RVSDNGYIYK
     KNYEAKYCVG CESEKTDGEL VNGYCQEHPG IDLKIINEEN YFFKYSAFGD KLLEFYNKNP
     NFVIPDFRLN EIKNFVKSGL QDFSISRLKE KMPWGIPVPG DDTQVMYVWF DALVNYISTL
     GWPASEGNFE KYWVNGNPTQ YCGKDNTRFQ SAMWQAMLMA AGVENSRQIV VNGFITGEGG
     IRMSKTLGNV VDPRDIVKEY GTDALRYFLL REVGSFEDSP FTIERFKDSY NSGLANGLGN
     LASRILTLSE KYLEKCPEIP EVSDFTEYFK FYESFDIKKA TDYVWEKIAE LDKIIQDTQP
     FKVVKTDEEK GKEMIKDLVL KLYVIARMLN PIMPETNIKL KELIKQNKKP ETPLFLRK
//