ID A0A0F9YU70_9BACT Unreviewed; 493 AA.
AC A0A0F9YU70;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=UR19_C0005G0028 {ECO:0000313|EMBL:KKP30026.1};
OS Candidatus Nomurabacteria bacterium GW2011_GWF1_31_48.
OC Bacteria; Candidatus Nomurabacteria.
OX NCBI_TaxID=1618767 {ECO:0000313|EMBL:KKP30026.1, ECO:0000313|Proteomes:UP000034934};
RN [1] {ECO:0000313|EMBL:KKP30026.1, ECO:0000313|Proteomes:UP000034934}
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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
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:KKP30026.1}.
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DR EMBL; LBOG01000005; KKP30026.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F9YU70; -.
DR PATRIC; fig|1618767.3.peg.581; -.
DR Proteomes; UP000034934; 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:0046872; F:metal ion 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; IPR032678; tRNA-synt_1_cat_dom.
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; PF01406; tRNA-synt_1e; 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.
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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU363039};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW ECO:0000256|RuleBase:RU363039}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 15..128
FT /note="tRNA synthetases class I catalytic"
FT /evidence="ECO:0000259|Pfam:PF01406"
FT DOMAIN 140..366
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
SQ SEQUENCE 493 AA; 57041 MW; 3BD8059EDEAF93F3 CRC64;
MKKESFYITT TLPYVNAPLH MGHALELVRA DAIARYKKLI GYDVFFNTGT DEHGIKIYQK
AKENEIEIQD FVDQGFDTFK KQLKMFGMSD DIHFVRTTDK HHEAAAQEFW KKVNDNGYIY
KKNYETKYCI GCESEKTDSE LEDDECRDHP GIKVSIINEE NYFFKYSAFG DKLLGFYEKN
PDFIVPDFRF NEIKAFVKKG LQDFSISRLK SKMPWGIAVP GDEDHVMYVW FDALTNYIST
LGWPEDTEQF KKYWENGNPT QYCGKDNTRF QGAMWQAMLI AADLPNSHQV VVDGFITGEG
GVRMSKTLGN VVDPREIVSE YGTDALRYFL LREVGSFEDS PFTLERFKDA YNSGLANGLG
NLSSRIMTMA VSNNITISEF PSFEDVLEIF SEDEEIQFHK YIEKFDIKKA IDLVWFQVQL
LDGIIQKSQP FKLVKSENLE DSEKGKKQIE ELILGLYYIA KLLEPILPET SKKIQQLIKE
NKKPDAPLFL RKE
//
