ID A0A0G1LR07_9BACT Unreviewed; 473 AA.
AC A0A0G1LR07;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=UX00_C0004G0013 {ECO:0000313|EMBL:KKT98170.1};
OS Microgenomates group bacterium GW2011_GWB1_45_17.
OC Bacteria.
OX NCBI_TaxID=1618506 {ECO:0000313|EMBL:KKT98170.1, ECO:0000313|Proteomes:UP000034461};
RN [1] {ECO:0000313|EMBL:KKT98170.1, ECO:0000313|Proteomes:UP000034461}
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:KKT98170.1}.
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DR EMBL; LCKN01000004; KKT98170.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1LR07; -.
DR PATRIC; fig|1618506.3.peg.284; -.
DR Proteomes; UP000034461; 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:SF2; METHIONINE--TRNA LIGASE; 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.
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 5..362
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
SQ SEQUENCE 473 AA; 53482 MW; A81D20BF29739096 CRC64;
MTKFYITAAI PYVNAKPHIG HALEFVQGDV IARYHRLAGD ETMYLTGSDE NALKNVQAAE
KAGQEVRAFC TLHADEFVEL AEKLSVQFDV FQRSSSEKHH VSSQELWKLC AKNGDIYKKT
YEGLYCVGCE AFYTPDELNK NGECFEHPGK KLEKVGEENY FFKLSSYKEK ILQLIESGEL
EIIPEKQKNE VVRFLQGDVR DISISRSKER AHNWGVEVPG DSTQMMYVWF DALNVYQSGV
GFGIDEQKYK KWWPADVHLI GKGIIRFHAV YWPAMLLSAK LPLPKRIYSH GYITVNGQKM
SKTLGNVIDP IEIIEKYGVE PVRYYVLREI PTTEDGDISI DRVGEMYSSA LANELGNLVS
RLAKLCEGSS IAATNVKTFS PAVSQAINRF ALRGALDDIW NRISALNKRI SDEKVWEKKG
DDRLKTLNEL VAGVIAVGYD LQPFLPETAK RMLSIFTEKT ITQPAPLFPR LSA
//
