ID A0A1F6D2Q0_9BACT Unreviewed; 486 AA.
AC A0A1F6D2Q0;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
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=A3D62_01725 {ECO:0000313|EMBL:OGG55322.1};
OS Candidatus Kaiserbacteria bacterium RIFCSPHIGHO2_02_FULL_49_11.
OC Bacteria; Candidatus Kaiserbacteria.
OX NCBI_TaxID=1798489 {ECO:0000313|EMBL:OGG55322.1, ECO:0000313|Proteomes:UP000177659};
RN [1] {ECO:0000313|EMBL:OGG55322.1, ECO:0000313|Proteomes:UP000177659}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGG55322.1}.
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DR EMBL; MFLC01000005; OGG55322.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F6D2Q0; -.
DR Proteomes; UP000177659; 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: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.
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 137..364
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
SQ SEQUENCE 486 AA; 55897 MW; E2939BE5916BC577 CRC64;
MSKPLYITTT LPYVNADPHI GFALEIIQAD ALARRARLMG REVFFSTGTD EHGQKIWEAA
QKAGKPIQEY VDYYAGEVQK LKESLNLSND AFIRTTDPHH IEAAKEMWRR CDASGDIYKK
SYKGLYCVGC EAYKSERELE NDHCILHPNI ELQVIEEENY FFRFSKYEKE LLEYLSRPGV
IVPEWRRAEA INFVNGGLED FSISRDKSRL SWGVPVPGDD SQVMYVWFDA LTDYISTLGW
PEDTEGNFAK FWESGETLQM AGKDQVRFQS LMWQAMLMSA KIKNTDSIFY HGFINSGGQR
MSKSLGNVIS PFELVKKYGT DATRYLLLRH AHPVEDSDIT WEKLDEWYEA HLVNGLGNLV
ARVMKLSESH LQEPVRDPEG IQLDLSKLFQ NFRLDLAMDQ AWILIQYIDH TITTSEPFKV
IKTDREKGIE LIKELVRDLY HVAMLLQPFM PETSKKIEEA ILANKKPENL FPRLAKARGE
GGPRLG
//
