ID A0A1G2DBK7_9BACT Unreviewed; 495 AA.
AC A0A1G2DBK7;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=methionine--tRNA ligase {ECO:0000256|ARBA:ARBA00012838};
DE EC=6.1.1.10 {ECO:0000256|ARBA:ARBA00012838};
GN ORFNames=A3C93_01495 {ECO:0000313|EMBL:OGZ11004.1};
OS Candidatus Lloydbacteria bacterium RIFCSPHIGHO2_02_FULL_54_17.
OC Bacteria; Candidatus Lloydbacteria.
OX NCBI_TaxID=1798664 {ECO:0000313|EMBL:OGZ11004.1, ECO:0000313|Proteomes:UP000178636};
RN [1] {ECO:0000313|EMBL:OGZ11004.1, ECO:0000313|Proteomes:UP000178636}
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 -!- 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:OGZ11004.1}.
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DR EMBL; MHLO01000041; OGZ11004.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G2DBK7; -.
DR STRING; 1798664.A3C93_01495; -.
DR Proteomes; UP000178636; 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; IPR041872; Anticodon_Met.
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 PANTHER; PTHR43326:SF1; METHIONINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43326; METHIONYL-TRNA SYNTHETASE; 1.
DR Pfam; PF19303; Anticodon_3; 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 145..376
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 408..482
FT /note="Methionyl-tRNA synthetase anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF19303"
SQ SEQUENCE 495 AA; 56227 MW; 5018FA2FDDCBA4F6 CRC64;
MVDKKPIYIT TTLPYVNADP HVGFAMEIIR ADALARYYRL AGHEVYFNTG TDEHGAKIYE
AATNEGVDPE VYTDKLAERF RALAPALGLA ANIPGITFNF IRTTDKDHVA AAEEFWKKCE
AKGDIYKKLY SVKYCVGCEL EKTDSELENG RCPIHPNREL EFREEENYFF RFSNYTEKLK
KFYDDHPDFV IPDFRFNEMR AFVGRGLEDF SISRLKTKMP WGVPVPGDPD QVMYVWFDAL
VNYVSAIGWP KDMAKFTKWW PVIQYCGKDN NRQQSAMWQA MLMSADLPNS EHIVINGFIN
SAGGQKMSKS LGNVLNPFDV IDAFKDVTPF PDDVLRFVLL HDIPSFEDGD LTMESIKASY
AAHLQNGLGN LTSRIMKMAT SYAVVYTDYP GDATVETQKS AVVSGACEQF DLHKAIGEIW
SNGIGMLDAF IQREEPFKKI KTDPVRAKEN VAYLLNNLLS IAQALKPFLP RTAEEIGRLI
RENKMPEKPL FARLP
//
