ID G9EN87_9GAMM Unreviewed; 512 AA.
AC G9EN87;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Methionyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00030904};
GN ORFNames=LDG_6709 {ECO:0000313|EMBL:EHL31248.1};
OS Legionella drancourtii LLAP12.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=658187 {ECO:0000313|EMBL:EHL31248.1, ECO:0000313|Proteomes:UP000002770};
RN [1] {ECO:0000313|EMBL:EHL31248.1, ECO:0000313|Proteomes:UP000002770}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LLAP12 {ECO:0000313|EMBL:EHL31248.1,
RC ECO:0000313|Proteomes:UP000002770};
RX PubMed=22047552; DOI=10.1186/1471-2164-12-542;
RA Gimenez G., Bertelli C., Moliner C., Robert C., Raoult D., Fournier P.E.,
RA Greub G.;
RT "Insight into cross-talk between intra-amoebal pathogens.";
RL BMC Genomics 12:542-542(2011).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-methionine + tRNA(Met) = AMP + diphosphate + L-
CC methionyl-tRNA(Met); Xref=Rhea:RHEA:13481, Rhea:RHEA-COMP:9667,
CC Rhea:RHEA-COMP:9698, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:57844, ChEBI:CHEBI:78442, ChEBI:CHEBI:78530,
CC ChEBI:CHEBI:456215; EC=6.1.1.10;
CC Evidence={ECO:0000256|ARBA:ARBA00001234};
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|RuleBase:RU363039}.
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DR EMBL; JH413817; EHL31248.1; -; Genomic_DNA.
DR RefSeq; WP_006870639.1; NZ_JH413817.1.
DR AlphaFoldDB; G9EN87; -.
DR STRING; 658187.LDG_6709; -.
DR eggNOG; COG0143; Bacteria.
DR HOGENOM; CLU_009710_10_1_6; -.
DR InParanoid; G9EN87; -.
DR OrthoDB; 9810191at2; -.
DR Proteomes; UP000002770; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004825; F:methionine-tRNA ligase activity; IEA:InterPro.
DR GO; GO:0006418; P:tRNA aminoacylation for protein translation; IEA:InterPro.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 2.20.28.20; Methionyl-tRNA synthetase, Zn-domain; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR023458; Met-tRNA_ligase_1.
DR InterPro; IPR015413; Methionyl/Leucyl_tRNA_Synth.
DR InterPro; IPR029038; MetRS_Zn.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR PANTHER; PTHR45765; METHIONINE--TRNA LIGASE; 1.
DR PANTHER; PTHR45765:SF1; METHIONINE--TRNA LIGASE, CYTOPLASMIC; 1.
DR Pfam; PF09334; tRNA-synt_1g; 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 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000002770}.
FT DOMAIN 21..397
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
SQ SEQUENCE 512 AA; 58725 MW; FA6AE5EA3759D512 CRC64;
MSKKGKSTNI NRTLLLYLVF PTPNGRLHLG HIGGPYLKLD VIKRYNQQIG NKAYIYGGTD
SYDSYVLLKA LDENKKPEEI CEYYHQCIKQ DLLKMNIALD DFVNPLHEKE LFSKIAKKIH
DRIIPFTISE QESYPFTKER GFLPPSFITG NCPNCEQKIH SFICEHCGLY FKPEQAKNLS
CKTSDNMIEL KKIHSMFLPI QTHELTKQIS SKTNSKVLLD KVATLCSQTD TSRLSIPISW
GVETGQKNSV FYTYGNFFHY LYTLGEKFKE QHQLEKNPLD ELHTDKPGYV ETVASFGFDN
IMSFMINTLN YAITIKSPGL THYLPSYFLT LDGEKFSTSR KHAIWVDSLA NEVSIDILRF
YLLKINVDNI FNDFKTNEFI NFHNQVATRL TKVLGNQAIK VRSGLNSLQI KARYDELIEQ
SYAITMPENY SATQIYHNLT LFLAQDPKDS VAHTLWLKCF AVLFYPVMPE LSGKIWSGLG
FHGFPNPNES LQAEGYLPLD ISIPLISIEH LK
//
