ID   A0A1Y4H4V2_9FIRM        Unreviewed;       807 AA.
AC   A0A1Y4H4V2;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   29-SEP-2021, entry version 19.
DE   RecName: Full=Leucine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00049};
DE            EC=6.1.1.4 {ECO:0000256|HAMAP-Rule:MF_00049};
DE   AltName: Full=Leucyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00049};
DE            Short=LeuRS {ECO:0000256|HAMAP-Rule:MF_00049};
GN   Name=leuS {ECO:0000256|HAMAP-Rule:MF_00049};
GN   ORFNames=B5F37_00420 {ECO:0000313|EMBL:OUP03147.1};
OS   Drancourtella sp. An210.
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Drancourtella; unclassified Drancourtella.
OX   NCBI_TaxID=1965589 {ECO:0000313|EMBL:OUP03147.1, ECO:0000313|Proteomes:UP000196338};
RN   [1] {ECO:0000313|Proteomes:UP000196338}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=An210 {ECO:0000313|Proteomes:UP000196338};
RA   Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA   Rychlik I.;
RT   "Function of individual gut microbiota members based on whole genome
RT   sequencing of pure cultures obtained from chicken caecum.";
RL   Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-leucine + tRNA(Leu) = AMP + diphosphate + L-leucyl-
CC         tRNA(Leu); Xref=Rhea:RHEA:11688, Rhea:RHEA-COMP:9613, Rhea:RHEA-
CC         COMP:9622, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57427,
CC         ChEBI:CHEBI:78442, ChEBI:CHEBI:78494, ChEBI:CHEBI:456215; EC=6.1.1.4;
CC         Evidence={ECO:0000256|ARBA:ARBA00001372, ECO:0000256|HAMAP-
CC         Rule:MF_00049};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00049}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|HAMAP-Rule:MF_00049,
CC       ECO:0000256|RuleBase:RU363039}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00049}.
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:OUP03147.1}.
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DR   EMBL; NFJS01000001; OUP03147.1; -; Genomic_DNA.
DR   EnsemblBacteria; OUP03147; OUP03147; B5F37_00420.
DR   Proteomes; UP000196338; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004823; F:leucine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006429; P:leucyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.620; -; 2.
DR   HAMAP; MF_00049_B; Leu_tRNA_synth_B; 1.
DR   InterPro; IPR002300; aa-tRNA-synth_Ia.
DR   InterPro; IPR002302; Leu-tRNA-ligase.
DR   InterPro; IPR025709; Leu_tRNA-synth_edit.
DR   InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd.
DR   InterPro; IPR015413; Methionyl/Leucyl_tRNA_Synth.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR   InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
DR   PANTHER; PTHR43740; PTHR43740; 2.
DR   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF00133; tRNA-synt_1; 1.
DR   Pfam; PF13603; tRNA-synt_1_2; 1.
DR   Pfam; PF09334; tRNA-synt_1g; 1.
DR   PRINTS; PR00985; TRNASYNTHLEU.
DR   SUPFAM; SSF47323; SSF47323; 1.
DR   SUPFAM; SSF50677; SSF50677; 1.
DR   TIGRFAMs; TIGR00396; leuS_bact; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW   ECO:0000256|HAMAP-Rule:MF_00049};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00049}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00049};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00049};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00049};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW   Rule:MF_00049}.
FT   DOMAIN          42..185
FT                   /note="tRNA-synt_1g"
FT                   /evidence="ECO:0000259|Pfam:PF09334"
FT   DOMAIN          223..399
FT                   /note="tRNA-synt_1_2"
FT                   /evidence="ECO:0000259|Pfam:PF13603"
FT   DOMAIN          419..610
FT                   /note="tRNA-synt_1"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          654..774
FT                   /note="Anticodon_1"
FT                   /evidence="ECO:0000259|Pfam:PF08264"
FT   MOTIF           583..587
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT   BINDING         586
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   807 AA;  91964 MW;  3BD7985F0B8B572D CRC64;
     MSVPYNHRAI EKKWRQHWEE HPVNVQEDER GKHEKYYCLD MFPYPSGNGL HVGHWRGYVI
     SDVWSRYKLL QGYYIIHPMG WDAFGLPAEN YAIKMGVHPA KSTAENVKNI KRQINEIAAL
     YDWDREVNTT DPNFYKWTQW IFVKMFKAGL AYEKEFPINW CPSCKTGLAN EEVVNGKCER
     CGTEVTKKNL RQWMLKITKY AERLLADLDK LDWPEKVKKM QSDWIGKSYG AEVDFPVDGR
     DDKITVYTTR PDTLYGATFM VLAPEHALAK ELATDETREA VEKYIYDASM KSNVDRLQDK
     EKTGVFTGSY AVNPMNQKKI PIWLSDYVLA DYGTGAIMCV PAHDDRDFAF ATKFGIPIIQ
     VIAKDGKEIE NMTEAYTEAA GTMINSGEWD GMESAILKKE APMMIEERGI GRKTVNYKLR
     DWVFSRQRYW GEPIPIVHCP DCGAVPVPEE ELPLTLPDVD SYEPTGTGES PLAAIDSWVN
     TTCPVCGKPA KRETNTMPQW AGSSWYFLRY VDPHNDKELV SKEKADAMLP VDMYIGGVEH
     AVLHLLYSRF YTKFLYDIGA VDFDEPFTKL FNQGMITGKN GIKMSKSKGN VVSPDALVRD
     YGCDSLRMYE LFVGPPELDA EWDDRGIDGV YRFLNKLWNL VMDNKEKGVE PSKEMIKLRN
     KMVYDITSRL ESFSLNTVIS GFMEYNNKFI ELVKKEGGID KETLSTIAVL LAPFAPHMGE
     ELWEQLGHTG SVFHAGWPTY DEEAMKDDEI EVAVQINGKT RAVVTISAES TKEEAIAAGK
     EAIKEKLTGN IVKEIYVPGR IINIVMK
//