ID   A0A1Y4H4V2_9FIRM        Unreviewed;       807 AA.
AC   A0A1Y4H4V2;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-SEP-2017, entry version 2.
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; Clostridiales; Ruminococcaceae;
OC   Drancourtella.
OX   NCBI_TaxID=1965589 {ECO:0000313|EMBL:OUP03147.1};
RN   [1] {ECO:0000313|EMBL:OUP03147.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=An210 {ECO:0000313|EMBL:OUP03147.1};
RA   Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T.,
RA   Cizek A., 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: ATP + L-leucine + tRNA(Leu) = AMP +
CC       diphosphate + L-leucyl-tRNA(Leu). {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
CC       family. {ECO:0000256|HAMAP-Rule:MF_00049,
CC       ECO:0000256|RuleBase:RU363039}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00049}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:OUP03147.1}.
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DR   EMBL; NFJS01000001; OUP03147.1; -; Genomic_DNA.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.730.10; -; 1.
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; 1.
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|HAMAP-Rule:MF_00049,
KW   ECO:0000256|RuleBase:RU363039};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00049,
KW   ECO:0000256|RuleBase:RU363039};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00049};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00049,
KW   ECO:0000256|RuleBase:RU363039, ECO:0000313|EMBL:OUP03147.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00049,
KW   ECO:0000256|RuleBase:RU363039};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00049,
KW   ECO:0000256|RuleBase:RU363039}.
FT   DOMAIN       42    183       tRNA-synt_1g. {ECO:0000259|Pfam:PF09334}.
FT   DOMAIN      223    399       tRNA-synt_1_2. {ECO:0000259|Pfam:
FT                                PF13603}.
FT   DOMAIN      419    609       tRNA-synt_1. {ECO:0000259|Pfam:PF00133}.
FT   DOMAIN      654    774       Anticodon_1. {ECO:0000259|Pfam:PF08264}.
FT   MOTIF       583    587       "KMSKS" region. {ECO:0000256|HAMAP-Rule:
FT                                MF_00049}.
FT   BINDING     586    586       ATP. {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
//