ID A0A0C1LYU0_9LACO Unreviewed; 805 AA.
AC A0A0C1LYU0;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 50.
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=LfDm3_0470 {ECO:0000313|EMBL:KID42065.1};
OS Fructilactobacillus fructivorans.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Fructilactobacillus.
OX NCBI_TaxID=1614 {ECO:0000313|EMBL:KID42065.1, ECO:0000313|Proteomes:UP000031397};
RN [1] {ECO:0000313|EMBL:KID42065.1, ECO:0000313|Proteomes:UP000031397}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DmCS_002 {ECO:0000313|EMBL:KID42065.1,
RC ECO:0000313|Proteomes:UP000031397};
RA Newell P.D., Chaston J.M., Douglas A.E.;
RT "Functional and comparative genomic analyses of the Drosophila gut
RT microbiota identify candidate symbiosis factors.";
RL Submitted (JUN-2014) 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:RU363035}.
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:KID42065.1}.
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DR EMBL; JOJZ01000010; KID42065.1; -; Genomic_DNA.
DR RefSeq; WP_039143849.1; NZ_RIHD01000006.1.
DR AlphaFoldDB; A0A0C1LYU0; -.
DR GeneID; 74913155; -.
DR PATRIC; fig|1614.7.peg.458; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000031397; 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 CDD; cd07958; Anticodon_Ia_Leu_BEm; 1.
DR CDD; cd00812; LeuRS_core; 1.
DR Gene3D; 3.10.20.590; -; 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
DR HAMAP; MF_00049_B; Leu_tRNA_synth_B; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
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 NCBIfam; TIGR00396; leuS_bact; 1.
DR PANTHER; PTHR43740:SF2; LEUCINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43740; LEUCYL-TRNA SYNTHETASE; 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; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR SUPFAM; SSF50677; ValRS/IleRS/LeuRS editing domain; 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|HAMAP-Rule:MF_00049};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00049};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, 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}; Reference proteome {ECO:0000313|Proteomes:UP000031397}.
FT DOMAIN 38..159
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 221..400
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 414..603
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 657..765
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 577..581
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT BINDING 580
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 805 AA; 92562 MW; 63E4CA1753A968F1 CRC64;
MAYDHSKIEK KWQKYWEDHQ TFKTSDKQEK DKYYVLDMFP YPSGQGLHVG HPEGYTATDI
MARFKRMQGK NVLHPIGWDA FGLPAEQYAL KTGHNPRDFT KKNIENFKRQ IKSLGFSYDW
DREVNTSDPS YYKWTQWIFE QLYKMGLAYE DEIEVNWAPD FMGGTVVSNE EVVNGKTERG
GYDVYRKPMK QWVLKITAYA DRLLDDLDDL DWPESIKQMQ RNWIGRSVGA SISFDVNEED
QKIEVFTTRP DTIYGVSYLV LSPENPIVDQ IMTPEQKSEV ENYRAKIASK SDLERTDLNK
DKSGVFTGAY AINPVNGKRI PIWIGDYVLP SYGTGAVMAV PAHDQRDFDF AKKFDLPIIP
VIEGGDVSEA AYTGDGVHIN SGFLDGMDKK QAIDKIIEWL KDHHAGNKKV NYRLRDWIFS
RQRYWGEPIP VIHWDDGTTS LVPEDQLPLR LPKTADIQPS GTGESPLANL TDWVNVTDKN
GRHGRRETNT MPQWAGSSWY YLRYVDPHND KMIADPEKLK YWLPIDLYVG GAEHAVLHLL
YARFWHKVLY DLGVVPTKEP FQKLVNQGMI LGTNHEKMSK SKGNVVNPDD IVKQYGADTL
RLYEMFMGPL SESKPWNTDG IVGANRWIKR IWRLYMNDDN TLSDVIVDDN DGSLDKIYNQ
TVKKVTDDFE NMRFNVAISQ MMVFINEAYK ANKLPKKYAE GFIKLLSPIT PHVAEELWQQ
LGHDRSIELS QWPEADESKL QEDQVELVVQ VNGKVRGHIK VSVDAGKDET EQIALDDENV
KSFLDGKTVR KVIVVPKKIV NIVAK
//