ID A0A0W8JJ12_9VIBR Unreviewed; 857 AA.
AC A0A0W8JJ12;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
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=VRK_09380 {ECO:0000313|EMBL:KUJ00225.1};
OS Vibrio sp. MEBiC08052.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=1761910 {ECO:0000313|EMBL:KUJ00225.1, ECO:0000313|Proteomes:UP000054473};
RN [1] {ECO:0000313|EMBL:KUJ00225.1, ECO:0000313|Proteomes:UP000054473}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MEBiC08052 {ECO:0000313|EMBL:KUJ00225.1,
RC ECO:0000313|Proteomes:UP000054473};
RA Kim Y.J., Lee J.-H., Kwon K.K.;
RT "Genome sequence of Vibrio sp. MEBiC08052.";
RL Submitted (DEC-2015) 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: 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:KUJ00225.1}.
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DR EMBL; LQIY01000004; KUJ00225.1; -; Genomic_DNA.
DR RefSeq; WP_059120271.1; NZ_KQ947475.1.
DR AlphaFoldDB; A0A0W8JJ12; -.
DR STRING; 1761910.VRK_09380; -.
DR PATRIC; fig|1761910.3.peg.945; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000054473; 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; 2.20.28.290; -; 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; 2.
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}.
FT DOMAIN 39..180
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 221..403
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 416..570
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 617..650
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 697..821
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 42..52
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT MOTIF 617..621
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT BINDING 620
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 857 AA; 96709 MW; 52D9E1C727598704 CRC64;
MQEQYNPQEI EPKVQAYWEN SKTFTVTENP SKEKFYCLSM FPYPSGRLHM GHVRNYTIGD
VISRFQRLQG KNVMQPIGWD AFGLPAENAA VKNKTAPAPW TYENIEYMKN QLKLLGFGYD
WNREFATCRP EYYRWEQEFF TKLYEKGLVY KKTSSVNWCP TDQTVLANEQ VENGCCWRCD
TPVEQKEIPQ WFIKITAYAQ ELLDDLDTLD GWPEMVKTMQ RNWIGRSEGV ELQFDVPNYG
ALEVYTTRPD TLMGVTYVGI AAGHPLAAIA AQNTPAIEKF IDECKNTKVA EAELATMEKK
GIDTGLKAIH PLNGREVPVY IANFVLMDYG TGAVMAVPAH DQRDFEFATK YGLDIQPVIQ
PADGSALDIS EAAYTDKGVL FNSGEFDGLD FEQALNAIAA KLESQGKGHK TVNFRLRDWG
VSRQRYWGAP IPMVTTQDGE IHPVPADQLP VLLPEDVVMD GVTSPIKADK TWAETTYNGQ
PALRETDTFD TFMESSWYYA RYCSPQADQI VDTEQANYWL PVDQYVGGIE HACMHLLYSR
FFHKLLRDAG YLSSDEPFKK LLCQGMVLAD AFSYQNEKGG KEWVSPTEVK IERDGKGRIT
SAVDAQGRQV EHSGMVKMSK SKNNGIDPQE MVNKYGADTV RLFMMFASPA DMTLEWQESG
VEGANRFLKR VWKLVLEHTS QGEAPAVEPQ SLNNEQKALR REVHKTIAKV TDDIERRQTF
NTAIAAIMEL MNKLGKAPQE NPQDRAILDE ALKAIVVMLS PITPHICFEM WQALGGSDLD
HAPWPAYDEK ALVEDEKLIV LQVNGKVRGK LTVAADAPQE QVESLGLQDE NVQKFTDGLT
IRKVIYVPGK LLSIVAN
//
