ID A0A0G2AJC0_9BACT Unreviewed; 616 AA.
AC A0A0G2AJC0;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=leucine--tRNA ligase {ECO:0000256|ARBA:ARBA00013164};
DE EC=6.1.1.4 {ECO:0000256|ARBA:ARBA00013164};
GN ORFNames=UY76_C0020G0007 {ECO:0000313|EMBL:KKW32674.1};
OS Candidatus Uhrbacteria bacterium GW2011_GWA2_52_8d.
OC Bacteria; Candidatus Uhrbacteria.
OX NCBI_TaxID=1618979 {ECO:0000313|EMBL:KKW32674.1, ECO:0000313|Proteomes:UP000034054};
RN [1] {ECO:0000313|EMBL:KKW32674.1, ECO:0000313|Proteomes:UP000034054}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
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};
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00005594, 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:KKW32674.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LCRH01000020; KKW32674.1; -; Genomic_DNA.
DR PATRIC; fig|1618979.3.peg.345; -.
DR Proteomes; UP000034054; Unassembled WGS sequence.
DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004823; F:leucine-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0006429; P:leucyl-tRNA aminoacylation; IEA:InterPro.
DR CDD; cd00812; LeuRS_core; 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
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; IPR015413; Methionyl/Leucyl_tRNA_Synth.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
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; 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; 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|RuleBase:RU363035};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU363035};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU363035};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU363035};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW ECO:0000256|RuleBase:RU363035}.
FT DOMAIN 39..187
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 219..406
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 420..610
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
SQ SEQUENCE 616 AA; 70783 MW; AF26586B647A61A0 CRC64;
MVYPHQAIEK KWQDRWETSG VFHAKDGGEK QKFYCLIEFP YPSGAGLHIG HPRSYTALDV
VSRKRRHQGY NVLYPIGWDA FGLPTENYAI KTGRKPQDIT RENTDTFRRQ LKSLGFSFDW
SREVNTTDPA YYKWTQWMFL EFFKAGLTYK TKQPINWCLS CKIGLANEEV VNGKCERCGG
STEKRDKEQW MIAITKYAER LLEDLDGVDY LEKIKTQQRN WIGRSEGINI RYDVDGLDDQ
VEIFTTRPDT NFGATFIALA PDGDFIKRHI QDCPERLAVE VYVKEVAQKS EIDRVAEGRK
KTGVFTGLYA INQLTNRRMQ IWVADFALGN VGTGVLVGVP GHDRRDFEFA TTFGLDIVRV
VVGSDGDTSE ITREEQVQEE SGMMINSGFL NGLDIHEATE KIKDYIESKG WGKRVVNYKL
RDWVFSRQRY WGEPIPLVWC ESHQWVAVPD EQLPVVLPDV DKYEPTDTGE SPLAAMTDWV
NTTCPQCGGP ARRETDTMPN WAGSSWYFLR YIDSHNDKEF ASQEKLKYWM PVDLYNGGNE
HTTLHLLYSR FWNKFLFDRG YVPTSEPYTR RHSHGLLLAS DGTKMSKSKG NGVDPDEIIS
QYGADALRMX XXTRGS
//