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Database: UniProt
Entry: A0A0G1YLI7_9BACT
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Original site: A0A0G1YLI7_9BACT 
ID   A0A0G1YLI7_9BACT        Unreviewed;       458 AA.
AC   A0A0G1YLI7;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=leucine--tRNA ligase {ECO:0000256|ARBA:ARBA00013164};
DE            EC=6.1.1.4 {ECO:0000256|ARBA:ARBA00013164};
DE   Flags: Fragment;
GN   ORFNames=UY90_C0021G0001 {ECO:0000313|EMBL:KKW44070.1};
OS   Candidatus Peregrinibacteria bacterium GW2011_GWA2_54_9.
OC   Bacteria; Candidatus Peregrinibacteria.
OX   NCBI_TaxID=1619059 {ECO:0000313|EMBL:KKW44070.1, ECO:0000313|Proteomes:UP000034940};
RN   [1] {ECO:0000313|EMBL:KKW44070.1, ECO:0000313|Proteomes:UP000034940}
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}.
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:KKW44070.1}.
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DR   EMBL; LCRV01000021; KKW44070.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G1YLI7; -.
DR   PATRIC; fig|1619059.3.peg.380; -.
DR   Proteomes; UP000034940; 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; cd07958; Anticodon_Ia_Leu_BEm; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 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; 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   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.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:KKW44070.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917}.
FT   DOMAIN          4..117
FT                   /note="Leucyl-tRNA synthetase editing"
FT                   /evidence="ECO:0000259|Pfam:PF13603"
FT   DOMAIN          129..322
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          376..446
FT                   /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT                   anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF08264"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KKW44070.1"
SQ   SEQUENCE   458 AA;  52052 MW;  F80FA081EB9DA1EA CRC64;
     KSERERQENK EKTGVELKGV KAINPVNGEE LPIWTADYVL AHYGTGAVMA VPAHDQRDFE
     FAQKFKLPIT IVVCPHYPEK TCPVLDEAYE GEGHLVASGQ FDGLPSAKAK EEIVKWLSQK
     GLAEKKISYK LRDWIFSRQR YWGEPIPIIK CEKCGNQPVP EEDLPVELPK VKNYEPTGEA
     ESPLAGIKKW VNVKCPKCGG SAKRETNTMP QWAGSCWYYL AYIMRGTSNF QLTTSNAFSY
     WLPVDLYVGG VEHAVLHLLY VRFWHKFLYD IGVVGTKEPF QKLVNQGLIL GPDNQKMSKS
     RGNVINPDDL VKEFGADSLR LYEMFIGPLE DAKPWQTEGI IGVHRFLSRV YNLISKIKNQ
     KSKLQIKNKK NTDKIIHQTI KKVTEDIQNF RFNTAISAMM ILLNELEKQP ESVVIGHLSL
     FIRLLFPFAP HLAQECWEMI GSPSIRSGQA LPRHPELS
//
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