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Database: UniProt
Entry: A0A0G1HK26_9BACT
LinkDB: A0A0G1HK26_9BACT
Original site: A0A0G1HK26_9BACT 
ID   A0A0G1HK26_9BACT        Unreviewed;       291 AA.
AC   A0A0G1HK26;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=leucine--tRNA ligase {ECO:0000256|ARBA:ARBA00013164};
DE            EC=6.1.1.4 {ECO:0000256|ARBA:ARBA00013164};
GN   ORFNames=UW39_C0011G0020 {ECO:0000313|EMBL:KKT47295.1};
OS   Parcubacteria group bacterium GW2011_GWC2_44_17.
OC   Bacteria.
OX   NCBI_TaxID=1618929 {ECO:0000313|EMBL:KKT47295.1, ECO:0000313|Proteomes:UP000034811};
RN   [1] {ECO:0000313|EMBL:KKT47295.1, ECO:0000313|Proteomes:UP000034811}
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:KKT47295.1}.
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DR   EMBL; LCIC01000011; KKT47295.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G1HK26; -.
DR   STRING; 1618929.UW39_C0011G0020; -.
DR   PATRIC; fig|1618929.3.peg.597; -.
DR   Proteomes; UP000034811; Unassembled WGS sequence.
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; 3.10.20.590; -; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   InterPro; IPR002300; aa-tRNA-synth_Ia.
DR   InterPro; IPR002302; Leu-tRNA-ligase.
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   PANTHER; PTHR43740:SF2; LEUCINE--TRNA LIGASE, MITOCHONDRIAL-RELATED; 1.
DR   PANTHER; PTHR43740; LEUCYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF00133; tRNA-synt_1; 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.
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:KKT47295.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917}.
FT   DOMAIN          36..85
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          137..254
FT                   /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT                   anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF08264"
SQ   SEQUENCE   291 AA;  33591 MW;  45395E67CC1F1890 CRC64;
     MAYWLPVDLY VGGAEHAVMH LLYARFFCKA LYDAKYITFD EPFTKLINQG LIIGEDGQKM
     SKSRGNVINP DDVVSEYGAD CLRMYEMFMG PFEDAKPWST QGINGIRRFL EKVYILFPKS
     NHESFHGQIS KFQRLEQLLH KTIKKVTEDI ESFKFNTAIS QMMIFINEFQ KQKDDLDTVH
     YKLFTTNFLL LLAPFAPHIA EELWSRTGHT ASIFKTNWPL YKEEFIKDET ITVVVQINGK
     ARGEVNIARD ADQSFVLSEA RSNERVAKFL AGKEVKREVY VKGKIVNFVV A
//
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