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Database: UniProt
Entry: A0A0G1EAY4_9BACT
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ID   A0A0G1EAY4_9BACT        Unreviewed;       672 AA.
AC   A0A0G1EAY4;
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=UV54_C0013G0001 {ECO:0000313|EMBL:KKS80201.1};
OS   Candidatus Beckwithbacteria bacterium GW2011_GWA2_43_10.
OC   Bacteria; Candidatus Beckwithbacteria.
OX   NCBI_TaxID=1618369 {ECO:0000313|EMBL:KKS80201.1, ECO:0000313|Proteomes:UP000034213};
RN   [1] {ECO:0000313|EMBL:KKS80201.1, ECO:0000313|Proteomes:UP000034213}
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:KKS80201.1}.
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DR   EMBL; LCEW01000013; KKS80201.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G1EAY4; -.
DR   STRING; 1618369.UV54_C0013G0001; -.
DR   PATRIC; fig|1618369.3.peg.221; -.
DR   Proteomes; UP000034213; 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; 3.10.20.590; -; 1.
DR   Gene3D; 3.40.50.620; HUPs; 2.
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:KKS80201.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917}.
FT   DOMAIN          69..262
FT                   /note="Leucyl-tRNA synthetase editing"
FT                   /evidence="ECO:0000259|Pfam:PF13603"
FT   DOMAIN          276..466
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          510..631
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:KKS80201.1"
SQ   SEQUENCE   672 AA;  76898 MW;  F30604DBAC461178 CRC64;
     KKSLLNWCPS CKTVLADEQA EAGVCERCKT VTEKKETFQW FFKITDYAQR LLDNLDKINW
     PEKIKIAQRN WIGRKEGINI TYRVKVPNSL KVRNLLTSVT VFTTAPVNFG ATFIVIGPEH
     ELARKAAKTD IKVKEYIEKA LKKSDIDRIA EGKEKTGVFT GLYAINHVTK KEIPIYVTDF
     VLGHVGTGAV QGCPGHDKRD FEFAKKFKLP IPRVIVGKDG DDSPIERIEQ VVEHGMEGQF
     VNSEFLNGLD FEEGLQKTMD YFEEKDWGRR VITYRLRDWC ISRQRYWGPP IPMIECKKCG
     WQPVDEKDLP VKLPYVKNFK PTGDGKSPLE KAAKSWLDTK CPKCGGKAKR ETDVSDTFLD
     SAWYYLRYPS VNSNVEITKK WLPVDAYIGG AEHAVLHLLY SRFVWMALQD WGYLDKSLGE
     EPFPFLYGHG LIIKDGAKMS KSKGNIVNPD EYIDKYGADA LRLYLMFIGP YDQGGDFRDT
     GMKGMKRFLN RVWKLVNKPI SEVKEVHRLR HKTIKKLTEL MSNFRFNVGI ATLMEYVNGL
     SRHNAEDPRR KSSGEKWGAD KESLRVLILL LAPFAPYTSE ELWLKLGGKF SVHQQAWPKF
     EERLATTGFT TVVVQINGKL RAKLELDRKA AQDKAKVLVL AKANNHIKTY IKDKKIVKEI
     FVPGRLVSLV VK
//
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