ID A0A0G1UDU0_9BACT Unreviewed; 476 AA.
AC A0A0G1UDU0;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=leucine--tRNA ligase {ECO:0000256|ARBA:ARBA00013164};
DE EC=6.1.1.4 {ECO:0000256|ARBA:ARBA00013164};
GN ORFNames=UY24_C0039G0002 {ECO:0000313|EMBL:KKU92296.1};
OS Parcubacteria group bacterium GW2011_GWA1_48_11b.
OC Bacteria.
OX NCBI_TaxID=1618795 {ECO:0000313|EMBL:KKU92296.1, ECO:0000313|Proteomes:UP000034426};
RN [1] {ECO:0000313|EMBL:KKU92296.1, ECO:0000313|Proteomes:UP000034426}
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 -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|RuleBase:RU363039}.
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:KKU92296.1}.
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DR EMBL; LCPG01000039; KKU92296.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1UDU0; -.
DR PATRIC; fig|1618795.3.peg.610; -.
DR Proteomes; UP000034426; 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; 1.
DR Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
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 PANTHER; PTHR43740:SF2; LEUCINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43740; LEUCYL-TRNA SYNTHETASE; 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:RU363039};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU363039};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU363039};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU363039};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW ECO:0000256|RuleBase:RU363039}.
FT DOMAIN 39..184
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 220..362
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
SQ SEQUENCE 476 AA; 55232 MW; CB63E068531893F1 CRC64;
MGYDFGKIEK KWQKVWAKNK YKIWAAEAKK PHKAYVLDMF PYPSGEGLHV GHVEGYTASD
IYARYLRMNG FNVLHPMGWD AFGLPAENYA IKTKTHPSLV VKKNVKNFTS QLRSLGFSYD
WQREINTTDP EYYKWTQWIF LQLFKKGLAY EAEVPVNWCP TDKTVLSNEE ITDGACERCG
SQVERRNLKQ WLLKITAYAD RLLQDLEGLD WPERVKEMQR NWIGRSEGAL IRFPLYCDRV
CYGDIEVFTT RPDTLTGATY LVLAPEHPWI KNYASRIRNY EEVRKYAEKA KNRSDRERQE
NKEKTGVELK GVRAINPINK KEVPVWISDY VLTHYGTGAI MAVPQHDERD REFAEKFKLL
IADEPLIPKD EVIAKVGGKK TVNYKLRDWI FSRQRYWGEP IPIIKCEKCG NVPVLEKDLP
VKLPNVKNYE PTGKAESPLA GIEKWVNVKC PKCSAPAKRE TNTMPQWAGT TSRTYL
//
