ID A0A0G1Y511_9BACT Unreviewed; 391 AA.
AC A0A0G1Y511;
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};
GN ORFNames=UY48_C0050G0006 {ECO:0000313|EMBL:KKW09977.1};
OS Candidatus Gottesmanbacteria bacterium GW2011_GWB1_49_7.
OC Bacteria; Candidatus Gottesmanbacteria.
OX NCBI_TaxID=1618448 {ECO:0000313|EMBL:KKW09977.1, ECO:0000313|Proteomes:UP000034588};
RN [1] {ECO:0000313|EMBL:KKW09977.1, ECO:0000313|Proteomes:UP000034588}
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}.
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:KKW09977.1}.
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DR EMBL; LCQD01000050; KKW09977.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1Y511; -.
DR PATRIC; fig|1618448.3.peg.1160; -.
DR Proteomes; UP000034588; 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 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; IPR002300; aa-tRNA-synth_Ia.
DR InterPro; IPR002302; Leu-tRNA-ligase.
DR InterPro; IPR025709; Leu_tRNA-synth_edit.
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; PF00133; tRNA-synt_1; 1.
DR Pfam; PF13603; tRNA-synt_1_2; 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 ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:KKW09977.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917}.
FT DOMAIN 22..232
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 271..325
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
SQ SEQUENCE 391 AA; 45636 MW; E2B747C59F216B7F CRC64;
MERVYNLAMS EGKYDHKTVE GKWQEEWAKR GLDQTDLKDA KRPFYNLMMF PYPSAEGLHV
GNMYAFTASD VYGRFKRMQG FDVFEPIGLD GFGIHSENYA LKIGRHPKEH ARITQENFYK
QLHQIGNMFD WSKTLETYDP DYYKWTQWIF VQMYKAGLAY KAKSEVNWCP HCKTVLADEQ
VIDGKCERCK TEVLKKELEQ WFFRITKYAQ KLLDNLEKLD WVEKIKASQR NWIGRSEGMK
LKFGKYEVFT TRPDTVHGAT FLAVAGKSDK FTGEMVKNPA TGVEIPVWEA EYIVADYGTG
AVMGVPAHDE RDMAFAKKHK IGMVEMEPDE SMRKYGEKTI HFHLRDWLIS RQRYWGPPIP
MIVCPKCGWQ PVPEKDLPVL LAGYIRLSAR R
//
