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Database: UniProt
Entry: A0A285N345_9AQUI
LinkDB: A0A285N345_9AQUI
Original site: A0A285N345_9AQUI 
ID   A0A285N345_9AQUI        Unreviewed;       288 AA.
AC   A0A285N345;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   RecName: Full=leucine--tRNA ligase {ECO:0000256|ARBA:ARBA00013164};
DE            EC=6.1.1.4 {ECO:0000256|ARBA:ARBA00013164};
GN   ORFNames=SAMN06265182_0502 {ECO:0000313|EMBL:SNZ03904.1};
OS   Persephonella hydrogeniphila.
OC   Bacteria; Aquificota; Aquificae; Aquificales; Hydrogenothermaceae;
OC   Persephonella.
OX   NCBI_TaxID=198703 {ECO:0000313|EMBL:SNZ03904.1, ECO:0000313|Proteomes:UP000219036};
RN   [1] {ECO:0000313|EMBL:SNZ03904.1, ECO:0000313|Proteomes:UP000219036}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15103 {ECO:0000313|EMBL:SNZ03904.1,
RC   ECO:0000313|Proteomes:UP000219036};
RA   Ehlers B., Leendertz F.H.;
RL   Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; OBEI01000001; SNZ03904.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A285N345; -.
DR   OrthoDB; 9810365at2; -.
DR   Proteomes; UP000219036; 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   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; IPR009080; tRNAsynth_Ia_anticodon-bd.
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   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   ECO:0000313|EMBL:SNZ03904.1}; ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917}.
FT   DOMAIN          45..77
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          128..251
FT                   /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT                   anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF08264"
SQ   SEQUENCE   288 AA;  33458 MW;  1272080665D49947 CRC64;
     MNKTLKEFLE ENHLTVNDNA KLLFEKLDLD TDILKELEEK YGKSDKMSKS KHNTVDPDEM
     IEKYGADTVR LYILFAAPPQ NSFDWVDSGI EGAHRFLKRV WNFVIDKAED IKNVRYTKED
     FKNLNEEDQK LRRKLHQTIK KVNDDINREY QFNTAIAAIM EFFNELSSYK GNNLKLIKES
     IENMVLLLSP FTPFIADTLW REIGNEGFTI NQPFPEPDEE ALIEKTKEIP VQVNGKVRAK
     ITVPSDADEE TVKKLAFENE NVKRWTEGKD IVKVIFIKGK ILNIVVKG
//
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