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Database: UniProt
Entry: A0A1Y1SEX8_9GAMM
LinkDB: A0A1Y1SEX8_9GAMM
Original site: A0A1Y1SEX8_9GAMM 
ID   A0A1Y1SEX8_9GAMM        Unreviewed;       859 AA.
AC   A0A1Y1SEX8;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Leucine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00049};
DE            EC=6.1.1.4 {ECO:0000256|HAMAP-Rule:MF_00049};
DE   AltName: Full=Leucyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00049};
DE            Short=LeuRS {ECO:0000256|HAMAP-Rule:MF_00049};
GN   Name=leuS {ECO:0000256|HAMAP-Rule:MF_00049};
GN   ORFNames=ATO7_09442 {ECO:0000313|EMBL:ORE87254.1};
OS   Oceanococcus atlanticus.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Oceanococcus.
OX   NCBI_TaxID=1317117 {ECO:0000313|EMBL:ORE87254.1, ECO:0000313|Proteomes:UP000192342};
RN   [1] {ECO:0000313|EMBL:ORE87254.1, ECO:0000313|Proteomes:UP000192342}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=22II-S10r2 {ECO:0000313|EMBL:ORE87254.1,
RC   ECO:0000313|Proteomes:UP000192342};
RA   Lai Q., Li G., Shao Z.;
RT   "Oceanococcus atlanticus 22II-S10r2 Genome Sequencing.";
RL   Submitted (APR-2013) 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, ECO:0000256|HAMAP-
CC         Rule:MF_00049};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00049}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|HAMAP-Rule:MF_00049,
CC       ECO:0000256|RuleBase:RU363035}.
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:ORE87254.1}.
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DR   EMBL; AQQV01000002; ORE87254.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y1SEX8; -.
DR   STRING; 1317117.ATO7_09442; -.
DR   OrthoDB; 9810365at2; -.
DR   Proteomes; UP000192342; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004823; F:leucine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006429; P:leucyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   CDD; cd07958; Anticodon_Ia_Leu_BEm; 1.
DR   CDD; cd00812; LeuRS_core; 1.
DR   Gene3D; 2.20.28.290; -; 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   HAMAP; MF_00049_B; Leu_tRNA_synth_B; 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; IPR013155; M/V/L/I-tRNA-synth_anticd-bd.
DR   InterPro; IPR015413; Methionyl/Leucyl_tRNA_Synth.
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; 2.
DR   Pfam; PF13603; tRNA-synt_1_2; 1.
DR   Pfam; PF09334; tRNA-synt_1g; 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.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW   ECO:0000256|HAMAP-Rule:MF_00049};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00049};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00049};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00049};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00049};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW   Rule:MF_00049}; Reference proteome {ECO:0000313|Proteomes:UP000192342}.
FT   DOMAIN          39..171
FT                   /note="Methionyl/Leucyl tRNA synthetase"
FT                   /evidence="ECO:0000259|Pfam:PF09334"
FT   DOMAIN          221..402
FT                   /note="Leucyl-tRNA synthetase editing"
FT                   /evidence="ECO:0000259|Pfam:PF13603"
FT   DOMAIN          414..570
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          608..657
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          700..823
FT                   /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT                   anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF08264"
FT   MOTIF           42..52
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT   MOTIF           618..622
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT   BINDING         621
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   859 AA;  95646 MW;  B10B905AC44B5CED CRC64;
     MQDQYDPQAI ETAVQQRWNE AQAFKASEDP AREKYYCLSM FPYPSGRLHM GHVRNYTIGD
     VLARYHRMCG KNVLQPMGWD AFGLPAENAA IKNQVPPAAW TRENIDYMRG QLQRLGFAYD
     WSRELATCDP GYYRWEQWLF TRLMKKGLVY RKNSVVNWDP VDNTVLANEQ VIDGRGWRSG
     ALVEQREIPQ WFLKITDYAE ELLSSLDELE HWPEAVKTMQ RNWIGRSEGL RIRFAVPDAE
     PLEVFTTRPD TLMGVTYLAV AAGHPLAQQA AQDKPEVAAF VAECQRGGTA AADLETQDKK
     GIALGIDAVH PVTGEKVPVW AANFVLMSYG TGAVMSVPAH DQRDWEFAQA YGLPLKAVIS
     ADGEQVPDIS EAAYTARGRL INSGDFDGLD FDAAFAALQQ HLGEAAEKQV NFRLRDWGVS
     RQRYWGCPIP VIYCDQCGDQ PVPEDQLPVA LPEDVTVTGG ASPLATMDEW IKVKCPSCGG
     DARRETDTFD TFFESSWYYA RFACPDADSA MLDARADYWA PVDQYIGGIE HAILHLLYAR
     FFHKLMRDEG LLSSNEPFKR LLTQGMVLAD SWFTRDDKGG QQWVSPLDVE IERDADGRIV
     GGTLKSDGSV VEYDGMNKMS KSKNNGIDPQ VMIERYGADT VRLFMMFAAP PDQSLEWSDA
     GVDGALRFIK RLWRQVHAHV QGGAVVALDV DALSREQKGL RAKVHETLSK AGDDIGRRMT
     FNTAIAAVME LLNAVSRFAD DSAQGRAVVQ EALDTAVLLL APITPHVCDQ LWQALGHEGA
     VIDANWPQVD ERALVSDSIA LVVQVNGKLR GRIEVDAAAD KDAILAQAKA DENVKRHLEG
     MTLRKEIYVP GKLVNLVVG
//
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