SYL_AMOA5
ID SYL_AMOA5 Reviewed; 923 AA.
AC B3ETW5;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Leucine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00049};
DE EC=6.1.1.4 {ECO:0000255|HAMAP-Rule:MF_00049};
DE AltName: Full=Leucyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00049};
DE Short=LeuRS {ECO:0000255|HAMAP-Rule:MF_00049};
GN Name=leuS {ECO:0000255|HAMAP-Rule:MF_00049}; OrderedLocusNames=Aasi_1363;
OS Amoebophilus asiaticus (strain 5a2).
OC Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Amoebophilaceae;
OC Candidatus Amoebophilus.
OX NCBI_TaxID=452471;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5a2;
RX PubMed=20023027; DOI=10.1128/jb.01379-09;
RA Schmitz-Esser S., Tischler P., Arnold R., Montanaro J., Wagner M.,
RA Rattei T., Horn M.;
RT "The genome of the amoeba symbiont 'Candidatus Amoebophilus asiaticus'
RT reveals common mechanisms for host cell interaction among amoeba-associated
RT bacteria.";
RL J. Bacteriol. 192:1045-1057(2010).
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:0000255|HAMAP-Rule:MF_00049};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00049}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000255|HAMAP-Rule:MF_00049}.
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DR EMBL; CP001102; ACE06667.1; -; Genomic_DNA.
DR RefSeq; WP_012473409.1; NC_010830.1.
DR AlphaFoldDB; B3ETW5; -.
DR SMR; B3ETW5; -.
DR STRING; 452471.Aasi_1363; -.
DR PRIDE; B3ETW5; -.
DR EnsemblBacteria; ACE06667; ACE06667; Aasi_1363.
DR KEGG; aas:Aasi_1363; -.
DR eggNOG; COG0495; Bacteria.
DR HOGENOM; CLU_004427_0_0_10; -.
DR OMA; TFMVLAP; -.
DR OrthoDB; 32262at2; -.
DR Proteomes; UP000001227; Chromosome.
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 Gene3D; 3.40.50.620; -; 3.
DR Gene3D; 3.90.740.10; -; 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; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
DR PANTHER; PTHR43740; PTHR43740; 1.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF00133; tRNA-synt_1; 2.
DR Pfam; PF13603; tRNA-synt_1_2; 1.
DR PRINTS; PR00985; TRNASYNTHLEU.
DR SUPFAM; SSF47323; SSF47323; 1.
DR SUPFAM; SSF50677; SSF50677; 1.
DR TIGRFAMs; TIGR00396; leuS_bact; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..923
FT /note="Leucine--tRNA ligase"
FT /id="PRO_1000091287"
FT MOTIF 41..52
FT /note="'HIGH' region"
FT MOTIF 698..702
FT /note="'KMSKS' region"
FT BINDING 701
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ SEQUENCE 923 AA; 105607 MW; AAB6AE51D668398C CRC64;
MSHYDFKAIE QKWQQYWKNN QIFRTTIEPS KPKYYILDMF PYPSGEGLHV GHPLGYIASD
IVARYKRSKG YQVLHPMGFD AFGLPAEQFA IQTGQHPAIT TAKNIGRYKQ QLCQLGLSYD
WDRCISTCEP AYYKWTQWIF IQLFNSWYDI SLQKARPIDE LITLFDQQGN QQVQASCDKE
VSLFTAKEWQ AMDEESKQQH LLAYRLAFLE DTTVNWCPEL GTVLANEEVK DGLSERGGYP
VIRKQMKQWS LRITAYTDRL LAGLEHLKWP LSTKEMQRNW IGRSIGAELN FTVIANGQEH
TIPVFTTRPD TLFGVTYLAL SPEHPLAKLI STGTQQAAID TYITQATNRS ERDRLADVNH
VTGMFTGAYA IHPFTKQPLP IWIADYVLAG YGTGAVMGVP AHDSRDYAFA QHFQLPIIQV
VAGGDTAQSA YEAREGSLFN SQFLNGLSIQ EATKQAIQKL ESLGIGKQKT TYRLRNAIFS
RQRYWGEPIP IYYKNNIPYP IPAEELPLEL PSLASFKPTP TGEPPLGHAP NWKTKEGYPI
ELSTMPGWAG SSWYFFRYMD PNNEASFVGS TAQNYWQAVD LYLGGAEHAT GHLLYARFWT
QFLYDLGYVN IEEPFQELIH QGMIQGKSSF VYRIKGTNQF VSYNLRHAYE TTAMHVDIHL
VKNNILDLER FKNWRPDLQT ATFVLENGQY ICGSEVEKMS KSKYNTVNPD TVVEQYGADT
LRLYTMFLGP IEQAKPWDMH GIEGVFRFLV KVWRLFYLEK GAIITNEVPT KEVQKAIHKA
IKKVEEDIKR YAFNTAVSNL MICVNELTAL KCNNRAALTN LVLILAPFAP HLAEELWEIL
GHQHSIAQAP FPTYEEIYLQ EETYEYPIAI NGKVRAKINF PVDMPQGQIE EQVLTHESIQ
KWIQGQQIKR VIVISSKMVN IVI
