ID   SYL_AERPE               Reviewed;         959 AA.
AC   Q9YD97;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   27-MAR-2024, entry version 136.
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};
GN   OrderedLocusNames=APE_1015;
OS   Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 /
OS   K1).
OC   Archaea; Thermoproteota; Thermoprotei; Desulfurococcales;
OC   Desulfurococcaceae; Aeropyrum.
OX   NCBI_TaxID=272557;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1;
RX   PubMed=10382966; DOI=10.1093/dnares/6.2.83;
RA   Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K.,
RA   Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A.,
RA   Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S.,
RA   Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A.,
RA   Aoki K., Kubota K., Nakamura Y., Nomura N., Sako Y., Kikuchi H.;
RT   "Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon,
RT   Aeropyrum pernix K1.";
RL   DNA Res. 6:83-101(1999).
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; BA000002; BAA80000.1; -; Genomic_DNA.
DR   PIR; H72699; H72699.
DR   AlphaFoldDB; Q9YD97; -.
DR   SMR; Q9YD97; -.
DR   STRING; 272557.APE_1015; -.
DR   EnsemblBacteria; BAA80000; BAA80000; APE_1015.
DR   KEGG; ape:APE_1015; -.
DR   PATRIC; fig|272557.25.peg.731; -.
DR   eggNOG; arCOG00809; Archaea.
DR   Proteomes; UP000002518; 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   CDD; cd07959; Anticodon_Ia_Leu_AEc; 1.
DR   CDD; cd00812; LeuRS_core; 1.
DR   Gene3D; 3.30.2320.20; Class I aminoacyl-tRNA synthetases (RS); 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   Gene3D; 1.10.10.720; leucyl-tRNA synthetase; 1.
DR   Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 1.
DR   HAMAP; MF_00049_A; Leu_tRNA_synth_A; 1.
DR   InterPro; IPR002300; aa-tRNA-synth_Ia.
DR   InterPro; IPR020791; Leu-tRNA-lgase_arc.
DR   InterPro; IPR004493; Leu-tRNA-synth_Ia_arc/euk.
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   NCBIfam; TIGR00395; leuS_arch; 1.
DR   PANTHER; PTHR45794:SF1; LEUCINE--TRNA LIGASE, CYTOPLASMIC; 1.
DR   PANTHER; PTHR45794; 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.
DR   SUPFAM; SSF50677; ValRS/IleRS/LeuRS editing domain; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..959
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000152127"
FT   REGION          933..959
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           39..49
FT                   /note="'HIGH' region"
FT   MOTIF           637..641
FT                   /note="'KMSKS' region"
FT   BINDING         640
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   959 AA;  110519 MW;  985CB5168728F7AB CRC64;
     MERLKAVEEK WQERWREARL FEADPQPGRR KFFITFPYPY VNAYPHLGSA FTILRVDIMA
     RYKRMRGYNV LFPQGWHATG GPIVSSALRV REGDPRIIKT LRDMGIPEED IPRFRDPRYW
     VEFFTKAWRR DLERYGMSID WRREFYTTSL NPAYSRFIEW QYLKLREKGF VGKGRHPVVW
     CPKEQKVVGD HDRPDEYAGI SPQEAVIIKF RGRDGLVYPA LTYRPETVFG VTNLWVHPDA
     TYLVAEVDGE ERWIIGEQAA RELADQGHRV VILERIEGRR LLGRIVVNPA DGREVPVLPA
     SFVRPDLGTG VVMSVPAHAP YDYVALMELK RRPETLREYG LEPGVVESLE PIQLIAVPRA
     EGLLVVEEVR RRGVESQMDR EKLDEATREV YAREFYEGIM LETTGRFSGL KVAEAKEKVV
     EWLEERGAAL RIYTLPQEVY CRCGARTHVK IVEDQWFLLY SKPEWKALAR EAVARMEFLP
     GHVRRDFEAI IEALRDWAFT HKGELGTPLP WDREWVIESL SDSTIYMAYY TIAKYTQHPE
     KYGVEPEMLT PEVFDYVFLG AGDPGEVSRR SGIPQGLLEE MRREFLYWYP LDMRISGKDL
     IPNHLVFFIF HHTAIFPREL WPRAIGVNGW VLVAGEKMSK SKGNFILLRQ ALDWWGADAT
     RWAEVLAGAD SGLDDANFEP SVADSAVSLL SQWLDFVREN YGRPARREER WVDRWFESRL
     NSTIARVTRL MEEANFKTAL VEAWYKLQES YRWYLRRSGG EPREDLLRRF IEVQTLLIAP
     FAPHTAEEAW EAMGREGFAS TASWPEPDES KISPEVEAAE ETVQAVLEDA REVLSLIGGA
     DTLVVTVAAE WKYRAVEAVR RARERGASMK EALREAFKVE GVDKREAARL VQQLSRAPEV
     LRRAAPRSVE LEALRDAAQL LQEELGVKVV VETEEDGGSP RRANALPGRP ALYAEKRGG
//