ID   SYL_HALSA               Reviewed;         885 AA.
AC   Q9HN72;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   27-MAR-2024, entry version 131.
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=VNG_2223G;
OS   Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)
OS   (Halobacterium halobium).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Halobacteriaceae; Halobacterium; Halobacterium salinarum NRC-34001.
OX   NCBI_TaxID=64091;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700922 / JCM 11081 / NRC-1;
RX   PubMed=11016950; DOI=10.1073/pnas.190337797;
RA   Ng W.V., Kennedy S.P., Mahairas G.G., Berquist B., Pan M., Shukla H.D.,
RA   Lasky S.R., Baliga N.S., Thorsson V., Sbrogna J., Swartzell S., Weir D.,
RA   Hall J., Dahl T.A., Welti R., Goo Y.A., Leithauser B., Keller K., Cruz R.,
RA   Danson M.J., Hough D.W., Maddocks D.G., Jablonski P.E., Krebs M.P.,
RA   Angevine C.M., Dale H., Isenbarger T.A., Peck R.F., Pohlschroder M.,
RA   Spudich J.L., Jung K.-H., Alam M., Freitas T., Hou S., Daniels C.J.,
RA   Dennis P.P., Omer A.D., Ebhardt H., Lowe T.M., Liang P., Riley M., Hood L.,
RA   DasSarma S.;
RT   "Genome sequence of Halobacterium species NRC-1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:12176-12181(2000).
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; AE004437; AAG20349.1; -; Genomic_DNA.
DR   PIR; A84373; A84373.
DR   RefSeq; WP_010903650.1; NC_002607.1.
DR   AlphaFoldDB; Q9HN72; -.
DR   SMR; Q9HN72; -.
DR   STRING; 64091.VNG_2223G; -.
DR   PaxDb; 64091-VNG_2223G; -.
DR   GeneID; 68694780; -.
DR   KEGG; hal:VNG_2223G; -.
DR   PATRIC; fig|64091.14.peg.1709; -.
DR   HOGENOM; CLU_004427_0_0_2; -.
DR   InParanoid; Q9HN72; -.
DR   OrthoDB; 23906at2157; -.
DR   PhylomeDB; Q9HN72; -.
DR   Proteomes; UP000000554; 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-KW.
DR   GO; GO:0004823; F:leucine-tRNA ligase activity; IBA:GO_Central.
DR   GO; GO:0006429; P:leucyl-tRNA aminoacylation; IBA:GO_Central.
DR   CDD; cd07958; Anticodon_Ia_Leu_BEm; 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; 2.
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_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; 1.
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; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..885
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000152129"
FT   REGION          866..885
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           43..53
FT                   /note="'HIGH' region"
FT   MOTIF           571..575
FT                   /note="'KMSKS' region"
FT   BINDING         574
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   885 AA;  97527 MW;  CA697263BE4D58F7 CRC64;
     MGEQATYDHH AIEQHWQREW DDADVFRVPD DADDPEYVLA MFPYTSGQLH MGHVRNYAIT
     DAFARYRRMD GEDVLHPMGW DSFGLPAENA ANERDTNPRE WTERCIDQMR DQFEALGFGY
     DWEREITTCD PDYYKWNQWL FTEFRDAGLV DRRAATVNWC PSCETVLADE QVEGDDELCW
     RCDTPVTERD LDQWFFETTA YADELLDGLD ELDGWPSNVR DMQRNWVGRT DGVEVPFTVH
     TPDGDEDVVA FTTRVDTIHG ATYFALAPDH PLAEAAADRD DDVAHFVEEV ADPDGDEPQG
     VETEFTATNP ATGAEIPVVV ADFVLSDVGT GALMAVPAHD DRDHEFAQAH DLPVRQVVAP
     AGDEDADVEA AAYTADGVLV NAGDYTGLDS ETAREELTAD IDGAASAVQY QLRDWGVSRQ
     RYWGTPIPIV HCESCGPVSV PDDDLPVELP EFVHTTGNPL DAAEDWKQTT CPDCGAPAVR
     ETDTMDTFLD SSWYFLRFAS PAFDDAPFDT QRANDWLPVD EYVGGDEHAV MHLLYSRFVT
     KAFADLDMLE HREPFAGLTT QGMVLGEDGT KMSKSKDNGV APERIVDEYG ADTARLFTLR
     AARPSKAFPW SEEGVRSSHT FLERLLSMAR AVNADATADG DLDPAAEYVA RETAATVQAA
     TTHFDDMEFN RAVQAVDELV SLLVRYRDRD DAAPAVVARG VTAAVKLLAP IAPHVAEECW
     TALGGDGFVA EAAWPTPDRD VSDHDRATSL IEQTREDVRD IVDTAGIENP TGVDVVTAPE
     WMYDVLARAK AADGNVVGSV MSDQSLQQHG EDAADYAKDL AAQAPAFPDV LGPDGERDAL
     GRAVWLLEAE FDAPVRVLAA EDAADSVANK AEPGRPAIHV DEADD
//