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}; 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
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