ID   SYL_PYRAR               Reviewed;         945 AA.
AC   A4WHK6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   27-MAR-2024, entry version 100.
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=Pars_0260;
OS   Pyrobaculum arsenaticum (strain DSM 13514 / JCM 11321 / PZ6).
OC   Archaea; Thermoproteota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Pyrobaculum.
OX   NCBI_TaxID=340102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700994 / DSM 13514 / JCM 11321 / PZ6;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Cozen A.E.,
RA   Fitz-Gibbon S.T., House C.H., Saltikov C., Lowe T.M., Richardson P.;
RT   "Complete sequence of Pyrobaculum arsenaticum DSM 13514.";
RL   Submitted (APR-2007) 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: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; CP000660; ABP49873.1; -; Genomic_DNA.
DR   AlphaFoldDB; A4WHK6; -.
DR   SMR; A4WHK6; -.
DR   STRING; 340102.Pars_0260; -.
DR   KEGG; pas:Pars_0260; -.
DR   HOGENOM; CLU_004174_0_0_2; -.
DR   OrthoDB; 23906at2157; -.
DR   PhylomeDB; A4WHK6; -.
DR   Proteomes; UP000001567; 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; 3.30.2320.20; 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; IPR001412; aa-tRNA-synth_I_CS.
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.
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.
FT   CHAIN           1..945
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000009403"
FT   MOTIF           43..53
FT                   /note="'HIGH' region"
FT   MOTIF           638..642
FT                   /note="'KMSKS' region"
FT   BINDING         641
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   945 AA;  107394 MW;  FBF96F309DE85956 CRC64;
     MSELARFFIE LGEKWQKRWA EARVYEPAPT LGVPKFFITA AYPYPNGAIH IGHGRTYLIA
     DVLARFHRHL GRAVLFPMAF HYTGTPILTI AEAIAAGDET VVEEYMAIYG VPEEEMRKMG
     DPLYLARYFH EQSKRAMQKF GLSIDWTREF TTIDPEYQRF IQWQFEKLRK KGLIVRGRHP
     VGWCPRHSMP VGAHDTKDDK EPDIGEWTLI YFADRDGLIF PAATLRPETV LGVTNMWINP
     EGEYVVAEYD GRKMVLSRDA AYRLSFQGSV KVLREAKGRE FVGREVQNPV TGEWVPIYGA
     KFVDPKVGTG VVMSVPAHAP YDYAALRDIG AIRLIPLIKV EGYGEYPAKD VVERMEIKSQ
     TDPALEEATK EVYSAEYARG VMREDVVELV GRHLPEPARS MVMAVFKMYF AGRPVREARE
     FISKWLAEAG LGGVMYDIMN KPVYCRCGTE IVVKVLEDQW FINYGEPRWK ELAKKLVEEM
     TIVPPEAKAQ FFATIDWLDK RACARTRGLG TPLPWSHGWV IESLSDSTIY MAYYAVIKGI
     RRHNLRPEQL TEEFWDYVFL GVGTPEEVSA KTGIPAEALR AIREEFEFWY PLDSRNSGKD
     LIPNHLTFFI FNHVAIFPRE KWPRQIVANG WVLREGEKMS KSKRNVLPLD KAVEMYGPDP
     LRATLAISAE VEQDLDFRHA EAVRNAQQLM SIYTLAQRLA QSAEDREPTW LDRWLLSEVA
     LALERVRDAY EKVRVRQAAV ELLYNIKNIF DSYMTAVERP SRLAVEVAKA WAVALEPIAP
     HLAEEVWSLL GGEGFVTSAK WPQLKPDPAA LLARRYVDMV VEDVKKIPAY GEGVRRVVLY
     INPNFTWVKA ALNNDVKSAI AAGTPPQLAK RLVELVRTLG DEVRSLIAAV ENFDEREALL
     SYKNYVEKAL GAPVEVYTAE DPAAPDLGGK KKAALPLKPG IFIER
//