ID   SYL_PYRAE               Reviewed;         945 AA.
AC   Q8ZXT6;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   27-MAR-2024, entry version 119.
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=PAE1107;
OS   Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP
OS   104966 / NBRC 100827 / IM2).
OC   Archaea; Thermoproteota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Pyrobaculum.
OX   NCBI_TaxID=178306;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 /
RC   IM2;
RX   PubMed=11792869; DOI=10.1073/pnas.241636498;
RA   Fitz-Gibbon S.T., Ladner H., Kim U.-J., Stetter K.O., Simon M.I.,
RA   Miller J.H.;
RT   "Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum
RT   aerophilum.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:984-989(2002).
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; AE009441; AAL63260.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8ZXT6; -.
DR   SMR; Q8ZXT6; -.
DR   STRING; 178306.PAE1107; -.
DR   EnsemblBacteria; AAL63260; AAL63260; PAE1107.
DR   KEGG; pai:PAE1107; -.
DR   PATRIC; fig|178306.9.peg.821; -.
DR   eggNOG; arCOG00809; Archaea.
DR   HOGENOM; CLU_004174_0_0_2; -.
DR   InParanoid; Q8ZXT6; -.
DR   Proteomes; UP000002439; 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; IBA:GO_Central.
DR   GO; GO:0006429; P:leucyl-tRNA aminoacylation; IBA:GO_Central.
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; 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; 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   Pfam; PF09334; tRNA-synt_1g; 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; Reference proteome.
FT   CHAIN           1..945
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000152138"
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;  106850 MW;  2ECDFFE9EE85F243 CRC64;
     MSELSSLFIK MAEKWQAKWA EARVYEPEPR PGAAKFFVTA AYPYPNGAIH IGHGRTYLIA
     DVLARFHRHM GRVVLFPMGF HYTGTPILTI AEAIASGDAT VIEEYMAIYG VPKDEIEKMG
     NPLYLARYFH EQSKRAMQKF GLGIDWTREF TTIDPEYQRF IQWQFEKLRE RGLIVRGRHP
     VGWCPRHSMP VGAHDTKDDK EPEIGQWTLI YFADGEGLVF PAATLRPETV LGVTNMWINP
     DAEYAVIEHN GRKMVVSKDA AFRLSFQGDV RILREARGRE FVGRSVQNPV TGEWVPVYEA
     KFVDPKVGTG VVMSVPAHAP YDYAALRDLN AVRLIPLIRV EGYGDYPAKE VVERMGIKSQ
     TDPALEEATR EVYSAEYTKG VMREDVVGRV GAHLSEPARS MLRAVFKMYF AGRPVREARE
     FISKWLVEAG IGGVMYDIMN KPVYCRCGTE IVVKVLEDQW FINYGEGRWK ELARKLVEEM
     AIVPPEAKAH FLATIDWLDK RACARTRGLG TPLPWSDGWV IESLSDSTIY MAFYTVIKRI
     RQFGIKPEQL IKEFWDYVFL GVGTPEEVAK RTGVPPEQLK AIREEFDFWY PLDSRNSGKD
     LIPNHLTFFI FNHVAIFPRE KWPRQIVANG WVLREGEKMS KSKRNVLPLD KAVDMYGPDP
     LRATLAITAE VEQDLDFRHA EAIRNAQQLM SIYSLAQRLA QTAEDRSPNW LDKWLVSEIA
     LVLERAREAY EKVRVRQAAV EVLYNAKSVF DQYLASVERP SKLAVEAARA WAVAMEPIAP
     HLAEEIWSIL GGEGLVVKAP WPQLRPDPVA LLAKRYVDMV IDDVKRIPAF GEGVKRVVIY
     VNPNYAWVKA ALSGDVKAVI NAGAPPQAAK RVVDIVKTLG DELRGLISAV GKFDEAEALA
     SYKNYMEKAL GAPMEIYNAD DPSAPDLGSK KKVALPLRPG IYIEK
//