ID   SYL_PYRCJ               Reviewed;         946 AA.
AC   A3MU00;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   03-AUG-2022, entry version 91.
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=Pcal_0691;
OS   Pyrobaculum calidifontis (strain DSM 21063 / JCM 11548 / VA1).
OC   Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Pyrobaculum.
OX   NCBI_TaxID=410359;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21063 / JCM 11548 / VA1;
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 calidifontis JCM 11548.";
RL   Submitted (FEB-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; CP000561; ABO08117.1; -; Genomic_DNA.
DR   AlphaFoldDB; A3MU00; -.
DR   SMR; A3MU00; -.
DR   STRING; 410359.Pcal_0691; -.
DR   EnsemblBacteria; ABO08117; ABO08117; Pcal_0691.
DR   KEGG; pcl:Pcal_0691; -.
DR   eggNOG; arCOG00809; Archaea.
DR   HOGENOM; CLU_004174_0_0_2; -.
DR   OMA; AWNMAFQ; -.
DR   Proteomes; UP000001431; 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; 3.40.50.620; -; 1.
DR   Gene3D; 3.90.740.10; -; 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   PANTHER; PTHR45794; PTHR45794; 2.
DR   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF00133; tRNA-synt_1; 1.
DR   SUPFAM; SSF47323; SSF47323; 1.
DR   SUPFAM; SSF50677; SSF50677; 1.
DR   TIGRFAMs; TIGR00395; leuS_arch; 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..946
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000009404"
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   946 AA;  107481 MW;  F0D3BC3EC9CB671B CRC64;
     MSELAKFFIE VAEKWQRRWA EAKVFEPSPQ PGRPKFFITA AYPYPNGTIH IGHGRTYLVA
     DVMARFRRHL GYNVLFPMAF HYTGTPILTI AEVIAAGDKA VIEEYKEIYG VSDDDIKKMG
     DPLYLAQYFH RRSKEAMIKF GLGIDWSREF TTIDPEYQRF IQWQFEKLRK RGLIVRGRHP
     VGWCPRHQMP VGAHDTKDDK EPEIGQWTLI YFVDGEGLVY PTATLRPETV PGVTNIWINP
     DAEYVVAEFE GRKMVLSKDA AYRLSFQGNV KVIREARGRE FVGRRVLNPV TGEWVPVYEA
     KFVDPKVGTG VVMSVPAHAP YDYAALRDMG EVKLIPLIRV EGYGEYPAKE VVERMGIKSQ
     TDPALEEATR EVYSAEYTRG VVREDVVDRI APHLPEPARS MVRAVFKLYF AGRPVKEARE
     FISKWLAEAG LGGVMYDIMN KPVYCRCGTE IVVKVLEDQW FINYGERGWK QLARQLVEEM
     AIIPQEAKAQ FLATIDWLDK RACARTRGLG TPLPWSQGWV IESLSDSTIY MAFYTVIKKI
     RALGLRPEQL TEEFWDYVFL GQGSAAEVAK RIGVDPAALE EIRREFDYWY PLDSRNSGKD
     LIPNHLTFFI FNHVAIFPRE KWPRQIVANG WVLREGEKMS KSKRNVLPLD KAVALYGPDP
     LRATLAIAAE VEQDLDFRDA EARRNSQQLM SIYNLVQRLA QSAVEREETW LDKWLISEVA
     HVLERAREAY EKVRLRQAAV ELLYNAEAVF SQYLSMVDKP SKSAVEAAKA WVVALEPIVP
     HFAEELWQIL GGEGFAATAP WPKLSPDPAA LLAKRYVDML IEDVKNIPAY KAGAKRVAIY
     VNGNYQWLRA AVGKDVKAAI EAGAPPQLAK RLVDFAKSMG EEVRGLVERV EQFDEYAALQ
     SYKRYVEKAL GVPVDIYKAD DPQAPDLGGK KKAALPLKPG IFIEVG