ID   SYL_PYRIL               Reviewed;         945 AA.
AC   A1RTX9;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 90.
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=Pisl_1246;
OS   Pyrobaculum islandicum (strain DSM 4184 / JCM 9189 / GEO3).
OC   Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Pyrobaculum.
OX   NCBI_TaxID=384616;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 4184 / JCM 9189 / GEO3;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Dalin E., Tice H., Pitluck S., Meincke L., Brettin T.,
RA   Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Lowe T., Richardson P.;
RT   "Complete sequence of Pyrobaculum islandicum DSM 4184.";
RL   Submitted (DEC-2006) 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; CP000504; ABL88411.1; -; Genomic_DNA.
DR   RefSeq; WP_011762986.1; NC_008701.1.
DR   AlphaFoldDB; A1RTX9; -.
DR   SMR; A1RTX9; -.
DR   STRING; 384616.Pisl_1246; -.
DR   EnsemblBacteria; ABL88411; ABL88411; Pisl_1246.
DR   GeneID; 4616435; -.
DR   KEGG; pis:Pisl_1246; -.
DR   eggNOG; arCOG00809; Archaea.
DR   HOGENOM; CLU_004174_0_0_2; -.
DR   OMA; AWNMAFQ; -.
DR   OrthoDB; 4914at2157; -.
DR   Proteomes; UP000002595; 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..945
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000009405"
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;  107947 MW;  66351DCA0CEB630D CRC64;
     MSELSRFFIE IAERWQKRWK ESRVFEPEPT PGVAKYFITA AYPYPNGAVH IGHGRTYLIA
     DVLARFYRHM GRVVLYPMGF HYTGTPILTI AEVIAAGDKT VIEEYMEIYG VPEEEIKKMG
     DPLYLARYFH NRSKMAMERF GLSIDWTREF TTIDPEYQRF IQWQFEKLRK KGLIVRGRHP
     VGWCPRHSMP VGAHDTKDDK EPEIGQWTLI YFTDSEGLTF PAATLRPETV PGVTNLWINP
     DAEYVVAEFD GKRVVISRDA AYRLSFQAEV KILREARGRE FVGRSVQNPV TGEWVPIYEA
     WFVDPRVGTG VVMSVPAHAP YDYVALRDLG IEKLIPLIKV EGYGDYPAKE VVERMGIKSQ
     TDPALEEATK EVYSTEYTRG VMREDVTERI GIHLQEPARS MLRAVFKMYF AGRPVREARE
     FIAKWLVEAR LGGVMYDIMN KPVYCRCGTE IVVKVLEDQW FINYGDPKWK ETARKLVDEM
     VIIPGEAKAH FFATIDWLDK RACARTRGLG TPLPWSSGWI IESLSDSTIY MAFYTVIKKI
     RQFGIRPEQL TEEFWDFVFL GQGSADEVSK KTGVPVEALK AIREEFEYWY PLDSRNSGKD
     LIPNHLTFFI FNHVAIFPRE KWPRQIVANG WVLREGEKMS KSKRNVLPLD RAVEMYGPDP
     LRATLALAAE VEQDLDFRDA EARRNAQQLM AIYTLVQRLI QNAENRPAGW IDQWLIAEIS
     RILDKAREAY EKVRVRQAAV EVIYNAKAVF DQYLAMVEKP TKLALEAARA WVVAMEPIVP
     HIAEELWALL GGSGFVATAP WPRLKAESAA LLAKRYVDML IEDVKNIPAF GPGARRIVIY
     VNRNFSWAKA ALNGDVKTVV TAGAPPQVAK RLIDLVKTLG DEVRTLLAST EQFDELETLK
     SYKAYIERTL GTPIEIYSVD DPSAPDLGGK KRAALPLKPG IYIER