ID   SYL1_SACS2              Reviewed;         934 AA.
AC   P58176;
DT   20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   20-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=Leucine--tRNA ligase 1 {ECO:0000255|HAMAP-Rule:MF_00049};
DE            EC=6.1.1.4 {ECO:0000255|HAMAP-Rule:MF_00049};
DE   AltName: Full=Leucyl-tRNA synthetase 1 {ECO:0000255|HAMAP-Rule:MF_00049};
DE            Short=LeuRS 1 {ECO:0000255|HAMAP-Rule:MF_00049};
GN   Name=leuS1 {ECO:0000255|HAMAP-Rule:MF_00049}; OrderedLocusNames=SSO0504;
OS   Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS   (Sulfolobus solfataricus).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Saccharolobus.
OX   NCBI_TaxID=273057;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX   PubMed=11427726; DOI=10.1073/pnas.141222098;
RA   She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA   Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA   Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA   Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA   Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA   Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT   "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
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; AE006641; AAK40823.1; -; Genomic_DNA.
DR   PIR; H90195; H90195.
DR   RefSeq; WP_009991397.1; NC_002754.1.
DR   AlphaFoldDB; P58176; -.
DR   SMR; P58176; -.
DR   STRING; 273057.SSO0504; -.
DR   PRIDE; P58176; -.
DR   EnsemblBacteria; AAK40823; AAK40823; SSO0504.
DR   GeneID; 44129493; -.
DR   KEGG; sso:SSO0504; -.
DR   PATRIC; fig|273057.12.peg.498; -.
DR   eggNOG; arCOG00809; Archaea.
DR   HOGENOM; CLU_004174_0_0_2; -.
DR   InParanoid; P58176; -.
DR   OMA; QKWWEES; -.
DR   PhylomeDB; P58176; -.
DR   Proteomes; UP000001974; 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; 3.40.50.620; -; 1.
DR   Gene3D; 3.90.740.10; -; 1.
DR   HAMAP; MF_00049_A; Leu_tRNA_synth_A; 1.
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.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..934
FT                   /note="Leucine--tRNA ligase 1"
FT                   /id="PRO_0000152144"
FT   MOTIF           41..51
FT                   /note="'HIGH' region"
FT   MOTIF           616..620
FT                   /note="'KMSKS' region"
FT   BINDING         619
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   934 AA;  108527 MW;  350A9D7C8424DBD0 CRC64;
     MYSDFFNSIA FKWQAEWEKS KVFETNMDYS KPKFFITVPF PYTNSPMHVG HGRTYITADI
     YARYLRMKGY NVLFPFAFQF TGTPVLAIAD SIRRGEVDVI EFFKNVYEVP QDKIKELEDP
     YKLAEYFKEE MKNTAKSIGM SIDWRRTFTT TDPRFEKFIH WQLGKLKELG YLVTEDDVVG
     YCPNDGFPVG MHDTRGDIEP EITTMNVIMF EGSDSYNFMV ATSRPELIFG VVALMVNHDA
     NYVVVEYEGK NFIISEKAYK KLSFQKNMKL VKTITTSDIV KLYAINPITG RKLEIIKNKY
     VDPSLGTGVV MSYPAHDPFH YLAMTETNKE FEVIPVVETE ELDEIPGESA VLQTKNPYAL
     KDFMESIYKT EYYKGYMKDI ILSLVPDFLK QYVKENIVGK QVQEARKNTI ELLKSLNIYD
     TIYEISNGPI YCRCGSEIVP KRIKDQWFIA YDNPKWKASA LKAINNIELI PNPTKTELEK
     IVFNARKEPI GRSRGIGVKL PWDESQIVES LSDSTLYTLL YTVIYKMPIN IEKEIFDFIF
     LGKGDAKELE RKYGTDLIQL REEFLYWYPV DQRHTGRDLI QNHIPFYIYN HLAIFGEKYL
     PKRIVINGFV RVGGRKMSKS LRNIYTLSKA IKEFGVDPVR IALTSTSDLL QDLDFNENLV
     NPIAEQLKKI YDLIDRLLSI NTEIKELRTA DEWISSKVRD IIEKVNNNIT SFKYRDAVNL
     LLYEIYEILR DYFDLVEIPN QEVIRKILSI WIRALAPFVP HIAEELWHKI SSTFVSLEKY
     PEPNELNLYP DAILEISYIN KIIENVRELE DIVHKKAEKV IIYINESEKV KELMKNAIKA
     VNEEIPLREF TANTEDKIAE KVYVVVSKLD KAIRDYLLNN EIDEEQIIVK NMNFLLRRLG
     VSEIVIYNAE DPTVPDVKGK KSQALPLSPA IVVE