ID   SYL1_SULAC              Reviewed;         942 AA.
AC   Q4JBP0;
DT   27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   27-MAR-2024, entry version 105.
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};
GN   OrderedLocusNames=Saci_0373;
OS   Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC
OS   15157 / NCIMB 11770).
OC   Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=330779;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX   PubMed=15995215; DOI=10.1128/jb.187.14.4992-4999.2005;
RA   Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E.,
RA   Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.;
RT   "The genome of Sulfolobus acidocaldarius, a model organism of the
RT   Crenarchaeota.";
RL   J. Bacteriol. 187:4992-4999(2005).
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; CP000077; AAY79789.1; -; Genomic_DNA.
DR   RefSeq; WP_011277291.1; NZ_CP046615.1.
DR   AlphaFoldDB; Q4JBP0; -.
DR   SMR; Q4JBP0; -.
DR   STRING; 330779.Saci_0373; -.
DR   GeneID; 78440723; -.
DR   KEGG; sai:Saci_0373; -.
DR   PATRIC; fig|330779.12.peg.371; -.
DR   eggNOG; arCOG00809; Archaea.
DR   HOGENOM; CLU_004174_0_0_2; -.
DR   Proteomes; UP000001018; 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   CDD; cd07959; Anticodon_Ia_Leu_AEc; 1.
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; 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; 2.
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.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..942
FT                   /note="Leucine--tRNA ligase 1"
FT                   /id="PRO_0000152142"
FT   MOTIF           39..49
FT                   /note="'HIGH' region"
FT   MOTIF           624..628
FT                   /note="'KMSKS' region"
FT   BINDING         627
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   942 AA;  108215 MW;  C62D780A5A6C432F CRC64;
     MDFLNEIASK WQKVWDSERV YEADVDRTKE KKFITVAFPY TNSPLHIGHG RTYITADIYA
     RYLRMKGYNV LFPFAFQFTG TPILSIADAV KRGDEEIIST FTNVYQIPIG VISKFSDPSY
     LSAYFKEDMR NTALTLGLSI DRRREFTTID PAFERFVQWQ YKRLQEIGYI KKEKAPVAYC
     PVDEFPVGMH DTRGDIEPEI IDLDVIYFQG EKLLFLTATS RPETIFGAVA ILINPDSDYS
     IVVDNKNGKR LVMSTEAFKK LSFQMSLTEE ERKKGGELIG LNVTNPVTLK KLTVLPSKYV
     ESKQGTGVVM AVPAHEPLHY LALSELKESF EIVPVIKSED YGDFPAMEVL ETAQTTSAQE
     LKDYIDTLYR IEFHKGSIRD EVVDLVPDYM KQFVGERIAG KSVREARSSV VELLRNLGVH
     GNIYEIINGP VYCRCGAEVV VKVFDDQWFI DYSNSTWKSS VLKSLDKIEI LPQDAKREIS
     KIIFNMKPRP FTRSRGLGVR LPWDDRQIID SLSDSTIYTV FYIVANKVKS YPTSILNERF
     WDYVVLGRGD SSQLSRELGI PKEQLEELRM EVEYWYPVDS RHSGRDLVQN HIPYYLYHHV
     GVLGEDKVPK RIVLNGFIRV GGKKMSKSFG NVYPLNKAIR EYGVDTVRLA LTSTSSLSDD
     IEFSPNIAKS IGEQLKHIHD FIENLIKLQS VNEIRKVDLW ISSLISEYID LIDNCLSNLD
     LRTAYKTIYY DIYEDLKDYL ELGNGKINSD IIKNVISVWI RLMAPFTPHL AEELWHKLDN
     SLVVRQRFPS KGELQYDKRA LLEIEYLRYT IDLINSMKSK MSKEPETVII YVNEDNTQRD
     LIRKAIESLK ERKSLPDFEK EVGDREMARL AYEIAGDLPD KIKNLAEIGI NESEILTSNA
     QFLLNKLDVK EIYIYNSKDP STPDIKGKKS IALPYKPGII LT
//