ID   SYL1_SULTO              Reviewed;         945 AA.
AC   Q974N4; F9VN59;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   27-MAR-2024, entry version 121.
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=STK_06250;
OS   Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
OS   (Sulfolobus tokodaii).
OC   Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfurisphaera.
OX   NCBI_TaxID=273063;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16993 / JCM 10545 / NBRC 100140 / 7;
RX   PubMed=11572479; DOI=10.1093/dnares/8.4.123;
RA   Kawarabayasi Y., Hino Y., Horikawa H., Jin-no K., Takahashi M., Sekine M.,
RA   Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S., Nagai Y.,
RA   Nishijima K., Otsuka R., Nakazawa H., Takamiya M., Kato Y., Yoshizawa T.,
RA   Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K.,
RA   Masuda S., Yanagii M., Nishimura M., Yamagishi A., Oshima T., Kikuchi H.;
RT   "Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon,
RT   Sulfolobus tokodaii strain7.";
RL   DNA Res. 8:123-140(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; BA000023; BAK54356.1; -; Genomic_DNA.
DR   RefSeq; WP_010978606.1; NC_003106.2.
DR   AlphaFoldDB; Q974N4; -.
DR   SMR; Q974N4; -.
DR   STRING; 273063.STK_06250; -.
DR   GeneID; 1458573; -.
DR   KEGG; sto:STK_06250; -.
DR   PATRIC; fig|273063.9.peg.709; -.
DR   eggNOG; arCOG00809; Archaea.
DR   OrthoDB; 23906at2157; -.
DR   Proteomes; UP000001015; 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..945
FT                   /note="Leucine--tRNA ligase 1"
FT                   /id="PRO_0000152146"
FT   MOTIF           42..52
FT                   /note="'HIGH' region"
FT   MOTIF           625..629
FT                   /note="'KMSKS' region"
FT   BINDING         628
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   945 AA;  109513 MW;  7DEA1C56838C0AF9 CRC64;
     MSLANFFNEI AFKWQKEWEN SKVYEANPET DKPKKFITVA FPYTNSPLHI GHGRTYITAD
     IYARYLRMKG YNVLFPFAFQ FTGTPILSIS ESVKRGDEEI ISTFVNIYQI PKEEIEKFSD
     PTYLAEYFKN NMKNTAKKLG LGIDWRREFT TVDPIFEKFV QWQYRKLMEL GYIKREDSPV
     AYCPRDEFPV GMHDTKGDVE PEITDLDGIY FPSGDYFFIA ATPRPETIFG AVALLVNPEA
     DYVIATDSLN RKVIISRQAY DKLKYQISFR EEGEKKGKDL VGMIAKNPVT EKEIKVLPSK
     FVDPSIGTGV VMAVPSHEPL HYIALTELKE EFELIPVIKT DELGELPGVE AVGLAQTRNP
     AELKDYIDTI YRIEYHKGIM REDLVDLVPN FMKEFVKDKI AGKLVKDARE KTRELLDMLN
     SRITIYEISN GPVYCRCGAE IVVKVIKGQW FIDYSNPIWK TSVLKSLDKI NFIPTDSKKE
     MEKIIFNLQP RAFTRSRGLG VRLPWDEKEI IDSLSDSTIY TAFYTIVHKL KYPISLLSDK
     FWDYILLDRG TADEISKELG IPKEQLEEIK SEFKYWYPVD SRHSGRDLIQ NHLPYYLFHH
     FAIFGEKFLP RQIVTNGFIR VGGKKMSKSF GNIYPLNRAI DEYGVETVRI ALTSTSSISD
     DIEFNSNIAK SIAEQLKKIH DLISKLLEIE GVNERRDPDV WLLSIFRRYI EDVDKAYENL
     DLRTVYMTVY YTIYETIKDY IELTNAKINK DIIKKVISIW LRLMAPITPH LAEELWHKMS
     NTFVVKEKFP SINEVEYNEK SLLKVEYLRS IIEDVNRLSS ELGKEAEKVV IYVNDDNNLR
     ELLKKAIIAI KDRKSLRDFM IENNVDDKTA RRIYELANVL PSTIRDLIVT TDIDEEEVIV
     QNINFLMNKL DLREMIVYSS TDEKAPNILG KKDLALPYKP GIAIL
//