ID   SYL1_METS5              Reviewed;         938 AA.
AC   A4YE96;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 92.
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=Msed_0573;
OS   Metallosphaera sedula (strain ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509
OS   / TH2).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Metallosphaera.
OX   NCBI_TaxID=399549;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2;
RX   PubMed=18083856; DOI=10.1128/aem.02019-07;
RA   Auernik K.S., Maezato Y., Blum P.H., Kelly R.M.;
RT   "The genome sequence of the metal-mobilizing, extremely thermoacidophilic
RT   archaeon Metallosphaera sedula provides insights into bioleaching-
RT   associated metabolism.";
RL   Appl. Environ. Microbiol. 74:682-692(2008).
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; CP000682; ABP94748.1; -; Genomic_DNA.
DR   RefSeq; WP_012020536.1; NC_009440.1.
DR   AlphaFoldDB; A4YE96; -.
DR   SMR; A4YE96; -.
DR   STRING; 399549.Msed_0573; -.
DR   EnsemblBacteria; ABP94748; ABP94748; Msed_0573.
DR   GeneID; 5103733; -.
DR   GeneID; 59455976; -.
DR   KEGG; mse:Msed_0573; -.
DR   eggNOG; arCOG00809; Archaea.
DR   HOGENOM; CLU_004174_0_0_2; -.
DR   OMA; QKWWEES; -.
DR   Proteomes; UP000000242; 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; 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..938
FT                   /note="Leucine--tRNA ligase 1"
FT                   /id="PRO_0000334841"
FT   MOTIF           40..50
FT                   /note="'HIGH' region"
FT   MOTIF           620..624
FT                   /note="'KMSKS' region"
FT   BINDING         623
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   938 AA;  107432 MW;  FC5DCA901315932E CRC64;
     MDSAFFNEVA KKWQEKWENN KVFEANPSNS EKYFITVAFP YTNSPLHIGH GRTYITADIV
     ARYQRMIGKN VLFPFAFQFT GTPILSISES IKRGDSDIIS DFINLYKISP EKVREFEDPL
     KLAEYFKEDM KRMAKALGLS VDWRREFTTI DPRFGQFIKW QFRKLKEKGF ITTATDAVGY
     CPNDNFPVGM HDTKGDVEPE VQEMDVIEFE GNDVVFPTAT SRPETVFGAN AVLINPEATY
     VLIRGSNWVL SKEAFRKLSY QRELVPEREV QGKDLIGLTV KNPISGKDVK VYGSKFVDAK
     MGTGSVMAVP AHEPLHYLGL SEVLSEVEVI PVISTEGYGD FPGPEVLALA GTKNPAELKD
     YIDTLYREEY YKGVMREDIV DLVPDYMRSI VKDRIAGKRV PEARRETVEL LRSLGKHDLI
     YEISNGPIYC RCGAEIVVKV IRDQWYITYD NPLWKSWTMK ALDRISIVPE EARRDMAKAI
     FSMKRRACSR SRGLGVKLPW DESQIIDSLS DSTIYTGFYT VAHKLSHDPS KLNDQFWDFV
     LLGNGDASEV SKVTGISVEE LKDLRNEFSY WYPLDSRHSG RDLVQNHLPF LIYNHLAIFG
     ESLLPRQIVI NGFVRVGGKK MSKSFRNIYP LYKAVEEYGV DPVRLALTIS SELLEDTDFD
     VNTVKAVTDQ LRRMYDLAVN LSKLRENEST GLPEKWLLSI IHYKVKEVSD LMNSLDLRKA
     FNIILYEYYE ILRDYLSMVS NPNTSVLRKA IEIWARLISP GAPHIAEEIW HIFNEGFVSL
     TRYPVPEELE VDGQAVIQLE YIRHLINQVK EISSMANKQP EKLIIYVSNS DELGILRAVL
     RGLKERKNLR ELSSITGQRE EYLRSLVERV QSLPPILREL IVTYPLDEFK TITDNLNFLV
     RRLDVDEIQV YRSDEANAPD IKGKKSNALP LLPGIVII