ID   SYL_IGNH4               Reviewed;        1022 AA.
AC   A8A8T2;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 84.
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=Igni_0150;
OS   Ignicoccus hospitalis (strain KIN4/I / DSM 18386 / JCM 14125).
OC   Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC   Desulfurococcaceae; Ignicoccus.
OX   NCBI_TaxID=453591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KIN4/I / DSM 18386 / JCM 14125;
RX   PubMed=19000309; DOI=10.1186/gb-2008-9-11-r158;
RA   Podar M., Anderson I., Makarova K.S., Elkins J.G., Ivanova N., Wall M.A.,
RA   Lykidis A., Mavromatis K., Sun H., Hudson M.E., Chen W., Deciu C.,
RA   Hutchison D., Eads J.R., Anderson A., Fernandes F., Szeto E., Lapidus A.,
RA   Kyrpides N.C., Saier M.H. Jr., Richardson P.M., Rachel R., Huber H.,
RA   Eisen J.A., Koonin E.V., Keller M., Stetter K.O.;
RT   "A genomic analysis of the archaeal system Ignicoccus hospitalis-
RT   Nanoarchaeum equitans.";
RL   Genome Biol. 9:R158.1-R158.18(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; CP000816; ABU81334.1; -; Genomic_DNA.
DR   RefSeq; WP_011998186.1; NC_009776.1.
DR   AlphaFoldDB; A8A8T2; -.
DR   SMR; A8A8T2; -.
DR   STRING; 453591.Igni_0150; -.
DR   EnsemblBacteria; ABU81334; ABU81334; Igni_0150.
DR   GeneID; 5562862; -.
DR   KEGG; iho:Igni_0150; -.
DR   eggNOG; arCOG00809; Archaea.
DR   HOGENOM; CLU_004174_0_0_2; -.
DR   OMA; AWNMAFQ; -.
DR   OrthoDB; 4914at2157; -.
DR   PhylomeDB; A8A8T2; -.
DR   Proteomes; UP000000262; 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; IPR015413; Methionyl/Leucyl_tRNA_Synth.
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; 1.
DR   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF00133; tRNA-synt_1; 1.
DR   Pfam; PF09334; tRNA-synt_1g; 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..1022
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000334840"
FT   MOTIF           47..57
FT                   /note="'HIGH' region"
FT   MOTIF           697..701
FT                   /note="'KMSKS' region"
FT   BINDING         700
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   1022 AA;  118172 MW;  944517F2056D7283 CRC64;
     MGDFVEDFVR YLKEIAAKWR EEWERARLHE ADVDPNRPKF YVTAAFPYPN SPMHLGHSRT
     YSVTDAYARF KRMRGFNVLF PMGFHYTGTP IIAMSEKVKQ GLQALRSLGE VKTILEEIWK
     IKVERNLSIG EAIKEYLRGA GREDLMDKTD SIEYLVLFYK VFEIPVEDLE KLTEPLSMAN
     YFASITEEGM KELGYMIDWR RKFTTVDPDF QKFITWQFLK LYDLGYVEKG THPVAWDPVY
     DTPVSQHDTK GDVEPEIEEY DVILFKLKDE DLYLPAATLR AETVFGVTNV WLNPEAEYEV
     VEVDGKRWVL SKKAAYKIKF QKDEVKSLGP IDPKKLLKKM VINPATEEEV PVLPARFVDP
     NVATGVVMSV PAHAPFDYVA LKELEGDPEY SDIVKSIELV QVIRVPEEGL LVPQLVEKLG
     IRDTSDKKKL EEATREVYSK EYRKGRMLES VLERVKGDER LRAALKAFLG NDPVPDAREK
     TAKWLKLFGA GDVFYEIKNA PVYSRFGNEV VVKVLKDQWF LNYGDPQWKE LARKALARMR
     IIPENFLKEF EDTIDWLQKR ACARTRGLGT PLPWDKRWII ESLSDSTIYM AFYTVVNILR
     GASVEPEKLQ PEVWDYIMLG KGNPKELEEK YGISAAVLEE ARRSFDYWYP VDSRHSGKDL
     IRNHLTFFIF NHAAIFPEDK WPRQIVVNGF VNLEGKKMSK SLGNIIPITV AIRSFAPDII
     RLVLLHSAEL GSDADFRTEM VSRAISNLRE IKSIVEKVKD YNGPRPANLT MLDAWYLSSF
     VKDVENVTNM MEDLKIREVT NVLYFILLNR TKEYLNALEA MGRGLDEVAK WVLRYTVERW
     VKMMTPFTPF FAEEMWHELG FNTFVVTEPW PVKDEELVNP LAEAAKEYVE KVIEDIKEII
     KVAKIEKPKK VRIEVASPEQ VKMLKMAVEF VNSGKSLREF MAEATKVFGK KEAKSLRQAF
     ERATSLSESM RSVIARGEFD EKAVLEEFKR LIEEEVGSEV EIRRYEGGKK RPEPLRPAIY
     VE