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 27-MAR-2024, entry version 91.
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; Thermoproteota; 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 GeneID; 5562862; -.
DR KEGG; iho:Igni_0150; -.
DR eggNOG; arCOG00809; Archaea.
DR HOGENOM; CLU_004174_0_0_2; -.
DR OrthoDB; 23906at2157; -.
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 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; 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 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; 1.
DR Pfam; PF09334; tRNA-synt_1g; 1.
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..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
//
