ID   SYL_NANEQ               Reviewed;         977 AA.
AC   P61760;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2004, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Leucine--tRNA ligase;
DE            EC=6.1.1.4;
DE   AltName: Full=Leucyl-tRNA synthetase;
DE            Short=LeuRS;
GN   Name=leuS; OrderedLocusNames=NEQ239;
OS   Nanoarchaeum equitans (strain Kin4-M).
OC   Archaea; Nanoarchaeota; Candidatus Nanoarchaeia; Nanoarchaeales;
OC   Nanoarchaeaceae; Nanoarchaeum.
OX   NCBI_TaxID=228908;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Kin4-M;
RX   PubMed=14566062; DOI=10.1073/pnas.1735403100;
RA   Waters E., Hohn M.J., Ahel I., Graham D.E., Adams M.D., Barnstead M.,
RA   Beeson K.Y., Bibbs L., Bolanos R., Keller M., Kretz K., Lin X., Mathur E.,
RA   Ni J., Podar M., Richardson T., Sutton G.G., Simon M., Soell D.,
RA   Stetter K.O., Short J.M., Noorderwier M.;
RT   "The genome of Nanoarchaeum equitans: insights into early archaeal
RT   evolution and derived parasitism.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:12984-12988(2003).
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE017199; AAR39092.1; -; Genomic_DNA.
DR   AlphaFoldDB; P61760; -.
DR   SMR; P61760; -.
DR   STRING; 228908.NEQ239; -.
DR   PRIDE; P61760; -.
DR   EnsemblBacteria; AAR39092; AAR39092; NEQ239.
DR   KEGG; neq:NEQ239; -.
DR   PATRIC; fig|228908.8.peg.244; -.
DR   HOGENOM; CLU_004174_0_0_2; -.
DR   OMA; AWNMAFQ; -.
DR   Proteomes; UP000000578; 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-KW.
DR   GO; GO:0004823; F:leucine-tRNA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006429; P:leucyl-tRNA aminoacylation; IEA:InterPro.
DR   Gene3D; 3.40.50.620; -; 2.
DR   Gene3D; 3.90.740.10; -; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR002300; aa-tRNA-synth_Ia.
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; 2.
DR   SUPFAM; SSF47323; SSF47323; 1.
DR   SUPFAM; SSF50677; SSF50677; 2.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..977
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000152136"
FT   REGION          220..318
FT                   /note="Insert"
FT   MOTIF           11..21
FT                   /note="'HIGH' region"
FT   MOTIF           699..703
FT                   /note="'KMSKS' region"
FT   BINDING         702
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   977 AA;  115023 MW;  3B5F2A6AE3236ABF CRC64;
     MKKFFVTAAF PYVNGYLHLG HLVTYIKAEI TARYKKMRGY DVLFPMGFHA TGAPIYAAAY
     KVSIGDPKQI ETLKKMGIKD IEKFKDPAYW VEYFSKAAKE DLSKLGFMIE WERSFTTVFN
     KPFHKFVEWQ YHRLREKGYI YRGAHPIVWD PKVNMVIGDH DRPDDYAGIR PIEGVIIKFY
     SKDLDAYLPA FTLRPETVFG VVNIWVNPET EYVLAKVKKV FYVYELYSLY KKFGRLPLNI
     ENRDKLEKLI QDYNNLLDRL KQYEKGIDLI AHAEEIAYKP KEEFVKELKE FAEKEGIKIE
     EKDIELLYEY YNTKVETQEE KWILPNTIVI EELKNQDFEI EIIGKIDKLI KTLAENPVTK
     ELVPVLPAKF VDPEVGTGIV MSVPSHAPYD YVGLLDLIKT ELKEFAEQAL KNVRPVVKVE
     GFSEMPAKDI VESMNITSQE ERDKLEKATQ RLYSKEFYHG VLTEHAQQFQ GLPVKEAKMK
     IAEYLMENGY GYIYYTLPVR FKSRYGNKVV VKLVKGQWFI KYSDKQWKEL AHKAVENMKF
     YPPQVKELIK EKIDWYDDWA FTHQKELGTA LPWDPKWVIE SLSDSTIYTA YYTIAHILQH
     PEKYNIDWDK LTIDVFDYVF LGKGDPKEIA KKTGISEEIL KEMRNQFEYW YPVDIRFSAQ
     DLIANHLVFY IFHHVAIFPE SKWPRGIAVS GFVTVNGEKM SKSKGNFITI REAIQRYGRD
     AVRLAAAYAG NAELVDQNID LEFMEKAKNE IIPRIESYLD MEGYDRDENS LDKWIVNRIR
     LYFKKLEEYY ENIRPRDVIN EFFKLENDFN FYRALVLEKP HKRAIEYFKK AVKALWPIIP
     HVVREPAWIG KEEPDEPWIR VGQYVDQVIK DLANTLKLVR ISMARNVSHR LADLVKLYYE
     GAKLTEEEKE EIREFIEWKP VRIKIIYKNP SEFDILRDII PYIEKVFGGK VVLELASESK
     EEKAKRAKEF KPAFVIE