ID SYL_PYRHO Reviewed; 967 AA. AC O58698; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1998, sequence version 1. DT 27-MAR-2024, entry version 149. 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=PH0965; OS Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC OS 100139 / OT-3). OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae; OC Pyrococcus. OX NCBI_TaxID=70601; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3; RX PubMed=9679194; DOI=10.1093/dnares/5.2.55; RA Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S., RA Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K., RA Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T., RA Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T., RA Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.; RT "Complete sequence and gene organization of the genome of a hyper- RT thermophilic archaebacterium, Pyrococcus horikoshii OT3."; RL DNA Res. 5:55-76(1998). RN [2] RP X-RAY CRYSTALLOGRAPHY (3.21 ANGSTROMS). RG RIKEN structural genomics initiative (RSGI); RT "The crystal structure of leucyl-tRNA synthetase and tRNA(leucine) RT complex."; RL Submitted (SEP-2005) to the PDB data bank. 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}. 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; BA000001; BAA30062.1; -; Genomic_DNA. DR PIR; H71087; H71087. DR RefSeq; WP_010885055.1; NC_000961.1. DR PDB; 1WKB; X-ray; 2.05 A; A=1-810. DR PDB; 1WZ2; X-ray; 3.21 A; A/B=1-967. DR PDBsum; 1WKB; -. DR PDBsum; 1WZ2; -. DR AlphaFoldDB; O58698; -. DR SMR; O58698; -. DR STRING; 70601.gene:9377920; -. DR EnsemblBacteria; BAA30062; BAA30062; BAA30062. DR GeneID; 1443290; -. DR KEGG; pho:PH0965; -. DR eggNOG; arCOG00809; Archaea. DR OrthoDB; 23906at2157; -. DR BRENDA; 6.1.1.4; 5244. DR EvolutionaryTrace; O58698; -. DR Proteomes; UP000000752; 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 CDD; cd00812; LeuRS_core; 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; IPR001412; aa-tRNA-synth_I_CS. 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; 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. DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1. PE 1: Evidence at protein level; KW 3D-structure; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; KW Nucleotide-binding; Protein biosynthesis. FT CHAIN 1..967 FT /note="Leucine--tRNA ligase" FT /id="PRO_0000152140" FT MOTIF 43..53 FT /note="'HIGH' region" FT MOTIF 650..654 FT /note="'KMSKS' region" FT BINDING 653 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049" FT HELIX 7..19 FT /evidence="ECO:0007829|PDB:1WKB" FT TURN 20..23 FT /evidence="ECO:0007829|PDB:1WKB" FT HELIX 27..29 FT /evidence="ECO:0007829|PDB:1WKB" FT HELIX 32..34 FT /evidence="ECO:0007829|PDB:1WKB" FT STRAND 35..40 FT /evidence="ECO:0007829|PDB:1WKB" FT HELIX 51..70 FT /evidence="ECO:0007829|PDB:1WKB" FT STRAND 73..75 FT /evidence="ECO:0007829|PDB:1WKB" FT HELIX 86..95 FT /evidence="ECO:0007829|PDB:1WKB" FT HELIX 99..107 FT /evidence="ECO:0007829|PDB:1WKB" FT HELIX 113..117 FT /evidence="ECO:0007829|PDB:1WKB" FT HELIX 118..120 FT /evidence="ECO:0007829|PDB:1WKB" FT HELIX 122..139 FT /evidence="ECO:0007829|PDB:1WKB" FT HELIX 146..148 FT /evidence="ECO:0007829|PDB:1WKB" FT HELIX 157..172 FT /evidence="ECO:0007829|PDB:1WKB" FT STRAND 176..186 FT /evidence="ECO:0007829|PDB:1WKB" FT TURN 187..190 FT /evidence="ECO:0007829|PDB:1WKB" FT STRAND 195..197 FT /evidence="ECO:0007829|PDB:1WZ2" FT STRAND 206..215 FT /evidence="ECO:0007829|PDB:1WKB" FT STRAND 219..221 FT /evidence="ECO:0007829|PDB:1WZ2" FT STRAND 224..230 FT /evidence="ECO:0007829|PDB:1WKB" FT HELIX 232..237 FT /evidence="ECO:0007829|PDB:1WKB" FT STRAND 240..243 FT /evidence="ECO:0007829|PDB:1WKB" FT STRAND 245..247 FT /evidence="ECO:0007829|PDB:1WZ2" FT STRAND 249..256 FT /evidence="ECO:0007829|PDB:1WKB" FT STRAND 259..266 FT /evidence="ECO:0007829|PDB:1WKB" FT HELIX 267..273 FT /evidence="ECO:0007829|PDB:1WKB" FT STRAND 279..285 FT /evidence="ECO:0007829|PDB:1WKB" FT TURN 287..293 FT /evidence="ECO:0007829|PDB:1WKB" FT STRAND 295..297 FT /evidence="ECO:0007829|PDB:1WKB" FT STRAND 299..301 FT /evidence="ECO:0007829|PDB:1WKB" FT STRAND 304..309 FT /evidence="ECO:0007829|PDB:1WKB" FT STRAND 315..317 FT /evidence="ECO:0007829|PDB:1WZ2" FT STRAND 322..324 FT /evidence="ECO:0007829|PDB:1WKB" FT TURN 326..328 FT /evidence="ECO:0007829|PDB:1WKB" FT HELIX 330..336 FT /evidence="ECO:0007829|PDB:1WKB" FT HELIX 380..382 FT /evidence="ECO:0007829|PDB:1WKB" FT HELIX 394..406 FT /evidence="ECO:0007829|PDB:1WKB" FT HELIX 413..415 FT /evidence="ECO:0007829|PDB:1WKB" FT STRAND 417..419 FT /evidence="ECO:0007829|PDB:1WZ2" FT HELIX 420..432 FT /evidence="ECO:0007829|PDB:1WKB" FT TURN 433..435 FT /evidence="ECO:0007829|PDB:1WKB" FT STRAND 436..446 FT /evidence="ECO:0007829|PDB:1WKB" FT STRAND 451..455 FT /evidence="ECO:0007829|PDB:1WZ2" FT STRAND 457..467 FT /evidence="ECO:0007829|PDB:1WKB" FT HELIX 472..483 FT /evidence="ECO:0007829|PDB:1WKB" FT STRAND 485..489 FT /evidence="ECO:0007829|PDB:1WKB" FT HELIX 490..492 FT /evidence="ECO:0007829|PDB:1WKB" FT HELIX 493..502 FT /evidence="ECO:0007829|PDB:1WKB" FT STRAND 509..515 FT /evidence="ECO:0007829|PDB:1WKB" FT STRAND 521..526 FT /evidence="ECO:0007829|PDB:1WKB" FT TURN 528..530 FT /evidence="ECO:0007829|PDB:1WKB" FT STRAND 531..534 FT /evidence="ECO:0007829|PDB:1WKB" FT HELIX 535..550 FT /evidence="ECO:0007829|PDB:1WKB" FT HELIX 556..558 FT /evidence="ECO:0007829|PDB:1WKB" FT HELIX 561..569 FT /evidence="ECO:0007829|PDB:1WKB" FT HELIX 574..584 FT /evidence="ECO:0007829|PDB:1WKB" FT HELIX 588..601 FT /evidence="ECO:0007829|PDB:1WKB" FT STRAND 605..610 FT /evidence="ECO:0007829|PDB:1WKB" FT HELIX 611..613 FT /evidence="ECO:0007829|PDB:1WKB" FT TURN 614..616 FT /evidence="ECO:0007829|PDB:1WKB" FT HELIX 617..628 FT /evidence="ECO:0007829|PDB:1WKB" FT HELIX 631..633 FT /evidence="ECO:0007829|PDB:1WKB" FT STRAND 637..641 FT /evidence="ECO:0007829|PDB:1WKB" FT STRAND 644..646 FT /evidence="ECO:0007829|PDB:1WKB" FT TURN 653..656 FT /evidence="ECO:0007829|PDB:1WKB" FT HELIX 661..668 FT /evidence="ECO:0007829|PDB:1WKB" FT HELIX 670..680 FT /evidence="ECO:0007829|PDB:1WKB" FT STRAND 687..689 FT /evidence="ECO:0007829|PDB:1WKB" FT HELIX 691..712 FT /evidence="ECO:0007829|PDB:1WKB" FT HELIX 724..745 FT /evidence="ECO:0007829|PDB:1WKB" FT HELIX 749..756 FT /evidence="ECO:0007829|PDB:1WKB" FT HELIX 758..770 FT /evidence="ECO:0007829|PDB:1WKB" FT TURN 771..773 FT /evidence="ECO:0007829|PDB:1WKB" FT HELIX 777..794 FT /evidence="ECO:0007829|PDB:1WKB" FT TURN 795..797 FT /evidence="ECO:0007829|PDB:1WKB" FT HELIX 799..808 FT /evidence="ECO:0007829|PDB:1WKB" FT HELIX 815..817 FT /evidence="ECO:0007829|PDB:1WZ2" FT HELIX 830..851 FT /evidence="ECO:0007829|PDB:1WZ2" FT STRAND 858..863 FT /evidence="ECO:0007829|PDB:1WZ2" FT TURN 867..873 FT /evidence="ECO:0007829|PDB:1WZ2" FT HELIX 874..877 FT /evidence="ECO:0007829|PDB:1WZ2" FT TURN 878..880 FT /evidence="ECO:0007829|PDB:1WZ2" FT STRAND 882..884 FT /evidence="ECO:0007829|PDB:1WZ2" FT HELIX 885..891 FT /evidence="ECO:0007829|PDB:1WZ2" FT TURN 894..899 FT /evidence="ECO:0007829|PDB:1WZ2" FT HELIX 900..902 FT /evidence="ECO:0007829|PDB:1WZ2" FT HELIX 905..910 FT /evidence="ECO:0007829|PDB:1WZ2" FT HELIX 922..927 FT /evidence="ECO:0007829|PDB:1WZ2" FT TURN 928..930 FT /evidence="ECO:0007829|PDB:1WZ2" FT HELIX 931..938 FT /evidence="ECO:0007829|PDB:1WZ2" FT STRAND 963..966 FT /evidence="ECO:0007829|PDB:1WZ2" SQ SEQUENCE 967 AA; 113949 MW; DEFBD287679E9498 CRC64; MAELNFKAIE EKWQKRWLEA KIFEPNIRDK PKEKKFYITV AFPYLSGHLH VGHARTYTIP DVIARFKRMQ GYNVLFPMAW HITGSPIVGI AERIKNRDPK TIWIYRDVYK VPEEILWTFE DPINIVKYFM KAAKETFIRA GFSVDWSREF YTTSLFPPFS KFIEWQFWKL KEKGYIVKGA HRVRWDPVVG TPLGDHDLME GEDVPILDYI IIKFELRENG EVIYLPAATL RPETVYGVTN MWVNPNATYV KAKVRRKDKE ETWIVSKEAA YKLSFQDREI EVIEEFKGEK LIGKYVRNPV SGDEVIILPA EFVDPDNATG VVMSVPAHAP FDHVALEDLK RETEILEKYD IDPRIVENIT YISLIKLEGY GDFPAVEEVN KLGIKSQKDK EKLEQATKTI YKAEYHKGIF KVPPYEGKPV QEVKEAIAKE MLEKGIAEIM YEFAEKNVIS RFGNRAVIKI IHDQWFIDYG NPEWKEKARK ALERMKILPE TRRAQFEAII DWLDKKACAR KIGLGTPLPW DPEWVIESLS DSTIYMAYYT ISRHINKLRQ EGKLDPEKLT PEFFDYIFLE EFSEDKEKEL EKKTGIPAEI IHEMKEEFEY WYPLDWRCSG KDLIPNHLTF FIFNHVAIFR EEHWPKGIAV NGFGTLEGQK MSKSKGNVLN FIDAIEENGA DVVRLYIMSL AEHDSDFDWR RKEVGKLRKQ IERFYELISQ FAEYEVKGNV ELKDIDRWML HRLNKAIKET TNALEEFRTR TAVQWAFYSI MNDLRWYLRR TEGRDDEAKR YVLRTLADVW VRLMAPFTPH ICEELWEKLG GEGFVSLAKW PEPVEEWWNE TIEAEEEFIR SVMEDIKEII EVAKIENAKR AYIYTAEDWK WKVAEVVSEK RDFKSSMEEL MKDSEIRKHG KEVAKIVQKL IKERTFDVKR INEEKALREA KEFMEKELGI EIIINPTEDK GGKKKQAMPL KPAIFIE //