SYL_PYRFU
ID SYL_PYRFU Reviewed; 967 AA.
AC Q8U2E6;
DT 20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 108.
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=PF0890;
OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=186497;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA DiRuggiero J., Robb F.T.;
RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT horikoshii inferred from complete genomic sequences.";
RL Genetics 152:1299-1305(1999).
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; AE009950; AAL81014.1; -; Genomic_DNA.
DR RefSeq; WP_011012025.1; NZ_CP023154.1.
DR AlphaFoldDB; Q8U2E6; -.
DR SMR; Q8U2E6; -.
DR STRING; 186497.PF0890; -.
DR PRIDE; Q8U2E6; -.
DR EnsemblBacteria; AAL81014; AAL81014; PF0890.
DR GeneID; 41712698; -.
DR KEGG; pfu:PF0890; -.
DR PATRIC; fig|186497.12.peg.940; -.
DR eggNOG; arCOG00809; Archaea.
DR HOGENOM; CLU_004174_0_0_2; -.
DR OMA; AWNMAFQ; -.
DR OrthoDB; 4914at2157; -.
DR PhylomeDB; Q8U2E6; -.
DR Proteomes; UP000001013; 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; 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 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.
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..967
FT /note="Leucine--tRNA ligase"
FT /id="PRO_0000152139"
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"
SQ SEQUENCE 967 AA; 113720 MW; ADABF8E6A4FAD7E7 CRC64;
MPELNFKAIE EKWQKRWLEA KIFEPNIKDK PKEKKFYITV AFPYLSGHLH VGHARTYTIP
DVIARFKRMQ GYNVLFPMAW HITGSPIVGI AERIKNRDPQ TIWIYRDVYK VPEDILWTFE
DPVNIVKYFM KAAKETFIRA GFSVDWSREF YTTSLFPPFS KFIEWQFWKL KEKGYIVKGT
HRVRWDPVVG TPLGDHDLMD GEDVPILEYI LIKFELKEGE ETVYLPAATL RPETVYGVTN
MWLNPEATYV KAKVKKGDKV ETWIISKEAA YKLSFQDREI EVVEEFKGEK LIGKFVRNPV
TGDEVIILPA EFVDPDNATG VVMSVPAHAP FDHVALEDLK KQTDILLKYD IDPRIVENIT
YISLIKLEGY GEFPAVEEVQ KLGVKSQKDK DKLEQATKTI YRAEYHKGIF KIPPYEGKPV
SEVKELIAKD LMEKGIGEIM YEFAEKNVIS RFGNRAVIKI IHDQWFIDYG NPEWKEKARE
ALKRMKILPE SRRAQFEAII EWLDKKACAR KVGLGTPLPW DPDWVIESLS DSTIYMAYYT
ISRHINKLRE EGKLDPEKLT PEFFDYIFLE EFDEKKEKEL EEKTGISAEI IHEMKEEFEY
WYPLDWRCSA KDLIPNHLTF FIFNHVAIFP EKHWPKGIAV NGFGTLEGQK MSKSKGNVLN
FIDAIEENGA DVVRLYIMSL AEHDSDFDWR RKEVGRLRKQ IERFYELISQ FAEYEARENV
ELKDIDKWML HRLNKAIKGT TDALEEFRTR TAVQWAFYTI MNDLRWYLRR TEGRDDEAKR
YVLRTLADIW VRLMAPFTPH ICEELWEKLG GEGFVSLAKW PDPVEEWWNE TIEAEEEYVK
SVMEDIKEII EVAKIENARR AYIYTAEDWK WKVVEVVAEK RDFKAAMSEL MKDQELRKRG
KEIAKIVERL IKDRAFEVKR IDEEKVLREA KDFIEKELGI EIIINPSEDK GGKKKQAMPL
KPAIFIE
