SYL_PYRAB
ID SYL_PYRAB Reviewed; 967 AA.
AC Q9V0B9; G8ZI35;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 129.
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=PYRAB08710;
GN ORFNames=PAB1782;
OS Pyrococcus abyssi (strain GE5 / Orsay).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=272844;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GE5 / Orsay;
RX PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA Weissenbach J., Zivanovic Y., Forterre P.;
RT "An integrated analysis of the genome of the hyperthermophilic archaeon
RT Pyrococcus abyssi.";
RL Mol. Microbiol. 47:1495-1512(2003).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=GE5 / Orsay;
RX PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA Gao J., Wang J.;
RT "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT Pyrococcus furiosus DSM 3638.";
RL Curr. Microbiol. 64:118-129(2012).
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; AJ248285; CAB49785.1; -; Genomic_DNA.
DR EMBL; HE613800; CCE70276.1; -; Genomic_DNA.
DR PIR; H75133; H75133.
DR RefSeq; WP_010867994.1; NC_000868.1.
DR AlphaFoldDB; Q9V0B9; -.
DR SMR; Q9V0B9; -.
DR STRING; 272844.PAB1782; -.
DR EnsemblBacteria; CAB49785; CAB49785; PAB1782.
DR GeneID; 1496220; -.
DR KEGG; pab:PAB1782; -.
DR PATRIC; fig|272844.11.peg.919; -.
DR eggNOG; arCOG00809; Archaea.
DR HOGENOM; CLU_004174_0_0_2; -.
DR OMA; AWNMAFQ; -.
DR OrthoDB; 4914at2157; -.
DR PhylomeDB; Q9V0B9; -.
DR Proteomes; UP000000810; Chromosome.
DR Proteomes; UP000009139; 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.
FT CHAIN 1..967
FT /note="Leucine--tRNA ligase"
FT /id="PRO_0000152137"
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; 113824 MW; AA138311F00276A7 CRC64;
MPELNFRAIE EKWQKRWLEA KVFEPNIKDK PKEKKFYITV AFPYLSGHLH VGHARTYTIP
DVIARFKRMQ GYNVLFPMGW HITGSPIVGI AERIKNRDPH TIWIYRDVYK VPEEILWTFE
DPVNIVKYFM KAAKETFIRA GFSVDWSREF YTTSLFPPFS KFIEWQFLKL KEKGYIVKGA
HRVRWDPVVG TPLGDHDLME GEDVPILEYV IIKFELKEGD ETIYLPAATL RPETVYGVTN
MWINPNATYV KAKVKRGGKE ETWIISKEAA YKLSFQDREI EVIEEFKGEK LIGKYVRNPV
TGDEVIILPA EFVDPDNATG VVMSVPAHAP FDHVALEDLK RESEILVKYD IDPRIVEEIT
YISLIKLEGY GEFPAVEEVQ KLGIKSQKDR EKLEQATKTI YKAEYHKGIF KVPPYDGKPV
QEVKELIAKE MMEKGIAEIM YEFAEKNVIS RFGNRAVIKI IHDQWFIDYG NSEWKEKARK
ALARMKIYPE TRRAQFEAII DWLDKKACAR KVGLGTPLPW DPEWVIESLS DSTIYMAYYT
ISRHINRLRE EGRLDPEKLT PEFFDYIFLE EFSEEREKEL EKKTGIPAEI IHEMKEEFEY
WYPLDWRCSG KDLIPNHLTF FIFNHVAIFR EEHWPKGIAV NGFGTLEGQK MSKSKGNVLN
FIDAIEENGA DVVRLYIMSL AEHDSDFDWR RKEVGKLRRQ LERFYELISQ FAEYEAKENV
ELKTIDKWLL HRLNKAIEGT TKALEEFRTR TAVQWAFYSI MNDLRWYMRR TEGRDDEAKR
FVLRKLADIW VRLMAPFTPH ICEELWEKLG GEGFVSLAKW PEPVDEWWNE EVEVEEDFIK
SLIEDIKEII EVAKIESPKR AYIYTAPEWK WKVYEVVAEK REFKSAMAEL MKDEEIRKHG
KEVAKLVQAI IKERAFDVKR IDEEKVLRES KDFLEKELGL EVIINPEEDK GGKKRQAIPL
KPAVFIE
