SYK_NATPD
ID SYK_NATPD Reviewed; 545 AA.
AC Q3IRL7;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 25-MAY-2022, entry version 91.
DE RecName: Full=Lysine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00177};
DE EC=6.1.1.6 {ECO:0000255|HAMAP-Rule:MF_00177};
DE AltName: Full=Lysyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00177};
DE Short=LysRS {ECO:0000255|HAMAP-Rule:MF_00177};
GN Name=lysS {ECO:0000255|HAMAP-Rule:MF_00177}; OrderedLocusNames=NP_2270A;
OS Natronomonas pharaonis (strain ATCC 35678 / DSM 2160 / CIP 103997 / JCM
OS 8858 / NBRC 14720 / NCIMB 2260 / Gabara) (Halobacterium pharaonis).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Natronomonas.
OX NCBI_TaxID=348780;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB
RC 2260 / Gabara;
RX PubMed=16169924; DOI=10.1101/gr.3952905;
RA Falb M., Pfeiffer F., Palm P., Rodewald K., Hickmann V., Tittor J.,
RA Oesterhelt D.;
RT "Living with two extremes: conclusions from the genome sequence of
RT Natronomonas pharaonis.";
RL Genome Res. 15:1336-1343(2005).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-lysine + tRNA(Lys) = AMP + diphosphate + L-lysyl-
CC tRNA(Lys); Xref=Rhea:RHEA:20792, Rhea:RHEA-COMP:9696, Rhea:RHEA-
CC COMP:9697, ChEBI:CHEBI:30616, ChEBI:CHEBI:32551, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:78442, ChEBI:CHEBI:78529, ChEBI:CHEBI:456215; EC=6.1.1.6;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00177};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00177}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000255|HAMAP-Rule:MF_00177}.
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DR EMBL; CR936257; CAI49226.1; -; Genomic_DNA.
DR RefSeq; WP_011322853.1; NC_007426.1.
DR AlphaFoldDB; Q3IRL7; -.
DR SMR; Q3IRL7; -.
DR STRING; 348780.NP_2270A; -.
DR PRIDE; Q3IRL7; -.
DR EnsemblBacteria; CAI49226; CAI49226; NP_2270A.
DR GeneID; 3702894; -.
DR KEGG; nph:NP_2270A; -.
DR eggNOG; arCOG00485; Archaea.
DR HOGENOM; CLU_025562_1_0_2; -.
DR OMA; DWPMRWA; -.
DR OrthoDB; 9880at2157; -.
DR Proteomes; UP000002698; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004824; F:lysine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR GO; GO:0006430; P:lysyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.10.350; -; 1.
DR Gene3D; 3.40.50.620; -; 2.
DR Gene3D; 6.10.20.10; -; 1.
DR HAMAP; MF_00177; Lys_tRNA_synth_class1; 1.
DR InterPro; IPR020751; aa-tRNA-synth_I_codon-bd_sub2.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR008925; aa_tRNA-synth_I_cd-bd_sf.
DR InterPro; IPR002904; Lys-tRNA-ligase.
DR InterPro; IPR042078; Lys-tRNA-ligase_SC_fold.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR PANTHER; PTHR37940; PTHR37940; 1.
DR Pfam; PF01921; tRNA-synt_1f; 1.
DR SUPFAM; SSF48163; SSF48163; 1.
DR TIGRFAMs; TIGR00467; lysS_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..545
FT /note="Lysine--tRNA ligase"
FT /id="PRO_0000225643"
FT MOTIF 41..49
FT /note="'HIGH' region"
FT MOTIF 306..310
FT /note="'KMSKS' region"
SQ SEQUENCE 545 AA; 60979 MW; 37D4488CC0FC26BB CRC64;
MSDLYDLGTG EKRPFWADAA ADEVEARDPD EPVTIKGGVS PSGVPHLGHF NEIMRGYFVA
EALRERGYEV RQVFTTDDKD RLRKLPRKLA DLDWNVVGLG EVDAGALGRN LGRPYTDIPD
PFGCCDSYGA HFTELLRRSA EAIGVPIDLV SNTELYAGGD FDAAVEDALA NRDTAREVLS
EFQDKVDDEY VPFFPQCAEC GLLTETVTDI DLDDGTVGYV CSDVEAGDDV IEGCGHEGRA
TFRAGKLPWR FEWPAQWRVL GVDFEPFGKD HAEGSWPSGK AVSREVFDTE PPVPMVYEWF
TLNGDALSSS AGNIITVDEV LELLEPAVLR YFFTKNPKKQ RDFDVSNLDR FVDEFDRFEA
GYFGDESVED DERARADRAY PMVVDELPER QPVRIPYTFA AVLGMTDDRD LRLQMAQRSG
HIPDDATDDQ IERALERVEK ARAWAVRTDN EFNYRLAETL PAVDFDAETA AALDELAAFV
ETESPDDETL QGEIYETAKR NDVDVGDLFS AGYRLFLDES EGPRLGPLLS AMDETFVVER
LRREG