SYK_RICPR
ID SYK_RICPR Reviewed; 528 AA.
AC Q9ZDF8;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Lysine--tRNA ligase;
DE EC=6.1.1.6;
DE AltName: Full=Lysyl-tRNA synthetase;
DE Short=LysRS;
GN Name=lysS; OrderedLocusNames=RP371;
OS Rickettsia prowazekii (strain Madrid E).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX NCBI_TaxID=272947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Madrid E;
RX PubMed=9823893; DOI=10.1038/24094;
RA Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T.,
RA Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H.,
RA Kurland C.G.;
RT "The genome sequence of Rickettsia prowazekii and the origin of
RT mitochondria.";
RL Nature 396:133-140(1998).
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
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DR EMBL; AJ235271; CAA14830.1; -; Genomic_DNA.
DR PIR; D71694; D71694.
DR RefSeq; NP_220754.1; NC_000963.1.
DR RefSeq; WP_004597521.1; NC_000963.1.
DR AlphaFoldDB; Q9ZDF8; -.
DR SMR; Q9ZDF8; -.
DR STRING; 272947.RP371; -.
DR EnsemblBacteria; CAA14830; CAA14830; CAA14830.
DR GeneID; 57569495; -.
DR KEGG; rpr:RP371; -.
DR PATRIC; fig|272947.5.peg.382; -.
DR eggNOG; COG1384; Bacteria.
DR HOGENOM; CLU_025562_2_0_5; -.
DR OMA; DWPMRWA; -.
DR Proteomes; UP000002480; 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 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; 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..528
FT /note="Lysine--tRNA ligase"
FT /id="PRO_0000152743"
FT MOTIF 44..52
FT /note="'HIGH' region"
FT MOTIF 290..294
FT /note="'KMSKS' region"
FT BINDING 293
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 528 AA; 60592 MW; 2155599451A3E434 CRC64;
MSVVLEDAIR SNAWPFIEAK KILDSLNGKA PEKGYILFET GYGPSGLPHI GTFAENARMV
MVQKAFEQLS DIPTKLICFS DDMDGLRKVP SNIPHPEMVA QYMDMPLTSI PDPFGKCKSY
GHYMNAKLCA FLDKFGFKYE FYSSTNCYKA GMFDEMLIRV LEKYDEIMAL MLPTFRDERK
TTYAPFMPIC PKTGKVLQVP IEKWDAKAGT VSYKDEDGND VEVPVTGGHC KLQWKPDFGM
RWAALKVDYE MYGKDHLANS RLYSEICRIL GGKPPVQFCY ELFLDANGEK ISKSRGNSIS
VDDWLKYASV ESIALFMYKN PARAKRLFFD LIPKNVDEYI TLNQKYHLEE DMVTRFANPV
YHIHHGNVPK IETFGLTYSL LLNLTAVCNT SDKSVLWGFI TKYEPKATPN TSTYLDHLTE
FAIRYYNDFI QTHKSYLVVS EKHKIILHDI LDMLSNISDQ TEEESIQKAI YDIGMKSGYE
NLRYYFKDLY QILLGQNEGP RLGTFIKLYG VEETKKLVEE KLLCHTVA
