SYK_RICAH
ID SYK_RICAH Reviewed; 529 AA.
AC A8GN71;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 03-AUG-2022, entry version 81.
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=A1C_02755;
OS Rickettsia akari (strain Hartford).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX NCBI_TaxID=293614;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hartford;
RA Madan A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S.,
RA Sanchez A., Whiting M., Dasch G., Eremeeva M.;
RT "Complete genome sequence of Rickettsia akari.";
RL Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000847; ABV74846.1; -; Genomic_DNA.
DR RefSeq; WP_012149480.1; NC_009881.1.
DR AlphaFoldDB; A8GN71; -.
DR SMR; A8GN71; -.
DR STRING; 293614.A1C_02755; -.
DR EnsemblBacteria; ABV74846; ABV74846; A1C_02755.
DR KEGG; rak:A1C_02755; -.
DR eggNOG; COG1384; Bacteria.
DR HOGENOM; CLU_025562_2_0_5; -.
DR OMA; DWPMRWA; -.
DR Proteomes; UP000006830; 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.
FT CHAIN 1..529
FT /note="Lysine--tRNA ligase"
FT /id="PRO_1000040350"
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:0000255|HAMAP-Rule:MF_00177"
SQ SEQUENCE 529 AA; 60726 MW; 1A156B1EF7B2E031 CRC64;
MSEIWEDAIK SNAWPFVEAK KILDSLNGKT PEKGYLLFET GYGPSGLPHI GTFGENARIV
MVQKAFEQLS DIPTKLICFS DDMDGLRKVP SNIPHPEMVA GYMDMPLTSI PDPFGECESY
GHYMNAKLRS FLDKFGFKYE FYSSTNCYKA GMFDEMLIRV LEQYDKIMEL MLPTFREERK
ATYSPFMPVC LKTGKVLQVP IEKWDAKVGT VTYKDEAGNY IEVPVTGGHC KLQWKPDFGM
RWAALKVDYE MYGKDHLANA RLYSEICRIL GGKPPVQLCY ELFLDENGEK ISKSKGNSIS
VDDWLKYAPV ESMALFMYQN PTRAKRLFFD VIPKNVDEYI TFNQKYHLEE DRAKRFANPV
YHIHHGNVPK IETFGITYVL LLNLTSVCNP SDKTVLWGFI SKYEPKATPN TSPYLDHLAE
FAIRYYNDFI KAHKSYLAPS EKHNVILRDI LDMLSDISDQ TEAEGIQKAI YDIGMRAGYE
NLRDYFKDLY QILLGQSEGP RLGTFIKLYG VQETKKLVAG KLTMLSRKK