SYK_RICRS
ID SYK_RICRS Reviewed; 522 AA.
AC A8GRT7;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 03-AUG-2022, entry version 79.
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=A1G_02865;
OS Rickettsia rickettsii (strain Sheila Smith).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX NCBI_TaxID=392021;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sheila Smith;
RA Madan A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S.,
RA Sanchez A., Dasch G., Eremeeva M.;
RT "Complete genome sequence of Rickettsia rickettsii.";
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; CP000848; ABV76112.1; -; Genomic_DNA.
DR RefSeq; WP_012150703.1; NC_009882.1.
DR AlphaFoldDB; A8GRT7; -.
DR SMR; A8GRT7; -.
DR EnsemblBacteria; ABV76112; ABV76112; A1G_02865.
DR GeneID; 45539082; -.
DR KEGG; rri:A1G_02865; -.
DR HOGENOM; CLU_025562_2_0_5; -.
DR OMA; DWPMRWA; -.
DR Proteomes; UP000006832; 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..522
FT /note="Lysine--tRNA ligase"
FT /id="PRO_1000040353"
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 522 AA; 59891 MW; 5B9948D1903DC7D2 CRC64;
MSEIWEDAIK SNAWPFVEAK KILDSLNGQI PEKGYVLFET GYGPSGLPHI GTFGENARMV
MVQKAFEQLS DIPTKLICFS DDMDGLRKVP SNIPNPEMVA QYMDMPLTSI PDTFGECESY
GHYMNAKLRS FLDKFGFEYE FYSSTNCYKA GMFDEMLIMV LEKYDEIMEL MLPTFREERK
ATYSPFMPIC PKTGKVLQVP IEKWDAKAGT VTYKDKAGNY IEVPVTGGHC KLQWKPDFGM
RWAALKVDYE MYGKDHLANA RLYSEICRIL GGKPPVQLCY ELFLDENGEK ISKSKGNSIS
IDDWLKYAPV ESMALFMYQN PTRAKRLFFD VIPKNVDEYI TFNQKYHLEE DRAKRVANPV
YHIHHGNVPK IETFGITYSL LLNLTSVCNP SDKSVLWGFI SKYEPQATPN TNPYLDHLAE
FAIRYYNDFI KAHKSYLSPS EKHKVILQDI LDMLSDIADQ TEAEAIQKAI YDIGMKAGYA
NLRDYFKDLY QILLGQNEGP RLGTFIKLYG VQEMKKLVEG QL
