SYK_RICB8
ID SYK_RICB8 Reviewed; 522 AA.
AC A8GVK6;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 03-AUG-2022, entry version 84.
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=A1I_02545;
OS Rickettsia bellii (strain OSU 85-389).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; belli group.
OX NCBI_TaxID=391896;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OSU 85-389;
RA Madan A., Lee H., Madan A., Yoon J.-G., Ryu G.-Y., Dasch G., Ereemeva M.;
RT "Complete genome sequencing of Rickettsia bellii.";
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; CP000849; ABV78883.1; -; Genomic_DNA.
DR RefSeq; WP_012151715.1; NC_009883.1.
DR AlphaFoldDB; A8GVK6; -.
DR SMR; A8GVK6; -.
DR KEGG; rbo:A1I_02545; -.
DR HOGENOM; CLU_025562_2_0_5; -.
DR OMA; DWPMRWA; -.
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_1000040351"
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; 60157 MW; 72FF0CDD2E0F210A CRC64;
MSEILEDAIK SKAWPFEEAK KILDSLNGKT PEKGYVLFET GYGPSGLPHI GTFGENARMV
MVQKAFEQLS NIKTKLICFS DDMDGLRKVP SNIPNPEMVA GYMDMPLTSI PDPFGECESY
GHYMNAKLRS FLDKFGFEYE FYSSTEMYKA GMFDEMLIRV LEKYDEIMEL MLPTFREERK
ATYSPFMPIC PKTGKVLQVP IHKWDAKLGT ITYKDENGET IEVPVTKGHC KLQWKPDFSM
RWAALKVDYE MYGKDHLANG RLYSEICRIL GGKPPVQLCY ELFLDENGEK ISKSKGNSIS
VDDWLKYAPV ESMALFMYQN PTRAKRLFFD VIPKNVDEYI TFNQKYHLEE DRTKRFANPV
YHIHHGNVPK IETFGITYSL LLNLTSVCNP SDKSVLWGFI SRYEPKAMPN NSPYLDHLAE
FAIRYYNDFV KAHKSYLAPS EKHKAILQDI LDMLKGLPEQ IEAESIQKGI YDIGMKAGYE
NLRDYFKDLY QILLGQSDGP RLGTFIKLYG ISETMKLIEE KL
