SYK_METBF
ID SYK_METBF Reviewed; 537 AA.
AC Q46CD2;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 25-MAY-2022, entry version 96.
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=Mbar_A1507;
OS Methanosarcina barkeri (strain Fusaro / DSM 804).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=269797;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fusaro / DSM 804;
RX PubMed=16980466; DOI=10.1128/jb.00810-06;
RA Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P., Han C.S.,
RA Lapidus A., Metcalf W.W., Saunders E., Tapia R., Sowers K.R.;
RT "The Methanosarcina barkeri genome: comparative analysis with
RT Methanosarcina acetivorans and Methanosarcina mazei reveals extensive
RT rearrangement within methanosarcinal genomes.";
RL J. Bacteriol. 188:7922-7931(2006).
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; CP000099; AAZ70460.1; -; Genomic_DNA.
DR RefSeq; WP_011306506.1; NC_007355.1.
DR AlphaFoldDB; Q46CD2; -.
DR SMR; Q46CD2; -.
DR STRING; 269797.Mbar_A1507; -.
DR EnsemblBacteria; AAZ70460; AAZ70460; Mbar_A1507.
DR GeneID; 3627694; -.
DR KEGG; mba:Mbar_A1507; -.
DR eggNOG; arCOG00485; Archaea.
DR HOGENOM; CLU_025562_1_0_2; -.
DR OMA; DWPMRWA; -.
DR OrthoDB; 9880at2157; -.
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.
FT CHAIN 1..537
FT /note="Lysine--tRNA ligase"
FT /id="PRO_0000225642"
FT MOTIF 30..38
FT /note="'HIGH' region"
FT MOTIF 276..280
FT /note="'KMSKS' region"
SQ SEQUENCE 537 AA; 60158 MW; 29D2F4F72F657F58 CRC64;
MADTIHWADV IAEDVLKKSG KHLVATGITP SGNIHIGNMR EVVTADAVYR ALSNKGANAD
FIYIADNYDP LRKVYPFLPE SYVEHVGKPI SEIPCPCGNC ANYAEHFLKP FLEALRRLGI
NPQVYRADEM YKTGKYTEAI KTALVKRDAI AKILEEVSGK TVAADWSPFN PRCNQCGKIT
TTKVTGFDLE AETVDYVCAC GHSGIVPMAG GGKLTWRVDW PARWSVLGVT VEPFGKDHAS
KGGSYDTGKR IVREIFGHEP PYPIVYEWIM LGKQGAMSSS TGVVISISDM LEIIPPEVLR
YLIIRTKPEK HIQFDPGQPL LTLVDEYERL RTQFRENDPS LGTFQKRVYE LSRATGICQS
EIPFKQMVTI YQVARGDFAQ ILKIVKRSGF STEDKKCIKE LADNVSKWLK LYAPPFAKFK
VKEKVPVQAA TLSELQRAFL SAFAALIESR GEISGEEYHM LVYSAKDEGS ELNRKIAEKL
NTHAPQVDPR ELFKAIYFSL LGQKSGPKAG WFLSSFDKEF LVERFEEASN YSPEKQA