ID A0A1W6D1B6_9RHOB Unreviewed; 526 AA.
AC A0A1W6D1B6;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=Lysine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00177};
DE EC=6.1.1.6 {ECO:0000256|HAMAP-Rule:MF_00177};
DE AltName: Full=Lysyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00177};
DE Short=LysRS {ECO:0000256|HAMAP-Rule:MF_00177};
GN Name=lysS {ECO:0000256|HAMAP-Rule:MF_00177};
GN ORFNames=B0A89_12005 {ECO:0000313|EMBL:ARJ70901.1};
OS Paracoccus contaminans.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Paracoccus.
OX NCBI_TaxID=1945662 {ECO:0000313|EMBL:ARJ70901.1, ECO:0000313|Proteomes:UP000193017};
RN [1] {ECO:0000313|EMBL:ARJ70901.1, ECO:0000313|Proteomes:UP000193017}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RKI 16-01929T\LMG 29738T\CCM 8701T\CIP 111112T
RC {ECO:0000313|Proteomes:UP000193017};
RA Aurass P., Karste S., Trost E., Glaeser S.P., Kaempfer P., Flieger A.;
RT "Genome sequence of Paracoccus contaminans isolated from a water
RT microcosm.";
RL Submitted (MAR-2017) 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:0000256|ARBA:ARBA00000204, ECO:0000256|HAMAP-
CC Rule:MF_00177};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_00177}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|HAMAP-Rule:MF_00177}.
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DR EMBL; CP020612; ARJ70901.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W6D1B6; -.
DR STRING; 1945662.B0A89_12005; -.
DR KEGG; pcon:B0A89_12005; -.
DR OrthoDB; 9803151at2; -.
DR Proteomes; UP000193017; 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; HUPs; 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 NCBIfam; TIGR00467; lysS_arch; 1.
DR PANTHER; PTHR37940; LYSINE--TRNA LIGASE; 1.
DR PANTHER; PTHR37940:SF1; LYSINE--TRNA LIGASE; 1.
DR Pfam; PF01921; tRNA-synt_1f; 1.
DR SUPFAM; SSF48163; An anticodon-binding domain of class I aminoacyl-tRNA synthetases; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|HAMAP-Rule:MF_00177};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00177};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00177};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00177};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00177};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00177}; Reference proteome {ECO:0000313|Proteomes:UP000193017}.
FT MOTIF 44..52
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00177"
FT MOTIF 290..294
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00177"
FT BINDING 293
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00177"
SQ SEQUENCE 526 AA; 59133 MW; EDFB5C8B556E77E6 CRC64;
MTTLRDAAMN SKAWPFEEAR RVLKRYEKKP PEKGYVLFET GYGPSGLPHI GTFGEVARTT
MIRRAFEIIS DIPTRLFCFS DDMDGMRKVP ENVPQQDMLR AHLQKPLTSV PDPFGEYPSF
GDHNNAMLRR FLDTFGFEYE FISATAFYKS GQFDPTLRLA AERYDAIMEI MLASLREERQ
QTYSCFLPIH PETGRVLYVP IKHVDAADGT ITFDDESGRE WTLPVTGGQV KLQWKPDFGA
RWAALDVDFE MYGKDHSTNT PIYDGICEVL GGRKPEHFTY ELFLDDKGQK ISKSKGNGLS
IDEWLTYAAT ESLSYFMYQK PKTAKRMHFD VIPKAVDEYH QQLRAFPGQT PEQQLANPVW
HIHGGDVPDS NLAVPFQMLL NLAAASGAQD KEGLWGFIRN YAPDASPRTH PDLDAAAAFA
VRYFNDFVAP GRSFRAPSDK ERAALEDLDG RLAAWSGPAD AEALQTMVFA VGTEHGFEPL
RDWFQALYQV LLGADQGPRF GGFVALYGIR ETRALIARAL SGDLAG
//
