ID A0A245ZNT1_9SPHN Unreviewed; 528 AA.
AC A0A245ZNT1;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-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 ECO:0000313|EMBL:OWK31396.1};
GN ORFNames=SPDO_14050 {ECO:0000313|EMBL:OWK31396.1};
OS Sphingomonas dokdonensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=344880 {ECO:0000313|EMBL:OWK31396.1, ECO:0000313|Proteomes:UP000197290};
RN [1] {ECO:0000313|EMBL:OWK31396.1, ECO:0000313|Proteomes:UP000197290}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21029 {ECO:0000313|EMBL:OWK31396.1,
RC ECO:0000313|Proteomes:UP000197290};
RA Poehlein A., Wuebbeler J.H., Steinbuechel A., Daniel R.;
RT "Genome sequence of Sphingomonas dokdonensis DSM 21029.";
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OWK31396.1}.
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DR EMBL; NBBI01000002; OWK31396.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A245ZNT1; -.
DR OrthoDB; 9803151at2; -.
DR Proteomes; UP000197290; Unassembled WGS sequence.
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}.
FT MOTIF 49..57
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00177"
FT MOTIF 294..298
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00177"
FT BINDING 297
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00177"
SQ SEQUENCE 528 AA; 58922 MW; A1DE5E7C24864C72 CRC64;
MTDAFDPERR TAALESKAWP YEEARKLLKR WPEGKPDGEP MLFETGYGPS GLPHIGTFQE
VLRTTMVRRA YEEMTGRPTR LVAFSDDMDG LRKVPDNVPN KELLTANLGK PLSRIPDPFG
KFDSFAAHNN AMLRDFLDRF GFEYEFVSST DYYTAGRFDE PLRNVLRNYD KIMAVMLPTL
RAERQATYSP VLPISEKSGI VLQVPVEVVD AEAGIIRFED EGETVEQSIL GGKAKLQWKP
DWGMRWAALG VDYEMYGKDL IDSGVLGGKI AQVLGGRRPE GLIYELFLDA KGEKISKSKG
NGLSIEEWLT YGPDESLAFY IYREPKKAKS LHLGLIPRAV DDYWQFRANY PAQGWKEKLG
NPVHHIHNGD VPAATLPVTF GLLLNLVGVM GEGATNEQVW GYLGNYLPDA NAAAHPELDR
MIGYALSYHR DFIAPTLKRR APEGVEVAAL ERLDADLATL GEDASAEDIQ NAVYEIGKTG
GFAELRDWFK ALYETLLGSS QGPRMGSFIR LYGVANTRRL LAEALAAK
//
