ID A0A0B1ZS26_9SPHN Unreviewed; 537 AA.
AC A0A0B1ZS26;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 24-JAN-2024, entry version 40.
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=lysK {ECO:0000313|EMBL:KHK92002.1};
GN Synonyms=lysS {ECO:0000256|HAMAP-Rule:MF_00177};
GN ORFNames=LK12_12590 {ECO:0000313|EMBL:KHK92002.1};
OS Novosphingobium malaysiense.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=1348853 {ECO:0000313|EMBL:KHK92002.1, ECO:0000313|Proteomes:UP000031057};
RN [1] {ECO:0000313|EMBL:KHK92002.1, ECO:0000313|Proteomes:UP000031057}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MUSC 273 {ECO:0000313|EMBL:KHK92002.1,
RC ECO:0000313|Proteomes:UP000031057};
RA Lee L.-H.;
RT "Genome sequence of Novosphingobium malaysiense MUSC 273(T).";
RL Submitted (OCT-2014) 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:KHK92002.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JTDI01000003; KHK92002.1; -; Genomic_DNA.
DR RefSeq; WP_039285290.1; NZ_JTDI01000003.1.
DR AlphaFoldDB; A0A0B1ZS26; -.
DR STRING; 1348853.LK12_12590; -.
DR OrthoDB; 9803151at2; -.
DR Proteomes; UP000031057; 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 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:UP000031057}.
FT MOTIF 46..54
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00177"
FT MOTIF 293..297
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00177"
FT BINDING 296
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00177"
SQ SEQUENCE 537 AA; 59143 MW; 59D3432DCEA0ED16 CRC64;
MTDDALIEAA RVSKAWPFQE AQKLLKRYPN GKPGGEPVLF ETGYGPSGLP HIGTFQEVLR
TTLVRRAYEA LTGGAPTRLV AFSDDMDGLR KVPDNIPQPE MLAANLGKPL TRIPDPFGKF
ESFAHHNNAM LRDFLDRFGF EYEFVSASDR YNSGAFDAAL SRVLECNQAI LDVMLPTLRE
ERRKTYSPVL PVSPSTGIVL QVPVEVLDPA TGMIRFTDQD GSVVEQSVFG GQAKLQWKVD
WAMRWYALGV DYEMSGKDLT DSVTQSGKIV KVLGGRKPEG LIYELFLDEN GEKISKSKGN
GLTIEQWLTY GTEESLGFYL FREPKSAKQL HVGVIPKAVD EYWQFRGNLA NQPLDKQLGN
PVWHLLRVNG DCAGTTPKGA GDTPPVTFSL LLNLVGVLGA EATADQVWSY LGNYVAEATP
EAHPELEELV RAALATNRDF IAPSLQRRAP TANEAQALRA LDAELAKAGS DTSAEELQNT
VYEIGKDEAY GFENLRDWFK ALYETLLGSS QGPRMGSFIA LYGVPETRQL IAQALDA
//