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Database: UniProt
Entry: A0A0B1ZS26_9SPHN
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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}.
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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
//
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