ID A0A1Z1WGC2_9ACTN Unreviewed; 582 AA.
AC A0A1Z1WGC2;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 30.
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:ARX85487.1};
GN Synonyms=lysS {ECO:0000256|HAMAP-Rule:MF_00177};
GN ORFNames=SMD44_04951 {ECO:0000313|EMBL:ARX85487.1};
OS Streptomyces alboflavus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=67267 {ECO:0000313|EMBL:ARX85487.1, ECO:0000313|Proteomes:UP000195880};
RN [1] {ECO:0000313|EMBL:ARX85487.1, ECO:0000313|Proteomes:UP000195880}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MDJK44 {ECO:0000313|EMBL:ARX85487.1,
RC ECO:0000313|Proteomes:UP000195880};
RA Wang Y., Du B., Ding Y., Liu H., Hou Q., Liu K., Wang C., Yao L.;
RT "Streptomyces alboflavus Genome sequencing and assembly.";
RL Submitted (MAY-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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00177}.
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DR EMBL; CP021748; ARX85487.1; -; Genomic_DNA.
DR RefSeq; WP_030361102.1; NZ_RHGC01000001.1.
DR AlphaFoldDB; A0A1Z1WGC2; -.
DR STRING; 67267.GCA_000716675_06234; -.
DR KEGG; salf:SMD44_04951; -.
DR eggNOG; COG1384; Bacteria.
DR OrthoDB; 9803151at2; -.
DR Proteomes; UP000195880; 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 Gene3D; 6.10.20.10; Lysine tRNA ligase, stem contact fold domain; 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 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:UP000195880}.
FT REGION 177..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 42..50
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00177"
FT MOTIF 327..331
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00177"
FT COMPBIAS 177..194
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 582 AA; 63392 MW; 78752F71A694434A CRC64;
MPIVAQSTDT TDWVSRYADE VIAESERRAP GKPVVVASGL SPSGPIHLGN LREVMTPHLV
ADEIRRRGHQ VRHLISWDDY DRYRKVPAGV PGVDESWAEH IGRPLTSVPA PAGSAYPNWA
EHFKAAMAAS LADLGVEFDG ISQTEQYTSG AYREQILHAM RHRADIDAIL DQYRTKKDPA
KGKKQQKPAD EAELEAAEGS GAASEDDGSG GTGGYFPYKP YCGGCGKDLT TVTSYDDDST
ELAYVCTACG FEETVRLSEF NRGKLVWKVD WPMRWAYEGV IFEPSGVDHS SPGSSFVVGG
QIVRQIFDGV QPIGPMYAFV GISGMAKMSS SRGGVPTPAD ALKIMEAPLL RWLYARRRPN
QSFKIAFDQE IQRLYDEWDK LAAKVADGSV LPADAAAYTR AVGTAAGPLP TTPHPLPYRT
LASVADITAG AEDQTLRILS DLDPADPLAS LDEARPRLDK AEAWINTHVP ADQRTVVRDE
PDKELLGSLD EEGRESLRLL LDGLDSHWSL DGLTHLVYGV PKVRAGFAAD AGPKELPPEI
KTAQRTFFAL LYHLLVSRDT GPRLPTLLLA VGADRVRKLL GA
//
