GenomeNet

Database: UniProt
Entry: A0A1J4PVL5_9ACTN
LinkDB: A0A1J4PVL5_9ACTN
Original site: A0A1J4PVL5_9ACTN 
ID   A0A1J4PVL5_9ACTN        Unreviewed;       579 AA.
AC   A0A1J4PVL5;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 42.
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=VT52_024690 {ECO:0000313|EMBL:OIK24801.1};
OS   Streptomyces malaysiense.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1428626 {ECO:0000313|EMBL:OIK24801.1, ECO:0000313|Proteomes:UP000034838};
RN   [1] {ECO:0000313|Proteomes:UP000034838}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MUSC136T {ECO:0000313|Proteomes:UP000034838};
RA   Lee L.H., Chan K.-G.;
RT   "Genome sequencing of Streptomyces sp. MUSC136T.";
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:OIK24801.1, ECO:0000313|Proteomes:UP000034838}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MUSC136T {ECO:0000313|Proteomes:UP000034838};
RA   Lee L.-H., Ser H.-L.;
RT   "Genome sequence of Streptomyces malaysiense MUSC 136.";
RL   Submitted (OCT-2016) 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}.
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:OIK24801.1}.
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; LBDA02000057; OIK24801.1; -; Genomic_DNA.
DR   RefSeq; WP_046417269.1; NZ_LBDA02000057.1.
DR   AlphaFoldDB; A0A1J4PVL5; -.
DR   OrthoDB; 9803151at2; -.
DR   Proteomes; UP000034838; 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   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:UP000034838}.
FT   REGION          180..206
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           324..328
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00177"
SQ   SEQUENCE   579 AA;  63537 MW;  9711BD7CE86427BD CRC64;
     MPIVAQSTET TDWVSRFADE VIEESERRAP GKPVVVASGL SPSGPIHLGN LREVMTPHLV
     ADEIRRRGHQ VRHLISWDDY DRYRKVPAGI AGVDESWAEH IGKPLTSVPA PKGSAYPNWA
     EHFKAAMVRS LAEMGVEFDG ISQTAQYTSG VYREQVLHAM KHRGDIDAIL AQYRTRPKVK
     KQQQKAVDEA ELEAEEGSGA AAEDDGSAGG AGYFPYKPYC GGCAKDLTTV TSYDDDTTEL
     SYVCGECGFK ETVRLSEFNR GKLVWKVDWP MRWAYEGVVF EPSGVDHSSP GSSFQVGGQI
     VGIFGGEQPI GPMYAFVGIS GMAKMSSSRG GVPTPGDALK IMEPQLLRWL YARRRPNQSF
     KIAFDQEIQR LYDEWDKLAA KVADGSALPG DVAAYTRAVG TAAAELPKTP RPLPYRTLAS
     VADITAGHED QALRILSELD PRSPLSSLDQ ARPRYDKAEA WINTHVPADQ RTIVRAEPDA
     ELLKSLDEAS QRSVRLLLDG LAEHWSLDGL THLVYGVPKV QAGFSADATP KELPPEIKTA
     QRMFFALLYQ LLVGRDTGPR LPTLLLAVGQ ERVRALLGE
//
DBGET integrated database retrieval system