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Database: UniProt
Entry: A0A1X7JMJ6_9SPHI
LinkDB: A0A1X7JMJ6_9SPHI
Original site: A0A1X7JMJ6_9SPHI 
ID   A0A1X7JMJ6_9SPHI        Unreviewed;       568 AA.
AC   A0A1X7JMJ6;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=Lysine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00252};
DE            EC=6.1.1.6 {ECO:0000256|HAMAP-Rule:MF_00252};
DE   AltName: Full=Lysyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00252};
DE            Short=LysRS {ECO:0000256|HAMAP-Rule:MF_00252};
GN   Name=lysS {ECO:0000256|HAMAP-Rule:MF_00252};
GN   ORFNames=SAMN05660862_1929 {ECO:0000313|EMBL:SMG29438.1};
OS   Sphingobacterium psychroaquaticum.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Sphingobacterium.
OX   NCBI_TaxID=561061 {ECO:0000313|EMBL:SMG29438.1, ECO:0000313|Proteomes:UP000192980};
RN   [1] {ECO:0000313|EMBL:SMG29438.1, ECO:0000313|Proteomes:UP000192980}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22418 {ECO:0000313|EMBL:SMG29438.1,
RC   ECO:0000313|Proteomes:UP000192980};
RA   Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA   Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL   Submitted (APR-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_00252, ECO:0000256|RuleBase:RU000336};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00252,
CC         ECO:0000256|RuleBase:RU000336};
CC       Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000256|HAMAP-Rule:MF_00252,
CC       ECO:0000256|RuleBase:RU000336};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00252}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00252}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00252}.
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DR   EMBL; FXAU01000003; SMG29438.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X7JMJ6; -.
DR   STRING; 561061.SAMN05660862_1929; -.
DR   OrthoDB; 9801152at2; -.
DR   Proteomes; UP000192980; 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:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0006430; P:lysyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   CDD; cd00775; LysRS_core; 1.
DR   CDD; cd04322; LysRS_N; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   HAMAP; MF_00252; Lys_tRNA_synth_class2; 1.
DR   InterPro; IPR004364; Aa-tRNA-synt_II.
DR   InterPro; IPR006195; aa-tRNA-synth_II.
DR   InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR   InterPro; IPR002313; Lys-tRNA-ligase_II.
DR   InterPro; IPR044136; Lys-tRNA-ligase_II_N.
DR   InterPro; IPR018149; Lys-tRNA-synth_II_C.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR004365; NA-bd_OB_tRNA.
DR   NCBIfam; TIGR00499; lysS_bact; 1.
DR   PANTHER; PTHR42918:SF15; LYSINE--TRNA LIGASE, CHLOROPLASTIC/MITOCHONDRIAL; 1.
DR   PANTHER; PTHR42918; LYSYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF00152; tRNA-synt_2; 1.
DR   Pfam; PF01336; tRNA_anti-codon; 1.
DR   PRINTS; PR00982; TRNASYNTHLYS.
DR   SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW   ECO:0000256|HAMAP-Rule:MF_00252};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00252}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00252};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00252};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00252, ECO:0000256|RuleBase:RU000336};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_00252};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00252}; Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00252};
KW   Reference proteome {ECO:0000313|Proteomes:UP000192980}.
FT   DOMAIN          186..500
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
FT   BINDING         412
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00252"
FT   BINDING         419
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00252"
FT   BINDING         419
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00252"
SQ   SEQUENCE   568 AA;  64826 MW;  046F973EA84A67CB CRC64;
     MSTVLSEQEQ QRRLNLQAII DLGINPFPAD EFKVNVSAAD ILEHYERDKL NYKNIRFAGR
     IMGRRVMGSA SFMELQDSSG RIQAYVKRDD ICPGEDKTLY NTVFKKLLDI GDIVGVEGYV
     FTTQTGEISI HVEKLTLLTK SLRPLPVVKE AEGKTFDAFT DPEQRYRMRY VDLIVNPQNR
     DIFVKRTKLF NAMRDFFNSA GYMEVETPIL QSIPGGAAAR PFITHHNALD IPLYLRIANE
     LYLKRLIVGG FDGVYEFSKN FRNEGMDRTH NPEFTAMEIY VAYKDYNWMM EFTERLLEHC
     AVAVNGTTKA TFNEHHIDFK APFKRVTMAQ SIIDFTGFDI IGKSEDEIRE AAKGMGIAVN
     DTMGKGKLID EIFGAKCEGN YIQPTFITDY PIEMSPLTKK HRNNPELTER FELMVCGKEI
     ANAYSELNDP IDQRERFEHQ LQLSEKGDDE AMFIDQDFLR ALEYGMPPTS GLGIGMDRLI
     MFLTNNPSIQ EVLFFPQMRP EKKEVVIELT EEEKAVLALL GDEPKSLGEV KEATALSGKK
     WDIATKGLRQ KELIDIITEG DNKMIVKK
//
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