(data stored in SCRATCH zone)

SWISSPROT: A4F6T3_SACEN

ID   A4F6T3_SACEN            Unreviewed;       507 AA.
AC   A4F6T3;
DT   17-APR-2007, integrated into UniProtKB/TrEMBL.
DT   17-APR-2007, sequence version 1.
DT   08-MAY-2019, entry version 99.
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   ECO:0000313|EMBL:CAL99757.1};
GN   OrderedLocusNames=SACE_0409 {ECO:0000313|EMBL:CAL99757.1};
OS   Saccharopolyspora erythraea (strain ATCC 11635 / DSM 40517 / JCM 4748
OS   / NBRC 13426 / NCIMB 8594 / NRRL 2338).
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Saccharopolyspora.
OX   NCBI_TaxID=405948 {ECO:0000313|EMBL:CAL99757.1, ECO:0000313|Proteomes:UP000006728};
RN   [1] {ECO:0000313|EMBL:CAL99757.1, ECO:0000313|Proteomes:UP000006728}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 /
RC   NRRL 2338 {ECO:0000313|Proteomes:UP000006728};
RX   PubMed=17369815; DOI=10.1038/nbt1297;
RA   Oliynyk M., Samborskyy M., Lester J.B., Mironenko T., Scott N.,
RA   Dickens S., Haydock S.F., Leadlay P.F.;
RT   "Complete genome sequence of the erythromycin-producing bacterium
RT   Saccharopolyspora erythraea NRRL23338.";
RL   Nat. Biotechnol. 25:447-453(2007).
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,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:78442, ChEBI:CHEBI:78529,
CC         ChEBI:CHEBI:456215; EC=6.1.1.6; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00252, ECO:0000256|RuleBase:RU000336,
CC         ECO:0000256|SAAS:SAAS01119930};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00252, ECO:0000256|RuleBase:RU000336};
CC       Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_00252, 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
CC       family. {ECO:0000256|HAMAP-Rule:MF_00252,
CC       ECO:0000256|SAAS:SAAS00675054}.
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DR   EMBL; AM420293; CAL99757.1; -; Genomic_DNA.
DR   RefSeq; WP_009946421.1; NZ_PDBV01000001.1.
DR   STRING; 405948.SACE_0409; -.
DR   EnsemblBacteria; CAL99757; CAL99757; SACE_0409.
DR   KEGG; sen:SACE_0409; -.
DR   eggNOG; ENOG4105CRK; Bacteria.
DR   eggNOG; COG1190; LUCA.
DR   HOGENOM; HOG000236578; -.
DR   KO; K04567; -.
DR   OMA; EIFGEKC; -.
DR   OrthoDB; 63621at2; -.
DR   BioCyc; SERY405948:SACE_RS02010-MONOMER; -.
DR   Proteomes; UP000006728; 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: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   HAMAP; MF_00252; Lys_tRNA_synth_class2; 1.
DR   InterPro; IPR004364; aa-tRNA-synt_II.
DR   InterPro; IPR006195; aa-tRNA-synth_II.
DR   InterPro; IPR002313; Lys-tRNA-ligase_II.
DR   InterPro; IPR018149; Lys-tRNA-synth_II_C.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR004365; NA-bd_OB_tRNA.
DR   Pfam; PF00152; tRNA-synt_2; 1.
DR   Pfam; PF01336; tRNA_anti-codon; 1.
DR   PRINTS; PR00982; TRNASYNTHLYS.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   TIGRFAMs; TIGR00499; lysS_bact; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE   3: Inferred from homology;
DR   PRODOM; A4F6T3.
DR   SWISS-2DPAGE; A4F6T3.
KW   Aminoacyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00252,
KW   ECO:0000256|SAAS:SAAS00222048, ECO:0000313|EMBL:CAL99757.1};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00252,
KW   ECO:0000256|SAAS:SAAS00675071};
KW   Complete proteome {ECO:0000313|Proteomes:UP000006728};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00252};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00252,
KW   ECO:0000256|SAAS:SAAS00675072, ECO:0000313|EMBL:CAL99757.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00252,
KW   ECO:0000256|RuleBase:RU000336};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00252,
KW   ECO:0000256|RuleBase:RU000336};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00252,
KW   ECO:0000256|SAAS:SAAS00675044};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00252,
KW   ECO:0000256|SAAS:SAAS00470543};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006728}.
FT   DOMAIN      189    506       AA_TRNA_LIGASE_II. {ECO:0000259|PROSITE:
FT                                PS50862}.
FT   METAL       419    419       Magnesium 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_00252}.
FT   METAL       426    426       Magnesium 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_00252}.
FT   METAL       426    426       Magnesium 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_00252}.
SQ   SEQUENCE   507 AA;  56533 MW;  87C2062424680518 CRC64;
     MTDQDRSIPT AADAEGVDDL PEQLRVRREK RERMLAGGVD PYPVNLPITH TLAEVRAAHP
     DLAPDTYTGD QVGVAGRVMF LRNTGKLCFA TLRGGDGTEL QAMLSLKQVG EDALASWKSD
     VDLGDHVFVH GEVITSRRGE LSVMADEWRL AAKTLRPLPV AHKELGDETR VRQRYVDLIV
     RKQAADTVRT RATVQRSLRD SFQRRGFIEV ETPMLQTLHG GAAARPFVTH SNAFDMELYL
     RIAPELYLKR CVVGGIEKVF EINRNFRNEG SDSSHSPEFA MLEFYQAYSD YDGMARLTRQ
     LVQEAAEALT GSQVVTWFDG TEYDLSGEWS SVTMYGSLSE ALDSEITPET PVEVLRKHAD
     SVGLQTDPAH GHGKLVEELW EHLVGDHLYA PTFVRDFPLE TAPLTRQHRS EPGVAEKWDL
     YTRGFELATG YSELVDPVVE RARLEEQARL AASGDEEAMH VDEDFLRALE YGMPPSGGVG
     MGIDRLLMAL TGLGIRETIL FPLVRPE
//

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