GCW_00410
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Uniprot: A0A0F6CJX8
Description: lysyl-tRNA synthetase EC number: 6.1.1.6 Annotation score: 2 out of 5 Miscellaneous [CC]: Protein existence: Inferred from homology Catalytic activity: CATALYTIC ACTIVITY: ATP + L-lysine + tRNA(Lys) = AMP + diphosphate + L-lysyl-tRNA(Lys). {ECO:0000256|HAMAP-Rule:MF_00252, ECO:0000256|RuleBase:RU000336, ECO:0000256|SAAS:SAAS00105435}. Cofactor: COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-Rule:MF_00252, ECO:0000256|RuleBase:RU000336}; ; Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000256|HAMAP-Rule:MF_00252, ECO:0000256|RuleBase:RU000336} Enzyme regulation: Function [CC]: Pathway: Active site: Binding site: Calcium binding: DNA binding: Metal binding: METAL 403 403 Magnesium 1. {ECO:0000256|HAMAP-Rule:MF_00252}.; METAL 410 410 Magnesium 1. {ECO:0000256|HAMAP-Rule:MF_00252}.; METAL 410 410 Magnesium 2. {ECO:0000256|HAMAP-Rule:MF_00252}. Nucleotide binding: Site: Gene names (primary): lysS Gene names (synonym): Mass: 57,343 Subunit structure [CC]: SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00252}. Gene ontology (GO): cytoplasm [GO:0005737]; ATP binding [GO:0005524]; lysine-tRNA ligase activity [GO:0004824]; magnesium ion binding [GO:0000287]; nucleic acid binding [GO:0003676]; lysyl-tRNA aminoacylation [GO:0006430] Gene ontology IDs: GO:0000287; GO:0003676; GO:0004824; GO:0005524; GO:0005737; GO:0006430 Chain: Signal peptide: Domain [CC]: Sequence similarities: SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family. {ECO:0000256|HAMAP-Rule:MF_00252, ECO:0000256|SAAS:SAAS00546954}. Protein families: Class-II aminoacyl-tRNA synthetase family Coiled coil: Domain [FT]: DOMAIN 173 487 AA_TRNA_LIGASE_II. {ECO:0000259|PROSITE:PS50862}. Motif: Region: EMBL: CP006916 ProteinModelPortal: MEROPS: EnsemblBacteria KO: AHB99400 UniPathway: K04567 CDD: Gene3D: cd00775 HAMAP: 2.40.50.140 InterPro: MF_00252 PANTHER: IPR004364;IPR018150;IPR006195;IPR002313;IPR018149;IPR012340;IPR004365 PIRSF: PTHR22594 PRINTS: PROSITE: PR00982 Pfam: PS50862 ProDom: PF00152;PF01336 SMART: SUPFAM: TIGRFAMs: SSF50249 88385-89864(+) >nucleotide sequence GAATCTAAACAAAACCCATACGAGGTTACAAAAGTTGCTAACACTCACAACACAAAAAGC TTAAAAGAAAAATACGACCAATTTTCTAAAGAACAGTTAGCAGAGATGCAACTGGATAAG CCAATTACTGTTAGTGGGCGTGTAATCTTGATTAGAAGAACATTTATTCTAATTCAAGAT TTTCATTCAGAATTACAACTATATATAAATAAAAATAAACAACCTGATCTGTTTAAGTAT TTCAATGACTATTTAGATTTAGGTGATGTCGTTTGTGCTACTGGTAAACCAATGAAAACC AATACTAATGAACTTTCATTAGATCTGGAATCATTAAAGATTATCAGTAAATCTTTAAGA GTACCACCTGAAAAATTCCACGGGATCGCTGATGAAGAGATCCGTTCACGAAAACGTTAT TTAGACCTAGTTTATAATAAGGAATCAAAAGAAAGATTCGTTTATCGTTCAAAGATTATT GCAGCAATGCGCCAATATTTTAATGAAAACGGTTTTTTAGAAGTAGAAACACCATTTTTA CATGCCCAGATCGGAGGAGCTGCTGCTAAGCCTTTTATAACAAGATATAATGCACTTGAT CGTGATTATTATTTAAGAATTGCTCCTGAATTACCTCTTAAAAAACTTATCGTTGGAAGT TTTGAAAAGATATATGAGATCGGTAAGTGTTTTAGAAACGAAGGGATGGATTCAACTCAC AACCCTGAATTTACCAGTGTTGAAACTTACGTAGCTTATGTTGATTATATCTACATGATG GAACTAACCGAGGCTCTAATTAAGTATATTGCCAAAACAATTGGTATTAGTCACACTAAT ATCAAGAATGAAACGGTTGATTGGAATAAACCATTCAAACGAATTAAGATGACTGAATTA GTTAAACAAGAAACTGGGATCGATTTTACGCAAGTAAAAAAATTAGATGAAGCGTTAGAT TTAGCTAAAAAACATAAGGTTCATGTTAAAGAACATGAAAAGACAATAGGTCATATTATC AATTTATTTTTCGAGGAATTTTGCGAGAAAAAATTGGTTGAACCAACGTTTGTAACTCAC CATCCAGTAGAGATCTCACCGTTATCAAAATTAGATTATTCAGATCCAAGATATACTGAA AGATTCGAACTATTTGCGTTTGGTAAAGAATTATCTAACGGGTTTAGCGAATTAAACGAT CCAATCGATCAAAGACAACGATTTGAAAAGCAATTAGAAGAAAAACAAAAGGGTAATGAT GAAGCTTCTGAAATGGATGAAGATTTCCTAGAAGCTCTAGAAAATGGCCTGCCACCAACT GGTGGTTTGGGCATTGGAGTAGACCGTTTAGTGATGATGTTAACAGGCACAACATCAATC AGAGATATCTTGTTTTTTCCGCACGTACGTGAAGAATAA >protein sequence PITVSGRVILIRRTFILIQDFHSELQLYINKNKQPDLFKYFNDYLDLGDVVCATGKPMKT NTNELSLDLESLKIISKSLRVPPEKFHGIADEEIRSRKRYLDLVYNKESKERFVYRSKII AAMRQYFNENGFLEVETPFLHAQIGGAAAKPFITRYNALDRDYYLRIAPELPLKKLIVGS FEKIYEIGKCFRNEGMDSTHNPEFTSVETYVAYVDYIYMMELTEALIKYIAKTIGISHTN IKNETVDWNKPFKRIKMTELVKQETGIDFTQVKKLDEALDLAKKHKVHVKEHEKTIGHII NLFFEEFCEKKLVEPTFVTHHPVEISPLSKLDYSDPRYTERFELFAFGKELSNGFSELND PIDQRQRFEKQLEEKQKGNDEASEMDEDFLEALENGLPPTGGLGIGVDRLVMMLTGTTSI RDILFFPHVREE |
© Fisunov Lab of Proteomics, 2016.