SPM_001920
  | Uniprot: A0A037UQK8
Description: NAD-dependent DNA ligase LigA EC number: 6.5.1.2 Annotation score: 3 out of 5 Miscellaneous [CC]: Protein existence: Inferred from homology Catalytic activity: CATALYTIC ACTIVITY: NAD(+) + (deoxyribonucleotide)(n) + (deoxyribonucleotide)(m) = AMP + beta-nicotinamide D-ribonucleotide + (deoxyribonucleotide)(n+m). {ECO:0000256|HAMAP-Rule:MF_01588, ECO:0000256|SAAS:SAAS00572200}. Cofactor: COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-Rule:MF_01588}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000256|HAMAP-Rule:MF_01588}; ; COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000256|SAAS:SAAS00611843}; Enzyme regulation: Function [CC]: FUNCTION: DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA. {ECO:0000256|HAMAP-Rule:MF_01588, ECO:0000256|SAAS:SAAS00572229}. Pathway: Active site: ACT_SITE 116 116 N6-AMP-lysine intermediate. {ECO:0000256|HAMAP-Rule:MF_01588}. Binding site: BINDING 114 114 NAD. {ECO:0000256|HAMAP-Rule:MF_01588}.; BINDING 137 137 NAD. {ECO:0000256|HAMAP-Rule:MF_01588}.; BINDING 170 170 NAD. {ECO:0000256|HAMAP-Rule:MF_01588}.; BINDING 286 286 NAD. {ECO:0000256|HAMAP-Rule:MF_01588}.; BINDING 310 310 NAD. {ECO:0000256|HAMAP-Rule:MF_01588}. Calcium binding: DNA binding: Metal binding: METAL 404 404 Zinc. {ECO:0000256|HAMAP-Rule:MF_01588}.; METAL 407 407 Zinc. {ECO:0000256|HAMAP-Rule:MF_01588}.; METAL 422 422 Zinc. {ECO:0000256|HAMAP-Rule:MF_01588}.; METAL 427 427 Zinc. {ECO:0000256|HAMAP-Rule:MF_01588}. Nucleotide binding: NP_BIND 34 38 NAD. {ECO:0000256|HAMAP-Rule:MF_01588}.; NP_BIND 83 84 NAD. {ECO:0000256|HAMAP-Rule:MF_01588}. Site: Gene names (primary): ligA Gene names (synonym): Mass: 76,324 Subunit structure [CC]: Gene ontology (GO): DNA binding [GO:0003677]; DNA ligase (NAD+) activity [GO:0003911]; metal ion binding [GO:0046872]; DNA repair [GO:0006281]; DNA replication [GO:0006260] Gene ontology IDs: GO:0003677; GO:0003911; GO:0006260; GO:0006281; GO:0046872 Chain: Signal peptide: Domain [CC]: Sequence similarities: SIMILARITY: Belongs to the NAD-dependent DNA ligase family. LigA subfamily. {ECO:0000256|HAMAP-Rule:MF_01588, ECO:0000256|SAAS:SAAS00572184}.; SIMILARITY: Contains 1 BRCT domain. {ECO:0000256|HAMAP-Rule:MF_01588}. Protein families: NAD-dependent DNA ligase family, LigA subfamily Coiled coil: Domain [FT]: DOMAIN 588 667 BRCT. {ECO:0000259|PROSITE:PS50172}. Motif: Region: EMBL: AGBZ02000001 ProteinModelPortal: MEROPS: EnsemblBacteria KO: KAI92791 UniPathway: CDD: Gene3D: HAMAP: 2.40.50.140;3.40.50.10190 InterPro: MF_01588 PANTHER: IPR001357;IPR001679;IPR013839;IPR013840;IPR003583;IPR012340;IPR004150;IPR010994;IPR004149 PIRSF: PRINTS: PIRSF001604 PROSITE: Pfam: PS50172 ProDom: PF00533;PF01653;PF03120;PF03119 SMART: SUPFAM: SM00292;SM00278;SM00532 TIGRFAMs: SSF47781;SSF50249;SSF52113 |
349730-351734(-) >nucleotide sequence TTTTTGTGCTTTTACTAATTTATTACCAGCATCAGTTCCCGCCAGTAAATAAGTGGTTTT TGCACTAACACTTTCAGAAACTTGTCCACCATAACTTTCAATTAATTCTTTAAAGTATTC TCGTGATTTTGATAAGACTCCAGTAATCACAAACCGATAATTTTCAAACTTCTGTGCTAA ATGCTGATTAGTAGCAAAATACTCCATTTTAACCCCATTTTGGCGTAATAAAGCCAGTTC TTGTTGGTTAGCTGGAATTGCAAAATAATCCACAACACTAGCTGCTACAATTGGACCAAT ATCATTAATAATTGATAATTGTTCAATATTCATAGCAGCTAAATTATCAATTGTTTTAAA TTGTCGTGCTAATAATTTTGCTGTTTTTTGACCAACATGACGAATTCCTAACGCAAATAA TAGTCGTTCTAAGGAATTATTTTTTGAATTATTAATTGAAGTAATCATATTTTCAAACGA TTTTTCACCAAAATTTTCTAATTCAATAATTTCAGCGCGGTATTGTTCTAATTGATATAA ATCACTAAAACTTTTTAAATATTCTAATTTAAATAATCGTTCAATAATTTTTTCACTAAT TCCTTCAATATTCATCGCATTTCGTGAACAATAATGTTCTAATCCACGTGTAATTTTTTT GGGACAAACAGAATTAATGCAATACTGGTCAACCTCCCCTTCAACACGTTCTAATAAAGA ATTACATTCTGGGCAATGCGTTGCTTCTTGTCACTTCTGAGCATTTTTTTGGCGACGAGC TGCAACATAATTAATTACTTCTGGAATAATATCTCCCGCTTTTTTAACTTGGACATTATC ACCAATCCGAATATCACGTTCAGTAATAAAATCAGCATTATGTAATGTTGCAGCTCGTAC GATTGTTCCTGCAATACGAATTGGTTCAAGAACAGCATTATAAGTAATGCGCCCCGTTCT CCCAACGGAAGGAAAAATATTAAGCAATTTAGTAACCACAACTTCCGCTGGAAATTTATA AGCGATTGCTCATTTTGGATTTTTAGCAGTATAACCAATACGATTATATAAATTTAAGTT ATTAACTTTAATCACAATTCCATCAATTTCATAACCTAACTGATGACGTTTTGGCTCATA TTCTTGAATATATGCTCACACTGCCGCAATATTTGAGCAATAACGATATTCAGGATTTGT TTTAAATTTCAATTGTTCTAATCTTTGTAATGCTTCGTATTGTGATTGAATCCCATCCTG TAAAGCATTAACATAATAATATAAAAATGCATTTAACTTTCGTTTTGCAACAATTGTTGA ATCTAATTGACGTAAAGTGCCTGCTGCTGCATTTCGAGGATTAGCAAATTCAGATTCACC ATTTTTAACACGTTCTTCATTAATCTTATTAAACTCTTCAACTGATAAATAAACTTCTCC CCGAACAATTAAAGTTGGTTGGTCAATTCGAAGGGGAATTGATTTAATTTGTTTAATATT AATAGTAACATCTTCACCGGTAAGACCATCGCCCCGAGTTGCCCCCATCACTAAAAGATG ATTATCATAAACTAATGAAATTGATAATCCATCAATTTTTAATTCACAAGTATATTCAAT TTCTGGCAAACCAGTTAATTCTTTAATTTGCTCATCAAAATGAATTAAATCATCATAATT AAACGCGTTTCCTAAACTTAGCATTGGACTTGTATGAACATATTTATTAAACTTTTCACT AATTTGGCCAGAAACACGTTGCGTTGGTGAATCAATTGTAATTAATTCACTATATTGCTG TTCAATTGCAATTAATTCTTGCATTGCTCGATCATATTCTTGGTCACTAACACTAGGGTT ATCATTAACATAATATTCATAATTTCATTTTTCTAATTGTTCTTTTAACACTAAACTACG TTTTTTTGCTTGCTCAAAAGTCAT >protein sequence TQRVSGQISEKFNKYVHTSPMLSLGNAFNYDDLIHFDEQIKELTGLPEIEYTCELKIDGL SISLVYDNHLLVMGATRGDGLTGEDVTINIKQIKSIPLRIDQPTLIVRGEVYLSVEEFNK INEERVKNGESEFANPRNAAAGTLRQLDSTIVAKRKLNAFLYYYVNALQDGIQSQYEALQ RLEQLKFKTNPEYRYCSNIAAVWAYIQEYEPKRHQLGYEIDGIVIKVNNLNLYNRIGYTA KNPKWAIAYKFPAEVVVTKLLNIFPSVGRTGRITYNAVLEPIRIAGTIVRAATLHNADFI TERDIRIGDNVQVKKAGDIIPEVINYVAARRQKNAQKWQEATHCPECNSLLERVEGEVDQ YCINSVCPKKITRGLEHYCSRNAMNIEGISEKIIERLFKLEYLKSFSDLYQLEQYRAEII ELENFGEKSFENMITSINNSKNNSLERLLFALGIRHVGQKTAKLLARQFKTIDNLAAMNI EQLSIINDIGPIVAASVVDYFAIPANQQELALLRQNGVKMEYFATNQHLAQKFENYRFVI TGVLSKSREYFKELIESYGGQVSESVSAKTTYLLAGTDAGNKLVKAQKLNVKIINEEEFQ QLLNKED |
© Fisunov Lab of Proteomics, 2016.