ACL_RS06670
  | Uniprot: A9NHW0
Description: DNA ligase (NAD(+)) 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:0000255|HAMAP-Rule:MF_01588}. Cofactor: COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_01588}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|HAMAP-Rule:MF_01588}; 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:0000255|HAMAP-Rule:MF_01588}. Pathway: Active site: ACT_SITE 111 111 N6-AMP-lysine intermediate. {ECO:0000255|HAMAP-Rule:MF_01588}. Binding site: BINDING 109 109 NAD. {ECO:0000255|HAMAP-Rule:MF_01588}.; BINDING 132 132 NAD. {ECO:0000255|HAMAP-Rule:MF_01588}.; BINDING 166 166 NAD. {ECO:0000255|HAMAP-Rule:MF_01588}.; BINDING 281 281 NAD. {ECO:0000255|HAMAP-Rule:MF_01588}.; BINDING 305 305 NAD. {ECO:0000255|HAMAP-Rule:MF_01588}. Calcium binding: DNA binding: Metal binding: METAL 398 398 Zinc. {ECO:0000255|HAMAP-Rule:MF_01588}.; METAL 401 401 Zinc. {ECO:0000255|HAMAP-Rule:MF_01588}.; METAL 416 416 Zinc. {ECO:0000255|HAMAP-Rule:MF_01588}.; METAL 421 421 Zinc. {ECO:0000255|HAMAP-Rule:MF_01588}. Nucleotide binding: NP_BIND 31 35 NAD. {ECO:0000255|HAMAP-Rule:MF_01588}.; NP_BIND 80 81 NAD. {ECO:0000255|HAMAP-Rule:MF_01588}. Site: Gene names (primary): ligA Gene names (synonym): Mass: 74,009 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: CHAIN 1 659 DNA ligase. /FTId=PRO_0000340321. Signal peptide: Domain [CC]: Sequence similarities: SIMILARITY: Belongs to the NAD-dependent DNA ligase family. LigA subfamily. {ECO:0000255|HAMAP-Rule:MF_01588}.; SIMILARITY: Contains 1 BRCT domain. {ECO:0000255|HAMAP-Rule:MF_01588}. Protein families: NAD-dependent DNA ligase family, LigA subfamily Coiled coil: Domain [FT]: DOMAIN 581 659 BRCT. {ECO:0000255|HAMAP-Rule:MF_01588}. Motif: Region: EMBL: CP000896 ProteinModelPortal: A9NHW0 MEROPS: EnsemblBacteria KO: ABX81940 UniPathway: K01972 CDD: Gene3D: HAMAP: 2.40.50.140;3.40.50.10190 InterPro: MF_01588 PANTHER: IPR001357;IPR018239;IPR033136;IPR001679;IPR013839;IPR013840;IPR003583;IPR012340;IPR004150;IPR010994;IPR004149 PIRSF: PRINTS: PIRSF001604 PROSITE: Pfam: PS50172;PS01055;PS01056 ProDom: PF00533;PF01653;PF03120;PF03119 SMART: SUPFAM: SM00292;SM00278;SM00532 TIGRFAMs: SSF47781;SSF50249;SSF52113 |
1407905-1409885(-) >nucleotide sequence TGCTTTGGTCAGTTTAGAACCAGCCTCTTTACCTGCTAAAACATAATCTGTCTTTTTAGA AACAGATCCACTAACCTTGCCACCTAATTTTTCAATGATATCACTTGCCTCAGTTCTTGA AAAATCATCTAACGTACCTGTAACAACAAATGTCTTACCATTAAATGGATGTGTTGTAAC AACATCTATTTTGTAAGTCATTTGTAGTCCTAAGTTTTTTAATTCTTCTAACATATGTTG GTTTGATTCATTAGAAAAATAAGTTGTTACACTATCTGCAATTTCTGGACCAATATCAGG TATTTGAATTAAATCCTCATACTTCGCATCAGCTAATAACGTGATGGATGGATAATGATT TAATAATGTTTTAGCTACTTTGGCACCTACATTCTTAATACCCAATCCAAAGATAAGTCT ATCTAAGGTTTGCATCTTAGATGCTTCAATGGCATTAAGCAGTTTTTCTACCTTCTTTTT ACCAAATCCAGGTAGTTCTTCTAATTGATCTTTAAAGGTATGTAATTTATAGATATCTGG TATGGTTTGAAGATAGGTTTGGTCATGTAAGAGTTCAACAACTTTTTCTCCTAATGTATC AATATCCATAGCAGCTCTACTTGCAAAATGAATAAGCCCAAATACATTTTTACCTGGACA ATTATCATTTGCACAATAATAGTCTGCTTCACCTTGTTTTCTAACTAAATTAGATTCACA GGCTGGACAATGTTTAACCATTTCAAATGGTGCTTGATTGGTTCTACTACCTAGTACAAC TTCAATCACCTCAGGTATAATTTCACCTGCTTTATGAACTAATACTTGATCATCAATTCG AATGTCTTTATTTAATATATAATCTTCGTTATGTAGTGTAGCTCTAGATACTAAAGAACC TGATATAAATACTGGTGTTAATACAGCCACCGGTGTAATTACACCAGTACGCCCTACTTG AAAGATAATATCTTCAACTTTAGTAATTTGTTTTTCAGCCTCAAACTTATATGCGCCTGC ATACTTAGGATATTTAGCCGTGTAACCAATCGTTTCATAATGTTCAAACTGATTGACTTT AATAACTACACCATCTGTATCATAAGGTAATGTTTTTCTTAAAATGTCATAGTTATCAAT AGCATCTGATAATGCATCTAAATTATCAACAAGTTTATAATGAGGATTTACTGGAAAACC TAGTTCTGATAAAAACTCTAAGGTTTCTTTTTGTGTGCTATTAAAATTACTTGCACCTAC TACAGTGTAGGTAAAGAGATCCAACCTTCTTTTAGCAACCACTTTAGAATCTAGTTGTCT GACTGTACCGGCTGCTGCATTTCTAGGATTTACAAATAAATCTAGATTGCTATTAGCACG TTCTAAATTCACTTCTTTAAATGTCTTATGAGACATATAAATTTCACCACGTACTTCAAT ATCTAAAGGTTTAGATAATTGTAGTGGTAAGGTTTTAATGGTCTTAACATTTTCAGTAAT ATCTTCACCCACCACACCATTACCACGAGTCGCTGCCTTTTTAAATATACCTTTTTCATA AATAAGCGTTACTGCTAAACCATCTATTTTAAGCTCTGTTGTAAAACTAGTGTTTGGTAT AACTTTTTGAATTCTATCATAAAAGACCTTTAACTCTTCTTTGTTAAAGATATTAGATAA ACTCATCATTGGTACCGTATGTGTATGCTTTTTAAAGGCATCTAAAACAACACCACCAAT TTTTTTAGTTGGAGATGTTTCATCATCATATTCTGGATATTTAGTTTCAAGTTCAATCAA TTCACGCATTAATCCATCATAGACAAAATCACTAATAATCGGTTGATCTTTTGTATGATA TAGGTAGTTTGCTTCATTGATTTGTTTTCTTAGCTCTTTGATTCTAGTCTGTATGTCCAT >protein sequence IGGVVLDAFKKHTHTVPMMSLSNIFNKEELKVFYDRIQKVIPNTSFTTELKIDGLAVTLI YEKGIFKKAATRGNGVVGEDITENVKTIKTLPLQLSKPLDIEVRGEIYMSHKTFKEVNLE RANSNLDLFVNPRNAAAGTVRQLDSKVVAKRRLDLFTYTVVGASNFNSTQKETLEFLSEL GFPVNPHYKLVDNLDALSDAIDNYDILRKTLPYDTDGVVIKVNQFEHYETIGYTAKYPKY AGAYKFEAEKQITKVEDIIFQVGRTGVITPVAVLTPVFISGSLVSRATLHNEDYILNKDI RIDDQVLVHKAGEIIPEVIEVVLGSRTNQAPFEMVKHCPACESNLVRKQGEADYYCANDN CPGKNVFGLIHFASRAAMDIDTLGEKVVELLHDQTYLQTIPDIYKLHTFKDQLEELPGFG KKKVEKLLNAIEASKMQTLDRLIFGLGIKNVGAKVAKTLLNHYPSITLLADAKYEDLIQI PDIGPEIADSVTTYFSNESNQHMLEELKNLGLQMTYKIDVVTTHPFNGKTFVVTGTLDDF SRTEASDIIEKLGGKVSGSVSKKTDYVLAGKEAGSKLTKALELGIEVMDEATFKVKINE |
© Fisunov Lab of Proteomics, 2016.