ACL_RS01695
  | Uniprot: A9NF31
Description: DNA topoisomerase I EC number: 5.99.1.2 Annotation score: 3 out of 5 Miscellaneous [CC]: Protein existence: Inferred from homology Catalytic activity: CATALYTIC ACTIVITY: ATP-independent breakage of single-stranded DNA, followed by passage and rejoining. {ECO:0000256|HAMAP-Rule:MF_00952, ECO:0000256|SAAS:SAAS00046667}. Cofactor: COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-Rule:MF_00952}; ; Note=Binds two Mg(2+) per subunit. {ECO:0000256|HAMAP-Rule:MF_00952} Enzyme regulation: Function [CC]: FUNCTION: Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand, thus removing DNA supercoils. Finally, in the religation step, the DNA 3'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone. {ECO:0000256|HAMAP-Rule:MF_00952}. Pathway: Active site: ACT_SITE 290 290 O-(5'-phospho-DNA)-tyrosine intermediate. {ECO:0000256|HAMAP-Rule:MF_00952}. Binding site: Calcium binding: DNA binding: Metal binding: METAL 9 9 Magnesium 1; catalytic. {ECO:0000256|HAMAP-Rule:MF_00952}.; METAL 84 84 Magnesium 1; catalytic. {ECO:0000256|HAMAP-Rule:MF_00952}.; METAL 84 84 Magnesium 2. {ECO:0000256|HAMAP-Rule:MF_00952}.; METAL 86 86 Magnesium 2. {ECO:0000256|HAMAP-Rule:MF_00952}. Nucleotide binding: Site: SITE 33 33 Interaction with DNA. {ECO:0000256|HAMAP-Rule:MF_00952}.; SITE 141 141 Interaction with DNA. {ECO:0000256|HAMAP-Rule:MF_00952}.; SITE 142 142 Interaction with DNA. {ECO:0000256|HAMAP-Rule:MF_00952}.; SITE 145 145 Interaction with DNA. {ECO:0000256|HAMAP-Rule:MF_00952}.; SITE 474 474 Interaction with DNA. {ECO:0000256|HAMAP-Rule:MF_00952}. Gene names (primary): topA Gene names (synonym): Mass: 67,205 Subunit structure [CC]: SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00952, ECO:0000256|SAAS:SAAS00535586}. Gene ontology (GO): chromosome [GO:0005694]; DNA binding [GO:0003677]; DNA topoisomerase type I activity [GO:0003917]; magnesium ion binding [GO:0000287]; DNA topological change [GO:0006265] Gene ontology IDs: GO:0000287; GO:0003677; GO:0003917; GO:0005694; GO:0006265 Chain: Signal peptide: Domain [CC]: Sequence similarities: SIMILARITY: Belongs to the type IA topoisomerase family. {ECO:0000256|HAMAP-Rule:MF_00952, ECO:0000256|SAAS:SAAS00553561}.; SIMILARITY: Contains 1 Toprim domain. {ECO:0000256|HAMAP-Rule:MF_00952}. Protein families: Type IA topoisomerase family Coiled coil: Domain [FT]: DOMAIN 3 119 Toprim. {ECO:0000259|PROSITE:PS50880}. Motif: Region: REGION 164 169 Interaction with DNA. {ECO:0000256|HAMAP-Rule:MF_00952}. EMBL: CP000896 ProteinModelPortal: A9NF31 MEROPS: EnsemblBacteria KO: ABX80961 UniPathway: K03168 CDD: Gene3D: cd00186 HAMAP: 1.10.460.10;2.70.20.10;3.40.50.140 InterPro: MF_00952 PANTHER: IPR000380;IPR003601;IPR013497;IPR013824;IPR013825;IPR023405;IPR003602;IPR013498;IPR005733;IPR028612;IPR006171 PIRSF: PTHR11390 PRINTS: PROSITE: PR00417 Pfam: PS50880 ProDom: PF01131;PF01751;PF01396 SMART: SUPFAM: SM00437;SM00436;SM00493 TIGRFAMs: SSF56712 |
351024-352812(+) >nucleotide sequence TTCAACGATGAAGTAACTGTTTTATCATCGGTAGGTCATATTAGAGACCTAGCAACCTCT GGTAAGGGTGGTTTAGGTGTAGATGTAGATAACAATTTTGAACCTACCTATAAAATCATT ACTGGTAAAGGTAAACTGATTACTGATTTAAAGAAAAAAACAAAAGGTAAAGAAGTTTTA ATTGCAACCGACCCGGACCGCGAAGGAGAAGCTATCGCTTGGCATATCGCTGATGAGTTA GGTCTAGATTTAAACGAACATAACCGTATTGTTTTTAAAGAAATCACAAAACCTGCAGTT ATGGAAGCAATCAACCATAAACGTCAAATCGATTTAGGATTAGTCAACTCTCAAGAAAGT AGACGTATTTTAGACAGAATCATTGGTTTTAAACTATCTGCATTTTTAAGAGACAAAATT AAATCCAGATCAGCTGGTCGTGTTCAAAGTGTGGCTTTAAAACTAATTGTGGACTTAGAA CGTGAAATTGAAAAATTTGTGCCTGAAACATATTTCACCATGCATGCACATTTTAATGAC CATGTAGCAGATTATGTTATTCCAAAAGATACACGTATTGGATTAGAAGAAGCTACTAAA ATTGTTGAAACATCAACAAATCCATTTTTAGTAAGTGATATTACTCAAAAAGAAACAAAA AGAAACGCTAAACCACCTTACATGACATCTACCTTACTTCAAGATGGCGTAAACAGTCTA TATATGAGCTCTAGCCGTGTGATGTCAGTTGCATCTGAACTTTATCAAGGTATTGAAATC AATGGTCAAATTATCGGTTTAATCACGTATATGAAAACAGACTCTAATCGTTTATCTAAA GAGTTTGTAAATCCTGCAAAAGCATTCATTGAAACAAACTATGGAAAAGAATATGTTGGT TTTTATAAGACAAATAATAAAGACTCTAGTCAGGATGCCCACGAAGCAATCAGACCTACA GATATTCATTTAACACCAGAAAAAATAGAGCAATACTTATCAAAAGACCAATTTAAACTT TATAAGAGAATTTATGAACGTGCAGTAGGATCACTTATGGCACCTGCAGTATTTAACAAT ACTAAAATTACGCTAGATTCAAATGGCAATATTTATACAATGGATGGAAGTATTCAAGTA TTTGATGGTCACTTAAAAGTAACAGGTGATAAATCAAAAGATAAATTCTTACCTGAATAT AAAATTGGTGATAAACTAAATGCTGATTTAGTTGAAAAGATTGAAAAACAAACCCAACCA CCTGCTCGTTTTAATGAAGCATCACTCATTAAAGCATTAGAAGCAAACGGTATTGGTAGA CCATCTACATATGCAAGTATCATTAAAACGATTAAAGCACGCGACTATGTTATTGTAGAT GAAAAACGATTTATTCCAACAGAACAAGGAAAGCTGACAGTAGATACCTTGAATCAATAC TTTAATAAAATCATGAAAATTGATTATACATCTAATATGGAATCAGAACTTGACTTAATT GCAGATGGTAAAGTTGATCATATTCAATTATTGAAAGATTTTTACAATAAATTTATGCCG ATTTTAGAAGCTGCTCAACAAAATATGGAAAAAATAAAACCGGTTGTAACTGATAAAATA TGTCCACTGTGCGGTGGAAACCTAGTTATTAGAAAATCTAGATATGGTGAGTTCTATGGT TGCAGCAATTTTCCGAAGTGTAAACACATTGAACAGATGTCGGAATAA >protein sequence TGKGKLITDLKKKTKGKEVLIATDPDREGEAIAWHIADELGLDLNEHNRIVFKEITKPAV MEAINHKRQIDLGLVNSQESRRILDRIIGFKLSAFLRDKIKSRSAGRVQSVALKLIVDLE REIEKFVPETYFTMHAHFNDHVADYVIPKDTRIGLEEATKIVETSTNPFLVSDITQKETK RNAKPPYMTSTLLQDGVNSLYMSSSRVMSVASELYQGIEINGQIIGLITYMKTDSNRLSK EFVNPAKAFIETNYGKEYVGFYKTNNKDSSQDAHEAIRPTDIHLTPEKIEQYLSKDQFKL YKRIYERAVGSLMAPAVFNNTKITLDSNGNIYTMDGSIQVFDGHLKVTGDKSKDKFLPEY KIGDKLNADLVEKIEKQTQPPARFNEASLIKALEANGIGRPSTYASIIKTIKARDYVIVD EKRFIPTEQGKLTVDTLNQYFNKIMKIDYTSNMESELDLIADGKVDHIQLLKDFYNKFMP ILEAAQQNMEKIKPVVTDKICPLCGGNLVIRKSRYGEFYGCSNFPKCKHIEQMSE |
© Fisunov Lab of Proteomics, 2016.