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
ATGTCAGACAAAGTAATTATTGTAGAATCACCTGCAAAATCAAAAACTATCTCAAGTTAT
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
MSDKVIIVESPAKSKTISSYFNDEVTVLSSVGHIRDLATSGKGGLGVDVDNNFEPTYKII
TGKGKLITDLKKKTKGKEVLIATDPDREGEAIAWHIADELGLDLNEHNRIVFKEITKPAV
MEAINHKRQIDLGLVNSQESRRILDRIIGFKLSAFLRDKIKSRSAGRVQSVALKLIVDLE
REIEKFVPETYFTMHAHFNDHVADYVIPKDTRIGLEEATKIVETSTNPFLVSDITQKETK
RNAKPPYMTSTLLQDGVNSLYMSSSRVMSVASELYQGIEINGQIIGLITYMKTDSNRLSK
EFVNPAKAFIETNYGKEYVGFYKTNNKDSSQDAHEAIRPTDIHLTPEKIEQYLSKDQFKL
YKRIYERAVGSLMAPAVFNNTKITLDSNGNIYTMDGSIQVFDGHLKVTGDKSKDKFLPEY
KIGDKLNADLVEKIEKQTQPPARFNEASLIKALEANGIGRPSTYASIIKTIKARDYVIVD
EKRFIPTEQGKLTVDTLNQYFNKIMKIDYTSNMESELDLIADGKVDHIQLLKDFYNKFMP
ILEAAQQNMEKIKPVVTDKICPLCGGNLVIRKSRYGEFYGCSNFPKCKHIEQMSE






















© Fisunov Lab of Proteomics, 2016.