Tag | Content |
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CPLM ID | CPLM-004218 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | DNA topoisomerase 3 |
Protein Synonyms/Alias | DNA topoisomerase III |
Gene Name | topB |
Gene Synonyms/Alias | b1763; JW1752 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
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282 | IVTSYNDKRESESAP | acetylation | [1] | 303 | ALQIEAAKRFGLSAQ | acetylation | [1] |
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Reference | [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli. Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C. Mol Cell. 2013 Jul 25;51(2):265-72. [ PMID: 23830618] |
Functional Description | 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. TOP3 is a potent decatenase. |
Sequence Annotation | DOMAIN 1 134 Toprim. REGION 194 199 Interaction with DNA. ACT_SITE 328 328 O-(5'-phospho-DNA)-tyrosine intermediate. METAL 7 7 Magnesium 1; catalytic (By similarity). METAL 103 103 Magnesium 1; catalytic (By similarity). METAL 103 103 Magnesium 2 (By similarity). METAL 105 105 Magnesium 2 (By similarity). |
Keyword | 3D-structure; ATP-binding; Complete proteome; Direct protein sequencing; DNA-binding; Isomerase; Magnesium; Metal-binding; Nucleotide-binding; Reference proteome; Topoisomerase. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 653 AA |
Protein Sequence | MRLFIAEKPS LARAIADVLP KPHRKGDGFI ECGNGQVVTW CIGHLLEQAQ PDAYDSRYAR 60 WNLADLPIVP EKWQLQPRPS VTKQLNVIKR FLHEASEIVH AGDPDREGQL LVDEVLDYLQ 120 LAPEKRQQVQ RCLINDLNPQ AVERAIDRLR SNSEFVPLCV SALARARADW LYGINMTRAY 180 TILGRNAGYQ GVLSVGRVQT PVLGLVVRRD EEIENFVAKD FFEVKAHIVT PADERFTAIW 240 QPSEACEPYQ DEEGRLLHRP LAEHVVNRIS GQPAIVTSYN DKRESESAPL PFSLSALQIE 300 AAKRFGLSAQ NVLDICQKLY ETHKLITYPR SDCRYLPEEH FAGRHAVMNA ISVHAPDLLP 360 QPVVDPDIRN RCWDDKKVDA HHAIIPTARS SAINLTENEA KVYNLIARQY LMQFCPDAVF 420 RKCVIELDIA KGKFVAKARF LAEAGWRTLL GSKERDEEND GTPLPVVAKG DELLCEKGEV 480 VERQTQPPRH FTDATLLSAM TGIARFVQDK DLKKILRATD GLGTEATRAG IIELLFKRGF 540 LTKKGRYIHS TDAGKALFHS LPEMATRPDM TAHWESVLTQ ISEKQCRYQD FMQPLVGTLY 600 QLIDQAKRTP VRQFRGIVAP GSGGSADKKK AAPRKRSAKK SPPADEVGSG AIA 653 |
Gene Ontology | GO:0005694; C:chromosome; IEA:InterPro. GO:0005524; F:ATP binding; IEA:UniProtKB-KW. GO:0003917; F:DNA topoisomerase type I activity; IDA:EcoliWiki. GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. GO:0051304; P:chromosome separation; IMP:EcoliWiki. GO:0006310; P:DNA recombination; IMP:EcoliWiki. GO:0006265; P:DNA topological change; IEA:InterPro. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |