ID H7C4B0_HUMAN Unreviewed; 168 AA. AC H7C4B0; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 27-MAR-2024, entry version 67. DE RecName: Full=DNA topoisomerase {ECO:0000256|RuleBase:RU362092}; DE EC=5.6.2.1 {ECO:0000256|RuleBase:RU362092}; DE Flags: Fragment; GN Name=TOP3B {ECO:0000313|Ensembl:ENSP00000416451.1}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000416451.1, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Ensembl:ENSP00000416451.1, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=10591208; DOI=10.1038/990031; RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C., RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., RA Wright H.; RT "The DNA sequence of human chromosome 22."; RL Nature 402:489-495(1999). RN [2] {ECO:0000313|Ensembl:ENSP00000416451.1} RP IDENTIFICATION. RG Ensembl; RL Submitted (NOV-2023) to UniProtKB. CC -!- FUNCTION: Introduces a single-strand break via transesterification at a CC target site in duplex DNA. Releases the supercoiling and torsional CC tension of DNA introduced during the DNA replication and transcription CC by transiently cleaving and rejoining one strand of the DNA duplex. The CC scissile phosphodiester is attacked by the catalytic tyrosine of the CC enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme CC intermediate and the expulsion of a 3'-OH DNA strand. CC {ECO:0000256|RuleBase:RU362092}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP-independent breakage of single-stranded DNA, followed by CC passage and rejoining.; EC=5.6.2.1; CC Evidence={ECO:0000256|RuleBase:RU362092}; CC -!- SIMILARITY: Belongs to the type IA topoisomerase family. CC {ECO:0000256|RuleBase:RU362092}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AC245452; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR AlphaFoldDB; H7C4B0; -. DR SMR; H7C4B0; -. DR MassIVE; H7C4B0; -. DR MaxQB; H7C4B0; -. DR PeptideAtlas; H7C4B0; -. DR ProteomicsDB; 45612; -. DR Ensembl; ENST00000436282.1; ENSP00000416451.1; ENSG00000100038.20. DR UCSC; uc062cao.1; human. DR HGNC; HGNC:11993; TOP3B. DR VEuPathDB; HostDB:ENSG00000100038; -. DR GeneTree; ENSGT00940000156516; -. DR HOGENOM; CLU_1590189_0_0_1; -. DR ChiTaRS; TOP3B; human. DR Proteomes; UP000005640; Chromosome 22. DR Bgee; ENSG00000100038; Expressed in paraflocculus and 108 other cell types or tissues. DR ExpressionAtlas; H7C4B0; baseline and differential. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0003917; F:DNA topoisomerase type I (single strand cut, ATP-independent) activity; IEA:UniProtKB-EC. DR GO; GO:0006265; P:DNA topological change; IEA:InterPro. DR Gene3D; 2.70.20.10; Topoisomerase I, domain 3; 1. DR Gene3D; 1.10.290.10; Topoisomerase I, domain 4; 1. DR InterPro; IPR000380; Topo_IA. DR InterPro; IPR023406; Topo_IA_AS. DR InterPro; IPR013497; Topo_IA_cen. DR InterPro; IPR013825; Topo_IA_cen_sub2. DR InterPro; IPR013826; Topo_IA_cen_sub3. DR InterPro; IPR023405; Topo_IA_core_domain. DR InterPro; IPR003602; Topo_IA_DNA-bd_dom. DR PANTHER; PTHR11390:SF20; DNA TOPOISOMERASE 3-BETA-1; 1. DR PANTHER; PTHR11390; PROKARYOTIC DNA TOPOISOMERASE; 1. DR Pfam; PF01131; Topoisom_bac; 1. DR SMART; SM00437; TOP1Ac; 1. DR SUPFAM; SSF56712; Prokaryotic type I DNA topoisomerase; 1. DR PROSITE; PS00396; TOPOISOMERASE_I_PROK; 1. PE 1: Evidence at protein level; KW DNA-binding {ECO:0000256|RuleBase:RU362092}; KW Isomerase {ECO:0000256|RuleBase:RU362092}; KW Proteomics identification {ECO:0007829|EPD:H7C4B0, KW ECO:0007829|MaxQB:H7C4B0}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Topoisomerase {ECO:0000256|RuleBase:RU362092}. FT DOMAIN 21..168 FT /note="DNA topoisomerase type IA DNA-binding" FT /evidence="ECO:0000259|SMART:SM00437" FT NON_TER 1 FT /evidence="ECO:0000313|Ensembl:ENSP00000416451.1" SQ SEQUENCE 168 AA; 18658 MW; 22488C1D712B94FA CRC64; IAQMFLNMTK LEKEAQVEAT SRKEKAKQRP LALNTVEMLR VASSSLGMGP QHAMQTAERL YTQGYISYPR TETTHYPENF DLKGSLRQQA NHPYWADTVK RLLAEGINRP RKGHDAGDHP PITPMKSATE AELGFAVCPA QRLCKQELAA RARVLGAPHG QSPQLAPN //