ID A0A0K0CUE4_ANGCA Unreviewed; 712 AA. AC A0A0K0CUE4; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 22-FEB-2023, entry version 29. DE RecName: Full=DNA topoisomerase I {ECO:0000256|RuleBase:RU365101}; DE EC=5.6.2.1 {ECO:0000256|RuleBase:RU365101}; DE AltName: Full=DNA topoisomerase 1 {ECO:0000256|RuleBase:RU365101}; OS Angiostrongylus cantonensis (Rat lungworm). OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Strongylida; OC Metastrongyloidea; Angiostrongylidae; Angiostrongylus. OX NCBI_TaxID=6313 {ECO:0000313|Proteomes:UP000035642, ECO:0000313|WBParaSite:ACAC_0000083001-mRNA-1}; RN [1] {ECO:0000313|Proteomes:UP000035642} RP NUCLEOTIDE SEQUENCE. RA Martin A.A.; RL Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|WBParaSite:ACAC_0000083001-mRNA-1} RP IDENTIFICATION. RG WormBaseParasite; RL Submitted (FEB-2017) to UniProtKB. CC -!- FUNCTION: Releases the supercoiling and torsional tension of DNA CC introduced during the DNA replication and transcription by transiently CC cleaving and rejoining one strand of the DNA duplex. Introduces a CC single-strand break via transesterification at the specific target site CC 5'-[CT]CCTTp site in duplex DNA. The scissile phosphodiester is CC attacked by the catalytic tyrosine of the enzyme, resulting in the CC formation of a DNA-(3'-phosphotyrosyl)-enzyme intermediate and the CC expulsion of a 5'-OH DNA strand. The free DNA strand then undergoes CC passage around the unbroken strand thus removing DNA supercoils. CC Finally, in the religation step, the DNA 5'-OH attacks the covalent CC intermediate to expel the active-site tyrosine and restore the DNA CC phosphodiester backbone. {ECO:0000256|RuleBase:RU365101}. 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:RU365101}; CC -!- SIMILARITY: Belongs to the type IB topoisomerase family. CC {ECO:0000256|ARBA:ARBA00006645, ECO:0000256|RuleBase:RU365101}. 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 AlphaFoldDB; A0A0K0CUE4; -. DR STRING; 6313.A0A0K0CUE4; -. DR WBParaSite; ACAC_0000083001-mRNA-1; ACAC_0000083001-mRNA-1; ACAC_0000083001. DR Proteomes; UP000035642; Unassembled WGS sequence. DR GO; GO:0005694; C:chromosome; IEA:InterPro. DR GO; GO:0005634; C:nucleus; IEA:UniProt. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule. DR GO; GO:0003917; F:DNA topoisomerase type I (single strand cut, ATP-independent) activity; IEA:UniProtKB-UniRule. DR GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-UniRule. DR CDD; cd00659; Topo_IB_C; 1. DR CDD; cd03488; Topoisomer_IB_N_htopoI_like; 1. DR Gene3D; 1.10.132.10; -; 1. DR Gene3D; 2.170.11.10; DNA Topoisomerase I, domain 2; 1. DR Gene3D; 1.10.10.41; Yeast DNA topoisomerase - domain 1; 1. DR InterPro; IPR011010; DNA_brk_join_enz. DR InterPro; IPR013034; DNA_topo_DNA_db_N_dom1. DR InterPro; IPR013030; DNA_topo_DNA_db_N_dom2. DR InterPro; IPR001631; TopoI. DR InterPro; IPR018521; TopoI_AS. DR InterPro; IPR025834; TopoI_C_dom. DR InterPro; IPR014711; TopoI_cat_a-hlx-sub_euk. DR InterPro; IPR014727; TopoI_cat_a/b-sub_euk. DR InterPro; IPR013500; TopoI_cat_euk. DR InterPro; IPR008336; TopoI_DNA-bd_euk. DR InterPro; IPR036202; TopoI_DNA-bd_euk_N_sf. DR InterPro; IPR013499; TopoI_euk. DR PANTHER; PTHR10290:SF3; DNA TOPOISOMERASE 1; 1. DR PANTHER; PTHR10290; DNA TOPOISOMERASE I; 1. DR Pfam; PF14370; Topo_C_assoc; 1. DR Pfam; PF01028; Topoisom_I; 1. DR Pfam; PF02919; Topoisom_I_N; 1. DR PRINTS; PR00416; EUTPISMRASEI. DR SMART; SM00435; TOPEUc; 1. DR SUPFAM; SSF56349; DNA breaking-rejoining enzymes; 1. DR SUPFAM; SSF46596; Eukaryotic DNA topoisomerase I, dispensable insert domain; 1. DR SUPFAM; SSF56741; Eukaryotic DNA topoisomerase I, N-terminal DNA-binding fragment; 1. DR PROSITE; PS00176; TOPOISOMERASE_I_EUK; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU365101}; KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|RuleBase:RU365101}; KW Reference proteome {ECO:0000313|Proteomes:UP000035642}; KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, KW ECO:0000256|RuleBase:RU365101}. FT DOMAIN 344..681 FT /note="DNA topoisomerase I eukaryotic-type" FT /evidence="ECO:0000259|SMART:SM00435" FT REGION 15..178 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 595..648 FT /evidence="ECO:0000256|SAM:Coils" FT COMPBIAS 24..71 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 78..178 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 712 AA; 83296 MW; 478BA85369238EAE CRC64; MAPELSSFEA ALAAAAAGVN HRKKENAPPV KKEVYSDDDD IPWAERMAKE KKEKSIEKKK KKRKGSDSED EYRPEVLDED EIPWAERLKR DSISSSPKKK RKIEVDSDYE EKNVDKEKWT KKEDSGSNCV YTESRKDKRK KKKDKEARER NSSSSSLKKT PKKEVKNEEG EIPQKKKKKQ EEVEDVWEWW KEEKKPAGVK WNSLHHKGPL FAPPYERLPD HVNFKYDGKV VQLSDEAEEV ATFYAKMLNH DYTTKDAFNK NFFHDWRKVM SPAERELITD LKKCDFREMT VHFEKQSEIR KAMSKEEKAK IKEAKEAEAK IYGFAFIDGH KQKIGNFRIE PPGLFRGRGG HPKMGMDSEI PVPPDGHKWK EVRHDNTVTW LVSWTENVLG QNKYIMLNPS SKIKGEKDYE KYETARRLKS RIDDIRAVYT ADWKSKEMRL ALRAGNEKDV DEAADTVGCC SLRCEHIKLY EKLDDKEYVV EFDFLGKDSI RYFNQVPVEK RVFKNLQLFM DNKDPSDDLF DRLDTASLNE HLRSLMDGLT VKVFRTYNAS ITLQQQLAKL TKADDNVHQK MLSYNRANRM VAILCNHQRA VPKGHEKAME NLEQKIKDKK RELKEAKAEL EKAKGSAKEK AQKKVTRLKE QLKKLKISRT DRDENKQIAL STSKLNYLDP RISVAWCKKF DVPVEKVFNR TLREKFRWAI DMTMSSDEEF VF //