ID A0A0K0CUE4_ANGCA Unreviewed; 712 AA. AC A0A0K0CUE4; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 08-MAY-2019, entry version 16. DE RecName: Full=DNA topoisomerase I {ECO:0000256|RuleBase:RU365101}; DE EC=5.6.2.2 {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, ECO:0000313|WBParaSite:ACAC_0000083001-mRNA-1} 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 CC transiently cleaving and rejoining one strand of the DNA duplex. CC Introduces a single-strand break via transesterification at the CC specific target site 5'-[CT]CCTTp site in duplex DNA. The scissile CC phosphodiester is attacked by the catalytic tyrosine of the CC enzyme, resulting in the formation of a DNA-(3'-phosphotyrosyl)- CC enzyme intermediate and the expulsion of a 5'-OH DNA strand. The CC free DNA strand then undergoes passage around the unbroken strand CC thus removing DNA supercoils. Finally, in the religation step, the CC DNA 5'-OH attacks the covalent intermediate to expel the active- CC site tyrosine and restore the DNA phosphodiester backbone. CC {ECO:0000256|RuleBase:RU365101}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP-independent breakage of single-stranded DNA, followed CC by passage and rejoining.; EC=5.6.2.2; CC Evidence={ECO:0000256|RuleBase:RU365101}; CC -!- SIMILARITY: Belongs to the type IB topoisomerase family. CC {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 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:0003677; F:DNA binding; IEA:UniProtKB-UniRule. DR GO; GO:0003917; F:DNA topoisomerase type I activity; IEA:UniProtKB-UniRule. DR GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-UniRule. DR CDD; cd00659; Topo_IB_C; 1. DR Gene3D; 1.10.10.41; -; 1. DR Gene3D; 1.10.132.10; -; 1. DR Gene3D; 2.170.11.10; -; 1. DR Gene3D; 3.90.15.10; -; 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 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; SSF56349; 1. DR SUPFAM; SSF56741; SSF56741; 1. DR PROSITE; PS00176; TOPOISOMERASE_I_EUK; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000035642}; KW DNA-binding {ECO:0000256|RuleBase:RU365101}; KW Isomerase {ECO:0000256|RuleBase:RU365101}; KW Reference proteome {ECO:0000313|Proteomes:UP000035642}; KW Topoisomerase {ECO:0000256|RuleBase:RU365101}. FT DOMAIN 344 681 TOPEUc. {ECO:0000259|SMART:SM00435}. FT COILED 44 64 {ECO:0000256|SAM:Coils}. FT COILED 300 320 {ECO:0000256|SAM:Coils}. FT COILED 595 648 {ECO:0000256|SAM:Coils}. 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 //