ID A0A349H5N2_9BACT Unreviewed; 741 AA. AC A0A349H5N2; DT 07-NOV-2018, integrated into UniProtKB/TrEMBL. DT 07-NOV-2018, sequence version 1. DT 13-FEB-2019, entry version 4. DE RecName: Full=DNA topoisomerase 1 {ECO:0000256|HAMAP-Rule:MF_00952}; DE EC=5.99.1.2 {ECO:0000256|HAMAP-Rule:MF_00952}; DE AltName: Full=DNA topoisomerase I {ECO:0000256|HAMAP-Rule:MF_00952}; GN Name=topA {ECO:0000256|HAMAP-Rule:MF_00952}; GN ORFNames=DCS23_00765 {ECO:0000313|EMBL:HAS84595.1}; OS Candidatus Yonathbacteria bacterium. OC Bacteria; Candidatus Yonathbacteria. OX NCBI_TaxID=2053650 {ECO:0000313|EMBL:HAS84595.1}; RN [1] {ECO:0000313|EMBL:HAS84595.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=UBA11698 {ECO:0000313|EMBL:HAS84595.1}; RX PubMed=30148503; DOI=.1038/nbt.4229; RA Parks D.H., Chuvochina M., Waite D.W., Rinke C., Skarshewski A., RA Chaumeil P.A., Hugenholtz P.; RT "A standardized bacterial taxonomy based on genome phylogeny RT substantially revises the tree of life."; RL Nat. Biotechnol. 36:996-1004(2018). CC -!- FUNCTION: Releases the supercoiling and torsional tension of DNA, CC which is introduced during the DNA replication and transcription, CC by transiently cleaving and rejoining one strand of the DNA CC duplex. Introduces a single-strand break via transesterification CC at a target 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-(5'-phosphotyrosyl)-enzyme intermediate and the CC expulsion of a 3'-OH DNA strand. The free DNA strand then CC undergoes passage around the unbroken strand, thus removing DNA CC supercoils. Finally, in the religation step, the DNA 3'-OH attacks CC the covalent intermediate to expel the active-site tyrosine and CC restore the DNA phosphodiester backbone. {ECO:0000256|HAMAP- CC Rule:MF_00952}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP-independent breakage of single-stranded DNA, followed CC by passage and rejoining.; EC=5.99.1.2; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00952, CC ECO:0000256|SAAS:SAAS01117288}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|SAAS:SAAS00721088}; CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00952, CC ECO:0000256|SAAS:SAAS00709415}. CC -!- SIMILARITY: Belongs to the type IA topoisomerase family. CC {ECO:0000256|HAMAP-Rule:MF_00952, ECO:0000256|SAAS:SAAS00721110}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:HAS84595.1}. 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; DMXP01000002; HAS84595.1; -; Genomic_DNA. DR GO; GO:0005694; C:chromosome; IEA:InterPro. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0003917; F:DNA topoisomerase type I activity; IEA:UniProtKB-UniRule. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-UniRule. DR CDD; cd00186; TOP1Ac; 1. DR CDD; cd03363; TOPRIM_TopoIA_TopoI; 1. DR Gene3D; 1.10.290.10; -; 1. DR Gene3D; 1.10.460.10; -; 1. DR Gene3D; 2.70.20.10; -; 1. DR HAMAP; MF_00952; Topoisom_1_prok; 1. DR InterPro; IPR000380; Topo_IA. DR InterPro; IPR003601; Topo_IA_2. DR InterPro; IPR023406; Topo_IA_AS. DR InterPro; IPR013497; Topo_IA_cen. DR InterPro; IPR013824; Topo_IA_cen_sub1. 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 InterPro; IPR013498; Topo_IA_Znf. DR InterPro; IPR005733; TopoI_bac-type. DR InterPro; IPR028612; Topoisom_1_IA. DR InterPro; IPR006171; TOPRIM_domain. DR InterPro; IPR034149; TOPRIM_TopoI. DR PANTHER; PTHR42785; PTHR42785; 1. DR Pfam; PF01131; Topoisom_bac; 1. DR Pfam; PF01751; Toprim; 1. DR Pfam; PF01396; zf-C4_Topoisom; 3. DR PRINTS; PR00417; PRTPISMRASEI. DR SMART; SM00437; TOP1Ac; 1. DR SMART; SM00436; TOP1Bc; 1. DR SMART; SM00493; TOPRIM; 1. DR SUPFAM; SSF56712; SSF56712; 1. DR TIGRFAMs; TIGR01051; topA_bact; 1. DR PROSITE; PS00396; TOPOISOMERASE_I_PROK; 1. DR PROSITE; PS50880; TOPRIM; 1. PE 3: Inferred from homology; KW DNA-binding {ECO:0000256|HAMAP-Rule:MF_00952, KW ECO:0000256|SAAS:SAAS00721076}; KW Isomerase {ECO:0000256|HAMAP-Rule:MF_00952, KW ECO:0000256|SAAS:SAAS00721131, ECO:0000313|EMBL:HAS84595.1}; KW Magnesium {ECO:0000256|SAAS:SAAS00721141}; KW Metal-binding {ECO:0000256|SAAS:SAAS00721137}; KW Topoisomerase {ECO:0000256|HAMAP-Rule:MF_00952, KW ECO:0000256|SAAS:SAAS00721067}. FT DOMAIN 6 117 Toprim. {ECO:0000259|PROSITE:PS50880}. FT REGION 165 170 Interaction with DNA. {ECO:0000256|HAMAP- FT Rule:MF_00952}. FT ACT_SITE 286 286 O-(5'-phospho-DNA)-tyrosine intermediate. FT {ECO:0000256|HAMAP-Rule:MF_00952}. FT SITE 36 36 Interaction with DNA. {ECO:0000256|HAMAP- FT Rule:MF_00952}. FT SITE 141 141 Interaction with DNA. {ECO:0000256|HAMAP- FT Rule:MF_00952}. FT SITE 142 142 Interaction with DNA. {ECO:0000256|HAMAP- FT Rule:MF_00952}. FT SITE 145 145 Interaction with DNA. {ECO:0000256|HAMAP- FT Rule:MF_00952}. FT SITE 150 150 Interaction with DNA. {ECO:0000256|HAMAP- FT Rule:MF_00952}. FT SITE 157 157 Interaction with DNA. {ECO:0000256|HAMAP- FT Rule:MF_00952}. FT SITE 288 288 Interaction with DNA. {ECO:0000256|HAMAP- FT Rule:MF_00952}. FT SITE 471 471 Interaction with DNA. {ECO:0000256|HAMAP- FT Rule:MF_00952}. SQ SEQUENCE 741 AA; 82696 MW; 049E152844AECFF1 CRC64; MTVKQYKLLI VESPSKAKTI GKYLGDDYIV KASVGHVRDL PKSNKQAIDI PGGFIPHYEI SKGKAEVLSE IDSLAKKASE VLLATDPDRE GEAIAWHIAE ACKLKNPKRV TYHEITKTAI EEAIAHPRKI DQNLRKAQEA RRVLDRLVGY DLSGLIWKKV RYGLSAGRVQ SPALRIIMER EREIRAFIPE AYWSLTAKVK TEKGFELELS CTEEPRDEKI GKDILKIGRS NQWIVREVKE SEVGRAPKAP FITSTLQQAG SSRFGFAPSR TMGIAQKLYE KGFITYMRTD STTLSADAQK AVIAEATKRY GASSAEARVY KTKSKNAQEA HEAIRPTDMS KDNLGINPEE KKLYKLIWAR TMASQMVDAK LARTTILANV RDFSIPNFSV TGSRVIMPGW LSADPDSRGE DVELPKVAEG ESLILLSLND EAKFTEPPSR YSEAGLVKEL EKRDIGRPST YASIIKTICD RGYVIKDGKT LKPTDTGDVV SSFLEEHFAN YISDTFTAEM ENKLDDIANG EREYVKVLKE FYVPFTKDLK AKDEIEKQTN MGDADPKHKC PKCNGPMIIK LARNGKFLSC KKYPDCEGAR TIDGEELEGP RDTGELCPKC EKANLVERDG RFGRFIACGS YPKCKFIKKD ETAALLNHTG VGCPVCKKGF MTERKGRFGI FYSCTGYPDC KYAIKAKPTG KICQYPKVDG TPCGSLMMDG TKTIPERCSD KTCPNHNPHK LEKARIDAKG K //