ID A0A349H5N2_9BACT Unreviewed; 741 AA. AC A0A349H5N2; DT 07-NOV-2018, integrated into UniProtKB/TrEMBL. DT 07-NOV-2018, sequence version 1. DT 14-DEC-2022, entry version 14. DE RecName: Full=DNA topoisomerase 1 {ECO:0000256|HAMAP-Rule:MF_00952}; DE EC=5.6.2.1 {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, ECO:0000313|Proteomes:UP000261800}; RN [1] {ECO:0000313|EMBL:HAS84595.1, ECO:0000313|Proteomes:UP000261800} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 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 substantially RT revises the tree of life."; RL Nat. Biotechnol. 36:996-1004(2018). CC -!- FUNCTION: Releases the supercoiling and torsional tension of DNA, which CC is 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 a target CC site in duplex DNA. The scissile phosphodiester is attacked by the CC catalytic tyrosine of the enzyme, resulting in the formation of a DNA- CC (5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH CC DNA strand. The free DNA strand then undergoes passage around the CC unbroken strand, thus removing DNA supercoils. Finally, in the CC religation step, the DNA 3'-OH attacks the covalent intermediate to CC expel the active-site tyrosine and restore the DNA phosphodiester CC backbone. {ECO:0000256|HAMAP-Rule:MF_00952}. 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|ARBA:ARBA00000213, ECO:0000256|HAMAP- CC Rule:MF_00952}; CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00952}. CC -!- SIMILARITY: Belongs to the type IA topoisomerase family. CC {ECO:0000256|ARBA:ARBA00009446, ECO:0000256|HAMAP-Rule:MF_00952}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {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 AlphaFoldDB; A0A349H5N2; -. DR Proteomes; UP000261800; Unassembled WGS sequence. 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 (single strand cut, ATP-independent) 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; DNA TOPOISOMERASE, TYPE IA, CORE; 2. 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; Prokaryotic type I DNA topoisomerase; 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|ARBA:ARBA00023125, ECO:0000256|HAMAP- KW Rule:MF_00952}; KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_00952}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}; KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP- KW Rule:MF_00952}; Zinc {ECO:0000256|ARBA:ARBA00022833}; KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}. FT DOMAIN 6..117 FT /note="Toprim" FT /evidence="ECO:0000259|PROSITE:PS50880" FT REGION 165..170 FT /note="Interaction with DNA" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952" FT ACT_SITE 286 FT /note="O-(5'-phospho-DNA)-tyrosine intermediate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952" FT SITE 36 FT /note="Interaction with DNA" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952" FT SITE 141 FT /note="Interaction with DNA" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952" FT SITE 142 FT /note="Interaction with DNA" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952" FT SITE 145 FT /note="Interaction with DNA" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952" FT SITE 150 FT /note="Interaction with DNA" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952" FT SITE 157 FT /note="Interaction with DNA" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952" FT SITE 288 FT /note="Interaction with DNA" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952" FT SITE 471 FT /note="Interaction with DNA" FT /evidence="ECO:0000256|HAMAP-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 //