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Database: UniProt
Entry: A0A1Q9JR07_9FIRM
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Original site: A0A1Q9JR07_9FIRM 
ID   A0A1Q9JR07_9FIRM        Unreviewed;       672 AA.
AC   A0A1Q9JR07;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=DNA topoisomerase {ECO:0000256|ARBA:ARBA00012891};
DE            EC=5.6.2.1 {ECO:0000256|ARBA:ARBA00012891};
DE   AltName: Full=Omega-protein {ECO:0000256|ARBA:ARBA00032877};
DE   AltName: Full=Relaxing enzyme {ECO:0000256|ARBA:ARBA00032235};
DE   AltName: Full=Swivelase {ECO:0000256|ARBA:ARBA00030003};
DE   AltName: Full=Untwisting enzyme {ECO:0000256|ARBA:ARBA00031985};
GN   ORFNames=BHF70_02635 {ECO:0000313|EMBL:OLR58617.1};
OS   Anaerostipes sp. 494a.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Anaerostipes.
OX   NCBI_TaxID=1261636 {ECO:0000313|EMBL:OLR58617.1, ECO:0000313|Proteomes:UP000242190};
RN   [1] {ECO:0000313|EMBL:OLR58617.1, ECO:0000313|Proteomes:UP000242190}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=494a {ECO:0000313|EMBL:OLR58617.1,
RC   ECO:0000313|Proteomes:UP000242190};
RX   PubMed=27613689;
RA   Trachsel J., Bayles D.O., Looft T., Levine U.Y., Allen H.K.;
RT   "Function and Phylogeny of Bacterial Butyryl Coenzyme A:Acetate
RT   Transferases and Their Diversity in the Proximal Colon of Swine.";
RL   Appl. Environ. Microbiol. 82:6788-6798(2016).
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};
CC   -!- SIMILARITY: Belongs to the type IA topoisomerase family.
CC       {ECO:0000256|ARBA:ARBA00009446}.
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:OLR58617.1}.
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DR   EMBL; MJIF01000001; OLR58617.1; -; Genomic_DNA.
DR   RefSeq; WP_075758803.1; NZ_MJIF01000001.1.
DR   AlphaFoldDB; A0A1Q9JR07; -.
DR   STRING; 1261636.BHF70_02635; -.
DR   Proteomes; UP000242190; Unassembled WGS sequence.
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   CDD; cd00186; TOP1Ac; 1.
DR   CDD; cd03362; TOPRIM_TopoIA_TopoIII; 1.
DR   Gene3D; 3.40.50.140; -; 1.
DR   Gene3D; 1.10.460.10; Topoisomerase I, domain 2; 1.
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; 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; IPR006171; TOPRIM_domain.
DR   InterPro; IPR034144; TOPRIM_TopoIII.
DR   PANTHER; PTHR11390:SF21; DNA TOPOISOMERASE 3-ALPHA; 1.
DR   PANTHER; PTHR11390; PROKARYOTIC DNA TOPOISOMERASE; 1.
DR   Pfam; PF01131; Topoisom_bac; 1.
DR   Pfam; PF01751; Toprim; 1.
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   PROSITE; PS00396; TOPOISOMERASE_I_PROK; 1.
DR   PROSITE; PS50880; TOPRIM; 1.
PE   3: Inferred from homology;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:OLR58617.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000242190};
KW   Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT   DOMAIN          16..149
FT                   /note="Toprim"
FT                   /evidence="ECO:0000259|PROSITE:PS50880"
SQ   SEQUENCE   672 AA;  76485 MW;  BCEF02B71B6CFD40 CRC64;
     MNRICRNFSK AGIVLKSLFI TEKPSVAREF AAALNINAQN KDGYMEGEKA VITWCVGHLV
     TMSYPDKYDP ALKKWDLETI PFIPKEFKYE IIPSVKKQFD IVSMLLNRKD IDTIYVCTDS
     GREGEYIYRL VEQEAKVENK IRKRVWIDSQ TKEEVIRGVR EAKDLSEYDN LASAAYLRAK
     EDYLMGINFS RVLTLKYGWT LGNYLNQKKS LVVAVGRVMT CVLGMIVKRE REIRNFVPTS
     FYRVIAHLNC QGFEVEAEWK AVKGSRYYES SKLYKDNGFL DKKEARDFIE FLEDGSNGET
     IVKSSTRRTE KKNPPLLYNL AELQNQCSKM FKLSPDETLK IVQELYERKL VTYPRTDARV
     LSTAVSKEIY KNIKGLTGYA PLSTYASEIL EQKIYQGISR TKYVDDKKIT DHYAIIPTGQ
     AISGLGSISQ LGQKVYDVIV RRFLSIFMPP AVYTKIKLET ETKGETFFAN FKILKDPGYL
     KVAGTGNSKK EDGLTQEQMD AITSLKKGGK LPVKSYKIKN GTTTPPKRYN SGSLILAMEN
     AGQLIEDEDL REQIKGSGIG TSATRAEIVK KLITNKYIAL NKKTQIVTPT LTGEMIVNVV
     SASIGSLLNP ELTASWEKGL TYVAEGTVTE EEYMEKLDRF VSQKTNIVKQ NNYQYQLRQS
     FDQIAPYYKK NK
//
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