ID A0A1M5YGE9_9FIRM Unreviewed; 684 AA.
AC A0A1M5YGE9;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 28-JAN-2026, entry version 25.
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=SAMN02745180_02178 {ECO:0000313|EMBL:SHI10979.1};
OS Sporanaerobacter acetigenes DSM 13106.
OC Bacteria; Bacillati; Bacillota; Tissierellia; Tissierellales;
OC Sporanaerobacteraceae; Sporanaerobacter.
OX NCBI_TaxID=1123281 {ECO:0000313|EMBL:SHI10979.1, ECO:0000313|Proteomes:UP000184389};
RN [1] {ECO:0000313|EMBL:SHI10979.1, ECO:0000313|Proteomes:UP000184389}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13106 {ECO:0000313|EMBL:SHI10979.1,
RC ECO:0000313|Proteomes:UP000184389};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; FQXR01000011; SHI10979.1; -; Genomic_DNA.
DR RefSeq; WP_072744821.1; NZ_FQXR01000011.1.
DR AlphaFoldDB; A0A1M5YGE9; -.
DR STRING; 1123281.SAMN02745180_02178; -.
DR OrthoDB; 9803554at2; -.
DR Proteomes; UP000184389; Unassembled WGS sequence.
DR GO; GO:0043597; C:cytoplasmic replication fork; IEA:TreeGrafter.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006310; P:DNA recombination; IEA:TreeGrafter.
DR GO; GO:0006281; P:DNA repair; IEA:TreeGrafter.
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; IPR005738; TopoIII.
DR InterPro; IPR025589; Toprim_C_rpt.
DR InterPro; IPR006171; TOPRIM_dom.
DR InterPro; IPR034144; TOPRIM_TopoIII.
DR NCBIfam; NF005829; PRK07726.1; 1.
DR NCBIfam; TIGR01056; topB; 1.
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 Pfam; PF13342; Toprim_Crpt; 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; TOPO_IA_1; 1.
DR PROSITE; PS52039; TOPO_IA_2; 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:SHI10979.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000184389};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT DOMAIN 1..134
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT DOMAIN 151..574
FT /note="Topo IA-type catalytic"
FT /evidence="ECO:0000259|PROSITE:PS52039"
SQ SEQUENCE 684 AA; 78779 MW; 76B3BDC7140EB4AB CRC64;
MKLIITEKPS VAMSIAKVLG VHGRKDGYIE SKEYIISWCV GHLVGLAQAD KYNEKYKKWR
YEDLPIIPSK FQYDLFVKTK KQYEILNKLL NRSDVLEVIN ACDSGREGEL IFRLVYYHSK
CQKPMKRLWI SSMEDSAIED GFKNLKDGKE FNNLYKSALA RSQADWIVGI NATRLFTVLY
NQLLSVGRVQ TPTLALIVNR EEDIRSFRKE KFYHLDLYLD GFMASSERIK EKDEANELKN
LCIGEMAIAK DVKKEKKNVN PPLPFDLTSL QREANRLFGY TAKQTLDYTQ SLYEKKWVTY
PRTDSRYLTD DMMESLVNLI NGIDRDNLVE NPNYKRILDS KKVTDHHAII PTIQSLNMNI
EDIPKTEKNI YKLICLKLLE AVADTYVEEI VRVSLLVGDK IFTAKGKKVV NLGFKGIKSS
FDENFNTMEK EKDNSILLPE IEEGMVFEIQ NSEIREGFTQ SPKHFTEDTL LSAMERAGNE
ELDKELDVEK KGLGTPATRA GIIEKLISVG YLERKKKQLL PTDKGVSLIT VMPDNLKSPK
LTAEWENKLT EISLGKGSDE EFLKGIDEMI TDLVKTYSHI AVENKEKFQS NREVLGSCPR
CKSYIFEGKK NFYCSNKECG FSLLKEDRFF TDKRKKLTKE MVKTLLSKGE VIVKGLYSKK
TGKTYNAYIS IEDTGKYINY KMRF
//