ID A0A416GH88_9BACE Unreviewed; 696 AA.
AC A0A416GH88;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 13-SEP-2023, entry version 13.
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 Name=topB {ECO:0000313|EMBL:RHP66664.1};
GN ORFNames=DXA74_02205 {ECO:0000313|EMBL:RHP66664.1};
OS Bacteroides sp. OF04-15BH.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=2292281 {ECO:0000313|EMBL:RHP66664.1, ECO:0000313|Proteomes:UP000284249};
RN [1] {ECO:0000313|EMBL:RHP66664.1, ECO:0000313|Proteomes:UP000284249}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OF04-15BH {ECO:0000313|EMBL:RHP66664.1,
RC ECO:0000313|Proteomes:UP000284249};
RA Zou Y., Xue W., Luo G.;
RT "A genome reference for cultivated species of the human gut microbiota.";
RL Submitted (AUG-2018) 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}.
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:RHP66664.1}.
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DR EMBL; QUEM01000003; RHP66664.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A416GH88; -.
DR OrthoDB; 9803554at2; -.
DR Proteomes; UP000284249; 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; 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; IPR006171; TOPRIM_domain.
DR InterPro; IPR034144; TOPRIM_TopoIII.
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 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; PS50880; TOPRIM; 1.
PE 3: Inferred from homology;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:RHP66664.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000284249};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT DOMAIN 1..134
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 231..267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 628..661
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..267
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 628..642
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 696 AA; 78457 MW; 8A240D1FC5FE33E4 CRC64;
MIVCIAEKPS VAKDIAHVLG ANKTCNGYME GNGYQVTWTF GHLCELKEPH EYSPLWKAWS
LSALPMIPPR FGIKLKADSG IEKQFKVIEE LMQHADEIIN CGDAGQEGEL IQRWVMQKAG
ARCPVKRLWI SSLTEEAIKE GFSQLKDQKE YQSLYEAGLS RAIGDWTLGM NATRLYTLKY
GQGKQVLSIG RVQTPTLALI VKRQQEIENF TPEPYWVLTT VYRDTTFTAL MGQDEDGEEE
EEKKSKENDK KDADISRKGF TSQEEGREAL EKIKDAPFTI TAVNKKNGTE APPRLFDLTS
LQVECNKKFA FSADTTLQTI QSLYEKKITT YPRVDTTFLS DDIYPKCKNI LNGIAERYGE
LLQPLRGAQL KKSKKVFDSS KVTDHHAIIP TGVKPQNLTP DEEKVFDLIA RRFIAAFYPD
CKFSTTTVLG ETAGIPFKAT GKLIVVSGWR DVYAAEKKSM TGKNEEEQTL PDFRKGESGT
HIPDLAEKWT QAPKPYTEAT LLRAMETAGR LVEDESLRDA LKENGIGRPS TRAAIIETLF
KRRYIRKERK NLYATPTGVE LIGLIHEELL KSAELTGIWE RKLRQIEKKE YEAKTFLDEL
KQMVCDIVYA VLADNSNRRV ALTLEEKKKP AEKKTAEKTT RKKAASKSKK KEAAPPATVK
EGDICPLCGK GHIIKGKTAF GCSEWKNGCT FRQSFE
//
