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Database: UniProt
Entry: A0A1R1AS02_9BACL
LinkDB: A0A1R1AS02_9BACL
Original site: A0A1R1AS02_9BACL 
ID   A0A1R1AS02_9BACL        Unreviewed;       752 AA.
AC   A0A1R1AS02;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
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=BK120_02385 {ECO:0000313|EMBL:OME88180.1};
OS   Paenibacillus sp. FSL A5-0031.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1920420 {ECO:0000313|EMBL:OME88180.1, ECO:0000313|Proteomes:UP000187447};
RN   [1] {ECO:0000313|EMBL:OME88180.1, ECO:0000313|Proteomes:UP000187447}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FSL A5-0031 {ECO:0000313|EMBL:OME88180.1,
RC   ECO:0000313|Proteomes:UP000187447};
RA   Beno S.M.;
RT   "Paenibacillus species isolates.";
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}.
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:OME88180.1}.
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DR   EMBL; MRTD01000001; OME88180.1; -; Genomic_DNA.
DR   RefSeq; WP_076265853.1; NZ_MRTD01000001.1.
DR   AlphaFoldDB; A0A1R1AS02; -.
DR   OrthoDB; 9803554at2; -.
DR   Proteomes; UP000187447; 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; IPR005738; TopoIII.
DR   InterPro; IPR025589; Toprim_C_rpt.
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   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; 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:OME88180.1};
KW   Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT   DOMAIN          2..134
FT                   /note="Toprim"
FT                   /evidence="ECO:0000259|PROSITE:PS50880"
FT   REGION          438..457
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          613..654
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        629..647
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   752 AA;  83589 MW;  0274FD684359FF7C CRC64;
     MKTLIIAEKP DMGRNIAAAI DPKAKNHRSY IEGEHYIITW AIGHLIGLAE PDAYDDRYKK
     WNINDLPIIP TQFKLVPNKK TIDQLKVIGD LAKRSNLLVN SCDAGREGQY IFSLIQRHLK
     LNQPVKRLWI SDLTPETIRK GFEELKEGAE YENLTRAATA RSEADWLIGM NGSRAFTTKH
     NVLLSVGRVQ TPVLALIYDR QKQIEAFSSL KFFELEGHFT QDEMTYRGMW QAERMTDQAK
     VEAVAAKVKG KAGRIASYEV KDTKEYPFKL YDLTLLQREA NGKYAFSAKK TLDTAQALYE
     KHKVISYPRT NSNYVTEQNI PEMHKTLNAL QGTAYDDLVK GANRSLVHKG NKFICNPTKV
     EDHHAILPTN RKANGLSPDE QKLYDLIVRR FLSQFYPAAE YKVHTVLTEV ENEMFKTTVK
     ELLSLGWKVI YADQKKEKAK PSAKSKDKEE AEDEEIEVNE PFSISADAGI ICSDAIVKEK
     DTQPPKHYTE GTLLKAMESA GKQIEDEDVR DAMKDSGLGT PATRAATIER LKNVGYVEMQ
     GKKIQVTQKG RTAIELIRGA GIDLLTSPEM TGLWERRLNE ISRGTASDGQ FMENVKKFAT
     MIVDKVRVQS RAAKTSFESE APASGKGSGG KSGTATRTRT ASTKTAGAAK KAASAASTVS
     GSPTVIATCP RPGCGGSIFM GRKGYGCSHY KEGCKFVIWK ESFGRNLTDT QVKALVEKGK
     TTKLKLELPD GTPGEGKIVL RNVDTGELAI EQ
//
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