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Database: UniProt
Entry: A0A1I3HAU1_9BACL
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ID   A0A1I3HAU1_9BACL        Unreviewed;       812 AA.
AC   A0A1I3HAU1;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
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=SAMN02799624_00378 {ECO:0000313|EMBL:SFI32773.1};
OS   Paenibacillus sp. UNC496MF.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1502753 {ECO:0000313|EMBL:SFI32773.1, ECO:0000313|Proteomes:UP000198714};
RN   [1] {ECO:0000313|EMBL:SFI32773.1, ECO:0000313|Proteomes:UP000198714}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UNC496MF {ECO:0000313|EMBL:SFI32773.1,
RC   ECO:0000313|Proteomes:UP000198714};
RA   de Groot N.N.;
RL   Submitted (OCT-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; FORE01000004; SFI32773.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I3HAU1; -.
DR   STRING; 1502753.SAMN02799624_00378; -.
DR   Proteomes; UP000198714; 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; 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; PS00396; TOPOISOMERASE_I_PROK; 1.
PE   3: Inferred from homology;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:SFI32773.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198714};
KW   Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT   DOMAIN          4..113
FT                   /note="Toprim"
FT                   /evidence="ECO:0000259|SMART:SM00493"
FT   DOMAIN          113..203
FT                   /note="DNA topoisomerase type IA"
FT                   /evidence="ECO:0000259|SMART:SM00436"
FT   DOMAIN          248..550
FT                   /note="DNA topoisomerase type IA DNA-binding"
FT                   /evidence="ECO:0000259|SMART:SM00437"
FT   REGION          427..457
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          605..730
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        428..457
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   812 AA;  88894 MW;  378E40BE4D49B46A CRC64;
     MGRTIAAVVE PRAQNKRTYL EGERYIITWA IGHLVGLAEP DQYDPKYKRW NEADLPIIPD
     RFKLWPNART KDQLKTIGEL SKRCGRLVNA CDAGREGQLI FHLIRQYLKL PQPTDRLWIS
     DLTPETIRRG FDGLRSDTDF DDLTRAARAR SEADWLVGMN ASRAFTIRHK ALLSVGRVQT
     PVLALLYDRH KEITAFNSET YFIVQAAFTQ DDFGYKGIWQ GDRITKREEA EKLADKVKGK
     PGAIVSYTVN ESKEYPYRLY DLTLLQREAN GRYGYPAKKT LDIAQSLYEK HKVITYPRTS
     SNYVTEENIP VMGSVLNMLK GTAYADLANG ADRNRVHKGN RAVCNPPKVE DHHAILPTPK
     KPGTLSTEEQ NIYDMIVRRF LSHYYPPAVY NNHEVITEIE GETFRTRAKE QLELGWRVVL
     EQTEANAAKG KGKGKKKDDD ASAAVEGDED LVETDRPFSV DADRPVRCDD AAAVEKETKP
     PKPYTEGTLL KAMESAGKAI EDEELRDAMK QTGLGTPATR AATIERLKQV GYITSAGKRL
     DITTKGCTAI ELIRGAGVEL LASPEMTGRW EQRLHQISKG EASDEQFIAK VKQFAEMIVG
     KVKQQQQAPA SLFDEPDGGG KRGAKGKGRG AAASARKAGG TAPRAGTRSR GAAAADSAPV
     ASRARASARK GTSDSGRMLA APVEAAPASR AKAPAAASRP KTEGRAAKPA PANSEGSAGS
     RGTIAPCPRP GCGGQLIEGK RGYGCLRFRE GCSFVIWKEQ QGKHVTPAMA KALAENGVTR
     KSTFKLANGT AVSGKWTLTD PAKGTIAFQP AT
//
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