ID A0A1I5RFU7_9BURK Unreviewed; 983 AA.
AC A0A1I5RFU7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-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=SAMN05443579_112263 {ECO:0000313|EMBL:SFP57448.1};
OS Variovorax sp. PDC80.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Variovorax.
OX NCBI_TaxID=1882827 {ECO:0000313|EMBL:SFP57448.1, ECO:0000313|Proteomes:UP000199369};
RN [1] {ECO:0000313|Proteomes:UP000199369}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PDC80 {ECO:0000313|Proteomes:UP000199369};
RA Varghese N., Submissions S.;
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; FOWG01000012; SFP57448.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I5RFU7; -.
DR OrthoDB; 9803554at2; -.
DR Proteomes; UP000199369; 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; cd10567; SWIB-MDM2_like; 1.
DR CDD; cd00186; TOP1Ac; 1.
DR CDD; cd03362; TOPRIM_TopoIA_TopoIII; 1.
DR Gene3D; 3.40.50.140; -; 1.
DR Gene3D; 1.10.245.10; SWIB/MDM2 domain; 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; IPR019835; SWIB_domain.
DR InterPro; IPR036885; SWIB_MDM2_dom_sf.
DR InterPro; IPR003121; SWIB_MDM2_domain.
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; PF02201; SWIB; 1.
DR Pfam; PF01131; Topoisom_bac; 1.
DR Pfam; PF01751; Toprim; 1.
DR Pfam; PF13342; Toprim_Crpt; 2.
DR PRINTS; PR00417; PRTPISMRASEI.
DR SMART; SM00151; SWIB; 1.
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 SUPFAM; SSF47592; SWIB/MDM2 domain; 1.
DR PROSITE; PS51925; SWIB_MDM2; 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:SFP57448.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000199369};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT DOMAIN 3..144
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT DOMAIN 905..982
FT /note="DM2"
FT /evidence="ECO:0000259|PROSITE:PS51925"
FT REGION 284..307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 887..909
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..307
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 893..907
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 983 AA; 108379 MW; A6CC96F74CDB749F CRC64;
MTKTLVIAEK PSVAQDIVRA LTPVAGKFDK HDEHFENDQY VVTSAVGHLV EIQAPEEFDV
KRGKWSFANL PVIPPHFDLK PVDKTKTRLN AVVKQAKRKD VTQLVNACDA GREGELIFRL
IEQYAGGKTG LNKPVRRLWL QSMTPQAIRD GFDSLRTEKQ MQGLADAARS RSEADWLVGI
NGTRAMTAFN SRDGGFFLTT VGRVQTPTLS VVVEREEQIR KFVSRDYWEV HASFLAEAGH
YPGKWFDPAW KKASAPLLPS GEPDPEQRAD RIWNERDALA IAQAARGKPA SVTEESKPTT
QASPQLFDLT SLQREANSRF GFSAKTTLAL AQSLYERHKA LTYPRTDSRA LPEDYLPVVK
QTMGMLATSG MRHLAPFAQQ AIDQNYVKPS KRIFDNAKVS DHFAIIPTLQ APSGLSEAEQ
RLYDFVVRRF LSVFFPSAEY QVTTRISTVA QAGRNYAFRS DGKVLVKPGW LAIYGKEAVS
DDDEKDGKNL VPVKPGEMVL AETVDTKGLK TRPPARYSEA TLLGAMEGAG KTIDDEELRE
AMQEKGLGTP ATRAATIEGL IAEKYMLREG RELIPTAKAF QLMTLLRGLG VEELSKAELT
GEWEYKLAQM EKGSLSRDAF MREIAAMTEH IVKKAKEYDR DTVPGDYTTL ATPCPNCGGV
VKENYRRYGC TGKSGTGEDA CGFSFGKSPA GRTFEVAEAE ALLRDKHIGP LEGFRSKAGW
PFTSEIVLKY DEEAKNWKLE FDFGDDKNED SGEIVDFSEQ DTVGPCPICG APVFEHGSNY
ICEKSVPTNA QPTPSCTFKT GKIILQQPVE RAQMEKLLAT GKTDLLDKFV SMRTRRAFKA
FLTWNAEEGK VTFEFAPREG GSKFPPRKTF GKAAPAGKTA AAKKVAAKKA PAAKKAPAEK
KAPRKTGAGL KPSDALAAVI GNEPVARTEV VKKLWDYIKA NGLQDAKDKR SINADAKLKP
VFGKDQVTMF ELAGIVGKHL TAL
//
