ID A0A0Q7SRF6_9BURK Unreviewed; 873 AA.
AC A0A0Q7SRF6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
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=ASD35_21620 {ECO:0000313|EMBL:KQY86215.1};
OS Pelomonas sp. Root1444.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Roseateles.
OX NCBI_TaxID=1736464 {ECO:0000313|EMBL:KQY86215.1, ECO:0000313|Proteomes:UP000051648};
RN [1] {ECO:0000313|Proteomes:UP000051648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1444 {ECO:0000313|Proteomes:UP000051648};
RA Garrido-Oter R., Mueller D.B.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQY86215.1, ECO:0000313|Proteomes:UP000051648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1444 {ECO:0000313|EMBL:KQY86215.1,
RC ECO:0000313|Proteomes:UP000051648};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KQY86215.1}.
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DR EMBL; LMFP01000011; KQY86215.1; -; Genomic_DNA.
DR RefSeq; WP_056875360.1; NZ_LMFP01000011.1.
DR AlphaFoldDB; A0A0Q7SRF6; -.
DR STRING; 1736464.ASD35_21620; -.
DR OrthoDB; 9803554at2; -.
DR Proteomes; UP000051648; 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; 2.
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:KQY86215.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000051648};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT DOMAIN 3..143
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 849..873
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 873 AA; 96460 MW; 7673FD4B49B6CB9E CRC64;
MSKTLIIAEK PSVAQDIVRA LTPVAGKFDK HDDHFENEQY VVSSAVGHLV EIAAPEEFDV
KRGKWSFNNL PVIPPHFDLN PIDKNKGRLN ALTKLIRRKD VTALINACDA GREGELIFRL
IQQYAQPAKG PLNKPVQRLW LQSMTPAAIR EGFEKLRSDA QMLPLADAAR CRSEADWLVG
INGTRAMTAF NSRDGGFFLT TVGRVQTPTL SIVVEREEKI RKHVSRDYWE LRANFDAQAG
QYEGKWFDPA WKKNDDLERR ADRMWNAADA DAIAKAVLGQ PATVTEESKP STTSCGALYD
LTTLQREANS RFGFSAKTTL SIAQALYEKH KVLTYPRTDS RFLPEDYLAV AKDTAKMLAT
EDLPGPLGAL SQHAAKALKE GYIKPTKKVF DNAKVSDHFA IIPTLQAPKA LTEIEAKLYD
MVVKRFLGVF FPPAEFLVTT RISKVGAQGH THHFQTNGKV LVKPGWLAVY GKDVDDEDAN
LVPVQPNEVV RTESVDVKAL QTKPPARYTE ATLLSAMEGA GKLIDDDELR EAMAEKGLGT
PATRAATIEG LITEKYMLRE GRELIPTAKA FQLMTLLRGL EVEDLTKPEL TGDWESKLAQ
MEKGKLKREQ FMAEIAAMTE KMVAKAKGYD RDTIPGDYAT LKTPCPKCGG VVKENYRRFT
CTGKSGDGSD ACGFSIGKIP GGRSFELNEV ETFLRDKKIG PLEGFRSKAG WPFTAELALV
YDEEIQNWKL EFDFGEDAKK AEGDGEPVDF SGQNSLGACP KCAGHVYEHG ANYVCERSVG
ETVTCDFKTG KVILTQPIEP AQVHKLLTAG KTDLLENFVS NKTRRKFKAF LAYDKKEGKV
VFEFEPRAGK PAGKAAGKDA APAKKAARKT AKA
//
