ID A0A022QQM7_ERYGU Unreviewed; 986 AA.
AC A0A022QQM7;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
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=MIMGU_mgv1a000789mg {ECO:0000313|EMBL:EYU30256.1};
OS Erythranthe guttata (Yellow monkey flower) (Mimulus guttatus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Phrymaceae; Erythranthe.
OX NCBI_TaxID=4155 {ECO:0000313|EMBL:EYU30256.1, ECO:0000313|Proteomes:UP000030748};
RN [1] {ECO:0000313|EMBL:EYU30256.1, ECO:0000313|Proteomes:UP000030748}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DUN x IM62 {ECO:0000313|Proteomes:UP000030748};
RX PubMed=24225854; DOI=10.1073/pnas.1319032110;
RA Hellsten U., Wright K.M., Jenkins J., Shu S., Yuan Y., Wessler S.R.,
RA Schmutz J., Willis J.H., Rokhsar D.S.;
RT "Fine-scale variation in meiotic recombination in Mimulus inferred from
RT population shotgun sequencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:19478-19482(2013).
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; KI631110; EYU30256.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A022QQM7; -.
DR STRING; 4155.A0A022QQM7; -.
DR eggNOG; KOG1956; Eukaryota.
DR Proteomes; UP000030748; Unassembled WGS sequence.
DR GO; GO:0005694; C:chromosome; IEA:InterPro.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006265; P:DNA topological change; IEA:InterPro.
DR CDD; cd00186; TOP1Ac; 1.
DR CDD; cd03363; TOPRIM_TopoIA_TopoI; 1.
DR Gene3D; 3.40.50.140; -; 1.
DR Gene3D; 3.30.65.10; Bacterial Topoisomerase I, domain 1; 1.
DR Gene3D; 1.10.460.10; Topoisomerase I, domain 2; 2.
DR Gene3D; 1.10.290.10; Topoisomerase I, domain 4; 1.
DR HAMAP; MF_00952; Topoisom_1_prok; 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; IPR013826; Topo_IA_cen_sub3.
DR InterPro; IPR023405; Topo_IA_core_domain.
DR InterPro; IPR003602; Topo_IA_DNA-bd_dom.
DR InterPro; IPR013498; Topo_IA_Znf.
DR InterPro; IPR028612; Topoisom_1_IA.
DR InterPro; IPR025589; Toprim_C_rpt.
DR InterPro; IPR006171; TOPRIM_domain.
DR InterPro; IPR034149; TOPRIM_TopoI.
DR PANTHER; PTHR42785:SF1; DNA TOPOISOMERASE; 1.
DR PANTHER; PTHR42785; DNA TOPOISOMERASE, TYPE IA, CORE; 1.
DR Pfam; PF01131; Topoisom_bac; 2.
DR Pfam; PF01751; Toprim; 1.
DR Pfam; PF13368; Toprim_C_rpt; 1.
DR Pfam; PF01396; zf-C4_Topoisom; 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};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000030748};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 248..363
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 108..234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 967..986
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 112..128
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..157
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..200
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..225
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 986 AA; 109667 MW; 653EFBF29FCEC7E1 CRC64;
MFLKCLSANA EKSVNLPLEN KPEKKIHPLR SFANTHPSFS AFKVPVNASY YGLLSGGMCS
NYCSSSSRSF SQMAKAIAQN NIVKTESRSS EMNNLFEIFN KDSETSLVRK KNVHIPKGKA
KSKQQSRSKK KQNQSSGAGS VDTSHMPKNP GNISQAKETR NNKRKKTPIS LEVNSTSNTT
ELVDSNISTE TVQNNARSST KKGKSKTKSH SSPKSNEELI EPKDSQVINK TKPQGQKVWN
QLYPPVAKSV VVVESATKAK VIQAYLGEMY EVVPSYGHVR DLAARSGSVR PEKDFSMVWE
VPSAAWSHLK SIKVALCGAE NLILASDPDR EGEAIAWHIL EMLKQQDALR EDVTVARVVF
NEITESSIKN ALRAPREIDV DLVHAYLARR ALDYLIGFNV SPLLLRKLPG CQSAGRVQSA
ALSLLCINMS KFEVTGSITS KSRRNPPMPY ITSSLQQDAG DKLNFAASHT MKVAQKLFEG
VELSDGKAAG LITYMRTDGL HLSDEATKEI QSFVVEKFGQ NFAEKNKRNY FKKVKNAEEA
HEAIRPTDIR TLPSMLAGVL DEDSLKLYTL IWNRTVACQM EPAIIEHIQC DIANANQSIV
FRSSCSRVEF EGFQAVYEDE ENHRSEEAHE VLSALKCGQP LSLTKIELSQ HSTQPPTRYS
EGSLVKKLEE LGIGRPSTYA TTIKVLKDRN YVTVKSSTLH PEFRGRMVSA FLAHYFSEVT
DYSFTADMET ELDNVSSGIT EWKGLMKDYW TRFSKHCECA SGVSIHQVEK VLGKTFGSFL
FASLQDGNKT CPSCNEGTLV FKVSRFGVGY FIGCDQHPNC KYIAKTLYGE EDDENTPENE
KNIAAEEPKL LGLKPGSNEK VILKCGPYSS YVQLGDDRKG HVPKRVTLKI KNPESITLED
ALELLKYPLK LGKHPDDDKP VILRIRDDGF SINHGRTNAA VPKNMNANEV TFEKALILLQ
GDVTQVGRPK QSDVTKIRRP KRKKSG
//
