ID A0A2G5F5R1_AQUCA Unreviewed; 1207 AA.
AC A0A2G5F5R1;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
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=AQUCO_00200976v1 {ECO:0000313|EMBL:PIA63324.1};
OS Aquilegia coerulea (Rocky mountain columbine).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Ranunculales; Ranunculaceae; Thalictroideae;
OC Aquilegia.
OX NCBI_TaxID=218851 {ECO:0000313|EMBL:PIA63324.1, ECO:0000313|Proteomes:UP000230069};
RN [1] {ECO:0000313|EMBL:PIA63324.1, ECO:0000313|Proteomes:UP000230069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Goldsmith {ECO:0000313|Proteomes:UP000230069};
RA Hodges S., Kramer E., Nordborg M., Tomkins J., Borevitz J., Derieg N.,
RA Yan J., Mihaltcheva S., Hayes R.D., Rokhsar D.;
RT "WGS assembly of Aquilegia coerulea Goldsmith.";
RL Submitted (SEP-2017) 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; KZ305019; PIA63324.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G5F5R1; -.
DR Proteomes; UP000230069; 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; 1.
DR Gene3D; 2.70.20.10; Topoisomerase I, domain 3; 1.
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; 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; IPR013498; Topo_IA_Znf.
DR InterPro; IPR005733; TopoI_bac-type.
DR InterPro; IPR028612; Topoisom_1_IA.
DR InterPro; IPR025589; Toprim_C_rpt.
DR InterPro; IPR006171; TOPRIM_domain.
DR InterPro; IPR034149; TOPRIM_TopoI.
DR NCBIfam; TIGR01051; topA_bact; 1.
DR PANTHER; PTHR42785:SF1; DNA TOPOISOMERASE; 1.
DR PANTHER; PTHR42785; DNA TOPOISOMERASE, TYPE IA, CORE; 1.
DR Pfam; PF01131; Topoisom_bac; 1.
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; 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};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000230069};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 423..538
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 193..398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..209
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..262
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..289
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 290..319
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 320..368
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1207 AA; 134046 MW; E93F25E4902EA43F CRC64;
MGFQLHRFFV STNLHRKLST SSSSSSRLPT TMLHCRTLQN YPSTCLQLVP FSNGGKFSKS
AQLRFRKSGD TCDGQLKSHR VKVERDSCLV RSSLGDNRLS YAVTFPTTLR LPFSFPMKFS
NSSSYSRLES NKRLKFASEE RFGRRFFSVK ASESSQVEQK TMKISGNNTT VGDVNGGVNN
SPVKLSDRFR KLGKSSVTRS SSSDREVAVS SQAVEKGASV ASKSVRKTAP KPKNGKKDVK
LKSTSPTSPK SGGTNQKPEA QVEKKQLGNK KEKALSGTTT PLGEAKINGS KQDSHTKKNN
VTKIDGSKQV ARTKKDNVTK VNGSKQASHT KANMTESAGE PSQASQIAGE TPLSTLDNSN
LLHEKSKTTV GKPTSKKKPH RKVTVHMKPD KAPAKPKINP VPVEVKKMPL KKGLRSLYPP
TGKSVVVVES LTKAKVIQGY LGNMYEVLPS YGHVRDLAGR SGSVRPDDDF SMVWEVPSAA
WTHLKSIKVA LNGAENLILA SDPDREGEAI AWHITEMLQQ QDALPDDINV SRVVFHEITE
SSIKSALQAP RNIDADLVHA YLARRALDYL IGFSISPLLW RKLPACQSAG RVQSAALALI
CDREMEIDEF KPQEYWTVDV GFNKNEPGSS TKVYSFPSHL THLAFKKLEQ LSISCSEEAN
AIEQKMTSST FEVLTAKRSK SRRNPPTPYI TSTLQQDAAS KLNFTASYTM KLAQKLYEGV
KLANEEATGL ITYMRTDGLH VSDAAANDIH SLVIERYGKD FASESIRKYF KKVKNAQEAH
EAIRPTSIRR LPSMLTGVLD EDSLKLYALI WSRAMACQMV PTIIDQIQVD IGGAGNFFGL
RSVCSRVEFY GFQAVYKDAE AAAIGYNEKE GDAREEAFEV LCKLKTGDSL HLSKVELKQH
STQPPSRYSE ASLVKKLEEL GIGRPSTYAS TIKVLQDRHY VTVKNRALHP EFRGRMVSAF
LSHHFSEVTD YSFTADMETE LDNVSAGTTE WKGLLKDYWT RFKSYCDLAG KVDIRQVEKM
LEKTFGNFIF ASLPNQSRTC PSCSTGTLVF KVSRFGAGYF IGCDQHPECK YIARRISGED
DTTDDDIPEK IEFGSEPKEL GLHPVSNEKI LLKHGPYGFY IQHGEDRRGH SPKRASVSQI
KDVSAISLED ALDLLQYPVL LGNHPDDGVP VYIKIASRGF SIRHRRTIAP VPKQFVLEKN
YTFYSMY
//
