ID B9SPT5_RICCO Unreviewed; 1071 AA.
AC B9SPT5;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=DNA topoisomerase {ECO:0000256|ARBA:ARBA00012891};
DE EC=5.6.2.1 {ECO:0000256|ARBA:ARBA00012891};
GN ORFNames=RCOM_0205460 {ECO:0000313|EMBL:EEF34415.1};
OS Ricinus communis (Castor bean).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Euphorbiaceae; Acalyphoideae; Acalypheae;
OC Ricinus.
OX NCBI_TaxID=3988 {ECO:0000313|Proteomes:UP000008311};
RN [1] {ECO:0000313|Proteomes:UP000008311}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Hale {ECO:0000313|Proteomes:UP000008311};
RX PubMed=20729833; DOI=10.1038/nbt.1674;
RA Chan A.P., Crabtree J., Zhao Q., Lorenzi H., Orvis J., Puiu D.,
RA Melake-Berhan A., Jones K.M., Redman J., Chen G., Cahoon E.B., Gedil M.,
RA Stanke M., Haas B.J., Wortman J.R., Fraser-Liggett C.M., Ravel J.,
RA Rabinowicz P.D.;
RT "Draft genome sequence of the oilseed species Ricinus communis.";
RL Nat. Biotechnol. 28:951-956(2010).
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; EQ974072; EEF34415.1; -; Genomic_DNA.
DR AlphaFoldDB; B9SPT5; -.
DR STRING; 3988.B9SPT5; -.
DR eggNOG; KOG1956; Eukaryota.
DR InParanoid; B9SPT5; -.
DR Proteomes; UP000008311; 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: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; 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; 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; 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:EEF34415.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000008311};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT DOMAIN 289..404
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 149..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1052..1071
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..185
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 199..219
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1071 AA; 119555 MW; 768114E8BF6A4DE2 CRC64;
MSASQLAFGS SLYASDCLPG CTHSAVCIAR LIACSLINHK NKTKETNEGE AMTGFLLVWT
SPSSFFRLPP FMAAAKLQCR VALSLHSHPF SRRVSSINPS MLPQTSPPLF LSSLTPPHLF
LTSHRHFSSV NQRSAGFSKY WKRTKPFTAH LNNKDNDANP TEQSSGDVNL DSTAPVTTPN
SKPTPTTTRH KKHSKTNSKK QQSSTSVEEA AQAKTSSSTK TKTKPKELLD ASASTKPQPN
KKTRKPTGKP KAIKTVKVSP DKQQQHKPMH KSKPFRQGSL KPLYPPTAKS VVVVESVTKA
KVIQGYLGPM FEVLPSYGHV RDLAARSGSV RPDDDFSMVW EVPSPAWTHL KTIKVALNGA
ENLVLASDPD REGEAIAWHI IEMLQQQDAL HQGVTVARVV FHEITEQSIK NALQAPREID
LNLVHAYLAR RALDYLIGFN ISPLLWRKLP GCQSAGRVQS AALSLICDRE MEIDEFTPQE
YWTIDVELYI METGSSVNAR LTHFDFNKLN QLSVRSHTEA RDIEQKINVA SFLVAGAKES
KMRRNPPTPY ITSTLQQDAA NKLHFSSMYT MKLAQKLYEG VQLSDGKTTG LITYIRTDGL
HISGEAVKEI HSLVIERYGQ DFASDSPRKY FKKVKNAQEA HEAVRPTNVR MLPSMLANVL
DEDSLKLYTL IWSRTVACQM EPATIEQIQV DIGNANGSIT LRSACSGVGF LGYQIVYEDK
EAGAIKNKES EVNDHNEAFG ILKSLKPGDP FNLSEVKLKQ HFTQPPPRYS EGTLVKKLEE
LGIGRPSTYA STLKVLQDRN YVTVKNRVLN PEFRGRMVSA FLSQHFTEVT DYSFTADMET
ELDNVSAGLT EWKGLLRDYW TRFSSYCSHA ESVHIHQVEK MLEKTFGDFL FGSLPDDSRT
CPSCLEGTLI FKYMLDIYGD DEDEETPQNN SVEEPKLLGV HPVSTEKVLL KNGPYGFYLQ
LGEDRKGYTP KRASVSHIKD VDNITLEDAL ELLRYPVTLG NHPKDGHPII LKLAKVGFAV
RHRRTIASVP KNMKPDNVSL EKALELLSGD DVRRSGRPKR KPKVEEVVEA M
//
