ID   TOP1_RFVKA              Reviewed;         314 AA.
AC   P16472; Q77PC2;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   02-DEC-2020, entry version 108.
DE   RecName: Full=DNA topoisomerase 1;
DE            EC=5.6.2.1 {ECO:0000255|PROSITE-ProRule:PRU10130};
DE   AltName: Full=DNA topoisomerase I;
GN   Name=TOP1; ORFNames=s074R;
OS   Rabbit fibroma virus (strain Kasza) (RFV) (Shope fibroma virus (strain
OS   Kasza)).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Leporipoxvirus.
OX   NCBI_TaxID=10272;
OH   NCBI_TaxID=9986; Oryctolagus cuniculus (Rabbit).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2161144; DOI=10.1016/0042-6822(90)90013-h;
RA   Upton C., Opgenorth A., Traktman P., McFadden G.;
RT   "Identification and DNA sequence of the Shope fibroma virus DNA
RT   topoisomerase gene.";
RL   Virology 176:439-447(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1660196; DOI=10.1016/0042-6822(91)90529-k;
RA   Strayer D.S., Jerng H.H., O'Connor K.;
RT   "Sequence and analysis of a portion of the genomes of Shope fibroma virus
RT   and malignant rabbit fibroma virus that is important for viral replication
RT   in lymphocytes.";
RL   Virology 185:585-595(1991).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10074403; DOI=10.1006/jmbi.1999.2586;
RA   Palaniyar N., Gerasimopoulos E., Evans D.H.;
RT   "Shope fibroma virus DNA topoisomerase catalyses holliday junction
RT   resolution and hairpin formation in vitro.";
RL   J. Mol. Biol. 287:9-20(1999).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=10562495; DOI=10.1006/viro.1999.0002;
RA   Willer D.O., McFadden G., Evans D.H.;
RT   "The complete genome sequence of shope (Rabbit) fibroma virus.";
RL   Virology 264:319-343(1999).
CC   -!- FUNCTION: Releases the supercoiling and torsional tension of DNA
CC       introduced during the DNA replication and transcription by transiently
CC       cleaving and rejoining one strand of the DNA duplex. Introduces a
CC       single-strand break via transesterification at a target site in duplex
CC       DNA. The scissile phosphodiester is attacked by the catalytic tyrosine
CC       of the enzyme, resulting in the formation of a DNA-(3'-phosphotyrosyl)-
CC       enzyme intermediate and the expulsion of a 5'-OH DNA strand. The free
CC       DNA strand then undergoes passage around the unbroken strand thus
CC       removing DNA supercoils. Finally, in the religation step, the DNA 5'-OH
CC       attacks the covalent intermediate to expel the active-site tyrosine and
CC       restore the DNA phosphodiester backbone (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP-independent breakage of single-stranded DNA, followed by
CC         passage and rejoining.; EC=5.6.2.1; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU10130};
CC   -!- SIMILARITY: Belongs to the type IB topoisomerase family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M31723; AAA47228.1; -; Genomic_DNA.
DR   EMBL; AF170722; AAF17956.1; -; Genomic_DNA.
DR   PIR; A34769; ITVZKA.
DR   RefSeq; NP_051963.1; NC_001266.1.
DR   SMR; P16472; -.
DR   GeneID; 1486917; -.
DR   KEGG; vg:1486917; -.
DR   Proteomes; UP000000868; Genome.
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   Gene3D; 1.20.120.380; -; 1.
DR   Gene3D; 3.30.66.10; -; 1.
DR   Gene3D; 3.90.15.10; -; 1.
DR   InterPro; IPR011010; DNA_brk_join_enz.
DR   InterPro; IPR035447; DNA_topo_I_N.
DR   InterPro; IPR001631; TopoI.
DR   InterPro; IPR018521; TopoI_AS.
DR   InterPro; IPR027362; TopoI_C.
DR   InterPro; IPR014711; TopoI_cat_a-hlx-sub_euk.
DR   InterPro; IPR013500; TopoI_cat_euk.
DR   InterPro; IPR015346; TopoI_N_vir.
DR   Pfam; PF01028; Topoisom_I; 1.
DR   Pfam; PF09266; VirDNA-topo-I_N; 1.
DR   PRINTS; PR00416; EUTPISMRASEI.
DR   SUPFAM; SSF55869; SSF55869; 1.
DR   SUPFAM; SSF56349; SSF56349; 1.
DR   PROSITE; PS00176; TOPOISOMERASE_I_EUK; 1.
PE   3: Inferred from homology;
KW   DNA-binding; Isomerase; Late protein; Reference proteome; Topoisomerase.
FT   CHAIN           1..314
FT                   /note="DNA topoisomerase 1"
FT                   /id="PRO_0000145213"
FT   ACT_SITE        273
FT                   /note="O-(3'-phospho-DNA)-tyrosine intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10130"
FT   SITE            167
FT                   /note="Involved in religation"
FT                   /evidence="ECO:0000250|UniProtKB:P32989"
SQ   SEQUENCE   314 AA;  36999 MW;  AF602490AD148161 CRC64;
     MRAFTYKDGK LYEDKELTIP VHCSNPTYEI LKHVKIPSHL TDVIVYEQTY EQSLSRLIFV
     GLDSKGRRQY FYGKMHVQRR NSARDTIFIK VHRVIDKIHK FIDDTIEHKN DVLFQLGVFM
     LMETSFFIRM GKVKYLKEND TVGLLTLKNK NIVRENRKIL IHFVGKDKII HNFTVHSSNR
     LYKPLLRLIG RKEPDSFLFH KLSEKKVYKA VQQFGIRLKD LRTYGVNYTF LYNFWTNVKS
     LNPIPPIKKM ISTSIKQTAD IVGHTPSISK RAYIANTVLE YLTHDSELIN TIRDISFDEF
     IRLITDYITN TQTV