TOP1_VACCW
ID TOP1_VACCW Reviewed; 314 AA.
AC P68698; P08585;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 25-MAY-2022, entry version 101.
DE RecName: Full=DNA topoisomerase 1B;
DE Short=TopIB;
DE EC=5.6.2.1 {ECO:0000255|PROSITE-ProRule:PRU10130};
DE AltName: Full=DNA topoisomerase I;
DE AltName: Full=Late protein H6;
GN Name=TOP1; OrderedLocusNames=VACWR104; ORFNames=H6R;
OS Vaccinia virus (strain Western Reserve) (VACV) (Vaccinia virus (strain
OS WR)).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus; Vaccinia virus.
OX NCBI_TaxID=10254;
OH NCBI_TaxID=9913; Bos taurus (Bovine).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3021979; DOI=10.1128/jvi.60.2.436-449.1986;
RA Rosel J.L., Earl P.L., Weir J.P., Moss B.;
RT "Conserved TAAATG sequence at the transcriptional and translational
RT initiation sites of vaccinia virus late genes deduced by structural and
RT functional analysis of the HindIII H genome fragment.";
RL J. Virol. 60:436-449(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE, AND MUTAGENESIS.
RX PubMed=8393454; DOI=10.1016/s0021-9258(18)82336-5;
RA Klemperer N., Traktman P.;
RT "Biochemical analysis of mutant alleles of the vaccinia virus topoisomerase
RT I carrying targeted substitutions in a highly conserved domain.";
RL J. Biol. Chem. 268:15887-15899(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Esposito J.J., Frace A.M., Sammons S.A., Olsen-Rasmussen M., Osborne J.,
RA Wohlhueter R.;
RT "Sequencing of the coding region of Vaccinia-WR to an average 9-fold
RT redundancy and an error rate of 0.16/10kb.";
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PROTEIN SEQUENCE OF 1-22, AND IDENTIFICATION.
RX PubMed=2823264; DOI=10.1073/pnas.84.21.7478;
RA Shuman S., Moss B.;
RT "Identification of a vaccinia virus gene encoding a type I DNA
RT topoisomerase.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:7478-7482(1987).
RN [5]
RP ACTIVE SITE, AND MUTAGENESIS OF TYR-274.
RX PubMed=15755148; DOI=10.1021/ja044182z;
RA Gao R., Zhang Y., Choudhury A.K., Dedkova L.M., Hecht S.M.;
RT "Analogues of vaccinia virus DNA topoisomerase I modified at the active
RT site tyrosine.";
RL J. Am. Chem. Soc. 127:3321-3331(2005).
RN [6]
RP FUNCTION.
RX PubMed=16669621; DOI=10.1021/bi060133i;
RA Nagarajan R., Stivers J.T.;
RT "Major groove interactions of vaccinia Topo I provide specificity by
RT optimally positioning the covalent phosphotyrosine linkage.";
RL Biochemistry 45:5775-5782(2006).
RN [7]
RP FUNCTION.
RX PubMed=20187656; DOI=10.1021/bi902204v;
RA Stahley M.R., Stivers J.T.;
RT "Mechanism and specificity of DNA strand exchange catalyzed by vaccinia DNA
RT topoisomerase type I.";
RL Biochemistry 49:2786-2795(2010).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 1-77.
RX PubMed=7994576; DOI=10.1016/s0969-2126(94)00077-8;
RA Sharma A., Hanai R., Mondragon A.;
RT "Crystal structure of the amino-terminal fragment of vaccinia virus DNA
RT topoisomerase I at 1.6-A resolution.";
RL Structure 2:767-777(1994).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 81-314.
RX PubMed=9529259; DOI=10.1016/s0092-8674(00)81411-7;
RA Cheng C., Kussie P., Pavletich N., Shuman S.;
RT "Conservation of structure and mechanism between eukaryotic topoisomerase I
RT and site-specific recombinases.";
RL Cell 92:841-850(1998).
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 the specific target site
CC 5'-[CT]CCTTp site in duplex DNA. The scissile phosphodiester is
CC attacked by the catalytic tyrosine of the enzyme, resulting in the
CC formation of a DNA-(3'-phosphotyrosyl)-enzyme intermediate and the
CC expulsion of a 5'-OH DNA strand. The free DNA strand then undergoes
CC passage around the unbroken strand thus removing DNA supercoils.
CC Finally, in the religation step, the DNA 5'-OH attacks the covalent
CC intermediate to expel the active-site tyrosine and restore the DNA
CC phosphodiester backbone. {ECO:0000269|PubMed:16669621,
CC ECO:0000269|PubMed:20187656}.
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 -!- SUBCELLULAR LOCATION: Virion {ECO:0000305}.
CC -!- INDUCTION: Expressed in the late phase of the viral replicative cycle.
CC -!- SIMILARITY: Belongs to the type IB topoisomerase family. {ECO:0000305}.
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DR EMBL; M13209; AAB59842.1; -; Genomic_DNA.
DR EMBL; L13447; AAA02841.1; -; Unassigned_DNA.
DR EMBL; AY243312; AAO89383.1; -; Genomic_DNA.
DR PIR; G24481; QQVZH7.
DR RefSeq; YP_232986.1; NC_006998.1.
DR PDB; 1A41; X-ray; 2.30 A; A=81-314.
DR PDB; 1VCC; X-ray; 1.60 A; A=1-77.
DR PDBsum; 1A41; -.
DR PDBsum; 1VCC; -.
DR SMR; P68698; -.
DR DNASU; 3707560; -.
DR GeneID; 3707560; -.
DR KEGG; vg:3707560; -.
DR BRENDA; 5.6.2.1; 908.
DR EvolutionaryTrace; P68698; -.
DR Proteomes; UP000000344; 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 CDD; cd00659; Topo_IB_C; 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; 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 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; DNA-binding; Isomerase;
KW Late protein; Reference proteome; Topoisomerase; Virion.
FT CHAIN 1..314
FT /note="DNA topoisomerase 1B"
FT /id="PRO_0000145216"
FT ACT_SITE 274
FT /note="O-(3'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10130,
FT ECO:0000269|PubMed:15755148"
FT SITE 168
FT /note="Involved in religation"
FT /evidence="ECO:0000250|UniProtKB:P32989"
FT MUTAGEN 216
FT /note="G->E,K: No change in activity."
FT /evidence="ECO:0000269|PubMed:8393454"
FT MUTAGEN 217
FT /note="I->P: Temperature-sensitive for DNA relaxation in
FT vitro."
FT /evidence="ECO:0000269|PubMed:8393454"
FT MUTAGEN 220
FT /note="K->D: Loss of activity."
FT /evidence="ECO:0000269|PubMed:8393454"
FT MUTAGEN 220
FT /note="K->I,N: Reduced activity."
FT /evidence="ECO:0000269|PubMed:8393454"
FT MUTAGEN 223
FT /note="R->E,G: Loss of activity."
FT /evidence="ECO:0000269|PubMed:8393454"
FT MUTAGEN 223
FT /note="R->K: Reduced activity."
FT /evidence="ECO:0000269|PubMed:8393454"
FT MUTAGEN 224
FT /note="T->G,P: Reduced activity."
FT /evidence="ECO:0000269|PubMed:8393454"
FT MUTAGEN 225
FT /note="Y->H: No change in activity."
FT /evidence="ECO:0000269|PubMed:8393454"
FT MUTAGEN 225
FT /note="Y->R,S: Reduced activity."
FT /evidence="ECO:0000269|PubMed:8393454"
FT MUTAGEN 274
FT /note="Y->F: Complete loss of activity."
FT /evidence="ECO:0000269|PubMed:15755148"
FT STRAND 3..7
FT /evidence="ECO:0007829|PDB:1VCC"
FT STRAND 10..14
FT /evidence="ECO:0007829|PDB:1VCC"
FT HELIX 27..33
FT /evidence="ECO:0007829|PDB:1VCC"
FT STRAND 41..46
FT /evidence="ECO:0007829|PDB:1VCC"
FT HELIX 50..53
FT /evidence="ECO:0007829|PDB:1VCC"
FT STRAND 56..62
FT /evidence="ECO:0007829|PDB:1VCC"
FT STRAND 68..72
FT /evidence="ECO:0007829|PDB:1VCC"
FT HELIX 82..105
FT /evidence="ECO:0007829|PDB:1A41"
FT TURN 109..111
FT /evidence="ECO:0007829|PDB:1A41"
FT HELIX 115..125
FT /evidence="ECO:0007829|PDB:1A41"
FT HELIX 140..146
FT /evidence="ECO:0007829|PDB:1A41"
FT HELIX 150..152
FT /evidence="ECO:0007829|PDB:1A41"
FT STRAND 153..156
FT /evidence="ECO:0007829|PDB:1A41"
FT STRAND 159..162
FT /evidence="ECO:0007829|PDB:1A41"
FT STRAND 164..166
FT /evidence="ECO:0007829|PDB:1A41"
FT TURN 167..169
FT /evidence="ECO:0007829|PDB:1A41"
FT STRAND 170..172
FT /evidence="ECO:0007829|PDB:1A41"
FT STRAND 175..177
FT /evidence="ECO:0007829|PDB:1A41"
FT STRAND 180..182
FT /evidence="ECO:0007829|PDB:1A41"
FT HELIX 183..189
FT /evidence="ECO:0007829|PDB:1A41"
FT STRAND 197..200
FT /evidence="ECO:0007829|PDB:1A41"
FT HELIX 205..214
FT /evidence="ECO:0007829|PDB:1A41"
FT HELIX 219..241
FT /evidence="ECO:0007829|PDB:1A41"
FT STRAND 242..244
FT /evidence="ECO:0007829|PDB:1A41"
FT HELIX 248..263
FT /evidence="ECO:0007829|PDB:1A41"
FT HELIX 269..282
FT /evidence="ECO:0007829|PDB:1A41"
FT HELIX 288..292
FT /evidence="ECO:0007829|PDB:1A41"
FT HELIX 297..309
FT /evidence="ECO:0007829|PDB:1A41"
SQ SEQUENCE 314 AA; 36666 MW; E76FBCFCBF259D27 CRC64;
MRALFYKDGK LFTDNNFLNP VSDDNPAYEV LQHVKIPTHL TDVVVYEQTW EEALTRLIFV
GSDSKGRRQY FYGKMHVQNR NAKRDRIFVR VYNVMKRINC FINKNIKKSS TDSNYQLAVF
MLMETMFFIR FGKMKYLKEN ETVGLLTLKN KHIEISPDEI VIKFVGKDKV SHEFVVHKSN
RLYKPLLKLT DDSSPEEFLF NKLSERKVYE CIKQFGIRIK DLRTYGVNYT FLYNFWTNVK
SISPLPSPKK LIALTIKQTA EVVGHTPSIS KRAYMATTIL EMVKDKNFLD VVSKTTFDEF
LSIVVDHVKS STDG
