TOP1_SCHPO
ID TOP1_SCHPO Reviewed; 814 AA.
AC P07799; Q9P7V7;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 2.
DT 25-MAY-2022, entry version 175.
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=SPBC1703.14c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=2827111; DOI=10.1093/nar/15.23.9727;
RA Uemura T., Morino K., Uzawa S., Shiozaki K., Yanagida M.;
RT "Cloning and sequencing of Schizosaccharomyces pombe DNA topoisomerase I
RT gene, and effect of gene disruption.";
RL Nucleic Acids Res. 15:9727-9739(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP ACTIVE SITE TYR-773.
RX PubMed=2547758; DOI=10.1016/s0021-9258(18)80002-3;
RA Eng W.-K., Pandit S.D., Sternglanz R.;
RT "Mapping of the active site tyrosine of eukaryotic DNA topoisomerase I.";
RL J. Biol. Chem. 264:13373-13376(1989).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52; SER-54; SER-136 AND
RP THR-138, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
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. TThe free
CC DNA strand then rotates around the intact phosphodiester bond on the
CC opposing strand, thus removing DNA supercoils. Finally, in the
CC religation step, the DNA 5'-OH attacks the covalent intermediate to
CC expel the active-site tyrosine and restore the DNA phosphodiester
CC 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 -!- SUBUNIT: Monomer.
CC -!- MISCELLANEOUS: Eukaryotic topoisomerase I and II can relax both
CC negative and positive supercoils, whereas prokaryotic enzymes relax
CC only negative supercoils.
CC -!- SIMILARITY: Belongs to the type IB topoisomerase family. {ECO:0000305}.
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DR EMBL; X06201; CAA29559.1; -; Genomic_DNA.
DR EMBL; CU329671; CAB66458.1; -; Genomic_DNA.
DR PIR; S03329; ISZPT1.
DR PIR; T50327; T50327.
DR RefSeq; NP_596209.1; NM_001022128.2.
DR AlphaFoldDB; P07799; -.
DR SMR; P07799; -.
DR BioGRID; 276575; 86.
DR STRING; 4896.SPBC1703.14c.1; -.
DR iPTMnet; P07799; -.
DR SwissPalm; P07799; -.
DR MaxQB; P07799; -.
DR PaxDb; P07799; -.
DR PRIDE; P07799; -.
DR EnsemblFungi; SPBC1703.14c.1; SPBC1703.14c.1:pep; SPBC1703.14c.
DR GeneID; 2540032; -.
DR KEGG; spo:SPBC1703.14c; -.
DR PomBase; SPBC1703.14c; top1.
DR VEuPathDB; FungiDB:SPBC1703.14c; -.
DR eggNOG; KOG0981; Eukaryota.
DR HOGENOM; CLU_009193_1_0_1; -.
DR InParanoid; P07799; -.
DR OMA; GLRYQKW; -.
DR PhylomeDB; P07799; -.
DR Reactome; R-SPO-4615885; SUMOylation of DNA replication proteins.
DR PRO; PR:P07799; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0000785; C:chromatin; NAS:PomBase.
DR GO; GO:0005829; C:cytosol; IDA:PomBase.
DR GO; GO:0005730; C:nucleolus; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0003677; F:DNA binding; IDA:PomBase.
DR GO; GO:0003917; F:DNA topoisomerase type I (single strand cut, ATP-independent) activity; IDA:PomBase.
DR GO; GO:0007059; P:chromosome segregation; IBA:GO_Central.
DR GO; GO:0006260; P:DNA replication; IBA:GO_Central.
DR GO; GO:0006265; P:DNA topological change; IMP:PomBase.
DR GO; GO:0007076; P:mitotic chromosome condensation; ISO:PomBase.
DR CDD; cd00659; Topo_IB_C; 1.
DR Gene3D; 1.10.10.41; -; 1.
DR Gene3D; 1.10.132.10; -; 1.
DR Gene3D; 2.170.11.10; -; 1.
DR Gene3D; 3.90.15.10; -; 1.
DR InterPro; IPR011010; DNA_brk_join_enz.
DR InterPro; IPR013034; DNA_topo_DNA_db_N_dom1.
DR InterPro; IPR013030; DNA_topo_DNA_db_N_dom2.
DR InterPro; IPR001631; TopoI.
DR InterPro; IPR018521; TopoI_AS.
DR InterPro; IPR025834; TopoI_C_dom.
DR InterPro; IPR014711; TopoI_cat_a-hlx-sub_euk.
DR InterPro; IPR014727; TopoI_cat_a/b-sub_euk.
DR InterPro; IPR013500; TopoI_cat_euk.
DR InterPro; IPR008336; TopoI_DNA-bd_euk.
DR InterPro; IPR036202; TopoI_DNA-bd_euk_N_sf.
DR InterPro; IPR013499; TopoI_euk.
DR Pfam; PF14370; Topo_C_assoc; 1.
DR Pfam; PF01028; Topoisom_I; 1.
DR Pfam; PF02919; Topoisom_I_N; 1.
DR PRINTS; PR00416; EUTPISMRASEI.
DR SMART; SM00435; TOPEUc; 1.
DR SUPFAM; SSF56349; SSF56349; 1.
DR SUPFAM; SSF56741; SSF56741; 1.
DR PROSITE; PS00176; TOPOISOMERASE_I_EUK; 1.
PE 1: Evidence at protein level;
KW DNA-binding; Isomerase; Phosphoprotein; Reference proteome; Topoisomerase.
FT CHAIN 1..814
FT /note="DNA topoisomerase 1"
FT /id="PRO_0000145209"
FT REGION 1..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 404..405
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT REGION 467..472
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT REGION 559..561
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT COMPBIAS 23..65
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 94..113
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..169
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 773
FT /note="O-(3'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10130,
FT ECO:0000269|PubMed:2547758"
FT SITE 343
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT SITE 391
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT SITE 422
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT SITE 479
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT SITE 505
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT SITE 548
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT SITE 605
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT MOD_RES 52
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 54
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 136
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 138
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT CONFLICT 7..8
FT /note="Missing (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 308
FT /note="Q -> E (in Ref. 1; CAA29559)"
FT /evidence="ECO:0000305"
FT CONFLICT 446
FT /note="S -> N (in Ref. 1; CAA29559)"
FT /evidence="ECO:0000305"
FT CONFLICT 698
FT /note="V -> M (in Ref. 1; CAA29559)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 814 AA; 93981 MW; 842D8D81C92CB0A3 CRC64;
MSSSDSDSVS LSIRRRQRRG SSKRISMKES DEESDSSENH PLSESLNKKS KSESDEDDIP
IRKRRASSKK NMSNSSSKKR AKVMGNGGLK NGKKTAVVKE EEDFNEIAKP SPKHKRVSKA
NGSKNGAKSA VKKEESDTDD SVPLRAVSTV SLTPYKSELP SGASTTQNRS PNDEEDEDED
YKWWTSENID DTQKWTTLEH NGVIFAPPYE PLPKNVKLIY DGNPVNLPPE AEEVAGFYAA
MLETDHAKNP VFQDNFFRDF LKVCDECNFN HNIKEFSKCD FTQMFHHFEQ KREEKKSMPK
EQKKAIKQKK DEEEEKYKWC ILDGRKEKVG NFRIEPPGLF RGRGSHPKTG SLKRRVYPEQ
ITINIGEGVP VPEPLPGHQW AEVKHDNTVT WLATWHENIN NNVKYVFLAA GSSLKGQSDL
KKYEKSRKLK DYIDDIRKGY RKDLKSELTV ERQRGTAMYL IDVFALRAGN EKGEDEADTV
GCCSLRYEHV TLKPPRTVVF DFLGKDSIRY YNEVEVDPQV FKNLKIFKRP PKKEGDLIFD
RLSTNSLNKY LTSLMDGLSA KVFRTYNASY TMAEELKKMP KNLTLADKIL FYNRANRTVA
ILCNHQRSVT KNHDVQMERF AERIKALQYQ RMRLRKMMLN LEPKLAKSKP ELLAKEEGIT
DSWIVKHHET LYELEKEKIK KKFDRENEKL AAEDPKSVLP ESELEVRLKA ADELKKALDA
ELKSKKVDPG RSSMEQLEKR LNKLNERINV MRTQMIDKDE NKTTALGTSK INYIDPRLTY
SFSKREDVPI EKLFSKTIRD KFNWAADTPP DWKW
