TOP1_USTMA
ID TOP1_USTMA Reviewed; 1019 AA.
AC P41511; A0A0D1C9J7; Q4P462;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 2.
DT 25-MAY-2022, entry version 134.
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=UMAG_05101;
OS Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX NCBI_TaxID=237631;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 90884 / UCM005;
RX PubMed=7937091; DOI=10.1093/nar/22.18.3773;
RA Gerhold D., Thiyagarajan M., Kmiec E.B.;
RT "The topoisomerase I gene from Ustilago maydis: sequence, disruption and
RT mutant phenotype.";
RL Nucleic Acids Res. 22:3773-3778(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=521 / FGSC 9021;
RX PubMed=17080091; DOI=10.1038/nature05248;
RA Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J.,
RA Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H.,
RA Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G.,
RA Snetselaar K., McCann M., Perez-Martin J., Feldbruegge M., Basse C.W.,
RA Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L.,
RA Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L.,
RA Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N.,
RA Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B.,
RA Meng S., Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J.,
RA Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P.,
RA Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G.,
RA Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A.,
RA Chen F., Vysotskaia V., Mannhaupt G., Gueldener U., Muensterkoetter M.,
RA Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M.,
RA Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E.,
RA Birren B.W.;
RT "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT maydis.";
RL Nature 444:97-101(2006).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=521 / FGSC 9021;
RA Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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 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; L32017; AAC37415.1; -; Genomic_DNA.
DR EMBL; CM003143; KIS70027.1; -; Genomic_DNA.
DR PIR; S53694; S53694.
DR RefSeq; XP_011388171.1; XM_011389869.1.
DR AlphaFoldDB; P41511; -.
DR SMR; P41511; -.
DR STRING; 5270.UM05101P0; -.
DR EnsemblFungi; KIS70027; KIS70027; UMAG_05101.
DR GeneID; 23565081; -.
DR KEGG; uma:UMAG_05101; -.
DR VEuPathDB; FungiDB:UMAG_05101; -.
DR eggNOG; KOG0981; Eukaryota.
DR HOGENOM; CLU_009193_1_0_1; -.
DR InParanoid; P41511; -.
DR OMA; INEWHLR; -.
DR OrthoDB; 303947at2759; -.
DR Proteomes; UP000000561; Chromosome 4.
DR GO; GO:0005694; C:chromosome; IEA:InterPro.
DR GO; GO:0005730; C:nucleolus; IBA:GO_Central.
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; IBA:GO_Central.
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; IBA:GO_Central.
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 3: Inferred from homology;
KW DNA-binding; Isomerase; Reference proteome; Topoisomerase.
FT CHAIN 1..1019
FT /note="DNA topoisomerase 1"
FT /id="PRO_0000145210"
FT REGION 1..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 379..380
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT REGION 442..447
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT REGION 556..558
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT REGION 716..737
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 843..890
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 940..1019
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..58
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..79
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..136
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 722..737
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 843..868
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 981..998
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 822
FT /note="O-(3'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10130"
FT SITE 317
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT SITE 366
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT SITE 397
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT SITE 454
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT SITE 480
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT SITE 545
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT SITE 613
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT SITE 632
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT CONFLICT 181
FT /note="P -> A (in Ref. 1; AAC37415)"
FT /evidence="ECO:0000305"
FT CONFLICT 197
FT /note="W -> C (in Ref. 1; AAC37415)"
FT /evidence="ECO:0000305"
FT CONFLICT 341
FT /note="A -> G (in Ref. 1; AAC37415)"
FT /evidence="ECO:0000305"
FT CONFLICT 434
FT /note="W -> C (in Ref. 1; AAC37415)"
FT /evidence="ECO:0000305"
FT CONFLICT 452
FT /note="A -> T (in Ref. 1; AAC37415)"
FT /evidence="ECO:0000305"
FT CONFLICT 1011
FT /note="E -> G (in Ref. 1; AAC37415)"
FT /evidence="ECO:0000305"
FT CONFLICT 1017
FT /note="A -> S (in Ref. 1; AAC37415)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1019 AA; 115545 MW; 7E89EDE7201E7FA2 CRC64;
MNSIQVKNEP MLASFASTST NGKAKRSAKP SLFSGSEVSS DDDEEKPLAK RPKVEDSDSD
APLTSTVSSQ NGVQKRSGSS NNDDNDDDSD SDSDAPLTAL VKKSNGSDDD EDDDDDDDEG
DDDDEEDDDD DDDDDDKPLS KSSKSNRKPP KTMSITGSGE KKWDVLIHKG PRFPDPYQPL
PKDVKLKYDG RPVDLPWQTE EIAMFYAVKL ETQHAQNAIF NRNFFDDFKT DLKKYPPRDG
TQIKSFDKLD FRDMYNYWRS LKDAELERKK ALAPSARKRE IEERKAEETK WKICLVDGVE
QRVGNVNVEP PGLFLGRGAH PKAGKVKRRI SPGDITINHS ADHPAPQPPA GMGDWAEVVE
KKDVTWLAYW KENINGQYKY VFLDATSNFK TNSDREKFEK ARKLDTVVKQ IRRDVNKNLK
SKVRHERQIA TIVWLIDNFS LRAGNEKGED EAETYGVCSL RCEHAQIKMP DTIHLEFLGK
DSMKFEEDLK ITNPDVFKNI AMFLKSNGMK DKSGNYVRKK PSDPIFCAPE SGSGKMQPLQ
PNSVNQFLSK YMKGLSAKVF RTYNASVTFQ GLLEQTEEWL KSRPNAAERE INQTNLRLAY
NEANRQVAIL CNHQKTVNPM LLNRNLERTQ DKIFQIRYEI MKEQQKILTF HKVSELKKEF
KVKEHPFMKQ FDKIMQKQDL DAEKVKQYEE QMISDKKSKL ESTFKRQQSE LQYQLEQKGL
TGDDGTPKKG KKAKNVEEEV RSSIKGFKDK KQVDEELKAL NETAKRLEKE RKTNKSQATS
CNFVSSAKKI LSKYEMIKKQ EAELVNKNNT SDVALSTSKL NYIDPRITLA WLKEWDDRLS
DLGQGKAAPK KKVKKEEEEN DIKPKKKDAK GAASKKRAAK TGLANSTGDS EKMELGLQVM
NISQFFANAL QKKFKWAASG DDGRDISAKW VFVKDAQSKM RKLDSAERKG QKGGSMAAMT
DAADSKEAQP KVNCVLKKQT SADRKMSKPI KAVDKTEESD DDLSSDSSDD EDKPLAAVV
