TOP1_DICDI
ID TOP1_DICDI Reviewed; 893 AA.
AC Q54RC3;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 114.
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=DDB_G0283205;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- MISCELLANEOUS: Eukaryotic topoisomerase I and II can relax both
CC negative and positive supercoils, whereas prokaryotic enzymes relax
CC only negative supercoils. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the type IB topoisomerase family. {ECO:0000305}.
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DR EMBL; AAFI02000051; EAL65841.1; -; Genomic_DNA.
DR RefSeq; XP_639222.1; XM_634130.1.
DR AlphaFoldDB; Q54RC3; -.
DR SMR; Q54RC3; -.
DR STRING; 44689.DDB0234191; -.
DR PaxDb; Q54RC3; -.
DR PRIDE; Q54RC3; -.
DR EnsemblProtists; EAL65841; EAL65841; DDB_G0283205.
DR GeneID; 8623995; -.
DR KEGG; ddi:DDB_G0283205; -.
DR dictyBase; DDB_G0283205; top1.
DR eggNOG; KOG0981; Eukaryota.
DR HOGENOM; CLU_009193_1_0_1; -.
DR InParanoid; Q54RC3; -.
DR OMA; GLRYQKW; -.
DR PhylomeDB; Q54RC3; -.
DR Reactome; R-DDI-4615885; SUMOylation of DNA replication proteins.
DR PRO; PR:Q54RC3; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0005694; C:chromosome; IEA:InterPro.
DR GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISS:dictyBase.
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; ISS:dictyBase.
DR GO; GO:0007059; P:chromosome segregation; IBA:GO_Central.
DR GO; GO:0006260; P:DNA replication; ISS:dictyBase.
DR GO; GO:0006265; P:DNA topological change; ISS:dictyBase.
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; Nucleus; Reference proteome; Topoisomerase.
FT CHAIN 1..893
FT /note="DNA topoisomerase 1"
FT /id="PRO_0000330481"
FT REGION 1..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 404..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 519..520
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT REGION 582..587
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT REGION 673..675
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT COMPBIAS 15..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..186
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 199..286
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 287..301
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 409..427
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 853
FT /note="O-(3'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10130"
FT SITE 409
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT SITE 457
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT SITE 506
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT SITE 537
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT SITE 594
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT SITE 620
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT SITE 662
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT SITE 721
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT SITE 739
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
SQ SEQUENCE 893 AA; 100612 MW; DD9BB5F99BF3331E CRC64;
MEVKQEILTP MKVEKTNGNV PTPPPTTTTT TVMDDDLFDD EASPPQPNKK LKAENGSIKK
LTPTPKPAPV TPKPTAAVNG KKPIPKKKPV DSSSDSDSSD SSSDSDSDSS DSDSDSSSSD
SSSSDSDVPK KKPISKIPNK PSGTVSKTSK NSPKTTTTTT TTTTTVKSKP APKVKPEQSS
SDDSSSDSSD DSSDDSSSDS SSEEEKPKKK PSKKPAAVKK EITVKKETTT TTKKTPVKKE
VEVKKETKTT TTKKVKKEES DDDGEDEKTT TKKKTTTRKR KLKEEEEGEE EEEEGVNKWW
DKEDDEDDGT KWTTLIHNGP VFPPAYVPHG IKFMYDGKVV KLTPKQEEVA TFYANYLETD
HVKKQAFKDN FFKEFKGLLT SEQKEIVKKM DKCDFSHIHT HLKTKKEQRK ARSKEEKDAE
TAEKKKIQEK HGFATIDGFK EKVGNYMIEP PGLFLGRGQH PKTGMLKQRI MPSDVTLNIG
EGEVIPPSPI PGEKWKEIVH NNTVTWLAFW RESVNGGFKY VWLAPSSKIK GQADRKKFEV
ARGLKNCIGD IRKGYQKSFN DESTEKRQLA VALYLIDFLA LRVGNEKGED QADTVGCCSL
RVEHIKLESN NTITLDFLGK DSMRYLNTVQ IREDAYKVLK TFVKGKKPTD LLFDSLTVTQ
LNNHLKKQMT GLSAKVFRTY NASITLQKEL DKMDTKEFQS IDEKILFYNR CNREVAILCN
HQKAPPKNLA ETMSKIDEKI QELRDLQDLC RIKIGKTPKS QQEDIESREA ERLPKLIQLA
ITNKKDKDKE KTDKEISFDV KAAFEKSRTL PDAKGKIKEK IAKYEEQIKK QEILKTGKDE
LKTVALGTSK INYLDPRITV AWCKKNKVPV DKIFTKSLRD KFPWSDVGTD YIF
