TOP1_XENLA
ID TOP1_XENLA Reviewed; 829 AA.
AC P41512;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 116.
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;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8836188; DOI=10.1093/nar/24.18.3593;
RA Pandit S.D., Richard R.E., Sternglanz R., Bogenhagen D.F.;
RT "Cloning and characterization of the gene for the somatic form of DNA
RT topoisomerase I from Xenopus laevis.";
RL Nucleic Acids Res. 24:3593-3600(1996).
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. May play a role in the circadian transcription of the core
CC circadian clock component ARNTL/BMAL1. {ECO:0000250|UniProtKB:P11387}.
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. {ECO:0000250|UniProtKB:P11387}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P11387}.
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; L07777; AAB36608.1; -; mRNA.
DR PIR; S72366; S72366.
DR RefSeq; NP_001084031.1; NM_001090562.1.
DR AlphaFoldDB; P41512; -.
DR SMR; P41512; -.
DR BioGRID; 100588; 1.
DR MaxQB; P41512; -.
DR PRIDE; P41512; -.
DR GeneID; 399263; -.
DR KEGG; xla:399263; -.
DR CTD; 399263; -.
DR Xenbase; XB-GENE-950006; top1.1.L.
DR OrthoDB; 303947at2759; -.
DR Proteomes; UP000186698; Chromosome 9_10L.
DR Bgee; 399263; Expressed in gastrula and 19 other tissues.
DR GO; GO:0005694; C:chromosome; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003917; F:DNA topoisomerase type I (single strand cut, ATP-independent) activity; IEA:UniProtKB-EC.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISS:UniProtKB.
DR GO; GO:0006338; P:chromatin remodeling; ISS:UniProtKB.
DR GO; GO:0032922; P:circadian regulation of gene expression; ISS:UniProtKB.
DR GO; GO:0006265; P:DNA topological change; IEA:InterPro.
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 2: Evidence at transcript level;
KW Biological rhythms; DNA-binding; Isomerase; Nucleus; Reference proteome;
KW Topoisomerase.
FT CHAIN 1..829
FT /note="DNA topoisomerase 1"
FT /id="PRO_0000145204"
FT REGION 1..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 481..482
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT REGION 544..549
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT REGION 641..643
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT COMPBIAS 33..164
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..248
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 779
FT /note="O-(3'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10130"
FT SITE 372
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT SITE 420
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT SITE 468
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT SITE 499
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT SITE 557
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT SITE 588
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT SITE 630
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT SITE 688
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT SITE 706
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
SQ SEQUENCE 829 AA; 98231 MW; 8D1FE4252A916219 CRC64;
MSEDHVQNDS QIEAVFRVND SHKHKKDKEH RHKEHKKDKD REKSKHNNSE HRDPSEKKHK
DKHKNNDKHR EKDGEKHRER DGEKHRDKNG EKHRDGEKHK EKDIEKHKEV EKHRVKDGEK
HKEKDVEKHK EKDVEKHRDG EKHKHRDKDR EKKKEEKMKS SSGGVKVKKE NGFSSPVRVK
DEPEDQGFYV SPKENKAMKR PREDDEDYKP KKIKSEDDKK GKKRKQEEED IKPKKKSKAK
GNEEGVKKKK VKKEEEEKWK WWEEERHRDG IKWKFLEHKG PVFAPPYEPV PDNVKFYYDG
NLVKLSPKAE EVATFFAKML DHEYTTKDIF RKNFFKDWKK EMTTDERNLI TNLSKCDFNA
MSLYFKEQSE ARKNMTKEEK LKIKAENERL LQEYGYCIMD NHKERIANFR IEPPGLFRGR
GDHPKMGKLK KRIMPEDIII NCSKDSKIPV APAGHKWKEV RHDGKVTWLV SWTENIQGSI
KYIMLNPSSR IKGEKDWQKY ETARRLKMCV EKIRNTYKED WKSKEMKVRQ RAVALYFIDK
LALRAGNEKE EGETADTVGC CSLRVEHINL FQELDGQEFV VEFDFPGKDS IRYYNKVPVE
KRVFKNLQLF MENKQPDDDL FDRLNTSILN KHLQDLMEGL TAKVFRTYNA SITLQQQLDE
LTNSDDNVPA KILSYNRANR AVAILCNHQR APPKTFEKSM MNLQGKIDAK KDQLADARRE
FKSAKADAKV RRDEKTKKLV ESKKKAVQRI EEQLMKLEVQ ATDREENKQI ALGTSKLNYL
DPRISVAWCK KYGVPIEKIY NKTQRKNLLG PSIWQTTTSN FNAEQRCFS
