TOP1_DAUCA
ID TOP1_DAUCA Reviewed; 790 AA.
AC P93119;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 25-MAY-2022, entry version 102.
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 Daucus carota (Wild carrot).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Apiales; Apiaceae; Apioideae; Scandiceae; Daucinae;
OC Daucus; Daucus sect. Daucus.
OX NCBI_TaxID=4039;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Lunga di Amsterdam;
RX PubMed=8996105; DOI=10.1016/s0378-1119(96)00557-4;
RA Balestrazzi A., Toscano I., Bernacchia G., Luo M., Otte S., Carbonera D.;
RT "Cloning of a cDNA encoding DNA topoisomerase I in Daucus carota and
RT expression analysis in relation to cell proliferation.";
RL Gene 183:183-190(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. 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 -!- 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.
CC -!- SIMILARITY: Belongs to the type IB topoisomerase family. {ECO:0000305}.
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DR EMBL; U60440; AAB41401.1; -; mRNA.
DR PIR; JC5749; JC5749.
DR AlphaFoldDB; P93119; -.
DR SMR; P93119; -.
DR GO; GO:0005694; C:chromosome; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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; 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 DNA-binding; Isomerase; Nucleus; Topoisomerase.
FT CHAIN 1..790
FT /note="DNA topoisomerase 1"
FT /id="PRO_0000145207"
FT REGION 1..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 426..427
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT REGION 490..495
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT REGION 581..583
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT COMPBIAS 1..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..43
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..69
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..152
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 153..171
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 179..194
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 749
FT /note="O-(3'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10130"
FT SITE 412
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT SITE 444
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT SITE 502
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT SITE 528
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT SITE 570
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT SITE 632
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT SITE 650
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
SQ SEQUENCE 790 AA; 89771 MW; CE1D7DA3FF3291F5 CRC64;
MKSNPGITVI KQNASNVMEK TLKEEGQSRS NSEDSDDDKP LSHKLSSGAL NGNSHHIRMG
SNLSCPSPYT SPKPRIIKGP EDEMLLSSEL QLNAGASNAE SSDSDESKPL ASELEDPSSS
LNKRPLIQPK NSDPSPSKKA KLSEPSAPTN RKLKTAEQEE AAADDDPSIS NRNKKSTTPA
SKVSDKKKRP DVSASVNKVD FSKSLKVPLV LVKGRNGQPL VHNGVIFPPL YKPHGVKMLY
RENPVDLTPE QEEVATMFAV MLETEYMTKP KFRENFMSDW RKILGEKHII QNLEDCDFTP
IYEWHQREKE KKKQMSTDEK KAIKEGKDET RKEKYMWAVV DGMSREKVGN FRVGTTRVVQ
RSWRASKDPQ VKKNVYSQID ITINIGKDAP IPEPPIPGER WKEIRHDNTV TWLAFWNDPI
NPKEFKYVFL AASSSLKGKV TREKYEKSRK LKDYIEGIRA AAYTKDFASK DSKKRQIAVA
TYLIDKLALR AGNEKDDDEA DTVGCCTLKV ENVETKRPNI LKFDFLGKDS IRYQNEVEVE
PRVFSAIEQF RSGKEGGDDL FDQLDTSKLN AHLKELMPGL TAKVFRTYNA SITLDEMVRC
KLLSRETKGG DVAEKVVVYQ HANKEVAIIC NHQRTVSKSH SAQMVRLNEK IEELKGLLKE
LQEDLTRVNK GKPPLKNSDG KPKRNLNLKR YKGKLLKLIQ KLRKWSETRR LSVTKKIAQT
NTKIEKMERD KETKEDLKTV ALGTSKINYL DPRITVAWCK RHDVPIEKIF NKSLLAKFAW
AMDVVLIFRF
