ID M0ZKN5_SOLTU Unreviewed; 905 AA.
AC M0ZKN5;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=DNA topoisomerase I {ECO:0000256|RuleBase:RU365101};
DE EC=5.6.2.1 {ECO:0000256|RuleBase:RU365101};
DE AltName: Full=DNA topoisomerase 1 {ECO:0000256|RuleBase:RU365101};
GN Name=102586125 {ECO:0000313|EnsemblPlants:PGSC0003DMT400002790};
OS Solanum tuberosum (Potato).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX NCBI_TaxID=4113 {ECO:0000313|EnsemblPlants:PGSC0003DMT400002790, ECO:0000313|Proteomes:UP000011115};
RN [1] {ECO:0000313|Proteomes:UP000011115}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DM1-3 516 R44 {ECO:0000313|Proteomes:UP000011115};
RX PubMed=21743474; DOI=10.1038/nature10158;
RG The Potato Genome Sequencing Consortium;
RT "Genome sequence and analysis of the tuber crop potato.";
RL Nature 475:189-195(2011).
RN [2] {ECO:0000313|EnsemblPlants:PGSC0003DMT400002790}
RP IDENTIFICATION.
RC STRAIN=DM1-3 516 R44 {ECO:0000313|EnsemblPlants:PGSC0003DMT400002790};
RG EnsemblPlants;
RL Submitted (JUN-2015) to UniProtKB.
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 the specific target site
CC 5'-[CT]CCTTp site in duplex DNA. The scissile phosphodiester is
CC attacked by the catalytic tyrosine of the enzyme, resulting in the
CC formation of a DNA-(3'-phosphotyrosyl)-enzyme intermediate and the
CC expulsion of a 5'-OH DNA strand. The free DNA strand then undergoes
CC passage around the unbroken strand thus removing DNA supercoils.
CC Finally, in the religation step, the DNA 5'-OH attacks the covalent
CC intermediate to expel the active-site tyrosine and restore the DNA
CC phosphodiester backbone. {ECO:0000256|RuleBase:RU365101}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP-independent breakage of single-stranded DNA, followed by
CC passage and rejoining.; EC=5.6.2.1;
CC Evidence={ECO:0000256|ARBA:ARBA00000213,
CC ECO:0000256|RuleBase:RU365101};
CC -!- SIMILARITY: Belongs to the type IB topoisomerase family.
CC {ECO:0000256|ARBA:ARBA00006645, ECO:0000256|RuleBase:RU365101}.
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DR RefSeq; XP_006364175.2; XM_006364113.2.
DR AlphaFoldDB; M0ZKN5; -.
DR STRING; 4113.M0ZKN5; -.
DR PaxDb; 4113-PGSC0003DMT400002790; -.
DR EnsemblPlants; PGSC0003DMT400002790; PGSC0003DMT400002790; PGSC0003DMG400001083.
DR GeneID; 102586125; -.
DR Gramene; PGSC0003DMT400002790; PGSC0003DMT400002790; PGSC0003DMG400001083.
DR Gramene; RHC07H1G1563.2.1; RHC07H1G1563.2.1; RHC07H1G1563.2.
DR KEGG; sot:102586125; -.
DR eggNOG; KOG0981; Eukaryota.
DR HOGENOM; CLU_009193_1_2_1; -.
DR InParanoid; M0ZKN5; -.
DR OMA; KHEYEDD; -.
DR OrthoDB; 10940at2759; -.
DR Proteomes; UP000011115; Unassembled WGS sequence.
DR ExpressionAtlas; M0ZKN5; baseline.
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-UniRule.
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 CDD; cd00660; Topoisomer_IB_N; 1.
DR Gene3D; 1.10.132.10; -; 1.
DR Gene3D; 2.170.11.10; DNA Topoisomerase I, domain 2; 1.
DR Gene3D; 1.10.10.41; Yeast DNA topoisomerase - domain 1; 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 PANTHER; PTHR10290:SF23; DNA TOPOISOMERASE 1; 1.
DR PANTHER; PTHR10290; DNA TOPOISOMERASE I; 1.
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; DNA breaking-rejoining enzymes; 1.
DR SUPFAM; SSF56741; Eukaryotic DNA topoisomerase I, N-terminal DNA-binding fragment; 1.
DR PROSITE; PS00176; TOPOISOMERASE_I_EUK; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU365101};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|RuleBase:RU365101};
KW Reference proteome {ECO:0000313|Proteomes:UP000011115};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029,
KW ECO:0000256|RuleBase:RU365101}.
FT DOMAIN 502..878
FT /note="DNA topoisomerase I eukaryotic-type"
FT /evidence="ECO:0000259|SMART:SM00435"
FT REGION 1..362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 452..479
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 781..808
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 25..105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..120
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..148
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..200
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..215
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..235
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..287
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..305
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 310..331
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..348
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 905 AA; 100707 MW; 8141AB7660B677B5 CRC64;
MAVEAFAKTN LMEDIDDDDD MPLVFKRSST TSKQNQSNSS SQKQDGRSGR QVPDVRSPNG
QSSSTHKVKT AASSKASPAV SPLTSPKAAP LSSRTSPAPN FRTSPAPNSR TPPAPNSRTS
PAPNSRPSSS AGNQAKNVNQ QSNIAPKESK QAIEPKSEPN DEAEDSEDDK PLSARVPSGL
SKSNSIHANN VLGTSTSVQK SRPPKKEDSD DEIPLASRFQ MKSSAGASTS KFSSSEEVKP
KIRQNGLPSA TVLSKRPPGE VKSAAQASVK KPRLSDASTP VSSKQPSVKT EKKTEDDDDE
VPLSQRIKKA VASASASASK VSSVKKATKV VSSSMKKTKK KLKKPKYSKS SKLQPSSGDG
QKWTTLEHNG VIFPPPYKPH GVKMLYKGKP VDLTPEQEEV ATMYAVMLDT EYLTKQQFKE
NFMNDWRKIL GKNHVIQKLE ECNFTPIYEW HQSEKEKKKQ MSSEEKKALR EEKLKQEEKY
MWAIVDGVKE KVGNFRVEPP GLFRGRGEHP KMGKLKRRIR PNDITINIGK GVPVPECPIP
GQRWKEVRHD NTVTWLAFWN DPINPREFKY VFLAASSSLK GQSDKEKYEK ARRLKDYIEG
IRSAYTKDFT SKDPVKRQIA VATYLIDKLA LRAGNEKDDD EADTVGCCTL KVENVEPVPP
NILKFDFLGK DSIRYQNEVA VYEPVFKAIQ QFRSGKKGGD DLFDKLDTSK LNAHLKELMP
GLTAKVFRTY NASFTLEQQL TKLTQGGELA DKVAVYNVAN KEVAIICNHQ RTVSKSHSVQ
ISRLNEKIDE LKAILEEFKV DLARAKKGKP PVKGADGKAK RNLTPEALQK KIDQTNVKID
NIERQIETKE ELKTVALGTS KINYLDPRIT VAWCKRHEVP IEKMFNKSLL AKFAWAMDVE
PSFTF
//
