ID A0A1S8BJ47_9PEZI Unreviewed; 890 AA.
AC A0A1S8BJ47;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
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 ORFNames=BK809_0007583 {ECO:0000313|EMBL:OMP87496.1};
OS Diplodia seriata.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC Diplodia.
OX NCBI_TaxID=420778 {ECO:0000313|EMBL:OMP87496.1, ECO:0000313|Proteomes:UP000190776};
RN [1] {ECO:0000313|EMBL:OMP87496.1, ECO:0000313|Proteomes:UP000190776}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F98.1 {ECO:0000313|EMBL:OMP87496.1,
RC ECO:0000313|Proteomes:UP000190776};
RA Robert-Siegwald G., Vallet J., Abou-Mansour E., Xu J., Rey P., Bertsch C.,
RA Rego C., Larignon P., Fontaine F., Lebrun M.-H.;
RT "Draft genome sequence of Diplodia seriata F98.1, a fungal species involved
RT in grapevine trunk diseases.";
RL Submitted (JAN-2017) 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 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OMP87496.1}.
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DR EMBL; MSZU01000076; OMP87496.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1S8BJ47; -.
DR STRING; 420778.A0A1S8BJ47; -.
DR OrthoDB; 10940at2759; -.
DR Proteomes; UP000190776; Unassembled WGS sequence.
DR GO; GO:0005694; C:chromosome; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IEA:UniProt.
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; IEA:UniProtKB-UniRule.
DR GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-UniRule.
DR CDD; cd00659; Topo_IB_C; 1.
DR CDD; cd03488; Topoisomer_IB_N_htopoI_like; 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 InterPro; IPR048045; Topoisomer_I_DNA-bd.
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:UP000190776};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029,
KW ECO:0000256|RuleBase:RU365101}.
FT DOMAIN 412..862
FT /note="DNA topoisomerase I eukaryotic-type"
FT /evidence="ECO:0000259|SMART:SM00435"
FT REGION 1..253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 774..836
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..28
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..49
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..80
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..180
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..233
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 890 AA; 101502 MW; 85DFADCF76FEEA9A CRC64;
MSADTIPKSV DSTMDRQVPS SNGQLEVDIS IRNGPVREMD IDEPNGVANG KRKQRASING
KSYKESSSSD EDDKPLSKRR KTSSPKATSA SDSELSDVPL AKKTARQQLP PKIKAADVGE
SSDSDIPLGR KLANEKKHIE QAAEKEAKAI RAAEKKAPVK RKPQKEESES DDDIPLSKKK
KPVARKANGV KKEESDDDVP LSKKAPPAKR GKAKVAEPKK TTKAKAAAKK ETDDDDEADA
EEEEYKWWED PTKGDNSIKW QTLEHNGVVF PPEYEPLPEN VKLKYNGMPV SLHKDAEEVA
TFFGSMLNST HNVENPTFQK NFFHDFKEVL DKTGHAKGPD GKKVKIEKFD KCDFKDIYEY
YAAQREAKKA LPAAEKKALK AAKDEAEAAY MHCLWDGRKQ KVGNFRVEPP GLFRGRGEHP
KTGKVKKRVL PEQITLNIGK EAKVPPPPAG HKWKEVKHDQ TGTWLAMWQE NINGAYKYVM
LAANSDIKGQ SDFKKFEKAR ELKKHIDRIR KDYTRDLKSE VMADRQRATA VYLIDKFALR
AGNEKGEDEA DTVGCCSLKY ENITLKPPNT VVFDFLGKDS IRFYDEVEVE PQVFKNLKIF
KKAPKKDGDE VFDRLTTSGL NKYLSTYMQG LTAKVFRTYN ASYTMARLLR EMKSTGSIAE
KVKDYNEANR KVAILCNHKR TVAANHSNQI EKMQEKINGL RYQQWRVKQM MIDLDTKVKK
KKGAEYFELP EDLTQEWVEQ HQQALVEEQR DKIKKKFEKD NEKRVAEGEK EMKAKELQER
LEVADDLEKK FKKENKTKKV EAEGKGVTVD KLENKVEQLQ QRIETAKVQL EDKDNNKEVA
LGTSKINYID PRLTVVFSKK FDVPIERFFS KTLREKFDWA IKSAGEDWEF
//
