ID A0A2T2NDB5_CORCC Unreviewed; 906 AA.
AC A0A2T2NDB5;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=BS50DRAFT_612606 {ECO:0000313|EMBL:PSN63423.1};
OS Corynespora cassiicola Philippines.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Corynesporascaceae; Corynespora.
OX NCBI_TaxID=1448308 {ECO:0000313|EMBL:PSN63423.1, ECO:0000313|Proteomes:UP000240883};
RN [1] {ECO:0000313|EMBL:PSN63423.1, ECO:0000313|Proteomes:UP000240883}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Philippines {ECO:0000313|EMBL:PSN63423.1,
RC ECO:0000313|Proteomes:UP000240883};
RX PubMed=29551995; DOI=10.3389/fmicb.2018.00276;
RA Lopez D., Ribeiro S., Label P., Fumanal B., Venisse J.S., Kohler A.,
RA de Oliveira R.R., Labutti K., Lipzen A., Lail K., Bauer D., Ohm R.A.,
RA Barry K.W., Spatafora J., Grigoriev I.V., Martin F.M., Pujade-Renaud V.;
RT "Genome-Wide Analysis of Corynespora cassiicola Leaf Fall Disease Putative
RT Effectors.";
RL Front. Microbiol. 9:276-276(2018).
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 EMBL; KZ678140; PSN63423.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T2NDB5; -.
DR STRING; 1448308.A0A2T2NDB5; -.
DR Proteomes; UP000240883; 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; 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.
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:UP000240883};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029,
KW ECO:0000256|RuleBase:RU365101}.
FT DOMAIN 428..878
FT /note="DNA topoisomerase I eukaryotic-type"
FT /evidence="ECO:0000259|SMART:SM00435"
FT REGION 1..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 790..852
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 62..84
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..123
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..195
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..220
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 231..250
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 906 AA; 103194 MW; 8D77BA5EFDCF9083 CRC64;
MSSSDDDTPL VKGRTNGVTK SDERIPKTID NAMDKQLPSN GHVEPGVSIR MGPVEDMEVD
SPATNGNVNG KRKARASLTN GKTYKEESSS EEDQPLSKRR RTSQQNKNFK EESESELSDV
PLRARKPPRA TAAQIGDSSD SDTPLNAKLV KEKASIEKAA EKEAKNIRNK EKAAAKRKPK
AESESEDDVP LAKKKKPAKK AANGVKKEES DSDAPLAKKK APAKKAIKVK AESATPVKKG
KVKGKEETEQ DREADEEEEE YRWWEAQAVG DGTKKWTTLE HNGVVFPPEY EPLPKHVKLI
YDGVPVTLQK DAEEVATFYG SMLNSTHNVE NPTFNKNFFE DFKAILDKTG HGKDKNGNTV
KIKQFEKCDF KPIFEWFEAE RAKKKALPAS EKKALKAEKD AAEAPYMYCT WDGRKQKVGN
FRVEPPSLFR GRGEHPKTGR VKKRVMPEQI TINIGKEAKV PDPPAGHSWK EVKHDQEGTW
LAMWQENING AYKYVMLAAN SDIKGQSDFK KFEKARELKK HIDRIRKDYQ RELKSEKMAD
RQRATAIYLI DQFALRAGNE KGEDEAETVG CCSLKYQHIT LKPPNYVIFD FLGKDSIRFY
DEVQVDPQVF KNLKIFKKAP KAEGDDIFDR LTTSALNKHL TSYMPGLTAK VFRTYNASWT
MARLLKDMKA TGTIAEKVKA YNDANREVAI LCNHKRTVAA GHAGSIEKMQ EKINGLRYQL
WRTKQMMIDV DPKIKKKKGA DYFARPEDLT DEWVKQHQES LVEEQRQKIQ KKFEKDNEKL
KADGEKEMKA KELDERLEVA EDLAKKFKKE NKTGKVEAEG KGPTIDKLET QVDKLNQRIE
TMRVQMEDKE GNKEVALGTS KINYIDPRLT VVFSKKFDVP IERFFSKTLR EKFDWAIKSV
DEDWEF
//
