ID A0A317SHR9_9PEZI Unreviewed; 954 AA.
AC A0A317SHR9;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
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=C7212DRAFT_353908 {ECO:0000313|EMBL:PWW73277.1};
OS Tuber magnatum (white Piedmont truffle).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC Pezizales; Tuberaceae; Tuber.
OX NCBI_TaxID=42249 {ECO:0000313|EMBL:PWW73277.1, ECO:0000313|Proteomes:UP000246991};
RN [1] {ECO:0000313|EMBL:PWW73277.1, ECO:0000313|Proteomes:UP000246991}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=091103-1 {ECO:0000313|EMBL:PWW73277.1};
RA Murat C., Payen T., Noel B., Kuo A., Martin F.M.;
RT "Genomes of Pezizomycetes fungi and the evolution of truffles.";
RL Submitted (MAR-2018) 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:PWW73277.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; PYWC01000082; PWW73277.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A317SHR9; -.
DR STRING; 42249.A0A317SHR9; -.
DR Proteomes; UP000246991; 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; -; 2.
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:UP000246991};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029,
KW ECO:0000256|RuleBase:RU365101}.
FT DOMAIN 477..926
FT /note="DNA topoisomerase I eukaryotic-type"
FT /evidence="ECO:0000259|SMART:SM00435"
FT REGION 1..310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 873..900
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 16..44
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..145
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 154..170
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..212
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 239..300
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 954 AA; 107370 MW; ABE8C336A0E43763 CRC64;
MSSSEDDRPL AAMHGARTNG TSSTVSADTN GTTPGPTFAN KNPKSVGHET GGRFDKMANK
STNGVRPVGT AVVPLVNGSV GDSGGLGRGK RKGRQAPIKE SGSSSEDSDA PLNKRRRTSN
AIRKENGLKQ EESSSDDDVP LAKKTAAKRR NAPSPTLVKR EKKPSAPLRR DSSDSDIPLA
AAKLAKEKQR IEQKAAKTAK EIRAEENKAA TAAGAKRKPA GNANTSELAK KTGKAPLKKA
NGIKKEESSD DDVPLAKKRK GVVQKPTEST KKVAPGKKIK EVDTKPIAGK GKGKAKEETP
GEADDEEEEE YKWWENQAET DGTQKWTTLV HNGVLFPPAY EPLPKHVKMK YAGVEVTLPV
EAEEVAGFFG AMLDTQHALN PTFAENFFKD FQTILKQSGG AKGPDGKSVN ILAFQKCDFK
PMYDYFEEKK AEKKALGTAG RKALKAEKDK AEEKYLYCYL DGRKEKVGNF RVEPPGLFRG
RGEHPKTGMV KARVQPEQVT INIGKEATVP APPPGHNWAD VIHDNTVTWL ATWKENINGN
IKYVMLAATS SLKGMSDFKK FEKARELKNH IDRIREDYTR DLKSELMADR QRATAMYLID
KLALRAGNEK SDDEADTVGC CSLRYEHITL ELPNIVVFDF LGKDSIRFYQ KTPVIHQVFK
NLKIFKKAPK TKGDMIFDRL DTTQLNKHLQ NYMQGLSAKV FRTYNASWTM QEQLDEIPNE
GAVHEKYAAY NLANKKVAIL CNHQRTVSTT HEIMMQKQEE KIKGLRYQKL RLKRMILSLE
PARKKKNPTF FRPDPEIDDE EWIRDHQVFL IEQEKDRITK KFEKENEKLR ESGEKGLKDK
DLKERLQIIK EMEAEFKTEN KTGKIDPKRG ATIEKLEAQV QKMEERIKKQ ETEAQVREDN
KTVALGTSKI NYIDPRLTVM FCKKYDVPIE KIFAKTLRDK FKWAIESADE DWKF
//
