ID A0A178F6F7_TRIRU Unreviewed; 892 AA.
AC A0A178F6F7;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
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=A7C99_0855 {ECO:0000313|EMBL:OAL67724.1};
OS Trichophyton rubrum (Athlete's foot fungus) (Epidermophyton rubrum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=5551 {ECO:0000313|EMBL:OAL67724.1, ECO:0000313|Proteomes:UP000243015};
RN [1] {ECO:0000313|EMBL:OAL67724.1, ECO:0000313|Proteomes:UP000243015}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CMCC(F)T1i {ECO:0000313|Proteomes:UP000243015};
RA Zhan P., Tao Y., Liu W.;
RT "Genome sequencing of Trichophyton rubrum CMCC(F)T1i isolated from hair.";
RL Submitted (MAY-2016) 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:OAL67724.1}.
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DR EMBL; LHPM01000009; OAL67724.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A178F6F7; -.
DR VEuPathDB; FungiDB:TERG_06182; -.
DR OrthoDB; 10940at2759; -.
DR Proteomes; UP000243015; 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:UP000243015};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029,
KW ECO:0000256|RuleBase:RU365101}.
FT DOMAIN 414..864
FT /note="DNA topoisomerase I eukaryotic-type"
FT /evidence="ECO:0000259|SMART:SM00435"
FT REGION 1..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 772..838
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 19..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..85
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..110
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 137..175
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..194
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..210
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 892 AA; 100741 MW; 0399B594B466EDF1 CRC64;
MSSSDDDAPL AGARRTNGSV QKPALSSPTV PQSNDTSTNG TTTQPGISIR YGPATDNEVD
MQDAETNGVA PSKRKSRSSA GRPSYVEAES SAEDDKPLSK RRRTVPKPEP SDSDEAPLIS
QAKKGKRASV NSAEAKRLVA EKADIEKSAE KEAQSLRQQD RQAAAKKKEA AKTAAKTTKA
KATTTNGKKS QTNGIKKSES SDEDVPLARK APAKKVAATP AKKSKPAAKK EPSEEAEAEE
EEAEEEYRWW EDPSKGDGTI KWTTLEHNGV VFPPPYEPLP KDVKLKYAGV PVTLHPDAEE
VASHFGTMLN STHNVENPIF QKNFFNDFQA IIKKTGGAKD PQGKPIQIKE FSKCDFRTIF
EHYEKLRAEK KAMSAAEKKA AKAEKDAAEA PYMYCMWDGR KQKVGNFRVE PPALFRGRGE
HPKTGTVKTR VMPEQITINI GKDAPVPAPP EGHRWKEVRH DQEGTWLAMW QENVNGNYKY
VMLAANSDVK GQSDYKKFEK ARELKKHIDR IRKDYKKGLK DELMVNRQRA TAVYLIDQFA
LRAGNEKGED EADTVGCCSL KFEHVTLKPP NTVVFDFLGK DSIRYYDEVE VDPQVFKNLK
IFKKPPKKEG DEIFDRLTTS ALNKHLSSYM PGLTAKVFRT YNASYTMATL LKKMSATGTI
PEKVKQYNDA NREVAILCNH KRTVAAGHAD QMEKLSDRIK GLQYQKWRIK QMILALDPKI
KKKKGAAYFE LDEDLDMEWI KEHQAFLAEE LRQKIRKKFD KENEKRAADG EKEMKAKELE
ERLKAADELE AKYKRENKTK KVEAEGRGPT VEKFEGQISK IDQRIENMLL QAEDKENNKE
VALGTSKLNY IDPRLTVVFS KKFNVPIEKF FSKTMREKFD WAIKSVDEDW EF
//
