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Database: UniProt
Entry: A0A2S4KSM0_9HYPO
LinkDB: A0A2S4KSM0_9HYPO
Original site: A0A2S4KSM0_9HYPO 
ID   A0A2S4KSM0_9HYPO        Unreviewed;       661 AA.
AC   A0A2S4KSM0;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   22-FEB-2023, entry version 17.
DE   RecName: Full=DNA topoisomerase {ECO:0000256|ARBA:ARBA00012891, ECO:0000256|RuleBase:RU362092};
DE            EC=5.6.2.1 {ECO:0000256|ARBA:ARBA00012891, ECO:0000256|RuleBase:RU362092};
GN   ORFNames=TPAR_06602 {ECO:0000313|EMBL:POR33202.1};
OS   Tolypocladium paradoxum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Tolypocladium.
OX   NCBI_TaxID=94208 {ECO:0000313|EMBL:POR33202.1, ECO:0000313|Proteomes:UP000237481};
RN   [1] {ECO:0000313|EMBL:POR33202.1, ECO:0000313|Proteomes:UP000237481}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRBC 100945 {ECO:0000313|EMBL:POR33202.1,
RC   ECO:0000313|Proteomes:UP000237481};
RA   Quandt C.A., Patterson W., Spatafora J.W.;
RT   "Harnessing the power of phylogenomics to disentangle the directionality
RT   and signatures of interkingdom host jumping in the parasitic fungal genus
RT   Tolypocladium.";
RL   Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Introduces a single-strand break via transesterification at a
CC       target site in duplex DNA. Releases the supercoiling and torsional
CC       tension of DNA introduced during the DNA replication and transcription
CC       by transiently cleaving and rejoining one strand of the DNA duplex. The
CC       scissile phosphodiester is attacked by the catalytic tyrosine of the
CC       enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme
CC       intermediate and the expulsion of a 3'-OH DNA strand.
CC       {ECO:0000256|RuleBase:RU362092}.
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:RU362092};
CC   -!- SIMILARITY: Belongs to the type IA topoisomerase family.
CC       {ECO:0000256|ARBA:ARBA00009446, ECO:0000256|RuleBase:RU362092}.
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:POR33202.1}.
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DR   EMBL; PKSG01000719; POR33202.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S4KSM0; -.
DR   STRING; 94208.A0A2S4KSM0; -.
DR   OrthoDB; 166270at2759; -.
DR   Proteomes; UP000237481; Unassembled WGS sequence.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003917; F:DNA topoisomerase type I (single strand cut, ATP-independent) activity; IEA:UniProtKB-EC.
DR   GO; GO:0006265; P:DNA topological change; IEA:InterPro.
DR   CDD; cd00186; TOP1Ac; 1.
DR   CDD; cd03362; TOPRIM_TopoIA_TopoIII; 1.
DR   Gene3D; 3.40.50.140; -; 1.
DR   Gene3D; 1.10.460.10; Topoisomerase I, domain 2; 1.
DR   Gene3D; 2.70.20.10; Topoisomerase I, domain 3; 1.
DR   Gene3D; 1.10.290.10; Topoisomerase I, domain 4; 1.
DR   InterPro; IPR000380; Topo_IA.
DR   InterPro; IPR003601; Topo_IA_2.
DR   InterPro; IPR013497; Topo_IA_cen.
DR   InterPro; IPR013824; Topo_IA_cen_sub1.
DR   InterPro; IPR013825; Topo_IA_cen_sub2.
DR   InterPro; IPR013826; Topo_IA_cen_sub3.
DR   InterPro; IPR023405; Topo_IA_core_domain.
DR   InterPro; IPR003602; Topo_IA_DNA-bd_dom.
DR   InterPro; IPR006171; TOPRIM_domain.
DR   InterPro; IPR034144; TOPRIM_TopoIII.
DR   PANTHER; PTHR11390:SF21; DNA TOPOISOMERASE 3-ALPHA; 1.
DR   PANTHER; PTHR11390; PROKARYOTIC DNA TOPOISOMERASE; 1.
DR   Pfam; PF01131; Topoisom_bac; 1.
DR   Pfam; PF01751; Toprim; 1.
DR   PRINTS; PR00417; PRTPISMRASEI.
DR   SMART; SM00437; TOP1Ac; 1.
DR   SMART; SM00436; TOP1Bc; 1.
DR   SMART; SM00493; TOPRIM; 1.
DR   SUPFAM; SSF56712; Prokaryotic type I DNA topoisomerase; 1.
DR   PROSITE; PS50880; TOPRIM; 1.
PE   3: Inferred from homology;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU362092};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|RuleBase:RU362092};
KW   Reference proteome {ECO:0000313|Proteomes:UP000237481};
KW   Topoisomerase {ECO:0000256|ARBA:ARBA00023029,
KW   ECO:0000256|RuleBase:RU362092}.
FT   DOMAIN          2..148
FT                   /note="Toprim"
FT                   /evidence="ECO:0000259|PROSITE:PS50880"
FT   REGION          532..572
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   661 AA;  73656 MW;  188D3AEA06E8215A CRC64;
     MRVLCVAEKP SISKAVAGHL SGGSLSTRNT RNQYIKNYSF TFDFQQSWGQ CEVTMTCVSG
     HLTHIEFTDE YRNWSHPPPE ALFSAPVITS IHDDKKTIAE NIENEAKYAR LLVIWTDCDR
     EGEHIGQEIV DAARKGNAGI PVKRARFSNV ERAHVLSAAR RLANLDGKQV NAVSTRIELD
     LRIGYAFSRF MTNSLRPLGG PMAELTLSYG SCQFPTLGFV VDRYFRVRNF VPEPFWGIRL
     THKKEGKAVN FSWARSRLFD RMTTVILYER CLAAKKAKVT KVQEKPTRNF KPLPLTTVEL
     QKAATRLLRM SGQQAMTIAE GLYNKGFISY PRTETDRFDK GMNLKALVQK QTPDQRWGQF
     AQGLVDGAFH QPREGRHDDK AHPPIHPITY AAPTVLSFDE GRLYEYVVRR FLACCSDDAK
     GMATDVDVQY GDEKFSARGV IVLERNYLDV FIYDKWENTA ELPNFTRGEE FEPTEAMMTE
     GKTSPPGYLT EADLISLMDA NGIGTDATMA EHIQKIQDRE YVATIARGGV AIGGGNGDEP
     DDASPARGGR GRGGGRGGRG GGSAAAGGRR GGGQKVLIPT QLGVALILGF DRMNFETSLG
     KPFLRKEMEL KMKAICEGNT TREVVLRESI AQYKQVFLQS QEQLGVLRRA CREFVFGQSV
     S
//
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