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Database: UniProt
Entry: A0A3N2PMP5_9PEZI
LinkDB: A0A3N2PMP5_9PEZI
Original site: A0A3N2PMP5_9PEZI 
ID   A0A3N2PMP5_9PEZI        Unreviewed;       657 AA.
AC   A0A3N2PMP5;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   22-FEB-2023, entry version 15.
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=SODALDRAFT_345978 {ECO:0000313|EMBL:ROT35700.1};
OS   Sodiomyces alkalinus F11.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Sodiomyces.
OX   NCBI_TaxID=1314773 {ECO:0000313|EMBL:ROT35700.1, ECO:0000313|Proteomes:UP000272025};
RN   [1] {ECO:0000313|EMBL:ROT35700.1, ECO:0000313|Proteomes:UP000272025}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F11 {ECO:0000313|EMBL:ROT35700.1,
RC   ECO:0000313|Proteomes:UP000272025};
RX   PubMed=30368956; DOI=10.1111/mec.14912;
RA   Grum-Grzhimaylo A.A., Falkoski D.L., van den Heuvel J.,
RA   Valero-Jimenez C.A., Min B., Choi I.G., Lipzen A., Daum C.G., Aanen D.K.,
RA   Tsang A., Henrissat B., Bilanenko E.N., de Vries R.P., van Kan J.A.L.,
RA   Grigoriev I.V., Debets A.J.M.;
RT   "The obligate alkalophilic soda-lake fungus Sodiomyces alkalinus has
RT   shifted to a protein diet.";
RL   Mol. Ecol. 27:4808-4819(2018).
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}.
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DR   EMBL; ML119060; ROT35700.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3N2PMP5; -.
DR   STRING; 1314773.A0A3N2PMP5; -.
DR   OrthoDB; 166270at2759; -.
DR   Proteomes; UP000272025; 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:UP000272025};
KW   Topoisomerase {ECO:0000256|ARBA:ARBA00023029,
KW   ECO:0000256|RuleBase:RU362092}.
FT   DOMAIN          3..156
FT                   /note="Toprim"
FT                   /evidence="ECO:0000259|PROSITE:PS50880"
FT   REGION          528..570
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   657 AA;  74412 MW;  2CCCE25ED94DAEAE CRC64;
     MTRVLCVAEK PSISKAVAGH LAGGNPQTRN TRDQYTKNYC FDFDFGPPWN HCSVTMTAVR
     GHLTTMEFTE ANRDWRYPPP ESLFTAPIVT VVPQDKRAIA DNISQQSRYA DLLIIWTDCD
     REGENIGKEI VDASKKGNRG MRVKRAKFSN IERSHILSAA RNLVDLDDRQ ADAVDTRIEL
     DLRIGYAFTR FLTNTLRPLG GPLLDMMLSY GSCQFPTLGF VVDRYFRVKN FVPEPFWSIQ
     VTHTRENKKV RFSWDRNRLF DRLSVTVLFE RCLRAKTAKV TKVQEKPTRK FKPLPLTTVE
     LQKAATRLLR MNGQHAMKVA EELYNKGFIS YPRTETDRFS KDINLQRSVQ KQTQSEAWGQ
     YAQSLLDGAF SQPRQGRHDD KAHPPIHPVT FASPSVLSHD ERRLYEYVVR RFLACCSEDA
     KGLSTNIDLL YGDETFHAHG LVVLETNYLD VFIYEKWSDT AELPKFTQGE TFEPTEAMMT
     EGKTSAPGYL TEADLIALMD INGIGTDATM AEHIQKIQDR QYVALTDQAG QQAQAHEDDD
     SDEDAVPPAR GGRGRGGRGG GSSASRSGGA RGRLKVFIPT KLGVALIVGF DRMEFETSLG
     KPFLRREMEA QMKAICEGRT TKSAVLQQNL RQYRHVFSHT QENITTLKMA CREFVFS
//
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