ID I3EDH5_NEMP3 Unreviewed; 853 AA.
AC I3EDH5;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 45.
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=NEQG_02607 {ECO:0000313|EMBL:EIJ87272.1};
OS Nematocida parisii (strain ERTm3) (Nematode killer fungus).
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Nematocida.
OX NCBI_TaxID=935791 {ECO:0000313|EMBL:EIJ87272.1, ECO:0000313|Proteomes:UP000002872};
RN [1] {ECO:0000313|EMBL:EIJ87272.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ERTm3 {ECO:0000313|EMBL:EIJ87272.1};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Cuomo C., Troemel E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M.,
RA Haas B., Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.,
RA Chapman S.B., Gearin G., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Heiman D., Howarth C., Larimer J., Lui A., MacDonald P.J.P., McCowen C.,
RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA Saif S., Shea T., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Nematocida parisii strain ERTm3.";
RL Submitted (JAN-2011) 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}.
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DR EMBL; GL870884; EIJ87272.1; -; Genomic_DNA.
DR AlphaFoldDB; I3EDH5; -.
DR STRING; 935791.I3EDH5; -.
DR EnsemblFungi; EIJ87272; EIJ87272; NEQG_02607.
DR VEuPathDB; MicrosporidiaDB:NEQG_02607; -.
DR HOGENOM; CLU_002929_1_1_1; -.
DR InParanoid; I3EDH5; -.
DR OMA; KGKTAYG; -.
DR Proteomes; UP000002872; 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:0008270; F:zinc ion binding; IEA:InterPro.
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; IPR023406; Topo_IA_AS.
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 InterPro; IPR010666; Znf_GRF.
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 Pfam; PF06839; zf-GRF; 2.
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; PS00396; TOPOISOMERASE_I_PROK; 1.
DR PROSITE; PS50880; TOPRIM; 1.
DR PROSITE; PS51999; ZF_GRF; 2.
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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000002872};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029,
KW ECO:0000256|RuleBase:RU362092}; Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU01343}.
FT DOMAIN 2..146
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT DOMAIN 735..774
FT /note="GRF-type"
FT /evidence="ECO:0000259|PROSITE:PS51999"
FT DOMAIN 808..848
FT /note="GRF-type"
FT /evidence="ECO:0000259|PROSITE:PS51999"
FT REGION 618..640
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 622..640
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 853 AA; 97476 MW; 7637726567FEA09A CRC64;
MRILNVAEKP SVAKSLADIL SNGRAQFSKG YNKYCSVFRF NHCIEGIPCE MVFTSVLGHL
YSLEFAKKTS WTEIDPIELF EEDIRWIIPK EMADVSRTLV HLSKDCDMLI IWTDCDREGE
NIGMQVANLV RDRIREVKRA RFSGLSKYDV MHAVENLCRL NAYESKAVES RIEIDLRIGA
ALTRLQTLQL QNILDSKSVI SYGSCQIPTL GFVCEREESI EEFVEEKNWT IEAEVQNNGE
RGVFKWERGV VYDEDYAGIK LRTISGEELV VNKVEIKKRH KSRPWPLRTV ELQKFFARGH
GVSSSHELMN IAESLYTSGY ISYPRTETDV FSSQFNYKDP LAALKGDSVL SEYAKKLVPG
RPSAGRHNDQ AHTPIYPLKA GSGLKGKERA VYEYIARRFL ACYSADAEGE EELIECQVKE
EKFIRKMLKV IKKNYLEIFI YEKWGDTEID LALKEGQTVK WAPNKKESHT NKPHLLTEAE
LIAKMDSNGI GTDATIHDHI ERIKTRMYIE MINKNSIRST WLGRSLINGY KSIGLTINQP
YLRKEFECNL KRVCSGEFPS SDLIAQEIIK YKEIYTIMEK NMPKFKEEFT KNKTSGDGGE
IEEKSQNKYT RYKKIEDSRS ITKTQTHSNI SSLKSRYQKP NSLKPEISGY SGYRAENQYD
SGENRYTKKK KEAKEPFDGI NIEGSFKTAL DINRATINDR SISDILKQKE ESCIAASDAS
NNSFVLTLPK GTIVCGCNIK AKEAIVKKEG PNKGKLFYTC SAGQCDYFGW GDSANVKKSS
EQAKPYRKEN QPAKNRNIKT VVKDSIKCEC GASAIYLLSK TEKNKNRGFF KCNKNYKPCT
FFKWEDEATQ NKN
//
