SPO11_ENCCU
ID SPO11_ENCCU Reviewed; 303 AA.
AC Q8SVS9;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Probable meiosis-specific protein SPO11 homolog;
GN Name=SPO11; OrderedLocusNames=ECU04_1110;
OS Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC Encephalitozoon.
OX NCBI_TaxID=284813;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GB-M1;
RX PubMed=11719806; DOI=10.1038/35106579;
RA Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA Vivares C.P.;
RT "Genome sequence and gene compaction of the eukaryote parasite
RT Encephalitozoon cuniculi.";
RL Nature 414:450-453(2001).
CC -!- FUNCTION: Required for meiotic recombination. Mediates DNA cleavage
CC that forms the double-strand breaks (DSB) that initiate meiotic
CC recombination (By similarity). {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q57815};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TOP6A family. {ECO:0000305}.
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DR EMBL; AL590444; CAD25299.1; -; Genomic_DNA.
DR RefSeq; NP_584795.1; NM_001041145.1.
DR AlphaFoldDB; Q8SVS9; -.
DR SMR; Q8SVS9; -.
DR STRING; 284813.Q8SVS9; -.
DR GeneID; 858943; -.
DR KEGG; ecu:ECU04_1110; -.
DR VEuPathDB; MicrosporidiaDB:ECU04_1110; -.
DR HOGENOM; CLU_037229_4_0_1; -.
DR InParanoid; Q8SVS9; -.
DR OMA; MEIEIFT; -.
DR OrthoDB; 1272299at2759; -.
DR Proteomes; UP000000819; Chromosome IV.
DR GO; GO:0005694; C:chromosome; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003918; F:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006259; P:DNA metabolic process; IEA:InterPro.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR CDD; cd00223; TOPRIM_TopoIIB_SPO; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR002815; Spo11/TopoVI_A.
DR InterPro; IPR013049; Spo11/TopoVI_A_N.
DR InterPro; IPR036078; Spo11/TopoVI_A_sf.
DR InterPro; IPR034136; TOPRIM_Topo6A/Spo11.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR PANTHER; PTHR10848; PTHR10848; 1.
DR Pfam; PF04406; TP6A_N; 1.
DR PRINTS; PR01550; TOP6AFAMILY.
DR SUPFAM; SSF56726; SSF56726; 1.
PE 3: Inferred from homology;
KW DNA-binding; Hydrolase; Magnesium; Meiosis; Metal-binding; Nucleus;
KW Reference proteome; Sporulation.
FT CHAIN 1..303
FT /note="Probable meiosis-specific protein SPO11 homolog"
FT /id="PRO_0000388416"
FT ACT_SITE 57
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q9M4A2"
FT BINDING 144
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q57815"
FT BINDING 196
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q57815"
SQ SEQUENCE 303 AA; 34749 MW; BFB8D57252E1FAC2 CRC64;
MALAPTSSAI SGSLRSSMLK LLMRLKSRTL ATRLRLYEII IEMQELGITR NEREIFYMDV
NVFRTQSVVR RLVSSIASEL QISKHDLGVR NTLKGIFIGR LGFVRHHGLG MVEMSSKGGC
PQLIPDMSDI AEVLCDYKKT VVVEKDTVLQ RIASEIEREK CLEEILFVCG KGYPCKNTVL
LLKMIEHKTA VAGLFDLDPF GIHIFCIYKY GSKETPDIRV ETIMRIGVCM EDVLEKNAYK
DVFVKLNVHD LKMINRLVRF GELSADLLFL RKIDGKVEME ALFSKEPRRL RYFLFRMLER
ISS