SPO11_CAEEL
ID SPO11_CAEEL Reviewed; 425 AA.
AC Q22236;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Meiotic recombination protein spo-11;
GN Name=spo-11; ORFNames=T05E11.4;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP FUNCTION.
RX PubMed=9708740; DOI=10.1016/s0092-8674(00)81481-6;
RA Dernburg A.F., McDonald K., Moulder G., Barstead R., Dresser M.,
RA Villeneuve A.M.;
RT "Meiotic recombination in C. elegans initiates by a conserved mechanism and
RT is dispensable for homologous chromosome synapsis.";
RL Cell 94:387-398(1998).
CC -!- FUNCTION: Required for meiotic recombination. Mediates DNA cleavage
CC that forms the double-strand breaks (DSB) that initiate meiotic
CC recombination. {ECO:0000269|PubMed:9708740}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Z68751; CAA92974.1; -; Genomic_DNA.
DR PIR; T24522; T24522.
DR RefSeq; NP_502081.1; NM_069680.4.
DR AlphaFoldDB; Q22236; -.
DR SMR; Q22236; -.
DR BioGRID; 56264; 2.
DR STRING; 6239.T05E11.4; -.
DR PaxDb; Q22236; -.
DR EnsemblMetazoa; T05E11.4a.1; T05E11.4a.1; WBGene00004985.
DR GeneID; 191771; -.
DR KEGG; cel:CELE_T05E11.4; -.
DR UCSC; T05E11.4; c. elegans.
DR CTD; 191771; -.
DR WormBase; T05E11.4a; CE06363; WBGene00004985; spo-11.
DR eggNOG; KOG2795; Eukaryota.
DR GeneTree; ENSGT00390000001787; -.
DR InParanoid; Q22236; -.
DR OMA; NWGEARF; -.
DR OrthoDB; 1272299at2759; -.
DR PhylomeDB; Q22236; -.
DR PRO; PR:Q22236; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00004985; Expressed in germ line (C elegans) and 4 other tissues.
DR ExpressionAtlas; Q22236; baseline and differential.
DR GO; GO:0000228; C:nuclear chromosome; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
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:0051321; P:meiotic cell cycle; IMP:WormBase.
DR GO; GO:0042138; P:meiotic DNA double-strand break formation; IBA:GO_Central.
DR GO; GO:0000706; P:meiotic DNA double-strand break processing; IMP:UniProtKB.
DR GO; GO:0007131; P:reciprocal meiotic recombination; IBA:GO_Central.
DR CDD; cd00223; TOPRIM_TopoIIB_SPO; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR013048; Meiotic_Spo11.
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; PR01551; SPO11HOMOLOG.
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.
FT CHAIN 1..425
FT /note="Meiotic recombination protein spo-11"
FT /id="PRO_0000145476"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 119
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q9M4A2"
FT BINDING 202
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q57815"
FT BINDING 255
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q57815"
SQ SEQUENCE 425 AA; 49169 MW; 47527351E558B120 CRC64;
MYEYSFNPNI DHEPGSVESQ QSTIYSDSDD SDDSFLDDEV IPPKEQAMRK IEFALADIKR
QMDNKEKSLT LRISTSKSHF CLRYTAKRKG KLDRDLHCLH QVYDLLENDK RSTKRELYYE
HKAVYGNQKY LDSSIKSICE LLNESRANLN ILSCGRGIIR GAITFLVENV GVIDARVQEV
LITDALLFSN IISEADFILV VEKDTTFQKL MDENFQAMFP RGILATSKGY PDIATRNVLK
MLSEKRKFPI YGLFDADPHG IEIYLTYKYG PTKEFAEGRG AFVPTIEWIG LFPTDFHRFT
IDQSQCLPLV RTDFVKIEKM IPRSIQLGEI VVTRELDWMI QNKFKMELES INMCGQEYMA
RFLIAPRVMS IEKEIPIQPE TIINEYHEDS QCSLSTDDDR EAKDDDYIDS DAEEKFQNMI
DNDSD