SPO11_YEAST
ID SPO11_YEAST Reviewed; 398 AA.
AC P23179; D3DKP3;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Meiosis-specific protein SPO11;
DE EC=5.6.2.2 {ECO:0000305};
DE AltName: Full=Sporulation-specific protein 11;
GN Name=SPO11; OrderedLocusNames=YHL022C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3317399; DOI=10.1073/pnas.84.22.8035;
RA Atcheson C.L., Didomenico B., Frackman S., Esposito R.E., Elder R.T.;
RT "Isolation, DNA sequence, and regulation of a meiosis-specific eukaryotic
RT recombination gene.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:8035-8039(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8091229; DOI=10.1126/science.8091229;
RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA Waterston R., Wilson R., Vaudin M.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT VIII.";
RL Science 265:2077-2082(1994).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP PROTEIN SEQUENCE OF 247-258; 323-334 AND 338-344, FUNCTION, AND SUBCELLULAR
RP LOCATION.
RX PubMed=9039264; DOI=10.1016/s0092-8674(00)81876-0;
RA Keeney S., Giroux C.N., Kleckner N.;
RT "Meiosis-specific DNA double-strand breaks are catalyzed by Spo11, a member
RT of a widely conserved protein family.";
RL Cell 88:375-384(1997).
RN [6]
RP POSSIBLE FUNCTION, AND MUTAGENESIS OF TYR-135.
RX PubMed=9121560; DOI=10.1038/386414a0;
RA Bergerat A., de Massy B., Gadelle D., Varoutas P.-C., Nicolas A.,
RA Forterre P.;
RT "An atypical topoisomerase II from Archaea with implications for meiotic
RT recombination.";
RL Nature 386:414-417(1997).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=7926789; DOI=10.1101/gad.8.9.1087;
RA Burns N., Grimwade B., Ross-Macdonald P.B., Choi E.Y., Finberg K.,
RA Roeder G.S., Snyder M.;
RT "Large-scale analysis of gene expression, protein localization, and gene
RT disruption in Saccharomyces cerevisiae.";
RL Genes Dev. 8:1087-1105(1994).
RN [8]
RP FUNCTION.
RX PubMed=11983174; DOI=10.1016/s1097-2765(02)00498-7;
RA Neale M.J., Ramachandran M., Trelles-Sticken E., Scherthan H.,
RA Goldman A.S.;
RT "Wild-type levels of Spo11-induced DSBs are required for normal single-
RT strand resection during meiosis.";
RL Mol. Cell 9:835-846(2002).
CC -!- FUNCTION: Required for meiotic recombination. Mediates DNA cleavage
CC that forms the double-strand breaks (DSB) that initiate meiotic
CC recombination. The action of SPO11 is important in setting off a
CC regulatory chain of events encompassing 5' to 3' resection. When there
CC are no SPO11-DSBs, resection of a site specific VDE-DSB takes place but
CC it is faster than in wild-type meiosis and increases the risk of
CC uncovering flanking homology. {ECO:0000269|PubMed:11983174,
CC ECO:0000269|PubMed:9039264}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP-dependent breakage, passage and rejoining of double-
CC stranded DNA.; EC=5.6.2.2; Evidence={ECO:0000305};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q57815};
CC -!- INTERACTION:
CC P23179; P33323: REC104; NbExp=7; IntAct=EBI-17705, EBI-16412992;
CC P23179; Q02793: SKI8; NbExp=9; IntAct=EBI-17705, EBI-17260;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:7926789,
CC ECO:0000269|PubMed:9039264}. Chromosome {ECO:0000269|PubMed:9039264}.
CC -!- DEVELOPMENTAL STAGE: Meiosis-specific.
CC -!- SIMILARITY: Belongs to the TOP6A family. {ECO:0000305}.
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DR EMBL; J02987; AAA65532.1; -; Genomic_DNA.
DR EMBL; U11582; AAB65075.1; -; Genomic_DNA.
DR EMBL; AY557836; AAS56162.1; -; Genomic_DNA.
DR EMBL; BK006934; DAA06663.1; -; Genomic_DNA.
DR PIR; S05854; BWBY11.
DR RefSeq; NP_011841.1; NM_001179102.1.
DR AlphaFoldDB; P23179; -.
DR SMR; P23179; -.
DR BioGRID; 36401; 129.
DR DIP; DIP-1652N; -.
DR IntAct; P23179; 5.
DR MINT; P23179; -.
DR STRING; 4932.YHL022C; -.
DR PaxDb; P23179; -.
DR EnsemblFungi; YHL022C_mRNA; YHL022C; YHL022C.
DR GeneID; 856364; -.
DR KEGG; sce:YHL022C; -.
DR SGD; S000001014; SPO11.
DR VEuPathDB; FungiDB:YHL022C; -.
DR eggNOG; KOG2795; Eukaryota.
DR GeneTree; ENSGT00390000001787; -.
DR HOGENOM; CLU_037229_2_1_1; -.
DR InParanoid; P23179; -.
DR OMA; YICTMAN; -.
DR BioCyc; YEAST:G3O-31042-MON; -.
DR PRO; PR:P23179; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P23179; protein.
DR GO; GO:0000794; C:condensed nuclear chromosome; IDA:SGD.
DR GO; GO:0000228; C:nuclear chromosome; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0003682; F:chromatin binding; IDA:SGD.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0045027; F:DNA end binding; IDA:SGD.
DR GO; GO:0003918; F:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity; IEA:UniProtKB-EC.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007129; P:homologous chromosome pairing at meiosis; IMP:SGD.
DR GO; GO:0042138; P:meiotic DNA double-strand break formation; IMP:SGD.
DR GO; GO:0000706; P:meiotic DNA double-strand break processing; IBA:GO_Central.
DR GO; GO:0007131; P:reciprocal meiotic recombination; IBA:GO_Central.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR GO; GO:0007130; P:synaptonemal complex assembly; IMP:SGD.
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 1: Evidence at protein level;
KW Chromosome; Direct protein sequencing; DNA-binding; Hydrolase; Isomerase;
KW Magnesium; Meiosis; Metal-binding; Nucleus; Reference proteome;
KW Sporulation.
FT CHAIN 1..398
FT /note="Meiosis-specific protein SPO11"
FT /id="PRO_0000145473"
FT ACT_SITE 135
FT /note="Nucleophile"
FT /evidence="ECO:0000305|PubMed:9121560"
FT BINDING 233
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q57815"
FT BINDING 288
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q57815"
FT MUTAGEN 135
FT /note="Y->F: Loss of activity."
FT /evidence="ECO:0000269|PubMed:9121560"
SQ SEQUENCE 398 AA; 45413 MW; FDDB079411DB3C71 CRC64;
MALEGLRKKY KTRQELVKAL TPKRRSIHLN SNGHSNGTPC SNADVLAHIK HFLSLAANSL
EQHQQPISIV FQNKKKKGDT SSPDIHTTLD FPLNGPHLCT HQFKLKRCAI LLNLLKVVME
KLPLGKNTTV RDIFYSNVEL FQRQANVVQW LDVIRFNFKL SPRKSLNIIP AQKGLVYSPF
PIDIYDNILT CENEPKMQKQ TIFPGKPCLI PFFQDDAVIK LGTTSMCNIV IVEKEAVFTK
LVNNYHKLST NTMLITGKGF PDFLTRLFLK KLEQYCSKLI SDCSIFTDAD PYGISIALNY
THSNERNAYI CTMANYKGIR ITQVLAQNNE VHNKSIQLLS LNQRDYSLAK NLIASLTANS
WDIATSPLKN VIIECQREIF FQKKAEMNEI DARIFEYK
