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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}.
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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
 
 
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