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Database: UniProt
Entry: E7A2J0_SPORE
LinkDB: E7A2J0_SPORE
Original site: E7A2J0_SPORE 
ID   E7A2J0_SPORE            Unreviewed;       354 AA.
AC   E7A2J0;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   24-JAN-2024, entry version 60.
DE   RecName: Full=DNA repair protein RAD51 homolog {ECO:0000256|RuleBase:RU364139};
GN   Name=Rad51 {ECO:0000313|EMBL:CBQ73697.1};
GN   ORFNames=sr14292 {ECO:0000313|EMBL:CBQ73697.1};
OS   Sporisorium reilianum (strain SRZ2) (Maize head smut fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Sporisorium.
OX   NCBI_TaxID=999809 {ECO:0000313|EMBL:CBQ73697.1, ECO:0000313|Proteomes:UP000008867};
RN   [1] {ECO:0000313|EMBL:CBQ73697.1, ECO:0000313|Proteomes:UP000008867}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SRZ2 {ECO:0000313|Proteomes:UP000008867};
RX   PubMed=21148393; DOI=10.1126/science.1195330;
RA   Schirawski J., Mannhaupt G., Muench K., Brefort T., Schipper K.,
RA   Doehlemann G., Di Stasio M., Roessel N., Mendoza-Mendoza A., Pester D.,
RA   Mueller O., Winterberg B., Meyer E., Ghareeb H., Wollenberg T.,
RA   Muensterkoetter M., Wong P., Walter M., Stukenbrock E., Gueldener U.,
RA   Kahmann R.;
RT   "Pathogenicity determinants in smut fungi revealed by genome comparison.";
RL   Science 330:1546-1548(2010).
CC   -!- FUNCTION: Required both for recombination and for the repair of DNA
CC       damage caused by X-rays. {ECO:0000256|RuleBase:RU364139}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC       ECO:0000256|RuleBase:RU364139}.
CC   -!- SIMILARITY: Belongs to the RecA family. RAD51 subfamily.
CC       {ECO:0000256|ARBA:ARBA00007095, ECO:0000256|RuleBase:RU364139}.
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DR   EMBL; FQ311473; CBQ73697.1; -; Genomic_DNA.
DR   AlphaFoldDB; E7A2J0; -.
DR   EnsemblFungi; CBQ73697; CBQ73697; sr14292.
DR   VEuPathDB; FungiDB:sr14292; -.
DR   eggNOG; KOG1433; Eukaryota.
DR   HOGENOM; CLU_041732_0_2_1; -.
DR   OrthoDB; 5477610at2759; -.
DR   Proteomes; UP000008867; Chromosome 8.
DR   GO; GO:0000775; C:chromosome, centromeric region; IEA:EnsemblFungi.
DR   GO; GO:0000794; C:condensed nuclear chromosome; IEA:EnsemblFungi.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:EnsemblFungi.
DR   GO; GO:0035861; C:site of double-strand break; IEA:EnsemblFungi.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
DR   GO; GO:0000150; F:DNA strand exchange activity; IEA:EnsemblFungi.
DR   GO; GO:0003690; F:double-stranded DNA binding; IEA:EnsemblFungi.
DR   GO; GO:0042802; F:identical protein binding; IEA:EnsemblFungi.
DR   GO; GO:0003697; F:single-stranded DNA binding; IEA:EnsemblFungi.
DR   GO; GO:1905334; F:Swi5-Sfr1 complex binding; IEA:EnsemblFungi.
DR   GO; GO:0000730; P:DNA recombinase assembly; IEA:EnsemblFungi.
DR   GO; GO:1990918; P:double-strand break repair involved in meiotic recombination; IEA:EnsemblFungi.
DR   GO; GO:0030491; P:heteroduplex formation; IEA:EnsemblFungi.
DR   GO; GO:0036297; P:interstrand cross-link repair; IEA:EnsemblFungi.
DR   GO; GO:0007533; P:mating type switching; IEA:EnsemblFungi.
DR   GO; GO:0000709; P:meiotic joint molecule formation; IEA:EnsemblFungi.
DR   GO; GO:0000708; P:meiotic strand invasion; IEA:EnsemblFungi.
DR   GO; GO:0043504; P:mitochondrial DNA repair; IEA:EnsemblFungi.
DR   GO; GO:1990426; P:mitotic recombination-dependent replication fork processing; IEA:EnsemblFungi.
DR   GO; GO:0006289; P:nucleotide-excision repair; IEA:EnsemblFungi.
DR   GO; GO:0051260; P:protein homooligomerization; IEA:EnsemblFungi.
DR   GO; GO:0120290; P:stalled replication fork localization to nuclear periphery; IEA:EnsemblFungi.
DR   GO; GO:0000722; P:telomere maintenance via recombination; IEA:EnsemblFungi.
DR   CDD; cd19513; Rad51; 1.
DR   Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR011941; DNA_recomb/repair_Rad51.
DR   InterPro; IPR013632; DNA_recomb/repair_Rad51_C.
DR   InterPro; IPR016467; DNA_recomb/repair_RecA-like.
DR   InterPro; IPR010995; DNA_repair_Rad51/TF_NusA_a-hlx.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR020588; RecA_ATP-bd.
DR   InterPro; IPR020587; RecA_monomer-monomer_interface.
DR   NCBIfam; TIGR02239; recomb_RAD51; 1.
DR   PANTHER; PTHR22942:SF39; DNA REPAIR PROTEIN RAD51 HOMOLOG 1; 1.
DR   PANTHER; PTHR22942; RECA/RAD51/RADA DNA STRAND-PAIRING FAMILY MEMBER; 1.
DR   Pfam; PF14520; HHH_5; 1.
DR   Pfam; PF08423; Rad51; 1.
DR   PIRSF; PIRSF005856; Rad51; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF47794; Rad51 N-terminal domain-like; 1.
DR   PROSITE; PS50162; RECA_2; 1.
DR   PROSITE; PS50163; RECA_3; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU003422};
KW   DNA damage {ECO:0000256|RuleBase:RU364139};
KW   DNA recombination {ECO:0000256|RuleBase:RU364139};
KW   DNA repair {ECO:0000256|RuleBase:RU364139};
KW   DNA-binding {ECO:0000256|RuleBase:RU364139};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU003422};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU364139}.
FT   DOMAIN          98..269
FT                   /note="RecA family profile 1"
FT                   /evidence="ECO:0000259|PROSITE:PS50162"
FT   DOMAIN          276..339
FT                   /note="RecA family profile 2"
FT                   /evidence="ECO:0000259|PROSITE:PS50163"
SQ   SEQUENCE   354 AA;  38023 MW;  74C3917626BDD1C5 CRC64;
     MSQSVQDPAQ MGEEDMGEAF GPLPVSKLED FGISSSDCKK LAEAGYNTVE SIAFTPKKSL
     LLVKGISEAK ADKILAEAAK LVPMGFTTAT EFHARRNELI SITTGSKNLD AILGGGMETG
     SITELYGEFR TGKSQLCHTL AVTCQLPVDM GGGEGKCLYI DTEGTFRPVR LLAVAERYGL
     NGEEVLDNVA YARAYNADHQ LQLLMQASAM MAESRFSLLI VDSLTSLYRT DFSGRGELSA
     RQMHLAKFLR GLMRLADEFG VAVVITNQVV AQVDGATAFT ADAKKPIGGN IVAHASTTRL
     SLRKGRGNQR ICRIADSPCL PEADAVFSIG PEGIIDPVSV LDLVRDLDLI VVLR
//
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