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DNA repair protein Rad51 homolog (Protein spindle-A) (RecA protein homolog)

 RAD51_DROME             Reviewed;         336 AA.
Q27297; Q8IGG8; Q8IMJ5; Q9VAA8;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 1.
25-APR-2018, entry version 160.
RecName: Full=DNA repair protein Rad51 homolog;
AltName: Full=Protein spindle-A;
AltName: Full=RecA protein homolog;
Name=spn-A; Synonyms=DMR, Rad51; ORFNames=CG7948;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM A).
STRAIN=Canton-S;
PubMed=7857671; DOI=10.1266/jjg.69.663;
Akaboshi E., Inoue Y., Ryo H.;
"Cloning of the cDNA and genomic DNA that correspond to the recA-like
gene of Drosophila melanogaster.";
Jpn. J. Genet. 69:663-670(1994).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM A), FUNCTION, AND TISSUE
SPECIFICITY.
STRAIN=Oregon-R;
PubMed=8625736; DOI=10.1007/BF00352112;
McKee B.D., Ren X.J., Hong C.S.;
"A recA-like gene in Drosophila melanogaster that is expressed at high
levels in female but not male meiotic tissues.";
Chromosoma 104:479-488(1996).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[4]
GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
STRAIN=Berkeley; TISSUE=Head;
PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
Rubin G.M., Celniker S.E.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[6]
FUNCTION.
PubMed=9362456;
Gonzalez-Reyes A., Elliott H., St Johnston D.;
"Oocyte determination and the origin of polarity in Drosophila: the
role of the spindle genes.";
Development 124:4927-4937(1997).
-!- FUNCTION: Binds to single and double-stranded DNA and exhibits
DNA-dependent ATPase activity. Underwinds duplex DNA (By
similarity). {ECO:0000250}.
-!- FUNCTION: Spindle genes are required for each of the symmetry-
breaking steps that generate polarity during egg axis formation;
oocyte positioning at the posterior of the cyst to generate the
first AP polarity and inhibition of gurken (grk) signaling to the
follicle cell layer to polarize first the AP axis and then DV
axis. May have a role in female meiosis.
{ECO:0000269|PubMed:8625736, ECO:0000269|PubMed:9362456}.
-!- INTERACTION:
Q9VWC8:Pmp70; NbExp=2; IntAct=EBI-458769, EBI-75504;
A1Z7Q1:Su(var)2-10; NbExp=3; IntAct=EBI-458769, EBI-497522;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=A;
IsoId=Q27297-1; Sequence=Displayed;
Name=B;
IsoId=Q27297-2; Sequence=VSP_012414;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Highly expressed in ovaries.
{ECO:0000269|PubMed:8625736}.
-!- SIMILARITY: Belongs to the RecA family. RAD51 subfamily.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; D37788; BAA07039.1; -; Genomic_DNA.
EMBL; D17726; BAA04580.1; -; mRNA.
EMBL; L41342; AAA64873.1; -; Genomic_DNA.
EMBL; AE014297; AAF57005.1; -; Genomic_DNA.
EMBL; AE014297; AAN14213.1; -; Genomic_DNA.
EMBL; BT001791; AAN71546.1; -; mRNA.
RefSeq; NP_524583.1; NM_079844.4. [Q27297-1]
RefSeq; NP_733342.1; NM_170463.3. [Q27297-2]
UniGene; Dm.1913; -.
ProteinModelPortal; Q27297; -.
SMR; Q27297; -.
BioGrid; 68433; 81.
DIP; DIP-20846N; -.
IntAct; Q27297; 70.
STRING; 7227.FBpp0084955; -.
PaxDb; Q27297; -.
PRIDE; Q27297; -.
EnsemblMetazoa; FBtr0085589; FBpp0084955; FBgn0003479. [Q27297-1]
EnsemblMetazoa; FBtr0085590; FBpp0084956; FBgn0003479. [Q27297-2]
GeneID; 43577; -.
KEGG; dme:Dmel_CG7948; -.
CTD; 43577; -.
FlyBase; FBgn0003479; spn-A.
eggNOG; KOG1433; Eukaryota.
eggNOG; COG0468; LUCA.
GeneTree; ENSGT00890000139508; -.
InParanoid; Q27297; -.
KO; K04482; -.
OMA; YNTDHQT; -.
OrthoDB; EOG091G09QY; -.
PhylomeDB; Q27297; -.
Reactome; R-DME-5693616; Presynaptic phase of homologous DNA pairing and strand exchange.
GenomeRNAi; 43577; -.
PRO; PR:Q27297; -.
Proteomes; UP000000803; Chromosome 3R.
Bgee; FBgn0003479; -.
ExpressionAtlas; Q27297; differential.
Genevisible; Q27297; DM.
GO; GO:0000794; C:condensed nuclear chromosome; IBA:GO_Central.
GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0008094; F:DNA-dependent ATPase activity; IBA:GO_Central.
GO; GO:0003690; F:double-stranded DNA binding; IBA:GO_Central.
GO; GO:0000400; F:four-way junction DNA binding; IBA:GO_Central.
GO; GO:0000150; F:recombinase activity; ISS:FlyBase.
GO; GO:0003697; F:single-stranded DNA binding; IBA:GO_Central.
GO; GO:0070192; P:chromosome organization involved in meiotic cell cycle; IBA:GO_Central.
GO; GO:0000730; P:DNA recombinase assembly; IBA:GO_Central.
GO; GO:0006310; P:DNA recombination; ISS:FlyBase.
GO; GO:0006281; P:DNA repair; IGI:FlyBase.
GO; GO:0006302; P:double-strand break repair; IMP:FlyBase.
GO; GO:0045003; P:double-strand break repair via synthesis-dependent strand annealing; IMP:FlyBase.
GO; GO:0007143; P:female meiotic nuclear division; IMP:FlyBase.
GO; GO:0007294; P:germarium-derived oocyte fate determination; IGI:FlyBase.
GO; GO:0008298; P:intracellular mRNA localization; IMP:FlyBase.
GO; GO:0006312; P:mitotic recombination; IBA:GO_Central.
GO; GO:1990426; P:mitotic recombination-dependent replication fork processing; IEA:InterPro.
GO; GO:0030716; P:oocyte fate determination; IMP:FlyBase.
GO; GO:0030717; P:oocyte karyosome formation; IMP:FlyBase.
GO; GO:0048477; P:oogenesis; IMP:FlyBase.
GO; GO:0009949; P:polarity specification of anterior/posterior axis; IMP:FlyBase.
GO; GO:0009951; P:polarity specification of dorsal/ventral axis; IMP:FlyBase.
GO; GO:0007131; P:reciprocal meiotic recombination; IBA:GO_Central.
GO; GO:0010569; P:regulation of double-strand break repair via homologous recombination; IMP:FlyBase.
GO; GO:0031000; P:response to caffeine; IGI:FlyBase.
GO; GO:0010212; P:response to ionizing radiation; IBA:GO_Central.
GO; GO:0042148; P:strand invasion; IBA:GO_Central.
CDD; cd01123; Rad51_DMC1_radA; 1.
InterPro; IPR003593; AAA+_ATPase.
InterPro; IPR011941; DNA_recomb/repair_Rad51.
InterPro; IPR013632; DNA_recomb/repair_Rad51_C.
InterPro; IPR016467; DNA_recomb/repair_RecA-like.
InterPro; IPR010995; DNA_repair_Rad51/TF_NusA_a-hlx.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR033925; Rad51_DMC1_RadA.
InterPro; IPR020588; RecA_ATP-bd.
InterPro; IPR020587; RecA_monomer-monomer_interface.
Pfam; PF08423; Rad51; 1.
PIRSF; PIRSF005856; Rad51; 1.
SMART; SM00382; AAA; 1.
SUPFAM; SSF47794; SSF47794; 1.
SUPFAM; SSF52540; SSF52540; 1.
TIGRFAMs; TIGR02239; recomb_RAD51; 1.
PROSITE; PS50162; RECA_2; 1.
PROSITE; PS50163; RECA_3; 1.
1: Evidence at protein level;
Alternative splicing; ATP-binding; Complete proteome;
Developmental protein; DNA-binding; Meiosis; Nucleotide-binding;
Nucleus; Reference proteome.
CHAIN 1 336 DNA repair protein Rad51 homolog.
/FTId=PRO_0000122938.
NP_BIND 124 131 ATP. {ECO:0000255}.
VAR_SEQ 1 57 Missing (in isoform B).
{ECO:0000303|PubMed:12537569}.
/FTId=VSP_012414.
CONFLICT 334 336 RES -> GRANCAHL (in Ref. 5; AAN71546).
{ECO:0000305}.
SEQUENCE 336 AA; 36647 MW; F9E9B21405B15DB0 CRC64;
MEKLTNVQAQ QEEEEEEGPL SVTKLIGGSI TAKDIKLLQQ ASLHTVESVA NATKKQLMAI
PGLGGGKVEQ IITEANKLVP LGFLSARTFY QMRADVVQLS TGSKELDKLL GGGIETGSIT
EIFGEFRCGK TQLCHTLAVT CQLPISQKGG EGKCMYIDTE NTFRPERLAA IAQRYKLNES
EVLDNVAFTR AHNSDQQTKL IQMAAGMLFE SRYALLIVDS AMALYRSDYI GRGELAARQN
HLGLFLRMLQ RLADEFGVAV VITNQVTASL DGAPGMFDAK KPIGGHIMAH SSTTRLYLRK
GKGETRICKI YDSPCLPESE AMFAILPDGI GDARES


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