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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.
16-JAN-2019, entry version 166.
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}.
-!- 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; 38.
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; ENSGT00940000156157; -.
InParanoid; Q27297; -.
KO; K04482; -.
OMA; YNTDHQT; -.
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; Expressed in 30 organ(s), highest expression level in cleaving embryo.
ExpressionAtlas; Q27297; baseline and differential.
Genevisible; Q27297; DM.
GO; GO:0000794; C:condensed nuclear chromosome; 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: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: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.
2: Evidence at transcript 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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Pathways :
WP1625: Base excision repair
WP1672: Mismatch repair
WP1678: Nucleotide excision repair
WP1049: G Protein Signaling Pathways
WP1165: G Protein Signaling Pathways
WP1371: G Protein Signaling Pathways
WP1438: Influenza A virus infection
WP1493: Carbon assimilation C4 pathway
WP1502: Mitochondrial biogenesis
WP1531: Vitamin D synthesis
WP1566: Citrate cycle (TCA cycle)
WP1613: 1,4-Dichlorobenzene degradation
WP1616: ABC transporters
WP1624: Bacterial secretion system
WP1644: DNA replication
WP1650: Fluorobenzoate degradation
WP1654: gamma-Hexachlorocyclohexane degradation
WP1657: Glycerolipid metabolism
WP1659: Glycine, serine and threonine metabolism
WP1661: Glyoxylate and dicarboxylate metabolism
WP1663: Homologous recombination
WP1665: Limonene and pinene degradation
WP1673: Naphthalene and anthracene degradation
WP1675: Nitrogen metabolism
WP1676: Non-homologous end-joining

Related Genes :
[RAD51 RAD51A RECA] DNA repair protein RAD51 homolog 1 (HsRAD51) (hRAD51) (RAD51 homolog A)
[Rad51 Rad51a Reca] DNA repair protein RAD51 homolog 1 (RAD51 homolog A)
[RAD51C RAD51L2] DNA repair protein RAD51 homolog 3 (R51H3) (RAD51 homolog C) (RAD51-like protein 2)
[RAD51B RAD51L1 REC2] DNA repair protein RAD51 homolog 2 (R51H2) (RAD51 homolog B) (Rad51B) (RAD51-like protein 1)
[RAD51D RAD51L3] DNA repair protein RAD51 homolog 4 (R51H3) (RAD51 homolog D) (RAD51-like protein 3) (TRAD)
[Rad51c Rad51l2] DNA repair protein RAD51 homolog 3 (R51H3) (RAD51 homolog C) (RAD51-like protein 2)
[Rad51d R51h3 Rad51l3] DNA repair protein RAD51 homolog 4 (R51H3) (RAD51 homolog D) (RAD51-like protein 3)
[RAD51C RAD51L2] DNA repair protein RAD51 homolog 3 (R51H3) (RAD51 homolog C) (RAD51-like protein 2)
[RAD51] DNA repair protein RAD51 homolog 1 (cRad51)
[RAD51] DNA repair protein RAD51 homolog 1
[RAD51 RAD51A] DNA repair protein RAD51 homolog 1
[rad-51 rad51 CELE_Y43C5A.6 Y43C5A.6] DNA repair protein RAD51 homolog
[RAD51] DNA repair protein RAD51 homolog 1
[Rad51b Rad51l1 Rec2] DNA repair protein RAD51 homolog 2 (R51H2) (RAD51 homolog B) (RAD51-like protein 1)
[rad-51 CELE_Y43C5A.6 Y43C5A.6] DNA repair protein RAD51 homolog
[RAD51AP1 PIR51] RAD51-associated protein 1 (RAD51-interacting protein)
[RAD51A] DNA repair protein RAD51 homolog A (Rad51-like protein A) (RAD51A) (ZmRAD51a)
[RAD51D RAD51L3] DNA repair protein RAD51 homolog 4 (R51H3) (RAD51 homolog D) (RAD51-like protein 3)
[RAD51C At2g45280 F4L23.21] DNA repair protein RAD51 homolog 3 (DNA repair-recombination protein RAD51C) (AtRAD51C)
[RAD51B At2g28560 T17D12.12] DNA repair protein RAD51 homolog 2 (AtRAD51B)
[RAD51D At1g07745 F24B9.14] DNA repair protein RAD51 homolog 4 (AtRAD51D)
[mei-3 NCU02741] DNA repair protein RAD51 homolog
[RDH54 TID1 YBR073W YBR0715] DNA repair and recombination protein RDH54 (RAD homolog 54) (Recombination factor TID1) (Two hybrid interaction with DMC1 protein 1) [Includes: DNA topoisomerase (EC 5.99.1.-); Putative helicase (EC 3.6.4.12)]
[Rad51ap1] RAD51-associated protein 1 (RAB22) (RAD51-interacting protein)
[rad-51 Cbr-rad-51 CBG04405 CBG_04405] DNA repair protein RAD51 homolog
[DMC1 DMC1H LIM15] Meiotic recombination protein DMC1/LIM15 homolog
[DMC1 LIM15 At3g22880 F5N5.6] Meiotic recombination protein DMC1 homolog (AtDMC1)
[RAD54B] DNA repair and recombination protein RAD54B (EC 3.6.4.-) (RAD54 homolog B)
[CHEK2 CDS1 CHK2 RAD53] Serine/threonine-protein kinase Chk2 (EC 2.7.11.1) (CHK2 checkpoint homolog) (Cds1 homolog) (Hucds1) (hCds1) (Checkpoint kinase 2)
[Brca2 Fancd1] Breast cancer type 2 susceptibility protein homolog (Fanconi anemia group D1 protein homolog)

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