RAD51_DROME
ID RAD51_DROME Reviewed; 336 AA.
AC Q27297; Q8IGG8; Q8IMJ5; Q9VAA8;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=DNA repair protein Rad51 homolog;
DE AltName: Full=Protein spindle-A;
DE AltName: Full=RecA protein homolog;
GN Name=spn-A; Synonyms=DMR, Rad51; ORFNames=CG7948;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM A).
RC STRAIN=Canton-S;
RX PubMed=7857671; DOI=10.1266/jjg.69.663;
RA Akaboshi E., Inoue Y., Ryo H.;
RT "Cloning of the cDNA and genomic DNA that correspond to the recA-like gene
RT of Drosophila melanogaster.";
RL Jpn. J. Genet. 69:663-670(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM A), FUNCTION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=Oregon-R;
RX PubMed=8625736; DOI=10.1007/bf00352112;
RA McKee B.D., Ren X.J., Hong C.S.;
RT "A recA-like gene in Drosophila melanogaster that is expressed at high
RT levels in female but not male meiotic tissues.";
RL Chromosoma 104:479-488(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [4]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
RC STRAIN=Berkeley; TISSUE=Head;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [6]
RP FUNCTION.
RX PubMed=9362456; DOI=10.1242/dev.124.24.4927;
RA Gonzalez-Reyes A., Elliott H., St Johnston D.;
RT "Oocyte determination and the origin of polarity in Drosophila: the role of
RT the spindle genes.";
RL Development 124:4927-4937(1997).
CC -!- FUNCTION: Binds to single and double-stranded DNA and exhibits DNA-
CC dependent ATPase activity. Underwinds duplex DNA (By similarity).
CC {ECO:0000250}.
CC -!- FUNCTION: Spindle genes are required for each of the symmetry-breaking
CC steps that generate polarity during egg axis formation; oocyte
CC positioning at the posterior of the cyst to generate the first AP
CC polarity and inhibition of gurken (grk) signaling to the follicle cell
CC layer to polarize first the AP axis and then DV axis. May have a role
CC in female meiosis. {ECO:0000269|PubMed:8625736,
CC ECO:0000269|PubMed:9362456}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=A;
CC IsoId=Q27297-1; Sequence=Displayed;
CC Name=B;
CC IsoId=Q27297-2; Sequence=VSP_012414;
CC -!- TISSUE SPECIFICITY: Highly expressed in ovaries.
CC {ECO:0000269|PubMed:8625736}.
CC -!- SIMILARITY: Belongs to the RecA family. RAD51 subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D37788; BAA07039.1; -; Genomic_DNA.
DR EMBL; D17726; BAA04580.1; -; mRNA.
DR EMBL; L41342; AAA64873.1; -; Genomic_DNA.
DR EMBL; AE014297; AAF57005.1; -; Genomic_DNA.
DR EMBL; AE014297; AAN14213.1; -; Genomic_DNA.
DR EMBL; BT001791; AAN71546.1; -; mRNA.
DR RefSeq; NP_524583.1; NM_079844.4. [Q27297-1]
DR RefSeq; NP_733342.1; NM_170463.3. [Q27297-2]
DR AlphaFoldDB; Q27297; -.
DR SMR; Q27297; -.
DR BioGRID; 68433; 82.
DR DIP; DIP-20846N; -.
DR IntAct; Q27297; 38.
DR STRING; 7227.FBpp0084955; -.
DR PaxDb; Q27297; -.
DR EnsemblMetazoa; FBtr0085589; FBpp0084955; FBgn0003479. [Q27297-1]
DR EnsemblMetazoa; FBtr0085590; FBpp0084956; FBgn0003479. [Q27297-2]
DR GeneID; 43577; -.
DR KEGG; dme:Dmel_CG7948; -.
DR CTD; 43577; -.
DR FlyBase; FBgn0003479; spn-A.
DR VEuPathDB; VectorBase:FBgn0003479; -.
DR eggNOG; KOG1433; Eukaryota.
DR GeneTree; ENSGT00940000156157; -.
DR InParanoid; Q27297; -.
DR OMA; TFRIYLR; -.
DR PhylomeDB; Q27297; -.
DR Reactome; R-DME-5693616; Presynaptic phase of homologous DNA pairing and strand exchange.
DR SignaLink; Q27297; -.
DR BioGRID-ORCS; 43577; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 43577; -.
DR PRO; PR:Q27297; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0003479; Expressed in cleaving embryo and 27 other tissues.
DR ExpressionAtlas; Q27297; baseline and differential.
DR Genevisible; Q27297; DM.
DR GO; GO:0000794; C:condensed nuclear chromosome; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; IBA:GO_Central.
DR GO; GO:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
DR GO; GO:0000150; F:DNA strand exchange activity; ISS:FlyBase.
DR GO; GO:0003690; F:double-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0003697; F:single-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0070192; P:chromosome organization involved in meiotic cell cycle; IBA:GO_Central.
DR GO; GO:0000730; P:DNA recombinase assembly; IBA:GO_Central.
DR GO; GO:0006310; P:DNA recombination; ISS:FlyBase.
DR GO; GO:0006281; P:DNA repair; IGI:FlyBase.
DR GO; GO:0006302; P:double-strand break repair; IMP:FlyBase.
DR GO; GO:0045003; P:double-strand break repair via synthesis-dependent strand annealing; IMP:FlyBase.
DR GO; GO:0007143; P:female meiotic nuclear division; IMP:FlyBase.
DR GO; GO:0007294; P:germarium-derived oocyte fate determination; IGI:FlyBase.
DR GO; GO:0008298; P:intracellular mRNA localization; IMP:FlyBase.
DR GO; GO:0006312; P:mitotic recombination; IBA:GO_Central.
DR GO; GO:1990426; P:mitotic recombination-dependent replication fork processing; IEA:InterPro.
DR GO; GO:0030716; P:oocyte fate determination; IMP:FlyBase.
DR GO; GO:0030717; P:oocyte karyosome formation; IMP:FlyBase.
DR GO; GO:0048477; P:oogenesis; IMP:FlyBase.
DR GO; GO:0009949; P:polarity specification of anterior/posterior axis; IMP:FlyBase.
DR GO; GO:0009951; P:polarity specification of dorsal/ventral axis; IMP:FlyBase.
DR GO; GO:0007131; P:reciprocal meiotic recombination; IBA:GO_Central.
DR GO; GO:0010569; P:regulation of double-strand break repair via homologous recombination; IMP:FlyBase.
DR GO; GO:0042148; P:strand invasion; IBA:GO_Central.
DR CDD; cd01123; Rad51_DMC1_radA; 1.
DR Gene3D; 3.40.50.300; -; 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; IPR033925; Rad51_DMC1_RadA.
DR InterPro; IPR020588; RecA_ATP-bd.
DR InterPro; IPR020587; RecA_monomer-monomer_interface.
DR Pfam; PF08423; Rad51; 1.
DR PIRSF; PIRSF005856; Rad51; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF47794; SSF47794; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR02239; recomb_RAD51; 1.
DR PROSITE; PS50162; RECA_2; 1.
DR PROSITE; PS50163; RECA_3; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; ATP-binding; Developmental protein; DNA-binding;
KW Meiosis; Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..336
FT /note="DNA repair protein Rad51 homolog"
FT /id="PRO_0000122938"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 124..131
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..57
FT /note="Missing (in isoform B)"
FT /evidence="ECO:0000303|PubMed:12537569"
FT /id="VSP_012414"
FT CONFLICT 334..336
FT /note="RES -> GRANCAHL (in Ref. 5; AAN71546)"
FT /evidence="ECO:0000305"
SQ 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
