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Q27297 (RAD51_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
DNA repair protein Rad51 homolog
Alternative name(s):
Protein spindle-A
RecA protein homolog
Gene names
Name:spn-A
Synonyms:DMR, Rad51
ORF Names:CG7948
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length336 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Binds to single and double-stranded DNA and exhibits DNA-dependent ATPase activity. Underwinds duplex DNA By similarity. Ref.2 Ref.6

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. Ref.2 Ref.6

Subcellular location

Nucleus Probable.

Tissue specificity

Highly expressed in ovaries. Ref.2

Sequence similarities

Belongs to the RecA family. RAD51 subfamily.

Contains 1 HhH domain.

Ontologies

Keywords
   Biological processMeiosis
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   LigandATP-binding
DNA-binding
Nucleotide-binding
   Molecular functionDevelopmental protein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA repair

Inferred from genetic interaction PubMed 22022278. Source: FlyBase

double-strand break repair via synthesis-dependent strand annealing

Inferred from mutant phenotype PubMed 15238522PubMed 17660539. Source: FlyBase

female meiosis

Inferred from mutant phenotype PubMed 14592983. Source: FlyBase

germarium-derived oocyte fate determination

Inferred from genetic interaction Ref.6. Source: FlyBase

intracellular mRNA localization

Inferred from mutant phenotype Ref.6. Source: FlyBase

karyosome formation

Inferred from mutant phenotype Ref.6. Source: FlyBase

oocyte differentiation

Non-traceable author statement PubMed 11131529. Source: FlyBase

oogenesis

Inferred from mutant phenotype Ref.6. Source: FlyBase

polarity specification of anterior/posterior axis

Inferred from mutant phenotype Ref.6. Source: FlyBase

polarity specification of dorsal/ventral axis

Inferred from mutant phenotype Ref.6. Source: FlyBase

   Cellular_componentnucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

DNA-dependent ATPase activity

Inferred from electronic annotation. Source: InterPro

damaged DNA binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform A (identifier: Q27297-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform B (identifier: Q27297-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-57: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 336336DNA repair protein Rad51 homolog
PRO_0000122938

Regions

Nucleotide binding124 – 1318ATP Potential

Natural variations

Alternative sequence1 – 5757Missing in isoform B.
VSP_012414

Experimental info

Sequence conflict334 – 3363RES → GRANCAHL in AAN71546. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Isoform A [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: F9E9B21405B15DB0

FASTA33636,647
        10         20         30         40         50         60 
MEKLTNVQAQ QEEEEEEGPL SVTKLIGGSI TAKDIKLLQQ ASLHTVESVA NATKKQLMAI 

        70         80         90        100        110        120 
PGLGGGKVEQ IITEANKLVP LGFLSARTFY QMRADVVQLS TGSKELDKLL GGGIETGSIT 

       130        140        150        160        170        180 
EIFGEFRCGK TQLCHTLAVT CQLPISQKGG EGKCMYIDTE NTFRPERLAA IAQRYKLNES 

       190        200        210        220        230        240 
EVLDNVAFTR AHNSDQQTKL IQMAAGMLFE SRYALLIVDS AMALYRSDYI GRGELAARQN 

       250        260        270        280        290        300 
HLGLFLRMLQ RLADEFGVAV VITNQVTASL DGAPGMFDAK KPIGGHIMAH SSTTRLYLRK 

       310        320        330 
GKGETRICKI YDSPCLPESE AMFAILPDGI GDARES 

« Hide

Isoform B [UniParc].

Checksum: BF82A5C319AB61F9
Show »

FASTA27930,459

References

« Hide 'large scale' references
[1]"Cloning of the cDNA and genomic DNA that correspond to the recA-like gene of Drosophila melanogaster."
Akaboshi E., Inoue Y., Ryo H.
Jpn. J. Genet. 69:663-670(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM A).
Strain: Canton-S.
[2]"A recA-like gene in Drosophila melanogaster that is expressed at high levels in female but not male meiotic tissues."
McKee B.D., Ren X.J., Hong C.S.
Chromosoma 104:479-488(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM A), FUNCTION, TISSUE SPECIFICITY.
Strain: Oregon-R.
[3]"The genome sequence of Drosophila melanogaster."
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. expand/collapse author list , 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.
Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[4]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
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. expand/collapse author list , 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.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
Strain: Berkeley.
[5]"A Drosophila full-length cDNA resource."
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.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
Strain: Berkeley.
Tissue: Head.
[6]"Oocyte determination and the origin of polarity in Drosophila: the role of the spindle genes."
Gonzalez-Reyes A., Elliott H., St Johnston D.
Development 124:4927-4937(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D37788 Genomic DNA. Translation: BAA07039.1.
D17726 mRNA. Translation: BAA04580.1.
L41342 Genomic DNA. Translation: AAA64873.1.
AE014297 Genomic DNA. Translation: AAF57005.1.
AE014297 Genomic DNA. Translation: AAN14213.1.
BT001791 mRNA. Translation: AAN71546.1.
RefSeqNP_524583.1. NM_079844.4.
NP_733342.1. NM_170463.3.
UniGeneDm.1913.

3D structure databases

ProteinModelPortalQ27297.
SMRQ27297. Positions 22-335.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid68433. 69 interactions.
DIPDIP-20846N.
IntActQ27297. 37 interactions.
MINTMINT-337614.

Proteomic databases

PaxDbQ27297.
PRIDEQ27297.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0085589; FBpp0084955; FBgn0003479. [Q27297-1]
GeneID43577.
KEGGdme:Dmel_CG7948.

Organism-specific databases

CTD43577.
FlyBaseFBgn0003479. spn-A.

Phylogenomic databases

eggNOGCOG0468.
GeneTreeENSGT00750000117750.
InParanoidQ27297.
KOK04482.
OMAMMAESRY.
OrthoDBEOG715Q4H.
PhylomeDBQ27297.

Gene expression databases

BgeeQ27297.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR003593. AAA+_ATPase.
IPR011941. DNA_recomb/repair_Rad51.
IPR013632. DNA_recomb/repair_Rad51_C.
IPR016467. DNA_recomb/repair_RecA-like.
IPR010995. DNA_repair_Rad51/TF_NusA_a-hlx.
IPR003583. Hlx-hairpin-Hlx_DNA-bd_motif.
IPR027417. P-loop_NTPase.
IPR020588. RecA_ATP-bd.
IPR020587. RecA_monomer-monomer_interface.
[Graphical view]
PANTHERPTHR22942:SF12. PTHR22942:SF12. 1 hit.
PfamPF08423. Rad51. 1 hit.
[Graphical view]
PIRSFPIRSF005856. Rad51. 1 hit.
SMARTSM00382. AAA. 1 hit.
SM00278. HhH1. 1 hit.
[Graphical view]
SUPFAMSSF47794. SSF47794. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR02239. recomb_RAD51. 1 hit.
PROSITEPS50162. RECA_2. 1 hit.
PS50163. RECA_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi43577.
NextBio834653.
PROQ27297.

Entry information

Entry nameRAD51_DROME
AccessionPrimary (citable) accession number: Q27297
Secondary accession number(s): Q8IGG8, Q8IMJ5, Q9VAA8
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: April 16, 2014
This is version 123 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase