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Protein

DNA repair protein Rad51 homolog

Gene

spn-A

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Binds to single and double-stranded DNA and exhibits DNA-dependent ATPase activity. Underwinds duplex DNA (By similarity).By similarity
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.2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi124 – 1318ATPSequence Analysis

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. damaged DNA binding Source: InterPro
  3. DNA-dependent ATPase activity Source: InterPro
  4. recombinase activity Source: FlyBase

GO - Biological processi

  1. DNA recombination Source: FlyBase
  2. DNA repair Source: FlyBase
  3. double-strand break repair Source: FlyBase
  4. double-strand break repair via synthesis-dependent strand annealing Source: FlyBase
  5. female meiotic division Source: FlyBase
  6. germarium-derived oocyte fate determination Source: FlyBase
  7. intracellular mRNA localization Source: FlyBase
  8. karyosome formation Source: FlyBase
  9. oocyte differentiation Source: FlyBase
  10. oogenesis Source: FlyBase
  11. polarity specification of anterior/posterior axis Source: FlyBase
  12. polarity specification of dorsal/ventral axis Source: FlyBase
  13. regulation of double-strand break repair via homologous recombination Source: FlyBase
  14. response to caffeine Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Meiosis

Keywords - Ligandi

ATP-binding, DNA-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_337890. Assembly of the RAD51-ssDNA nucleoprotein complex.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA repair protein Rad51 homolog
Alternative name(s):
Protein spindle-A
RecA protein homolog
Gene namesi
Name:spn-A
Synonyms:DMR, Rad51
ORF Names:CG7948
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803 Componenti: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0003479. spn-A.

Subcellular locationi

Nucleus Curated

GO - Cellular componenti

  1. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 336336DNA repair protein Rad51 homologPRO_0000122938Add
BLAST

Proteomic databases

PaxDbiQ27297.
PRIDEiQ27297.

Expressioni

Tissue specificityi

Highly expressed in ovaries.1 Publication

Gene expression databases

BgeeiQ27297.
ExpressionAtlasiQ27297. differential.

Interactioni

Protein-protein interaction databases

BioGridi68433. 69 interactions.
DIPiDIP-20846N.
IntActiQ27297. 38 interactions.
MINTiMINT-337614.

Structurei

3D structure databases

ProteinModelPortaliQ27297.
SMRiQ27297. Positions 22-335.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the RecA family. RAD51 subfamily.Curated
Contains 1 HhH domain.Curated

Phylogenomic databases

eggNOGiCOG0468.
GeneTreeiENSGT00770000120539.
InParanoidiQ27297.
KOiK04482.
OMAiCQLPIDQ.
OrthoDBiEOG715Q4H.
PhylomeDBiQ27297.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR003593. 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]
PfamiPF08423. Rad51. 1 hit.
[Graphical view]
PIRSFiPIRSF005856. Rad51. 1 hit.
SMARTiSM00382. AAA. 1 hit.
SM00278. HhH1. 1 hit.
[Graphical view]
SUPFAMiSSF47794. SSF47794. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR02239. recomb_RAD51. 1 hit.
PROSITEiPS50162. RECA_2. 1 hit.
PS50163. RECA_3. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform A (identifier: Q27297-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MEKLTNVQAQ QEEEEEEGPL SVTKLIGGSI TAKDIKLLQQ ASLHTVESVA
60 70 80 90 100
NATKKQLMAI PGLGGGKVEQ IITEANKLVP LGFLSARTFY QMRADVVQLS
110 120 130 140 150
TGSKELDKLL GGGIETGSIT EIFGEFRCGK TQLCHTLAVT CQLPISQKGG
160 170 180 190 200
EGKCMYIDTE NTFRPERLAA IAQRYKLNES EVLDNVAFTR AHNSDQQTKL
210 220 230 240 250
IQMAAGMLFE SRYALLIVDS AMALYRSDYI GRGELAARQN HLGLFLRMLQ
260 270 280 290 300
RLADEFGVAV VITNQVTASL DGAPGMFDAK KPIGGHIMAH SSTTRLYLRK
310 320 330
GKGETRICKI YDSPCLPESE AMFAILPDGI GDARES
Length:336
Mass (Da):36,647
Last modified:November 1, 1997 - v1
Checksum:iF9E9B21405B15DB0
GO
Isoform B (identifier: Q27297-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-57: Missing.

Note: No experimental confirmation available.

Show »
Length:279
Mass (Da):30,459
Checksum:iBF82A5C319AB61F9
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti334 – 3363RES → GRANCAHL in AAN71546 (PubMed:12537569).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 5757Missing in isoform B. 1 PublicationVSP_012414Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
RefSeqiNP_524583.1. NM_079844.4. [Q27297-1]
NP_733342.1. NM_170463.3. [Q27297-2]
UniGeneiDm.1913.

Genome annotation databases

EnsemblMetazoaiFBtr0085589; FBpp0084955; FBgn0003479. [Q27297-1]
GeneIDi43577.
KEGGidme:Dmel_CG7948.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
RefSeqiNP_524583.1. NM_079844.4. [Q27297-1]
NP_733342.1. NM_170463.3. [Q27297-2]
UniGeneiDm.1913.

3D structure databases

ProteinModelPortaliQ27297.
SMRiQ27297. Positions 22-335.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi68433. 69 interactions.
DIPiDIP-20846N.
IntActiQ27297. 38 interactions.
MINTiMINT-337614.

Proteomic databases

PaxDbiQ27297.
PRIDEiQ27297.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0085589; FBpp0084955; FBgn0003479. [Q27297-1]
GeneIDi43577.
KEGGidme:Dmel_CG7948.

Organism-specific databases

CTDi43577.
FlyBaseiFBgn0003479. spn-A.

Phylogenomic databases

eggNOGiCOG0468.
GeneTreeiENSGT00770000120539.
InParanoidiQ27297.
KOiK04482.
OMAiCQLPIDQ.
OrthoDBiEOG715Q4H.
PhylomeDBiQ27297.

Enzyme and pathway databases

ReactomeiREACT_337890. Assembly of the RAD51-ssDNA nucleoprotein complex.

Miscellaneous databases

GenomeRNAii43577.
NextBioi834653.
PROiQ27297.

Gene expression databases

BgeeiQ27297.
ExpressionAtlasiQ27297. differential.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR003593. 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]
PfamiPF08423. Rad51. 1 hit.
[Graphical view]
PIRSFiPIRSF005856. Rad51. 1 hit.
SMARTiSM00382. AAA. 1 hit.
SM00278. HhH1. 1 hit.
[Graphical view]
SUPFAMiSSF47794. SSF47794. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR02239. recomb_RAD51. 1 hit.
PROSITEiPS50162. RECA_2. 1 hit.
PS50163. RECA_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1993) [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(1995) [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.
    , 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(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  4. Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
    Strain: Berkeley.
  5. 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(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiRAD51_DROME
AccessioniPrimary (citable) accession number: Q27297
Secondary accession number(s): Q8IGG8, Q8IMJ5, Q9VAA8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: April 1, 2015
This is version 132 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.