Q27297 (RAD51_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Drosophila melanogaster (Fruit fly) [Reference proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Panarthropoda › Arthropoda › Mandibulata › Pancrustacea › Hexapoda › Insecta › Dicondylia › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Eremoneura › Cyclorrhapha › Schizophora › Acalyptratae › Ephydroidea › Drosophilidae › Drosophilinae › Drosophilini › Drosophilina › Drosophiliti › Drosophila › Sophophora › melanogaster group › melanogaster subgroup

Protein attributes

Sequence length	336 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	Meiosis
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Ligand	ATP-binding DNA-binding Nucleotide-binding
Molecular function	Developmental protein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell cycle checkpoint Inferred from mutant phenotype PubMed 14592983. 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 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_component	nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 336	336	DNA repair protein Rad51 homolog		PRO_0000122938
Regions
	Nucleotide binding	124 – 131	8	ATP Potential
Natural variations
	Alternative sequence	1 – 57	57	Missing in isoform B.		VSP_012414
Experimental info
	Sequence conflict	334 – 336	3	RES → GRANCAHL in AAN71546. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Isoform A [UniParc]. Last modified November 1, 1997. Version 1. Checksum: F9E9B21405B15DB0	FASTA	336	36,647
	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
	Isoform B [UniParc]. Checksum: BF82A5C319AB61F9	FASTA	279	30,459
	10 20 30 40 50 60 MAIPGLGGGK VEQIITEANK LVPLGFLSAR TFYQMRADVV QLSTGSKELD KLLGGGIETG 70 80 90 100 110 120 SITEIFGEFR CGKTQLCHTL AVTCQLPISQ KGGEGKCMYI DTENTFRPER LAAIAQRYKL 130 140 150 160 170 180 NESEVLDNVA FTRAHNSDQQ TKLIQMAAGM LFESRYALLI VDSAMALYRS DYIGRGELAA 190 200 210 220 230 240 RQNHLGLFLR MLQRLADEFG VAVVITNQVT ASLDGAPGMF DAKKPIGGHI MAHSSTTRLY 250 260 270 LRKGKGETRI CKIYDSPCLP ESEAMFAILP DGIGDARES

References

	« Hide 'large scale' referencesShow '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. , 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. , 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.
RefSeq	NP_524583.1. NM_079844.4. NP_733342.1. NM_170463.3.
UniGene	Dm.1913.
3D structure databases
ProteinModelPortal	Q27297.
SMR	Q27297. Positions 22-335.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-20846N.
IntAct	Q27297. 37 interactions.
MINT	MINT-337614.
Proteomic databases
PaxDb	Q27297.
PRIDE	Q27297.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0085589; FBpp0084955; FBgn0003479.
GeneID	43577.
KEGG	dme:Dmel_CG7948.
Organism-specific databases
CTD	43577.
FlyBase	FBgn0003479. spn-A.
Phylogenomic databases
eggNOG	COG0468.
GeneTree	ENSGT00550000074609.
InParanoid	Q27297.
KO	K04482.
OMA	MMAESRY.
OrthoDB	EOG4P2NHW.
PhylomeDB	Q27297.
Gene expression databases
Bgee	Q27297.
GermOnline	CG7948. Drosophila melanogaster.
Family and domain databases
InterPro	IPR003593. AAA+_ATPase. IPR011941. DNA_recomb/repair_Rad51. IPR013632. DNA_recomb/repair_Rad51_C. IPR016467. DNA_recomb/repair_RecA-like. IPR020588. DNA_recomb_RecA/RadB_ATP-bd. IPR010995. DNA_repair_Rad51/TF_NusA_a-hlx. IPR003583. Hlx-hairpin-Hlx_DNA-bd_motif. IPR020587. RecA_monomer-monomer_interface. [Graphical view]
PANTHER	PTHR22942:SF12. PTHR22942:SF12. 1 hit.
Pfam	PF08423. Rad51. 1 hit. [Graphical view]
PIRSF	PIRSF005856. Rad51. 1 hit.
SMART	SM00382. AAA. 1 hit. SM00278. HhH1. 1 hit. [Graphical view]
SUPFAM	SSF47794. Rad51_N. 1 hit.
TIGRFAMs	TIGR02239. recomb_RAD51. 1 hit.
PROSITE	PS50162. RECA_2. 1 hit. PS50163. RECA_3. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	43577.
NextBio	834653.

Entry information

Entry name

RAD51_DROME

Accession

Primary (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:	May 1, 2013
This is version 115 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project