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DNA repair protein RAD51 homolog

 F6WB93_MONDO            Unreviewed;       339 AA.
F6WB93;
27-JUL-2011, integrated into UniProtKB/TrEMBL.
09-JAN-2013, sequence version 2.
18-JUL-2018, entry version 60.
RecName: Full=DNA repair protein RAD51 homolog {ECO:0000256|RuleBase:RU364139};
Name=RAD51 {ECO:0000313|Ensembl:ENSMODP00000000325};
Monodelphis domestica (Gray short-tailed opossum).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Metatheria; Didelphimorphia; Didelphidae; Monodelphis.
NCBI_TaxID=13616 {ECO:0000313|Ensembl:ENSMODP00000000325, ECO:0000313|Proteomes:UP000002280};
[1] {ECO:0000313|Ensembl:ENSMODP00000000325, ECO:0000313|Proteomes:UP000002280}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=17495919; DOI=10.1038/nature05805;
Mikkelsen T.S., Wakefield M.J., Aken B., Amemiya C.T., Chang J.L.,
Duke S., Garber M., Gentles A.J., Goodstadt L., Heger A., Jurka J.,
Kamal M., Mauceli E., Searle S.M., Sharpe T., Baker M.L., Batzer M.A.,
Benos P.V., Belov K., Clamp M., Cook A., Cuff J., Das R., Davidow L.,
Deakin J.E., Fazzari M.J., Glass J.L., Grabherr M., Greally J.M.,
Gu W., Hore T.A., Huttley G.A., Kleber M., Jirtle R.L., Koina E.,
Lee J.T., Mahony S., Marra M.A., Miller R.D., Nicholls R.D., Oda M.,
Papenfuss A.T., Parra Z.E., Pollock D.D., Ray D.A., Schein J.E.,
Speed T.P., Thompson K., VandeBerg J.L., Wade C.M., Walker J.A.,
Waters P.D., Webber C., Weidman J.R., Xie X., Zody M.C., Baldwin J.,
Abdouelleil A., Abdulkadir J., Abebe A., Abera B., Abreu J.,
Acer S.C., Aftuck L., Alexander A., An P., Anderson E., Anderson S.,
Arachi H., Azer M., Bachantsang P., Barry A., Bayul T., Berlin A.,
Bessette D., Bloom T., Bloom T., Boguslavskiy L., Bonnet C.,
Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S.,
Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P.,
Costello M., D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C.,
Dhargay N., Dooley K., Dooley E., Doricent M., Dorje P., Dorjee K.,
Dupes A., Elong R., Falk J., Farina A., Faro S., Ferguson D.,
Fisher S., Foley C.D., Franke A., Friedrich D., Gadbois L., Gearin G.,
Gearin C.R., Giannoukos G., Goode T., Graham J., Grandbois E.,
Grewal S., Gyaltsen K., Hafez N., Hagos B., Hall J., Henson C.,
Hollinger A., Honan T., Huard M.D., Hughes L., Hurhula B., Husby M.E.,
Kamat A., Kanga B., Kashin S., Khazanovich D., Kisner P., Lance K.,
Lara M., Lee W., Lennon N., Letendre F., LeVine R., Lipovsky A.,
Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y., Lubonja R.,
Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C.,
McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O.,
Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A.,
Mulrain L., Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N.,
Nicol R., Norbu C., Norbu N., Novod N., O'Neill B., Osman S.,
Markiewicz E., Oyono O.L., Patti C., Phunkhang P., Pierre F.,
Priest M., Raghuraman S., Rege F., Reyes R., Rise C., Rogov P.,
Ross K., Ryan E., Settipalli S., Shea T., Sherpa N., Shi L., Shih D.,
Sparrow T., Spaulding J., Stalker J., Stange-Thomann N.,
Stavropoulos S., Stone C., Strader C., Tesfaye S., Thomson T.,
Thoulutsang Y., Thoulutsang D., Topham K., Topping I., Tsamla T.,
Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M., Wilkinson J.,
Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D., Zimmer A.,
Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J., Chin C.,
Gnerre S., MacCallum I., Graves J.A., Ponting C.P., Breen M.,
Samollow P.B., Lander E.S., Lindblad-Toh K.;
"Genome of the marsupial Monodelphis domestica reveals innovation in
non-coding sequences.";
Nature 447:167-177(2007).
[2] {ECO:0000313|Ensembl:ENSMODP00000000325}
IDENTIFICATION.
Ensembl;
Submitted (JUL-2011) to UniProtKB.
-!- FUNCTION: Plays an important role in homologous strand exchange, a
key step in DNA repair through homologous recombination. Binds to
single and double-stranded DNA and exhibits DNA-dependent ATPase
activity. Catalyzes the recognition of homology and strand
exchange between homologous DNA partners to form a joint molecule
between a processed DNA break and the repair template. Binds to
single-stranded DNA in an ATP-dependent manner to form
nucleoprotein filaments which are essential for the homology
search and strand exchange. {ECO:0000256|RuleBase:RU364139}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU364139}.
-!- SIMILARITY: Belongs to the RecA family. RAD51 subfamily.
{ECO:0000256|RuleBase:RU364139}.
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RefSeq; XP_001370830.1; XM_001370793.3.
RefSeq; XP_007480119.1; XM_007480057.2.
RefSeq; XP_007480120.1; XM_007480058.2.
RefSeq; XP_007480121.1; XM_007480059.2.
ProteinModelPortal; F6WB93; -.
STRING; 13616.ENSMODP00000000325; -.
Ensembl; ENSMODT00000000330; ENSMODP00000000325; ENSMODG00000000268.
GeneID; 100027424; -.
KEGG; mdo:100027424; -.
CTD; 5888; -.
eggNOG; KOG1433; Eukaryota.
eggNOG; COG0468; LUCA.
GeneTree; ENSGT00890000139508; -.
InParanoid; F6WB93; -.
KO; K04482; -.
OrthoDB; EOG091G09QY; -.
TreeFam; TF101218; -.
Proteomes; UP000002280; Chromosome 1.
Bgee; ENSMODG00000000268; -.
GO; GO:0000794; C:condensed nuclear chromosome; IBA:GO_Central.
GO; GO:0000800; C:lateral element; IEA:Ensembl.
GO; GO:0000784; C:nuclear chromosome, telomeric region; IEA:Ensembl.
GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
GO; GO:0008094; F:DNA-dependent ATPase activity; IBA:GO_Central.
GO; GO:0003690; F:double-stranded DNA binding; IBA:GO_Central.
GO; GO:0000400; F:four-way junction DNA binding; IBA:GO_Central.
GO; GO:0000150; F:recombinase activity; IBA:GO_Central.
GO; GO:0003697; F:single-stranded DNA binding; IBA:GO_Central.
GO; GO:0071312; P:cellular response to alkaloid; IEA:Ensembl.
GO; GO:0072711; P:cellular response to hydroxyurea; IEA:Ensembl.
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:0006312; P:mitotic recombination; IBA:GO_Central.
GO; GO:1990426; P:mitotic recombination-dependent replication fork processing; IEA:InterPro.
GO; GO:0007131; P:reciprocal meiotic recombination; IBA:GO_Central.
GO; GO:0001932; P:regulation of protein phosphorylation; IEA:Ensembl.
GO; GO:1990414; P:replication-born double-strand break repair via sister chromatid exchange; IEA:Ensembl.
GO; GO:0010212; P:response to ionizing radiation; IBA:GO_Central.
GO; GO:0042148; P:strand invasion; IBA:GO_Central.
GO; GO:0000722; P:telomere maintenance via recombination; IEA:Ensembl.
GO; GO:0010833; P:telomere maintenance via telomere lengthening; IEA:Ensembl.
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.
3: Inferred from homology;
ATP-binding {ECO:0000256|RuleBase:RU003422};
Complete proteome {ECO:0000313|Proteomes:UP000002280};
DNA damage {ECO:0000256|RuleBase:RU364139};
DNA recombination {ECO:0000256|RuleBase:RU364139};
DNA repair {ECO:0000256|RuleBase:RU364139};
DNA-binding {ECO:0000256|RuleBase:RU364139};
Nucleotide-binding {ECO:0000256|RuleBase:RU003422};
Nucleus {ECO:0000256|RuleBase:RU364139};
Reference proteome {ECO:0000313|Proteomes:UP000002280}.
DOMAIN 98 269 RECA_2. {ECO:0000259|PROSITE:PS50162}.
DOMAIN 276 339 RECA_3. {ECO:0000259|PROSITE:PS50163}.
SEQUENCE 339 AA; 36906 MW; B9D2F97606EA37DF CRC64;
MAMQMQFEAS ADTSVEEENI GPQPISRLEQ CGINANDLKK LEEAGYHTVE AVAYAPKKEL
INVKGISEAK ADKILAEAAK LVPMGFTTAT EFHQQRSEII QITTGSKELD KLLQGGIETG
SITEIFGEFR TGKTQICHTL AVTCQLPIDR GGGEGKAMYI DTEGTFRPER LLAVAERYGL
SGSDVLDNVA YARGFNTDHQ TQLLYQASAM MVESRYALLI VDSSTALYRT DYSGRGELSA
RQMHLARFLR MLLRLADEFG VAVVITNQVV AQVDGAAMFA ADPKKPIGGN IIAHASTTRL
YLRKGRGETR ICKIYDSPCL PEAEAVFAIN ADGVGDAKD


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