ID   RA51C_DICDI             Reviewed;         381 AA.
AC   Q54PJ7;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=DNA repair protein RAD51 homolog 3;
GN   Name=rad51c; ORFNames=DDB_G0284507;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
CC   -!- FUNCTION: Involved in the homologous recombination repair (HRR) pathway
CC       of double-stranded DNA breaks arising during DNA replication or induced
CC       by DNA-damaging agents. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the RecA family. RAD51 subfamily. {ECO:0000305}.
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DR   EMBL; AAFI02000066; EAL65180.1; -; Genomic_DNA.
DR   RefSeq; XP_638535.1; XM_633443.1.
DR   AlphaFoldDB; Q54PJ7; -.
DR   SMR; Q54PJ7; -.
DR   STRING; 44689.DDB0232315; -.
DR   PaxDb; Q54PJ7; -.
DR   EnsemblProtists; EAL65180; EAL65180; DDB_G0284507.
DR   GeneID; 8624628; -.
DR   KEGG; ddi:DDB_G0284507; -.
DR   dictyBase; DDB_G0284507; -.
DR   eggNOG; KOG1434; Eukaryota.
DR   HOGENOM; CLU_041732_1_1_1; -.
DR   InParanoid; Q54PJ7; -.
DR   OMA; YHIVITI; -.
DR   PhylomeDB; Q54PJ7; -.
DR   PRO; PR:Q54PJ7; -.
DR   Proteomes; UP000002195; Chromosome 4.
DR   GO; GO:0005634; C:nucleus; ISS:dictyBase.
DR   GO; GO:0033063; C:Rad51B-Rad51C-Rad51D-XRCC2 complex; IBA:GO_Central.
DR   GO; GO:0033065; C:Rad51C-XRCC3 complex; IBA:GO_Central.
DR   GO; GO:0005657; C:replication fork; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; ISS:dictyBase.
DR   GO; GO:0000707; P:meiotic DNA recombinase assembly; IBA:GO_Central.
DR   GO; GO:0007131; P:reciprocal meiotic recombination; IBA:GO_Central.
DR   CDD; cd01123; Rad51_DMC1_radA; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR013632; DNA_recomb/repair_Rad51_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR033925; Rad51_DMC1_RadA.
DR   InterPro; IPR020588; RecA_ATP-bd.
DR   Pfam; PF08423; Rad51; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS50162; RECA_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Coiled coil; DNA damage; DNA recombination; DNA repair;
KW   DNA-binding; Nucleotide-binding; Nucleus; Reference proteome.
FT   CHAIN           1..381
FT                   /note="DNA repair protein RAD51 homolog 3"
FT                   /id="PRO_0000377485"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          313..381
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          323..377
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        8..24
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        322..339
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        340..374
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         89..96
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   381 AA;  43955 MW;  AC3597ADF23F5403 CRC64;
     MDEDINKDTN NNNNTTDSNN NNNNINEDEI IFNNYINNYS NYLNNNGISA LDLLIQGRDG
     NNNIITFCSE IDQMLNGGTP LKKITEICGV PGIGKTNMAF QLLVNTSIPF DLGGVQGKAI
     YIDTEGSYSC QRVREMATHL VNHLECVLLK NPMTQTTYIP TVETVLNSIY YYRVYHYIEI
     ISLIHQLPLF LEKNKDVKLI VVDSITYPFR CDFKDMGLRT RSLLSLAQNL MNIATRYNLA
     VVVMNQVTTK ISPNQKESIL VPYLGESWTH ICTYRMVLFW KQKQRFCHLY KSPSFKSCFT
     PFDIVEYGIR DVGFNHPPPL NPEDQEQEKE KEKRKKKNNN NNNNNNNNNN NNNNNNNNNN
     NNNNNNNNNK NNDENEMYIE N