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Database: UniProt
Entry: D2A283_TRICA
LinkDB: D2A283_TRICA
Original site: D2A283_TRICA 
ID   D2A283_TRICA            Unreviewed;       338 AA.
AC   D2A283;
DT   09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT   09-FEB-2010, sequence version 1.
DT   27-MAR-2024, entry version 78.
DE   RecName: Full=DNA repair protein RAD51 homolog {ECO:0000256|RuleBase:RU364139};
GN   Name=AUGUSTUS-3.0.2_07805 {ECO:0000313|EMBL:EFA02865.1};
GN   ORFNames=TcasGA2_TC007805 {ECO:0000313|EMBL:EFA02865.1};
OS   Tribolium castaneum (Red flour beetle).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC   Tenebrionidae; Tenebrionidae incertae sedis; Tribolium.
OX   NCBI_TaxID=7070 {ECO:0000313|EMBL:EFA02865.1, ECO:0000313|Proteomes:UP000007266};
RN   [1] {ECO:0000313|EMBL:EFA02865.1, ECO:0000313|Proteomes:UP000007266}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Georgia GA2 {ECO:0000313|EMBL:EFA02865.1,
RC   ECO:0000313|Proteomes:UP000007266};
RX   PubMed=18362917; DOI=10.1038/nature06784;
RG   Tribolium Genome Sequencing Consortium;
RA   Richards S., Gibbs R.A., Weinstock G.M., Brown S.J., Denell R.,
RA   Beeman R.W., Gibbs R., Beeman R.W., Brown S.J., Bucher G., Friedrich M.,
RA   Grimmelikhuijzen C.J., Klingler M., Lorenzen M., Richards S., Roth S.,
RA   Schroder R., Tautz D., Zdobnov E.M., Muzny D., Gibbs R.A., Weinstock G.M.,
RA   Attaway T., Bell S., Buhay C.J., Chandrabose M.N., Chavez D.,
RA   Clerk-Blankenburg K.P., Cree A., Dao M., Davis C., Chacko J., Dinh H.,
RA   Dugan-Rocha S., Fowler G., Garner T.T., Garnes J., Gnirke A., Hawes A.,
RA   Hernandez J., Hines S., Holder M., Hume J., Jhangiani S.N., Joshi V.,
RA   Khan Z.M., Jackson L., Kovar C., Kowis A., Lee S., Lewis L.R., Margolis J.,
RA   Morgan M., Nazareth L.V., Nguyen N., Okwuonu G., Parker D., Richards S.,
RA   Ruiz S.J., Santibanez J., Savard J., Scherer S.E., Schneider B.,
RA   Sodergren E., Tautz D., Vattahil S., Villasana D., White C.S., Wright R.,
RA   Park Y., Beeman R.W., Lord J., Oppert B., Lorenzen M., Brown S., Wang L.,
RA   Savard J., Tautz D., Richards S., Weinstock G., Gibbs R.A., Liu Y.,
RA   Worley K., Weinstock G., Elsik C.G., Reese J.T., Elhaik E., Landan G.,
RA   Graur D., Arensburger P., Atkinson P., Beeman R.W., Beidler J., Brown S.J.,
RA   Demuth J.P., Drury D.W., Du Y.Z., Fujiwara H., Lorenzen M., Maselli V.,
RA   Osanai M., Park Y., Robertson H.M., Tu Z., Wang J.J., Wang S., Richards S.,
RA   Song H., Zhang L., Sodergren E., Werner D., Stanke M., Morgenstern B.,
RA   Solovyev V., Kosarev P., Brown G., Chen H.C., Ermolaeva O., Hlavina W.,
RA   Kapustin Y., Kiryutin B., Kitts P., Maglott D., Pruitt K., Sapojnikov V.,
RA   Souvorov A., Mackey A.J., Waterhouse R.M., Wyder S., Zdobnov E.M.,
RA   Zdobnov E.M., Wyder S., Kriventseva E.V., Kadowaki T., Bork P., Aranda M.,
RA   Bao R., Beermann A., Berns N., Bolognesi R., Bonneton F., Bopp D.,
RA   Brown S.J., Bucher G., Butts T., Chaumot A., Denell R.E., Ferrier D.E.,
RA   Friedrich M., Gordon C.M., Jindra M., Klingler M., Lan Q., Lattorff H.M.,
RA   Laudet V., von Levetsow C., Liu Z., Lutz R., Lynch J.A., da Fonseca R.N.,
RA   Posnien N., Reuter R., Roth S., Savard J., Schinko J.B., Schmitt C.,
RA   Schoppmeier M., Schroder R., Shippy T.D., Simonnet F., Marques-Souza H.,
RA   Tautz D., Tomoyasu Y., Trauner J., Van der Zee M., Vervoort M.,
RA   Wittkopp N., Wimmer E.A., Yang X., Jones A.K., Sattelle D.B., Ebert P.R.,
RA   Nelson D., Scott J.G., Beeman R.W., Muthukrishnan S., Kramer K.J.,
RA   Arakane Y., Beeman R.W., Zhu Q., Hogenkamp D., Dixit R., Oppert B.,
RA   Jiang H., Zou Z., Marshall J., Elpidina E., Vinokurov K., Oppert C.,
RA   Zou Z., Evans J., Lu Z., Zhao P., Sumathipala N., Altincicek B.,
RA   Vilcinskas A., Williams M., Hultmark D., Hetru C., Jiang H.,
RA   Grimmelikhuijzen C.J., Hauser F., Cazzamali G., Williamson M., Park Y.,
RA   Li B., Tanaka Y., Predel R., Neupert S., Schachtner J., Verleyen P.,
RA   Raible F., Bork P., Friedrich M., Walden K.K., Robertson H.M., Angeli S.,
RA   Foret S., Bucher G., Schuetz S., Maleszka R., Wimmer E.A., Beeman R.W.,
RA   Lorenzen M., Tomoyasu Y., Miller S.C., Grossmann D., Bucher G.;
RT   "The genome of the model beetle and pest Tribolium castaneum.";
RL   Nature 452:949-955(2008).
RN   [2] {ECO:0000313|EMBL:EFA02865.1, ECO:0000313|Proteomes:UP000007266}
RP   GENOME REANNOTATION.
RC   STRAIN=Georgia GA2 {ECO:0000313|EMBL:EFA02865.1,
RC   ECO:0000313|Proteomes:UP000007266};
RX   PubMed=19820115; DOI=10.1093/nar/gkp807;
RA   Kim H.S., Murphy T., Xia J., Caragea D., Park Y., Beeman R.W.,
RA   Lorenzen M.D., Butcher S., Manak J.R., Brown S.J.;
RT   "BeetleBase in 2010: revisions to provide comprehensive genomic information
RT   for Tribolium castaneum.";
RL   Nucleic Acids Res. 38:D437-D442(2010).
CC   -!- FUNCTION: Binds to single and double-stranded DNA and exhibits DNA-
CC       dependent ATPase activity. Underwinds duplex DNA.
CC       {ECO:0000256|RuleBase:RU364139}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC       ECO:0000256|RuleBase:RU364139}.
CC   -!- SIMILARITY: Belongs to the RecA family. RAD51 subfamily.
CC       {ECO:0000256|ARBA:ARBA00007095, ECO:0000256|RuleBase:RU364139}.
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DR   EMBL; KQ971338; EFA02865.1; -; Genomic_DNA.
DR   RefSeq; XP_974146.1; XM_969053.3.
DR   AlphaFoldDB; D2A283; -.
DR   STRING; 7070.D2A283; -.
DR   EnsemblMetazoa; TC007805_001; TC007805_001; TC007805.
DR   GeneID; 662986; -.
DR   KEGG; tca:662986; -.
DR   eggNOG; KOG1433; Eukaryota.
DR   HOGENOM; CLU_041732_0_2_1; -.
DR   InParanoid; D2A283; -.
DR   OMA; EMRICKI; -.
DR   OrthoDB; 5477610at2759; -.
DR   PhylomeDB; D2A283; -.
DR   Proteomes; UP000007266; Linkage group 4.
DR   GO; GO:0000794; C:condensed nuclear chromosome; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0008094; F:ATP-dependent activity, acting on DNA; IBA:GO_Central.
DR   GO; GO:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
DR   GO; GO:0000150; F:DNA strand exchange activity; IBA:GO_Central.
DR   GO; GO:0003690; F:double-stranded DNA binding; IBA:GO_Central.
DR   GO; GO:0003697; F:single-stranded DNA binding; IBA:GO_Central.
DR   GO; GO:0070192; P:chromosome organization involved in meiotic cell cycle; IBA:GO_Central.
DR   GO; GO:0000730; P:DNA recombinase assembly; IBA:GO_Central.
DR   GO; GO:0042148; P:DNA strand invasion; IBA:GO_Central.
DR   GO; GO:0006312; P:mitotic recombination; IBA:GO_Central.
DR   GO; GO:1990426; P:mitotic recombination-dependent replication fork processing; IEA:InterPro.
DR   GO; GO:0007131; P:reciprocal meiotic recombination; IBA:GO_Central.
DR   CDD; cd19513; Rad51; 1.
DR   Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR011941; DNA_recomb/repair_Rad51.
DR   InterPro; IPR013632; DNA_recomb/repair_Rad51_C.
DR   InterPro; IPR016467; DNA_recomb/repair_RecA-like.
DR   InterPro; IPR010995; DNA_repair_Rad51/TF_NusA_a-hlx.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR020588; RecA_ATP-bd.
DR   InterPro; IPR020587; RecA_monomer-monomer_interface.
DR   NCBIfam; TIGR02239; recomb_RAD51; 1.
DR   PANTHER; PTHR22942:SF39; DNA REPAIR PROTEIN RAD51 HOMOLOG 1; 1.
DR   PANTHER; PTHR22942; RECA/RAD51/RADA DNA STRAND-PAIRING FAMILY MEMBER; 1.
DR   Pfam; PF14520; HHH_5; 1.
DR   Pfam; PF08423; Rad51; 1.
DR   PIRSF; PIRSF005856; Rad51; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF47794; Rad51 N-terminal domain-like; 1.
DR   PROSITE; PS50162; RECA_2; 1.
DR   PROSITE; PS50163; RECA_3; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU003422};
KW   DNA damage {ECO:0000256|RuleBase:RU364139};
KW   DNA recombination {ECO:0000256|RuleBase:RU364139};
KW   DNA repair {ECO:0000256|RuleBase:RU364139};
KW   DNA-binding {ECO:0000256|RuleBase:RU364139};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU003422};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU364139};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007266}.
FT   DOMAIN          97..268
FT                   /note="RecA family profile 1"
FT                   /evidence="ECO:0000259|PROSITE:PS50162"
FT   DOMAIN          275..338
FT                   /note="RecA family profile 2"
FT                   /evidence="ECO:0000259|PROSITE:PS50163"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   338 AA;  36611 MW;  3BEA01573B7DF399 CRC64;
     MEASLASTDT VIDEEAKAGG PQPLSKLQVN GITAGDLKKL EDAGFHSIES IAYTPKKVLA
     AIKGISEAKV NKLLAEAAKF VNMGFTTATD IHRRRANIIQ LTTGSKELDK LLGGGIETGS
     ITEIFGEFRT GKTQICHTLA VTCQLSVESG GGEGKCLYID TEGTFRPERL LPVAERYNMD
     GQQVLDNVVF ARAFNTDHQT ELLVHAAAMM MESRYCLLIV DSATSLYRTD YSGRGELSAR
     QNHLARFLRM LLRLADEFGV AVVLTNQVVA QVDGAAMFNA DPKKPIGGNI MAHSSTTRLS
     LRKGRGEARV CKIYDSPCLP ESEAIFAIRP DGIGDVQE
//
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