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DNA repair protein RAD50 (EC 3.6.-.-)

 RAD50_DROME             Reviewed;        1318 AA.
Q9W252; B6UXS6; B6UXT1; B6UXT2; B6UXT3; B6UXT4; B6UXT5; B6UXT6;
B6UXT7; B6UXT8; B6UXT9; B6UXU1; B6UXU2; B6UXU3; B6UXU4; B6UXU5;
B6UXU6; B6UXU7; B6UXU8; B6UXU9; B6UXV0; B6UXV1; B6UXV2; Q86NZ9;
Q960E0;
01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
18-APR-2012, sequence version 4.
25-APR-2018, entry version 143.
RecName: Full=DNA repair protein RAD50;
EC=3.6.-.-;
Name=rad50; ORFNames=CG6339;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
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.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[2]
GENOME REANNOTATION.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
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.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Berkeley; TISSUE=Larva, and Pupae;
Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W.,
Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E.,
George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G.,
Miranda A., Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S.,
Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M.,
Celniker S.E.;
Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 25-657, AND VARIANTS ASP-208;
VAL-219; GLU-220; GLU-246; MET-249; GLN-281; THR-349; GLU-422;
ILE-450; ASN-480; GLN-490; ILE-491; SER-580; ILE-586; ASN-623; SER-646
AND ALA-657.
STRAIN=MW11, MW25, MW27, MW56, MW6, MW9, NC301, NC303, NC304, NC306,
NC322, NC335, NC336, NC350, NC357, NC358, NC359, NC361, NC362, NC375,
NC390, NC397, and NC399;
PubMed=18984573; DOI=10.1534/genetics.108.093807;
Anderson J.A., Gilliland W.D., Langley C.H.;
"Molecular population genetics and evolution of Drosophila meiosis
genes.";
Genetics 181:177-185(2009).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 500-1318.
STRAIN=Berkeley; TISSUE=Embryo;
PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
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.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[6]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=15296753; DOI=10.1016/j.cub.2004.07.019;
Ciapponi L., Cenci G., Ducau J., Flores C., Johnson-Schlitz D.,
Gorski M.M., Engels W.R., Gatti M.;
"The Drosophila Mre11/Rad50 complex is required to prevent both
telomeric fusion and chromosome breakage.";
Curr. Biol. 14:1360-1366(2004).
[7]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=15135728; DOI=10.1016/j.dnarep.2004.02.001;
Gorski M.M., Romeijn R.J., Eeken J.C.J., de Jong A.W.M.,
van Veen B.L., Szuhai K., Mullenders L.H., Ferro W., Pastink A.;
"Disruption of Drosophila Rad50 causes pupal lethality, the
accumulation of DNA double-strand breaks and the induction of
apoptosis in third instar larvae.";
DNA Repair 3:603-615(2004).
-!- FUNCTION: Essential component of the MRN complex, a complex that
possesses single-stranded DNA endonuclease and 3' to 5'
exonuclease activities, and plays a central role in double-strand
break (DSB) repair. The complex participates in processes such as
DNA recombination, DNA repair, genome stability, telomere
integrity and meiosis. The MRN complex may protect telomeres by
facilitating recruitment of HOAP and HP1 at chromosome ends. In
the complex, it mediates the ATP-binding and is probably required
to bind DNA ends and hold them in close proximity.
{ECO:0000269|PubMed:15135728, ECO:0000269|PubMed:15296753}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
Note=Binds 1 zinc ion per homodimer. {ECO:0000250};
-!- SUBUNIT: Homodimer. Probable component of the MRN complex with
mre11 (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15296753}.
Chromosome {ECO:0000269|PubMed:15296753}. Chromosome, telomere
{ECO:0000269|PubMed:15296753}. Note=Uniformly distributed along
mitotic chromosomes.
-!- DOMAIN: The zinc-hook, which separates the large intramolecular
coiled coil regions, contains 2 Cys residues that coordinate one
molecule of zinc with the help of the 2 Cys residues of the zinc-
hook of another RAD50 molecule, thereby forming a V-shaped
homodimer. The two heads of the homodimer, which constitute the
ATP-binding domain, interact with the MRE11 homodimer (By
similarity). {ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Death during pupal stage, possibly due to
the accumulation of DNA DSBs and the induction of apoptosis in
third instar larvae. {ECO:0000269|PubMed:15135728}.
-!- SIMILARITY: Belongs to the SMC family. RAD50 subfamily.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAK93530.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAO39559.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; AE013599; AAF46847.3; -; Genomic_DNA.
EMBL; BT003555; AAO39559.1; ALT_INIT; mRNA.
EMBL; FJ219324; ACI97309.1; -; Genomic_DNA.
EMBL; FJ219329; ACI97314.1; -; Genomic_DNA.
EMBL; FJ219330; ACI97315.1; -; Genomic_DNA.
EMBL; FJ219331; ACI97316.1; -; Genomic_DNA.
EMBL; FJ219332; ACI97317.1; -; Genomic_DNA.
EMBL; FJ219333; ACI97318.1; -; Genomic_DNA.
EMBL; FJ219334; ACI97319.1; -; Genomic_DNA.
EMBL; FJ219335; ACI97320.1; -; Genomic_DNA.
EMBL; FJ219336; ACI97321.1; -; Genomic_DNA.
EMBL; FJ219337; ACI97322.1; -; Genomic_DNA.
EMBL; FJ219338; ACI97323.1; -; Genomic_DNA.
EMBL; FJ219339; ACI97324.1; -; Genomic_DNA.
EMBL; FJ219340; ACI97325.1; -; Genomic_DNA.
EMBL; FJ219341; ACI97326.1; -; Genomic_DNA.
EMBL; FJ219342; ACI97327.1; -; Genomic_DNA.
EMBL; FJ219343; ACI97328.1; -; Genomic_DNA.
EMBL; FJ219344; ACI97329.1; -; Genomic_DNA.
EMBL; FJ219345; ACI97330.1; -; Genomic_DNA.
EMBL; FJ219346; ACI97331.1; -; Genomic_DNA.
EMBL; FJ219347; ACI97332.1; -; Genomic_DNA.
EMBL; FJ219348; ACI97333.1; -; Genomic_DNA.
EMBL; FJ219349; ACI97334.1; -; Genomic_DNA.
EMBL; FJ219350; ACI97335.1; -; Genomic_DNA.
EMBL; AY052106; AAK93530.1; ALT_INIT; mRNA.
RefSeq; NP_726199.3; NM_166533.4.
ProteinModelPortal; Q9W252; -.
SMR; Q9W252; -.
BioGrid; 63180; 15.
IntAct; Q9W252; 10.
STRING; 7227.FBpp0290882; -.
PaxDb; Q9W252; -.
PRIDE; Q9W252; -.
EnsemblMetazoa; FBtr0301668; FBpp0290882; FBgn0034728.
GeneID; 37564; -.
KEGG; dme:Dmel_CG6339; -.
UCSC; CG6339-RB; d. melanogaster.
CTD; 10111; -.
FlyBase; FBgn0034728; rad50.
eggNOG; KOG0962; Eukaryota.
eggNOG; COG0419; LUCA.
GeneTree; ENSGT00390000018781; -.
InParanoid; Q9W252; -.
KO; K10866; -.
OMA; RSMVCTQ; -.
OrthoDB; EOG091G01KA; -.
PhylomeDB; Q9W252; -.
Reactome; R-DME-2559586; DNA Damage/Telomere Stress Induced Senescence.
Reactome; R-DME-5685939; HDR through MMEJ (alt-NHEJ).
Reactome; R-DME-5693548; Sensing of DNA Double Strand Breaks.
Reactome; R-DME-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
Reactome; R-DME-5693571; Nonhomologous End-Joining (NHEJ).
Reactome; R-DME-5693607; Processing of DNA double-strand break ends.
GenomeRNAi; 37564; -.
PRO; PR:Q9W252; -.
Proteomes; UP000000803; Chromosome 2R.
Bgee; FBgn0034728; -.
ExpressionAtlas; Q9W252; differential.
Genevisible; Q9W252; DM.
GO; GO:0000793; C:condensed chromosome; IDA:UniProtKB.
GO; GO:0000794; C:condensed nuclear chromosome; IBA:GO_Central.
GO; GO:0030870; C:Mre11 complex; TAS:UniProtKB.
GO; GO:0000790; C:nuclear chromatin; IBA:GO_Central.
GO; GO:0000784; C:nuclear chromosome, telomeric region; IBA:GO_Central.
GO; GO:0005634; C:nucleus; IMP:FlyBase.
GO; GO:0035861; C:site of double-strand break; IBA:GO_Central.
GO; GO:0004017; F:adenylate kinase activity; IBA:GO_Central.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0016887; F:ATPase activity; IEA:InterPro.
GO; GO:0003690; F:double-stranded DNA binding; ISS:UniProtKB.
GO; GO:0003691; F:double-stranded telomeric DNA binding; IBA:GO_Central.
GO; GO:0051880; F:G-quadruplex DNA binding; IBA:GO_Central.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0043047; F:single-stranded telomeric DNA binding; IBA:GO_Central.
GO; GO:0051276; P:chromosome organization; IMP:FlyBase.
GO; GO:0070192; P:chromosome organization involved in meiotic cell cycle; IBA:GO_Central.
GO; GO:0032508; P:DNA duplex unwinding; IBA:GO_Central.
GO; GO:0006302; P:double-strand break repair; IMP:UniProtKB.
GO; GO:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central.
GO; GO:0090305; P:nucleic acid phosphodiester bond hydrolysis; IBA:GO_Central.
GO; GO:0008104; P:protein localization; IMP:UniProtKB.
GO; GO:0007131; P:reciprocal meiotic recombination; IBA:GO_Central.
GO; GO:0016233; P:telomere capping; IMP:FlyBase.
GO; GO:0000723; P:telomere maintenance; IMP:CACAO.
GO; GO:0000722; P:telomere maintenance via recombination; IMP:UniProtKB.
GO; GO:0007004; P:telomere maintenance via telomerase; IBA:GO_Central.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR038729; Rad50/SbcC_AAA.
InterPro; IPR004584; Rad50_eukaryotes.
InterPro; IPR013134; Zn_hook_RAD50.
Pfam; PF13476; AAA_23; 1.
Pfam; PF04423; Rad50_zn_hook; 1.
SUPFAM; SSF52540; SSF52540; 7.
TIGRFAMs; TIGR00606; rad50; 1.
PROSITE; PS51131; ZN_HOOK; 1.
2: Evidence at transcript level;
ATP-binding; Cell cycle; Chromosome; Coiled coil; Complete proteome;
DNA damage; DNA repair; Hydrolase; Meiosis; Metal-binding;
Nucleotide-binding; Nucleus; Reference proteome; Telomere; Zinc.
CHAIN 1 1318 DNA repair protein RAD50.
/FTId=PRO_0000138645.
DOMAIN 645 741 Zinc-hook. {ECO:0000255|PROSITE-
ProRule:PRU00471}.
NP_BIND 36 43 ATP. {ECO:0000255}.
COILED 189 256 {ECO:0000255}.
COILED 305 333 {ECO:0000255}.
COILED 434 641 {ECO:0000255}.
COILED 645 685 {ECO:0000255}.
COILED 713 741 {ECO:0000255}.
COILED 830 1101 {ECO:0000255}.
COMPBIAS 1208 1245 Ala/Asp-rich (DA-box).
METAL 689 689 Zinc. {ECO:0000255|PROSITE-
ProRule:PRU00471}.
METAL 692 692 Zinc. {ECO:0000255|PROSITE-
ProRule:PRU00471}.
VARIANT 208 208 E -> D (in strain: NC335, NC362 and
NC390). {ECO:0000269|PubMed:18984573}.
VARIANT 219 219 H -> V (in strain: NC335, NC362 and
NC390). {ECO:0000269|PubMed:18984573}.
VARIANT 220 220 V -> E (in strain: NC335, NC362 and
NC390). {ECO:0000269|PubMed:18984573}.
VARIANT 246 246 A -> E (in strain: MW25).
{ECO:0000269|PubMed:18984573}.
VARIANT 249 249 S -> M (in strain: MW25).
{ECO:0000269|PubMed:18984573}.
VARIANT 281 281 E -> Q (in strain: NC306).
{ECO:0000269|PubMed:18984573}.
VARIANT 349 349 K -> T (in strain: MW9).
{ECO:0000269|PubMed:18984573}.
VARIANT 422 422 V -> E (in strain: NC361 and NC375).
{ECO:0000269|PubMed:18984573}.
VARIANT 450 450 V -> I (in strain: MW6).
{ECO:0000269|PubMed:18984573}.
VARIANT 480 480 D -> N (in strain: MW6).
{ECO:0000269|PubMed:18984573}.
VARIANT 490 490 E -> Q (in strain: MW25, MW27, MW56, MW9,
NC303, NC306, NC335, NC336, NC390 and
NC399). {ECO:0000269|PubMed:18984573}.
VARIANT 491 491 V -> I (in strain: NC303, NC306 and
NC335). {ECO:0000269|PubMed:18984573}.
VARIANT 580 580 C -> S (in strain: MW25).
{ECO:0000269|PubMed:18984573}.
VARIANT 586 586 M -> I (in strain: MW25).
{ECO:0000269|PubMed:18984573}.
VARIANT 623 623 S -> N (in strain: NC336, NC358, NC361,
NC362 and NC375).
{ECO:0000269|PubMed:18984573}.
VARIANT 646 646 T -> S (in strain: NC357 and NC397).
{ECO:0000269|PubMed:18984573}.
VARIANT 657 657 T -> A (in strain: MW6, NC357, NC358,
NC361, NC362, NC375 and NC397).
{ECO:0000269|PubMed:18984573}.
CONFLICT 880 880 R -> K (in Ref. 5; AAK93530).
{ECO:0000305}.
CONFLICT 959 959 H -> Q (in Ref. 5; AAK93530).
{ECO:0000305}.
SEQUENCE 1318 AA; 152160 MW; 1C84EB7B3F9E3BB9 CRC64;
MSSIESLSIQ GIRSFGTYAD DLQSIKFSSP VTLILGENGC GKTTVVECLK YALTGECPPG
SDRGKSFVHD PKIFGLNEVL AQIKMQVRDR RGAQVSICRT MKVSKKRNKM SFETMDSTIN
FLTGAGQSKR EKQDSLSGRS VDIDVAISDF MGVSKAIINN VLFCHQEDSS WPLDESKKLK
EKFDAIFGIT EYNKALDKII KLRKEAMEEL KIKEANIKHV AYLKQEMEVK TLNLQKAQRK
CDAIKAQCSE CEEEMKPIEA RLVEIRNVEF EIGKYQAQKV EMDTKHKNCK DQISTLTLKI
KKPFRGTLDE LDQEISNFDQ RMLEMRQKRT EVEGDLSQIK RSSVAEQEKL GTQDRKHCLA
KQRHQSELAC RAQLLKRVKE FCRELHIPID CDLVEQPEKM GEVLRDIEAM IITKHCEITE
IVEQNEKADR SRQVKIDELR IELTKSEQSV TAQEKQRESS KRESETLGVE IKKIETSMQD
LKKLEKEINE VNELYESATK NIDQQAIKDA IARKKASIAE NQIQFKKLDE QLTFLGSMAK
LVAECSLKQK ELDKKNQEVH RVRSRHSDHF GKLFKEPITC NYRRSMQVVY EKLRREIQEL
NEKANTQKLK EQSYEIKRKN LISDISRMEK ELKDSEELIY QKCRSTPYDD LLERSKTTIS
KLQFDHGALK SSEALYKKYI QKMDEEPSCP LCHHNMTSDE ACDLTSELTD EIQKLPDNIT
RAEKALKAEQ IKYENLLQLK PTILKVKELK DSLPQKKEEL KKVEELLGDS VSEYETLIAL
IGEPTHNMEL ANSMMGDMSL LDEALKDSAR LTKDLDLQKG QLPASYDSSV SMDDLQAEKS
KVSKELETER KELESAQNAV QQQMDALNRL REKKNSLKDR QIHLREGLQS LPQLKERLEK
LNSFLTTVAS EISELKAKIQ PLKLNLRAAI EEKERLKKSE SEKLAQLNSK YNSYKSTDHD
IQRLNKEAED YAKLDLRNEI KKLDEIIMAS KDKLRKLEAE ISLKTDELET IKTECSNQQT
VERDLKDNRE LKQLEDKEAK LRESCQVLDK QLGNLDFHSV SKEKVNLTKQ RDKATVRKGE
LLGQLGEIHS QVNKLQREID EPRFKESLKN FRKANYEIEV TRLCIEDLGQ YRLALEWALI
QFHSEKMEMI NRLIREYWRK IYRGNDIDYI QVKTDEVSSD ASADRRKTYN YRVVQSKNYS
EIEMRGRCSA GQRVLASLII RLALAETFSS NCGVLALDEP TTNLDRANIN SLCEALNCIV
EERQSQSNFM LIIITHDENF VSSLGKITSY HRVFRNEECK SVIRRVEAGP SKKALIDQ


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