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DNA repair protein RAD50 (AtRAD50) (EC 3.6.-.-)

 RAD50_ARATH             Reviewed;        1316 AA.
Q9SL02; Q9M6P9;
04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
01-JUN-2002, sequence version 2.
25-APR-2018, entry version 125.
RecName: Full=DNA repair protein RAD50;
Short=AtRAD50;
EC=3.6.-.-;
Name=RAD50; OrderedLocusNames=At2g31970; ORFNames=F22D22.28;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
STRAIN=cv. Columbia;
PubMed=11169180; DOI=10.1046/j.1365-313x.2001.00928.x;
Gallego M.E., Jeanneau M., Granier F., Bouchez D., Bechtold N.,
White C.I.;
"Disruption of the Arabidopsis RAD50 gene leads to plant sterility and
MMS sensitivity.";
Plant J. 25:31-41(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10617197; DOI=10.1038/45471;
Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L.,
Moffat K.S., Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L.,
Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H.,
Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D.,
Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M.,
Venter J.C.;
"Sequence and analysis of chromosome 2 of the plant Arabidopsis
thaliana.";
Nature 402:761-768(1999).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[5]
FUNCTION.
PubMed=11306548; DOI=10.1093/embo-reports/kve069;
Gherbi H., Gallego M.E., Jalut N., Lucht J.M., Hohn B., White C.I.;
"Homologous recombination in planta is stimulated in the absence of
Rad50.";
EMBO Rep. 2:287-291(2001).
[6]
FUNCTION.
PubMed=11172016; DOI=10.1073/pnas.98.4.1711;
Gallego M.E., White C.I.;
"RAD50 function is essential for telomere maintenance in
Arabidopsis.";
Proc. Natl. Acad. Sci. U.S.A. 98:1711-1716(2001).
[7]
INTERACTION WITH MRE11.
PubMed=11959125; DOI=10.1016/S0014-5793(02)02536-X;
Daoudal-Cotterell S., Gallego M.E., White C.I.;
"The plant Rad50-Mre11 protein complex.";
FEBS Lett. 516:164-166(2002).
[8]
FUNCTION.
PubMed=15309561; DOI=10.1007/s00412-004-0309-1;
Bleuyard J.-Y., Gallego M.E., White C.I.;
"Meiotic defects in the Arabidopsis rad50 mutant point to conservation
of the MRX complex function in early stages of meiotic
recombination.";
Chromosoma 113:197-203(2004).
[9]
REVIEW ON DNA REPAIR.
PubMed=16202663; DOI=10.1016/j.dnarep.2005.08.017;
Bleuyard J.Y., Gallego M.E., White C.I.;
"Recent advances in understanding of the DNA double-strand break
repair machinery of plants.";
DNA Repair 5:1-12(2006).
[10]
INTERACTION WITH MRE11.
STRAIN=cv. Columbia;
PubMed=17672843; DOI=10.1111/j.1365-313X.2007.03220.x;
Waterworth W.M., Altun C., Armstrong S.J., Roberts N., Dean P.J.,
Young K., Weil C.F., Bray C.M., West C.E.;
"NBS1 is involved in DNA repair and plays a synergistic role with ATM
in mediating meiotic homologous recombination in plants.";
Plant J. 52:41-52(2007).
-!- FUNCTION: Implicated in double-strand breaks (DSBs) repair by non-
homologous end joining (NHEJ). Involved in telomere maintenance.
Involved in telomerase action on chromosome ends. Required during
meiosis for both male and female gametophytic development, for
pairing and synapsis of homologous chromosomes during the early
stages of meiotic recombination, especially during the pachytene
stage of the first division. {ECO:0000269|PubMed:11169180,
ECO:0000269|PubMed:11172016, ECO:0000269|PubMed:11306548,
ECO:0000269|PubMed:15309561}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
Note=Binds 1 zinc ion per homodimer. {ECO:0000250};
-!- SUBUNIT: Homodimer (By similarity). Interacts with MRE11.
{ECO:0000250, ECO:0000269|PubMed:11959125,
ECO:0000269|PubMed:17672843}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Chromosome, telomere
{ECO:0000305}.
-!- TISSUE SPECIFICITY: Widely expressed, predominantly in
meristematic and reproductive tissues.
{ECO:0000269|PubMed:11169180}.
-!- 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}.
-!- SIMILARITY: Belongs to the SMC family. RAD50 subfamily.
{ECO:0000305}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; AF168748; AAF36810.1; -; mRNA.
EMBL; AC006223; AAD15407.2; -; Genomic_DNA.
EMBL; CP002685; AEC08614.1; -; Genomic_DNA.
EMBL; AY139771; AAM98090.1; -; mRNA.
EMBL; BT005823; AAO64758.1; -; mRNA.
PIR; D84727; D84727.
RefSeq; NP_565733.1; NM_128757.4.
UniGene; At.65745; -.
ProteinModelPortal; Q9SL02; -.
SMR; Q9SL02; -.
STRING; 3702.AT2G31970.1; -.
PaxDb; Q9SL02; -.
PRIDE; Q9SL02; -.
EnsemblPlants; AT2G31970.1; AT2G31970.1; AT2G31970.
GeneID; 817756; -.
Gramene; AT2G31970.1; AT2G31970.1; AT2G31970.
KEGG; ath:AT2G31970; -.
Araport; AT2G31970; -.
TAIR; locus:2045437; AT2G31970.
eggNOG; KOG0962; Eukaryota.
eggNOG; COG0419; LUCA.
HOGENOM; HOG000264309; -.
InParanoid; Q9SL02; -.
KO; K10866; -.
OMA; RSMVCTQ; -.
OrthoDB; EOG0936019C; -.
PhylomeDB; Q9SL02; -.
Reactome; R-ATH-2559586; DNA Damage/Telomere Stress Induced Senescence.
Reactome; R-ATH-5685939; HDR through MMEJ (alt-NHEJ).
Reactome; R-ATH-5693548; Sensing of DNA Double Strand Breaks.
Reactome; R-ATH-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
Reactome; R-ATH-5693607; Processing of DNA double-strand break ends.
Reactome; R-ATH-5693616; Presynaptic phase of homologous DNA pairing and strand exchange.
PRO; PR:Q9SL02; -.
Proteomes; UP000006548; Chromosome 2.
ExpressionAtlas; Q9SL02; baseline and differential.
Genevisible; Q9SL02; AT.
GO; GO:0000794; C:condensed nuclear chromosome; IBA:GO_Central.
GO; GO:0005737; C:cytoplasm; IDA:TAIR.
GO; GO:0030870; C:Mre11 complex; TAS:TAIR.
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; IDA:TAIR.
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: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: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:TAIR.
GO; GO:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central.
GO; GO:0006312; P:mitotic recombination; IMP:TAIR.
GO; GO:0090305; P:nucleic acid phosphodiester bond hydrolysis; IBA:GO_Central.
GO; GO:0007131; P:reciprocal meiotic recombination; IBA:GO_Central.
GO; GO:0016233; P:telomere capping; IMP:TAIR.
GO; GO:0000723; P:telomere maintenance; IMP:TAIR.
GO; GO:0000722; P:telomere maintenance via recombination; IBA:GO_Central.
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; 4.
TIGRFAMs; TIGR00606; rad50; 1.
PROSITE; PS51131; ZN_HOOK; 1.
1: Evidence at protein 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 1316 DNA repair protein RAD50.
/FTId=PRO_0000138646.
DOMAIN 648 747 Zinc-hook. {ECO:0000255|PROSITE-
ProRule:PRU00471}.
NP_BIND 34 41 ATP. {ECO:0000255}.
COILED 194 343 {ECO:0000255}.
COILED 648 686 {ECO:0000255}.
COILED 719 747 {ECO:0000255}.
COILED 762 972 {ECO:0000255}.
COILED 999 1090 {ECO:0000255}.
COMPBIAS 1211 1248 Ala/Asp-rich (DA-box).
METAL 695 695 Zinc. {ECO:0000255|PROSITE-
ProRule:PRU00471}.
METAL 698 698 Zinc. {ECO:0000255|PROSITE-
ProRule:PRU00471}.
SEQUENCE 1316 AA; 152815 MW; 89DC4F6BCA39B0E8 CRC64;
MSTVDKMLIK GIRSFDPENK NVVTFFRPLT LIVGANGAGK TTIIECLKVS CTGELPPNAR
SGHSFIHDPK VAGETETKAQ IKLRFKTAAG KDVVCIRSFQ LTQKASKMEY KAIESVLQTI
NPHTGEKVCL SYRCADMDRE IPALMGVSKA ILENVIFVHQ DESNWPLQDP STLKKKFDDI
FSATRYTKAL EVIKKLHKDQ AQEIKTFKLK LENLQTLKDA AYKLRESIAQ DQERTESSKV
QMLELETSVQ KVDAEVHNKE MMLKDLRKLQ DQVSIKTAER STLFKEQQRQ YAALPEENED
TIEELKEWKS KFEERLALLG TKIRKMEREM VDTETTISSL HNAKTNYMLE ISKLQTEAEA
HMLLKNERDS TIQNIFFHYN LGNVPSTPFS TEVVLNLTNR IKSRLGELEM DLLDKKKSNE
TALSTAWDCY MDANDRWKSI EAQKRAKDEI KMGISKRIEE KEIERDSFEF EISTVDVKQT
DEREKQVQVE LERKTKQNSE RGFESKIEQK QHEIYSLEHK IKTLNRERDV MAGDAEDRVK
LSLKKTEQEN LKKKHKKIID ECKDRIRGVL KGRLPPEKDM KREIVQALRS IEREYDDLSL
KSREAEKEVN MLQMKIQEVN NSLFKHNKDT ESRKRYIESK LQALKQESVT IDAYPKLLES
AKDKRDDRKR EYNMANGMRQ MFEPFEKRAR QEHSCPCCER SFTADEEASF IKKQRVKASS
TGEHLKALAV ESSNADSVFQ QLDKLRAVFE EYSKLTTEII PLAEKTLQEH TEELGQKSEA
LDDVLGISAQ IKADKDSIEA LVQPLENADR IFQEIVSYQK QIEDLEYKLD FRGLGVKTME
EIQSELSSLQ SSKDKLHGEL EKLRDDQIYM ERDISCLQAR WHAVREEKAK AANLLRDVTK
AEEDLERLAE EKSQLDLDVK YLTEALGPLS KEKEQLLSDY NDMKIRRNQE YEELAEKKRN
YQQEVEALLK ASYKINEYHD LKKGERLDDI QEKQRLSDSQ LQSCEARKNE LAGELNRNKD
LMRNQDQLRR NIEDNLNYRT TKAKVEELTR EIESLEEQIL NIGGIAAVEA EIVKILRERE
RLLSELNRCR GTVSVYESSI SKNRVELKQA QYKDIDKRHF DQLIQLKTTE MANKDLDRYY
NALDKALMRF HTMKMEEINK IIRELWQQTY RGQDMDYIRI HSDSEGAGTR SYSYKVLMQT
GDTELEMRGR CSAGQKVLAS LIIRLALAET FCLNCGILAL DEPTTNLDGP NSESLAGALL
RIMEDRKGQE NFQLIVITHD ERFAQMIGQR QHAEKYYRVA KDDMQHSIIE AQEIFD


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