RAD50_ARATH
ID RAD50_ARATH Reviewed; 1316 AA.
AC Q9SL02; Q9M6P9;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=DNA repair protein RAD50;
DE Short=AtRAD50;
DE EC=3.6.-.-;
GN Name=RAD50; OrderedLocusNames=At2g31970; ORFNames=F22D22.28;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=11169180; DOI=10.1046/j.1365-313x.2001.00928.x;
RA Gallego M.E., Jeanneau M., Granier F., Bouchez D., Bechtold N., White C.I.;
RT "Disruption of the Arabidopsis RAD50 gene leads to plant sterility and MMS
RT sensitivity.";
RL Plant J. 25:31-41(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP FUNCTION.
RX PubMed=11306548; DOI=10.1093/embo-reports/kve069;
RA Gherbi H., Gallego M.E., Jalut N., Lucht J.M., Hohn B., White C.I.;
RT "Homologous recombination in planta is stimulated in the absence of
RT Rad50.";
RL EMBO Rep. 2:287-291(2001).
RN [6]
RP FUNCTION.
RX PubMed=11172016; DOI=10.1073/pnas.98.4.1711;
RA Gallego M.E., White C.I.;
RT "RAD50 function is essential for telomere maintenance in Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:1711-1716(2001).
RN [7]
RP INTERACTION WITH MRE11.
RX PubMed=11959125; DOI=10.1016/s0014-5793(02)02536-x;
RA Daoudal-Cotterell S., Gallego M.E., White C.I.;
RT "The plant Rad50-Mre11 protein complex.";
RL FEBS Lett. 516:164-166(2002).
RN [8]
RP FUNCTION.
RX PubMed=15309561; DOI=10.1007/s00412-004-0309-1;
RA Bleuyard J.-Y., Gallego M.E., White C.I.;
RT "Meiotic defects in the Arabidopsis rad50 mutant point to conservation of
RT the MRX complex function in early stages of meiotic recombination.";
RL Chromosoma 113:197-203(2004).
RN [9]
RP REVIEW ON DNA REPAIR.
RX PubMed=16202663; DOI=10.1016/j.dnarep.2005.08.017;
RA Bleuyard J.Y., Gallego M.E., White C.I.;
RT "Recent advances in understanding of the DNA double-strand break repair
RT machinery of plants.";
RL DNA Repair 5:1-12(2006).
RN [10]
RP INTERACTION WITH MRE11.
RC STRAIN=cv. Columbia;
RX PubMed=17672843; DOI=10.1111/j.1365-313x.2007.03220.x;
RA Waterworth W.M., Altun C., Armstrong S.J., Roberts N., Dean P.J., Young K.,
RA Weil C.F., Bray C.M., West C.E.;
RT "NBS1 is involved in DNA repair and plays a synergistic role with ATM in
RT mediating meiotic homologous recombination in plants.";
RL Plant J. 52:41-52(2007).
CC -!- FUNCTION: Implicated in double-strand breaks (DSBs) repair by non-
CC homologous end joining (NHEJ). Involved in telomere maintenance.
CC Involved in telomerase action on chromosome ends. Required during
CC meiosis for both male and female gametophytic development, for pairing
CC and synapsis of homologous chromosomes during the early stages of
CC meiotic recombination, especially during the pachytene stage of the
CC first division. {ECO:0000269|PubMed:11169180,
CC ECO:0000269|PubMed:11172016, ECO:0000269|PubMed:11306548,
CC ECO:0000269|PubMed:15309561}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per homodimer. {ECO:0000250};
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with MRE11. {ECO:0000250,
CC ECO:0000269|PubMed:11959125, ECO:0000269|PubMed:17672843}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Chromosome, telomere
CC {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Widely expressed, predominantly in meristematic and
CC reproductive tissues. {ECO:0000269|PubMed:11169180}.
CC -!- DOMAIN: The zinc-hook, which separates the large intramolecular coiled
CC coil regions, contains 2 Cys residues that coordinate one molecule of
CC zinc with the help of the 2 Cys residues of the zinc-hook of another
CC RAD50 molecule, thereby forming a V-shaped homodimer. The two heads of
CC the homodimer, which constitute the ATP-binding domain, interact with
CC the MRE11 homodimer (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SMC family. RAD50 subfamily. {ECO:0000305}.
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DR EMBL; AF168748; AAF36810.1; -; mRNA.
DR EMBL; AC006223; AAD15407.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC08614.1; -; Genomic_DNA.
DR EMBL; AY139771; AAM98090.1; -; mRNA.
DR EMBL; BT005823; AAO64758.1; -; mRNA.
DR PIR; D84727; D84727.
DR RefSeq; NP_565733.1; NM_128757.4.
DR AlphaFoldDB; Q9SL02; -.
DR SMR; Q9SL02; -.
DR BioGRID; 3103; 12.
DR STRING; 3702.AT2G31970.1; -.
DR PaxDb; Q9SL02; -.
DR PRIDE; Q9SL02; -.
DR ProteomicsDB; 236426; -.
DR EnsemblPlants; AT2G31970.1; AT2G31970.1; AT2G31970.
DR GeneID; 817756; -.
DR Gramene; AT2G31970.1; AT2G31970.1; AT2G31970.
DR KEGG; ath:AT2G31970; -.
DR Araport; AT2G31970; -.
DR TAIR; locus:2045437; AT2G31970.
DR eggNOG; KOG0962; Eukaryota.
DR HOGENOM; CLU_006184_0_0_1; -.
DR InParanoid; Q9SL02; -.
DR OMA; CFGVNCG; -.
DR OrthoDB; 179362at2759; -.
DR PhylomeDB; Q9SL02; -.
DR PRO; PR:Q9SL02; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SL02; baseline and differential.
DR Genevisible; Q9SL02; AT.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0000794; C:condensed nuclear chromosome; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0030870; C:Mre11 complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
DR GO; GO:0003691; F:double-stranded telomeric DNA binding; IBA:GO_Central.
DR GO; GO:0051880; F:G-quadruplex DNA binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043047; F:single-stranded telomeric DNA binding; IBA:GO_Central.
DR GO; GO:0070192; P:chromosome organization involved in meiotic cell cycle; IBA:GO_Central.
DR GO; GO:0032508; P:DNA duplex unwinding; IBA:GO_Central.
DR GO; GO:0006302; P:double-strand break repair; IMP:TAIR.
DR GO; GO:0006312; P:mitotic recombination; IMP:TAIR.
DR GO; GO:0090305; P:nucleic acid phosphodiester bond hydrolysis; IBA:GO_Central.
DR GO; GO:0016233; P:telomere capping; IMP:TAIR.
DR GO; GO:0000723; P:telomere maintenance; IMP:TAIR.
DR GO; GO:0000722; P:telomere maintenance via recombination; IBA:GO_Central.
DR GO; GO:0007004; P:telomere maintenance via telomerase; IBA:GO_Central.
DR CDD; cd03240; ABC_Rad50; 2.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR045171; ABC_Rad50.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038729; Rad50/SbcC_AAA.
DR InterPro; IPR004584; Rad50_eukaryotes.
DR InterPro; IPR013134; Zn_hook_RAD50.
DR Pfam; PF13476; AAA_23; 1.
DR Pfam; PF04423; Rad50_zn_hook; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR TIGRFAMs; TIGR00606; rad50; 1.
DR PROSITE; PS51131; ZN_HOOK; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell cycle; Chromosome; Coiled coil; DNA damage; DNA repair;
KW Hydrolase; Meiosis; Metal-binding; Nucleotide-binding; Nucleus;
KW Reference proteome; Telomere; Zinc.
FT CHAIN 1..1316
FT /note="DNA repair protein RAD50"
FT /id="PRO_0000138646"
FT DOMAIN 648..747
FT /note="Zinc-hook"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00471"
FT COILED 194..343
FT /evidence="ECO:0000255"
FT COILED 648..686
FT /evidence="ECO:0000255"
FT COILED 719..747
FT /evidence="ECO:0000255"
FT COILED 762..972
FT /evidence="ECO:0000255"
FT COILED 999..1090
FT /evidence="ECO:0000255"
FT BINDING 34..41
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 695
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00471"
FT BINDING 698
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00471"
SQ 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
