RAD50_CAEEL
ID RAD50_CAEEL Reviewed; 1298 AA.
AC O44199; Q22177;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=DNA repair protein rad-50;
DE EC=3.6.-.-;
GN Name=rad-50; ORFNames=T04H1.4;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=CB1489;
RA Offenberg H.H., Heyting C.;
RL Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP FUNCTION.
RA Chin G., Villeneuve A.;
RT "Identifying new genes that function in meiotic DNA repair and double-
RT strand break initiation.";
RL (In) Proceedings of the 13th international C. elegans meeting, pp.477-477,
RL Los Angeles (2001).
RN [4]
RP FUNCTION.
RX PubMed=12242227; DOI=10.1093/genetics/162.1.113;
RA Colaiacovo M.P., Stanfield G.M., Reddy K.C., Reinke V., Kim S.K.,
RA Villeneuve A.M.;
RT "A targeted RNAi screen for genes involved in chromosome morphogenesis and
RT nuclear organization in the Caenorhabditis elegans germline.";
RL Genetics 162:113-128(2002).
CC -!- FUNCTION: Essential component of the MRN complex, a complex that
CC possesses single-stranded DNA endonuclease and 3' to 5' exonuclease
CC activities, and plays a central role in double-strand break (DSB)
CC repair, chromosome morphogenesis, DNA repair and meiosis. In the
CC complex, it mediates the ATP-binding and is probably required to bind
CC DNA ends and hold them in close proximity.
CC {ECO:0000269|PubMed:12242227, ECO:0000269|Ref.3}.
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. Probable component of the MRN complex with mre-11
CC (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
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; Z75312; CAA99730.1; -; mRNA.
DR EMBL; Z78200; CAB01581.1; -; Genomic_DNA.
DR PIR; T24480; T24480.
DR RefSeq; NP_506070.1; NM_073669.6.
DR AlphaFoldDB; O44199; -.
DR SMR; O44199; -.
DR BioGRID; 44701; 3.
DR IntAct; O44199; 1.
DR MINT; O44199; -.
DR STRING; 6239.T04H1.4b.1; -.
DR EPD; O44199; -.
DR PaxDb; O44199; -.
DR PRIDE; O44199; -.
DR EnsemblMetazoa; T04H1.4a.1; T04H1.4a.1; WBGene00004296.
DR GeneID; 179678; -.
DR UCSC; T04H1.4b.1; c. elegans.
DR CTD; 179678; -.
DR WormBase; T04H1.4a; CE21149; WBGene00004296; rad-50.
DR eggNOG; KOG0962; Eukaryota.
DR GeneTree; ENSGT00390000018781; -.
DR HOGENOM; CLU_006184_0_0_1; -.
DR InParanoid; O44199; -.
DR Reactome; R-CEL-2559586; DNA Damage/Telomere Stress Induced Senescence.
DR Reactome; R-CEL-5685939; HDR through MMEJ (alt-NHEJ).
DR Reactome; R-CEL-5693548; Sensing of DNA Double Strand Breaks.
DR Reactome; R-CEL-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR Reactome; R-CEL-5693607; Processing of DNA double-strand break ends.
DR PRO; PR:O44199; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00004296; Expressed in adult organism and 4 other tissues.
DR ExpressionAtlas; O44199; baseline and differential.
DR GO; GO:0000794; C:condensed nuclear chromosome; IBA:GO_Central.
DR GO; GO:0030870; C:Mre11 complex; 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: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; IBA:GO_Central.
DR GO; GO:0090305; P:nucleic acid phosphodiester bond hydrolysis; IBA:GO_Central.
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; 1.
DR TIGRFAMs; TIGR00606; rad50; 1.
DR PROSITE; PS51131; ZN_HOOK; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cell cycle; Coiled coil; DNA damage; DNA repair; Hydrolase;
KW Meiosis; Metal-binding; Nucleotide-binding; Nucleus; Reference proteome;
KW Zinc.
FT CHAIN 1..1298
FT /note="DNA repair protein rad-50"
FT /id="PRO_0000138644"
FT DOMAIN 622..719
FT /note="Zinc-hook"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00471"
FT COILED 222..291
FT /evidence="ECO:0000255"
FT COILED 317..598
FT /evidence="ECO:0000255"
FT COILED 622..660
FT /evidence="ECO:0000255"
FT COILED 691..719
FT /evidence="ECO:0000255"
FT COILED 754..1092
FT /evidence="ECO:0000255"
FT BINDING 36..43
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 666
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00471"
FT BINDING 669
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00471"
SQ SEQUENCE 1298 AA; 150396 MW; 2971F63E754A44E3 CRC64;
MAKFLRLHIR GIRSVGDEDH DVHKIDFLSP CTLISGPNGT GKTTTIEALN FVTTGQMPTQ
KKQNFIHSTD VARKTRVDAS VTLEFIDVKG RECTAVRRLV VTSGTKAAAL AEEHTLAIKY
PDGTVNTLSS KVCDFNTALL KHLGVPRAVF KYVIFCHQED STWPLSEPKE LKKRFDDIFQ
LTKFVKAQER MKKIVLDFKK EMQTHEMSKQ LYETHVRDKL VARQNQEECE RKISKRKEET
DELKERKANG QKKIEEMRTS IHELEDTLTS FKKTELERQN LKKQLSLIRV EPYFGTEEEL
KREIEEFRGS EGRSYGEERA RIQKKIGKNN QERQELSQKK TEFENRISSL KAEVIHCQSL
KYDLERLENQ LRSELDLEHD ADIDIEIDNA ITLKIRGMSD KARMIAKNCA ELQSNLRTAQ
EAATKIEVEM KTLQNEKVKL EKEVEQLKFK IKQGQNATAG MKDLLKKEEA LRKSLADLPL
LDENALTECK LKREKYLKQL DILKKKCAEA EKNAEKDREK ESLKQTLSIA RKKMTAYQRI
YDNNWQGLIG QAPDFPWTPI LSKTFHKLRN DKKIMEEDLR DVQLNVQKLE TMQHQYRKQE
ESLTAQELKL SENIFEACSC EAEEVSEKLE NLRKRLKKAR KDLAPLSAKS NLYDSYIEES
KSSGCCPLCD RDFKTKKEIN EFSKKLENMT LSFPTEQEEL EKLVSKLEKE EIIIVKAEGQ
ANELQRIVKE LKEVREKNRK LSTEMAEEKS NLSKNEKQLE TVNAKLKLAE DLQTDVGVIQ
QLYEQTEENE KRYEQLVSES DSSDGLSYTE LRKKVEDKDE EYRKIVQEGE ELQKCSEERN
KLQSKLNELG THRVSLGEAA AQAGAFAEQL ETKIKEIQEC ITAISQKRNE DLPDAQFKKD
DLTRNVSSKE EEKKKAEMEV QMMKKELDQK IFHRKSLFKK VQEGGLCERQ LMDKENNIAT
LNASLEENQQ RQKRFEEDLR SFDSSHQRES ILKDQLTRMI IENKIKELKR TLATFDGQIN
EDRITEQKQA YNKLQNELRL IGNEEVKIYT QMQEYEKQKK IAEAKLSTKE CQNAESNYRD
AIIELAITKE SISDLTKYRN CLDASLIQFH SEKMGRVNGI IDDLWRKVYN STDITTIRIR
SDATSETSSK KVAYEYNVMM VHETGTEVEM RGRCSAGQKM LASLLIRIAL AEVFGGSCSM
IALDEPTTNL DESKVEGMAI VLADIIAERR GFDENGKLRG RDMQMVVITH DERLVNRITI
SCRPEYIYCL GKDEHGISFL SKRYPDGTVK RVNTKRRF
