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 29-MAY-2013, entry version 86.
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 Rhabditoidea; Rhabditidae; Peloderinae; 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
RT investigating 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,
RL pp.477-477, Los Angeles (2001).
RN [4]
RP FUNCTION.
RX PubMed=12242227;
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
RT and 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'
CC exonuclease activities, and plays a central role in double-strand
CC break (DSB) repair, chromosome morphogenesis, DNA repair and
CC meiosis. In the complex, it mediates the ATP-binding and is
CC probably required to bind DNA ends and hold them in close
CC proximity.
CC -!- COFACTOR: Binds 1 zinc ion per homodimer (By similarity).
CC -!- SUBUNIT: Homodimer. Probable component of the MRN complex with
CC mre-11 (By similarity).
CC -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC -!- DOMAIN: The zinc-hook, which separates the large intramolecular
CC coiled coil regions, contains 2 Cys residues that coordinate one
CC molecule of zinc with the help of the 2 Cys residues of the zinc-
CC hook of another RAD50 molecule, thereby forming a V-shaped
CC homodimer. The two heads of the homodimer, which constitute the
CC ATP-binding domain, interact with the MRE11A homodimer (By
CC similarity).
CC -!- SIMILARITY: Belongs to the SMC family. RAD50 subfamily.
CC -!- SIMILARITY: Contains 1 zinc-hook domain.
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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 UniGene; Cel.17973; -.
DR ProteinModelPortal; O44199; -.
DR SMR; O44199; 3-99.
DR IntAct; O44199; 1.
DR MINT; MINT-226697; -.
DR STRING; 6239.T04H1.4b.2; -.
DR PaxDb; O44199; -.
DR EnsemblMetazoa; T04H1.4a.1; T04H1.4a.1; T04H1.4.
DR EnsemblMetazoa; T04H1.4a.2; T04H1.4a.2; T04H1.4.
DR EnsemblMetazoa; T04H1.4a.3; T04H1.4a.3; T04H1.4.
DR GeneID; 179678; -.
DR KEGG; cel:CELE_T04H1.4; -.
DR UCSC; T04H1.4b.1; c. elegans.
DR CTD; 179678; -.
DR WormBase; T04H1.4a; CE21149; WBGene00004296; rad-50.
DR eggNOG; COG0419; -.
DR GeneTree; ENSGT00390000018781; -.
DR HOGENOM; HOG000280712; -.
DR KO; K10866; -.
DR NextBio; 906420; -.
DR ArrayExpress; O44199; -.
DR GO; GO:0030870; C:Mre11 complex; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004518; F:nuclease activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0007126; P:meiosis; IEA:UniProtKB-KW.
DR GO; GO:0090305; P:nucleic acid phosphodiester bond hydrolysis; IEA:GOC.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR004584; Rad50.
DR InterPro; IPR007517; Rad50_Zn_hook.
DR InterPro; IPR013134; Zn_hook_Rad50.
DR PANTHER; PTHR18867; PTHR18867; 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; Complete proteome; DNA damage;
KW DNA repair; Hydrolase; Meiosis; Metal-binding; Nucleotide-binding;
KW Nucleus; Reference proteome; Zinc.
FT CHAIN 1 1298 DNA repair protein rad-50.
FT /FTId=PRO_0000138644.
FT DOMAIN 622 719 Zinc-hook.
FT NP_BIND 36 43 ATP (Potential).
FT COILED 222 291 Potential.
FT COILED 317 598 Potential.
FT COILED 622 660 Potential.
FT COILED 691 719 Potential.
FT COILED 754 1092 Potential.
FT COMPBIAS 1174 1211 Ala/Asp-rich (DA-box).
FT METAL 666 666 Zinc (By similarity).
FT METAL 669 669 Zinc (By similarity).
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
//
