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Database: UniProt
Entry: G3V9X6_RAT
LinkDB: G3V9X6_RAT
Original site: G3V9X6_RAT 
ID   G3V9X6_RAT              Unreviewed;      1312 AA.
AC   G3V9X6;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 81.
DE   SubName: Full=RAD50 double strand break repair protein {ECO:0000313|Ensembl:ENSRNOP00000062378.1};
GN   Name=Rad50 {ECO:0000313|Ensembl:ENSRNOP00000062378.1,
GN   ECO:0000313|RGD:621542};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116 {ECO:0000313|Ensembl:ENSRNOP00000062378.1, ECO:0000313|Proteomes:UP000002494};
RN   [1] {ECO:0000313|Ensembl:ENSRNOP00000062378.1, ECO:0000313|Proteomes:UP000002494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000062378.1,
RC   ECO:0000313|Proteomes:UP000002494};
RX   PubMed=15057822; DOI=10.1038/nature02426;
RG   Rat Genome Sequencing Project Consortium;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [2] {ECO:0000313|Ensembl:ENSRNOP00000062378.1}
RP   IDENTIFICATION.
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000062378.1};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SUBCELLULAR LOCATION: Chromosome, telomere
CC       {ECO:0000256|ARBA:ARBA00004574}.
CC   -!- SIMILARITY: Belongs to the SMC family. RAD50 subfamily.
CC       {ECO:0000256|ARBA:ARBA00009439}.
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DR   SMR; G3V9X6; -.
DR   Ensembl; ENSRNOT00000063772.3; ENSRNOP00000062378.1; ENSRNOG00000033065.6.
DR   RGD; 621542; Rad50.
DR   GeneTree; ENSGT00390000018781; -.
DR   HOGENOM; CLU_006184_0_0_1; -.
DR   OMA; FSDYYYR; -.
DR   OrthoDB; 5477220at2759; -.
DR   Proteomes; UP000002494; Chromosome 10.
DR   Bgee; ENSRNOG00000033065; Expressed in testis and 20 other cell types or tissues.
DR   GO; GO:0070533; C:BRCA1-C complex; IEA:Ensembl.
DR   GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
DR   GO; GO:0030870; C:Mre11 complex; IEA:Ensembl.
DR   GO; GO:0035861; C:site of double-strand break; IEA:Ensembl.
DR   GO; GO:0008408; F:3'-5' exonuclease activity; IEA:Ensembl.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:Ensembl.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:Ensembl.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0030674; F:protein-macromolecule adaptor activity; IEA:Ensembl.
DR   GO; GO:0000014; F:single-stranded DNA endodeoxyribonuclease activity; IEA:Ensembl.
DR   GO; GO:0006310; P:DNA recombination; IEA:Ensembl.
DR   GO; GO:0006302; P:double-strand break repair; IEA:Ensembl.
DR   GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:1904354; P:negative regulation of telomere capping; IEA:Ensembl.
DR   GO; GO:0031954; P:positive regulation of protein autophosphorylation; IEA:Ensembl.
DR   GO; GO:0032206; P:positive regulation of telomere maintenance; IEA:Ensembl.
DR   GO; GO:0000019; P:regulation of mitotic recombination; IEA:Ensembl.
DR   GO; GO:0007004; P:telomere maintenance via telomerase; IEA:Ensembl.
DR   GO; GO:0031860; P:telomeric 3' overhang formation; IEA:Ensembl.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR038729; Rad50/SbcC_AAA.
DR   InterPro; IPR004584; Rad50_eukaryotes.
DR   InterPro; IPR013134; Zn_hook_RAD50.
DR   NCBIfam; TIGR00606; rad50; 1.
DR   PANTHER; PTHR18867:SF12; DNA REPAIR PROTEIN RAD50; 1.
DR   PANTHER; PTHR18867; RAD50; 1.
DR   Pfam; PF13476; AAA_23; 1.
DR   Pfam; PF04423; Rad50_zn_hook; 1.
DR   Pfam; PF13558; SbcC_Walker_B; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   SUPFAM; SSF75712; Rad50 coiled-coil Zn hook; 1.
DR   PROSITE; PS51131; ZN_HOOK; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Chromosome {ECO:0000256|ARBA:ARBA00022895};
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Meiosis {ECO:0000256|ARBA:ARBA00023254};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002494};
KW   Telomere {ECO:0000256|ARBA:ARBA00022895};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
SQ   SEQUENCE   1312 AA;  153838 MW;  EF07ECC10E50F411 CRC64;
     MSRIEKMSIL GVRSFGIEDK DKQIISFFSP LTILVGPNGA GKTTIIECLK YICTGDFPPG
     TKGNTFVHDP KVAQETDVRA QIRLQFRDVN GEMVLVQRSM LCSQKSKKTE FKTLEGVITR
     IKHGEKVSLS SKCAEIDREM ISCLGVSKSV LNNVIFCHQE DSNWPLSEGK ALKQKFDEIF
     SATRYIKALD TLRQVRQTQG QKVKECQTEL KYLRQNKEKA CEIRDQITSK EAQLASSREI
     VKAYENELEP LKNRLKEIEH NLSKIMRLDN EIKALDSRKK QMEKDNSELE QKMEKVFQGT
     DEQLNDLYHN HQRTVREKER RLVDCQRELE KLSKEARLLN QERAELLVEQ GRLQLQADRH
     QEHIRARDSL IQSLAAHLEL DGFERGPFSE RQIKNFHELV RERQEREAKT ASQLLSDLTD
     KEALKQRQMD EMRDKKSGLG RMIELKTEIL TKKQTELRNV RNELQQLEGS SDRILELDQE
     LTKAERELSK AEKNSSIETL KAEILNLQSE KADLDRNLRK LDQEMEQLNH HTTTRTQMEM
     LTKDKTDKDE QIRKIKSRHS DELTSLLGYF PNKKQLEDWL HSKSKEINQT RDRLAKLNKE
     LASAEQNKNH INNELKKKEE QLSSYEDKLF DVCGSQDFES DLDRLKEDIE KSSKQRAMLA
     GATAVYSQFI TQLTDENQSC CPVCQRVFQT EAELQEVISD LQSKLRLAPD KLKSTESELK
     KKERRRDEML GLVPMRQSII DLKEKEIPEL RNRLQSVNRD IQRLKNDIEE QETLLGTVMP
     EEESAKVCLT DVTIMERFQM ELKDVERKIA QQAAKLQGVD LDRTVQQVNQ EKQEKQHKLD
     TVSSKIELNR KLIQDQQEQI QHLKSKTNEL KSEKLQIATN LQRRQQMEEQ TVELSTEVQS
     LNREIKDAKE QINPLEIALE KLQQEKEELI HRKNTSNKMA QDKINDIKEK VKNIHGYMKD
     IENYIQDGKD DYKKQKETEL NEVVIQLNEC DKHKEKINKE MGTMRQDIDT QKIQERWLQD
     NLTLRKRREE LKEVEEERKQ HLKEMGQMQV LQMKNEHQKL EENIDTIKRN HSLALGRQKG
     YEEEILHFKK ELREPQFRDA EEKYREMMIV MRTTELVNKD LDIYYKTLDH AIMKFHSMKM
     EEINKIIRDL WRSTYRGQDI EYIEIRSDAD ENVSASDKRR NYNYRVVMLK GDTALDMRGR
     CSAGQKVLAS LIIRLALAET FCLNCGILAL DEPTTNLDRE NIESLAHALV EIIKSRSQQR
     NFQLLVITHD EDFVELLGRS EYVEKFYRVK KNIDQCSEIV KSSINSLGSY VH
//
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