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Database: UniProt
Entry: B4QH58_DROSI
LinkDB: B4QH58_DROSI
Original site: B4QH58_DROSI 
ID   B4QH58_DROSI            Unreviewed;      1301 AA.
AC   B4QH58;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 71.
DE   SubName: Full=GD11670 {ECO:0000313|EMBL:EDX08204.1};
GN   Name=Dsim\GD11670 {ECO:0000313|EMBL:EDX08204.1};
GN   ORFNames=Dsim_GD11670 {ECO:0000313|EMBL:EDX08204.1};
OS   Drosophila simulans (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7240 {ECO:0000313|EMBL:EDX08204.1, ECO:0000313|Proteomes:UP000000304};
RN   [1] {ECO:0000313|EMBL:EDX08204.1, ECO:0000313|Proteomes:UP000000304}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=mosaic {ECO:0000313|Proteomes:UP000000304};
RX   PubMed=17994087; DOI=10.1038/nature06341;
RG   Drosophila 12 genomes consortium;
RA   Clark A.G., Eisen M.B., Smith D.R., Bergman C.M., Oliver B., Markow T.A.,
RA   Kaufman T.C., Kellis M., Gelbart W., Iyer V.N., Pollard D.A., Sackton T.B.,
RA   Larracuente A.M., Singh N.D., Abad J.P., Abt D.N., Adryan B., Aguade M.,
RA   Akashi H., Anderson W.W., Aquadro C.F., Ardell D.H., Arguello R.,
RA   Artieri C.G., Barbash D.A., Barker D., Barsanti P., Batterham P.,
RA   Batzoglou S., Begun D., Bhutkar A., Blanco E., Bosak S.A., Bradley R.K.,
RA   Brand A.D., Brent M.R., Brooks A.N., Brown R.H., Butlin R.K., Caggese C.,
RA   Calvi B.R., Bernardo de Carvalho A., Caspi A., Castrezana S.,
RA   Celniker S.E., Chang J.L., Chapple C., Chatterji S., Chinwalla A.,
RA   Civetta A., Clifton S.W., Comeron J.M., Costello J.C., Coyne J.A., Daub J.,
RA   David R.G., Delcher A.L., Delehaunty K., Do C.B., Ebling H., Edwards K.,
RA   Eickbush T., Evans J.D., Filipski A., Findeiss S., Freyhult E., Fulton L.,
RA   Fulton R., Garcia A.C., Gardiner A., Garfield D.A., Garvin B.E., Gibson G.,
RA   Gilbert D., Gnerre S., Godfrey J., Good R., Gotea V., Gravely B.,
RA   Greenberg A.J., Griffiths-Jones S., Gross S., Guigo R., Gustafson E.A.,
RA   Haerty W., Hahn M.W., Halligan D.L., Halpern A.L., Halter G.M., Han M.V.,
RA   Heger A., Hillier L., Hinrichs A.S., Holmes I., Hoskins R.A., Hubisz M.J.,
RA   Hultmark D., Huntley M.A., Jaffe D.B., Jagadeeshan S., Jeck W.R.,
RA   Johnson J., Jones C.D., Jordan W.C., Karpen G.H., Kataoka E.,
RA   Keightley P.D., Kheradpour P., Kirkness E.F., Koerich L.B., Kristiansen K.,
RA   Kudrna D., Kulathinal R.J., Kumar S., Kwok R., Lander E., Langley C.H.,
RA   Lapoint R., Lazzaro B.P., Lee S.J., Levesque L., Li R., Lin C.F., Lin M.F.,
RA   Lindblad-Toh K., Llopart A., Long M., Low L., Lozovsky E., Lu J., Luo M.,
RA   Machado C.A., Makalowski W., Marzo M., Matsuda M., Matzkin L.,
RA   McAllister B., McBride C.S., McKernan B., McKernan K., Mendez-Lago M.,
RA   Minx P., Mollenhauer M.U., Montooth K., Mount S.M., Mu X., Myers E.,
RA   Negre B., Newfeld S., Nielsen R., Noor M.A., O'Grady P., Pachter L.,
RA   Papaceit M., Parisi M.J., Parisi M., Parts L., Pedersen J.S., Pesole G.,
RA   Phillippy A.M., Ponting C.P., Pop M., Porcelli D., Powell J.R.,
RA   Prohaska S., Pruitt K., Puig M., Quesneville H., Ram K.R., Rand D.,
RA   Rasmussen M.D., Reed L.K., Reenan R., Reily A., Remington K.A.,
RA   Rieger T.T., Ritchie M.G., Robin C., Rogers Y.H., Rohde C., Rozas J.,
RA   Rubenfield M.J., Ruiz A., Russo S., Salzberg S.L., Sanchez-Gracia A.,
RA   Saranga D.J., Sato H., Schaeffer S.W., Schatz M.C., Schlenke T.,
RA   Schwartz R., Segarra C., Singh R.S., Sirot L., Sirota M., Sisneros N.B.,
RA   Smith C.D., Smith T.F., Spieth J., Stage D.E., Stark A., Stephan W.,
RA   Strausberg R.L., Strempel S., Sturgill D., Sutton G., Sutton G.G., Tao W.,
RA   Teichmann S., Tobari Y.N., Tomimura Y., Tsolas J.M., Valente V.L.,
RA   Venter E., Venter J.C., Vicario S., Vieira F.G., Vilella A.J.,
RA   Villasante A., Walenz B., Wang J., Wasserman M., Watts T., Wilson D.,
RA   Wilson R.K., Wing R.A., Wolfner M.F., Wong A., Wong G.K., Wu C.I., Wu G.,
RA   Yamamoto D., Yang H.P., Yang S.P., Yorke J.A., Yoshida K., Zdobnov E.,
RA   Zhang P., Zhang Y., Zimin A.V., Baldwin J., Abdouelleil A., Abdulkadir J.,
RA   Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A., An P.,
RA   Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P., Barry A.,
RA   Bayul T., Berlin A., Bessette D., Bloom T., Blye J., Boguslavskiy L.,
RA   Bonnet C., Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S.,
RA   Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P., Costello M.,
RA   D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C., Dhargay N., Dooley K.,
RA   Dooley E., Doricent M., Dorje P., Dorjee K., Dupes A., Elong R., Falk J.,
RA   Farina A., Faro S., Ferguson D., Fisher S., Foley C.D., Franke A.,
RA   Friedrich D., Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T.,
RA   Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B.,
RA   Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L.,
RA   Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D.,
RA   Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F., LeVine R.,
RA   Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y.,
RA   Lubonja R., Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C.,
RA   McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O.,
RA   Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A., Mulrain L.,
RA   Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N., Nicol R., Norbu C.,
RA   Norbu N., Novod N., O'Neill B., Osman S., Markiewicz E., Oyono O.L.,
RA   Patti C., Phunkhang P., Pierre F., Priest M., Raghuraman S., Rege F.,
RA   Reyes R., Rise C., Rogov P., Ross K., Ryan E., Settipalli S., Shea T.,
RA   Sherpa N., Shi L., Shih D., Sparrow T., Spaulding J., Stalker J.,
RA   Stange-Thomann N., Stavropoulos S., Stone C., Strader C., Tesfaye S.,
RA   Thomson T., Thoulutsang Y., Thoulutsang D., Topham K., Topping I.,
RA   Tsamla T., Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M.,
RA   Wilkinson J., Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D.,
RA   Zimmer A., Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J.,
RA   Chin C., Gnerre S., Grabherr M., Kleber M., Mauceli E., MacCallum I.;
RT   "Evolution of genes and genomes on the Drosophila phylogeny.";
RL   Nature 450:203-218(2007).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the SMC family. RAD50 subfamily.
CC       {ECO:0000256|ARBA:ARBA00009439}.
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DR   EMBL; CM000362; EDX08204.1; -; Genomic_DNA.
DR   STRING; 7240.B4QH58; -.
DR   HOGENOM; CLU_006184_0_0_1; -.
DR   OMA; FSDYYYR; -.
DR   PhylomeDB; B4QH58; -.
DR   Proteomes; UP000000304; Chromosome 2r.
DR   GO; GO:0000793; C:condensed chromosome; IEA:EnsemblMetazoa.
DR   GO; GO:0030870; C:Mre11 complex; IEA:EnsemblMetazoa.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006302; P:double-strand break repair; IEA:EnsemblMetazoa.
DR   GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0008104; P:protein localization; IEA:EnsemblMetazoa.
DR   GO; GO:0000722; P:telomere maintenance via recombination; IEA:EnsemblMetazoa.
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   Coiled coil {ECO:0000256|SAM:Coils};
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, ECO:0000256|PROSITE-
KW   ProRule:PRU00471}; Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000304};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00471}.
FT   DOMAIN          645..741
FT                   /note="Zinc-hook"
FT                   /evidence="ECO:0000259|PROSITE:PS51131"
FT   COILED          189..254
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          308..342
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          436..501
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          583..638
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          719..766
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          832..880
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          912..1036
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   BINDING         689
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00471"
FT   BINDING         692
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00471"
SQ   SEQUENCE   1301 AA;  150240 MW;  BBBF3D56AF9C4F8B CRC64;
     MSSIESLSIQ GIRSFGTYAD DLQSIKFSSP VTLILGENGC GKTTVVECLK YALTGECPPG
     SDRGKSFVHD PKIFGLNEVL AQIKMQVRDR RGAQVSICRT MKVSKKRNKM SFETMDSTIN
     FLTGAGQSKR EKQDSLSGRS VDIDVAISDF MGVSKAIINN VLFCHQEDSS WPLDESKKLK
     EKFDAIFGIT EYNKALDKII KLRKEAMEEL KIKEGNMKHV AYLKQEMEVK TLNLQKAQRK
     CDAIKAQCSE CEEEMKPIEA RLVEIRNVEF EIGKYQAQKV EMDTKHKNCK DQISTLTLKI
     KNPFRGTLDE LDQEISNFDQ RMQEMRQKRT EVEGNLSQIK RSSVAEQEKL GTQDRKHCLA
     KQRHQSELAC RAQLLKRVKE FCRELHITID CDLVEQPEKM GEVLQDIEAM IITKHCEITE
     IFEQNEKADR SRQVKIDELR IDLTKSEQSV TAQEKQRESS KRESETLGVE IKKIETSMQD
     LKELEKEINE VNELYESANK SIDQQAIKDA IARKKASIAE NQIQFKKLDE QLTFLGSMAK
     LVAECSLKQK ELDKKNQEVH RVRSRHSDHF GKLFKEPITC NYRRSMQVVY EKLRREIQDL
     NEKANTQKLK EQSYEIKRKN LISDISRMEK ELKDSEELIY QKCRSTPYDD LLERSKTTIS
     KLQFDHGALK SSEALYKKYI QKMDEEPSCP LCHHNMTSDE ACDLTSELTD EIQKLPDNIT
     RAEKALKAEQ IKYENLLQIK PTILKVKELK DSLPQKKEEL KKVEELLGDS VSEYETLIAL
     IGEPTHNMEL ANSMMGDMSX LDEALKDSVR LTKDLDLQKG QLPASYDSSV SMDDLQTEKS
     KVSRELETER KELESAQNAV QQQMDALNRL REKKNSLKDR QIHLREGLQS LPQLKERLEK
     LNSFLTTVAS EISELKAKIQ PLKLNLRAAI EEKERLKKSE SEKLAQLNSK YNSYKSTDQD
     IQRLNKEAED YAKLDLRNEI KKLDEIIKAS KDQLRKLAKC SNQQTVERDL KDNRELKQLE
     DKEAKLKESC QMLDKQLGNL DFHSVSKEKV NLTKQRDKAT VRKGELLGQL GEINSQVNKL
     QREIDEPIFK ESLKNFRRAN YEIEVTRLCI EDLGQYRLAL EWALIQFHSE KMEMINRLIR
     EYWRKIYRGN DIDYIQVKTD EVSSDASADR RKTYNYRVVQ SKNYSEIEMR GRCSAGQRVL
     ASLIIRLALA ETFSSNCGVL ALDEPTTNLD RANITSLCEA LNCIERRSQS NFMLIIITHD
     ENFVSSLGKI TSYHRVFRNE ECKSVIRRVE AGPSKKALID Q
//
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