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Database: UniProt
Entry: B4N436_DROWI
LinkDB: B4N436_DROWI
Original site: B4N436_DROWI 
ID   B4N436_DROWI            Unreviewed;       911 AA.
AC   B4N436;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 64.
DE   RecName: Full=DNA repair and recombination protein RAD54-like {ECO:0000256|ARBA:ARBA00015341};
DE   AltName: Full=Protein okra {ECO:0000256|ARBA:ARBA00029956};
GN   Name=Dwil\GK11263 {ECO:0000313|EMBL:EDW78910.1};
GN   ORFNames=Dwil_GK11263 {ECO:0000313|EMBL:EDW78910.1};
OS   Drosophila willistoni (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7260 {ECO:0000313|EMBL:EDW78910.1, ECO:0000313|Proteomes:UP000007798};
RN   [1] {ECO:0000313|EMBL:EDW78910.1, ECO:0000313|Proteomes:UP000007798}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 14030-0811.24 {ECO:0000313|Proteomes:UP000007798};
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   -!- FUNCTION: Involved in mitotic DNA repair and meiotic recombination.
CC       Functions in the recombinational DNA repair pathway. Essential for
CC       interhomolog gene conversion (GC), but may have a less important role
CC       in intersister GC than spn-A/Rad51. In the presence of DNA, spn-A/Rad51
CC       enhances the ATPase activity of okr/Rad54.
CC       {ECO:0000256|ARBA:ARBA00024776}.
CC   -!- SUBUNIT: Interacts (via N-terminus) with spn-A/Rad51.
CC       {ECO:0000256|ARBA:ARBA00011467}.
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DR   EMBL; CH964095; EDW78910.1; -; Genomic_DNA.
DR   RefSeq; XP_002067924.1; XM_002067888.2.
DR   AlphaFoldDB; B4N436; -.
DR   STRING; 7260.B4N436; -.
DR   EnsemblMetazoa; FBtr0241914; FBpp0240406; FBgn0213274.
DR   GeneID; 6645589; -.
DR   KEGG; dwi:6645589; -.
DR   eggNOG; ENOG502TBHQ; Eukaryota.
DR   HOGENOM; CLU_303532_0_0_1; -.
DR   InParanoid; B4N436; -.
DR   OMA; LEQMFEP; -.
DR   OrthoDB; 3612931at2759; -.
DR   PhylomeDB; B4N436; -.
DR   Proteomes; UP000007798; Unassembled WGS sequence.
DR   GO; GO:0005725; C:intercalary heterochromatin; IEA:EnsemblMetazoa.
DR   GO; GO:0043596; C:nuclear replication fork; IEA:EnsemblMetazoa.
DR   GO; GO:0005721; C:pericentric heterochromatin; IEA:EnsemblMetazoa.
DR   GO; GO:0005700; C:polytene chromosome; IEA:EnsemblMetazoa.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR   GO; GO:0003682; F:chromatin binding; IEA:EnsemblMetazoa.
DR   GO; GO:0051276; P:chromosome organization; IEA:EnsemblMetazoa.
DR   GO; GO:0042023; P:DNA endoreduplication; IEA:EnsemblMetazoa.
DR   GO; GO:0031507; P:heterochromatin formation; IEA:EnsemblMetazoa.
DR   GO; GO:0045185; P:maintenance of protein location; IEA:EnsemblMetazoa.
DR   GO; GO:2000104; P:negative regulation of DNA-templated DNA replication; IEA:EnsemblMetazoa.
DR   GO; GO:0032877; P:positive regulation of DNA endoreduplication; IEA:EnsemblMetazoa.
DR   GO; GO:0034502; P:protein localization to chromosome; IEA:EnsemblMetazoa.
DR   Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR038718; SNF2-like_sf.
DR   InterPro; IPR000330; SNF2_N.
DR   PANTHER; PTHR45629:SF7; DNA EXCISION REPAIR PROTEIN ERCC-6-RELATED; 1.
DR   PANTHER; PTHR45629; SNF2/RAD54 FAMILY MEMBER; 1.
DR   Pfam; PF00176; SNF2-rel_dom; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW   Cell division {ECO:0000256|ARBA:ARBA00022618};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Meiosis {ECO:0000256|ARBA:ARBA00023254};
KW   Mitosis {ECO:0000256|ARBA:ARBA00022776};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007798}.
FT   DOMAIN          31..264
FT                   /note="SNF2 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00176"
FT   REGION          366..387
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          441..532
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          604..662
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          767..911
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        465..487
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        604..619
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        636..662
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        767..885
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   911 AA;  103084 MW;  6506C978F3C95302 CRC64;
     MYHFVSEQTP ELRLATNVLV SSQTTQYLKS FQLEAVQFIY ERLSKHQFCI YNDESGLGKS
     AAVVALLSAL EPAKKKTLIV MQNDDRLLSG WQFHFDILTD LPVYVIQDVK DSTESPHSVY
     LAKWSVLRNI GDLSRFNFDL VIVDNRGHTL NNNFCTSMLF KHYEKKVNLV ISSVDITSET
     KLLYNILRLG GCLENQYRTY RSFERKFHLP DAKEVFQKKV DLEEYYKQRG FLGEYIRDYR
     LRRYRHQFDQ YLPLVSVEHY NNNLKLWLTA NNSESTLSGS TLPTISSSDA RSTAGTDEIM
     ECIINLKRVR EGAQEPEKLS EHSDEVLAMS PLVFEMSEPE EEDRQPPIPA PPTSQAVFTV
     SSDDCEMVTP QKRNKRVPST PTTKRKAKKR LVPLKPLPVE ISESEVEMET VKHPSPVLAT
     RNVNIRLRRT TIATPQSNAI RNTVSPKSEP KVVKQEAETP SRPMTRGMQR LTRSASARMV
     SKYMNRNRTT ETPKRKAGRR PKRKSLAKEI PMAADNPTQP PPPITPTATP QLLSSSSISS
     EYLQCAQKVP ENLDVLELPG FRVPFTPSPA TPNSLLLPSA FNLFSDSELV VPIVSQKQRE
     IVVVSSSHDD SSHSQPTQSR RTRALKRKRN EDHHPQATPV SVSSSNFGSL ISQQQQRQQN
     KSPDIFSNYS ELSQMTLTQP QPFEGFKIFG SEVKQVQQQN AKTKPIGKKR RERSCLDILE
     QMFEPHRRPE KPANTQVMPT LPRRNLLEDE GDMDIFEITN NREFGSRLRL NSGGNVSPVQ
     QQQQQQHHQQ TQQASLRSPQ QPNKITNYLI SSGPTPEERT STQMANVRKS PKSIRATQQQ
     QQTTKLTRWF GATATGTANS SATNTQMSSG ESSSAPTTPK GPSTSANAAA AMRAGRTSRS
     PTKRKRLDLY K
//
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