GenomeNet

Database: UniProt
Entry: B3M1D3_DROAN
LinkDB: B3M1D3_DROAN
Original site: B3M1D3_DROAN 
ID   B3M1D3_DROAN            Unreviewed;      1185 AA.
AC   B3M1D3;
DT   02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   02-SEP-2008, sequence version 1.
DT   24-JAN-2024, entry version 89.
DE   RecName: Full=F-box domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   Name=Dana\GF17149 {ECO:0000313|EMBL:EDV42160.1};
GN   Synonyms=dana_GLEANR_18415 {ECO:0000313|EMBL:EDV42160.1};
GN   ORFNames=GF17149 {ECO:0000313|EMBL:EDV42160.1};
OS   Drosophila ananassae (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7217 {ECO:0000313|EMBL:EDV42160.1, ECO:0000313|Proteomes:UP000007801};
RN   [1] {ECO:0000313|EMBL:EDV42160.1, ECO:0000313|Proteomes:UP000007801}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 14024-0371.13 {ECO:0000313|Proteomes:UP000007801};
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CH902617; EDV42160.1; -; Genomic_DNA.
DR   RefSeq; XP_001953599.1; XM_001953563.2.
DR   AlphaFoldDB; B3M1D3; -.
DR   SMR; B3M1D3; -.
DR   STRING; 7217.B3M1D3; -.
DR   EnsemblMetazoa; FBtr0121849; FBpp0120341; FBgn0094168.
DR   GeneID; 6499937; -.
DR   KEGG; dan:6499937; -.
DR   eggNOG; KOG1777; Eukaryota.
DR   HOGENOM; CLU_005078_0_0_1; -.
DR   InParanoid; B3M1D3; -.
DR   OMA; KESFHQL; -.
DR   OrthoDB; 5491826at2759; -.
DR   PhylomeDB; B3M1D3; -.
DR   Proteomes; UP000007801; Unassembled WGS sequence.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:EnsemblMetazoa.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:1900368; P:regulation of post-transcriptional gene silencing by regulatory ncRNA; IEA:EnsemblMetazoa.
DR   GO; GO:0070922; P:RISC complex assembly; IEA:EnsemblMetazoa.
DR   CDD; cd22091; F-box_FBXO11; 1.
DR   CDD; cd19676; UBR-box_UBR6_FBXO11; 1.
DR   Gene3D; 1.20.1280.50; -; 1.
DR   Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 3.
DR   InterPro; IPR039448; Beta_helix.
DR   InterPro; IPR006633; Carb-bd_sugar_hydrolysis-dom.
DR   InterPro; IPR036047; F-box-like_dom_sf.
DR   InterPro; IPR001810; F-box_dom.
DR   InterPro; IPR047505; F-box_FBXO11.
DR   InterPro; IPR047504; FBXO11_UBR-box.
DR   InterPro; IPR007742; NosD_dom.
DR   InterPro; IPR022441; Para_beta_helix_rpt-2.
DR   InterPro; IPR006626; PbH1.
DR   InterPro; IPR012334; Pectin_lyas_fold.
DR   InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR   InterPro; IPR003126; Znf_UBR.
DR   NCBIfam; TIGR03804; para_beta_helix; 2.
DR   PANTHER; PTHR22990; F-BOX ONLY PROTEIN; 1.
DR   PANTHER; PTHR22990:SF20; F-BOX ONLY PROTEIN 11; 1.
DR   Pfam; PF13229; Beta_helix; 2.
DR   Pfam; PF12937; F-box-like; 1.
DR   Pfam; PF05048; NosD; 1.
DR   Pfam; PF02207; zf-UBR; 1.
DR   SMART; SM00722; CASH; 3.
DR   SMART; SM00256; FBOX; 1.
DR   SMART; SM00710; PbH1; 19.
DR   SMART; SM00396; ZnF_UBR1; 1.
DR   SUPFAM; SSF81383; F-box domain; 1.
DR   SUPFAM; SSF51126; Pectin lyase-like; 3.
DR   PROSITE; PS50181; FBOX; 1.
DR   PROSITE; PS51157; ZF_UBR; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007801};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          365..411
FT                   /note="F-box"
FT                   /evidence="ECO:0000259|PROSITE:PS50181"
FT   DOMAIN          1091..1162
FT                   /note="UBR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51157"
FT   ZN_FING         1091..1162
FT                   /note="UBR-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00508"
FT   REGION          1..112
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          133..164
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          184..301
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        34..78
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        94..112
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        184..300
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1185 AA;  124712 MW;  FF9061C82273F9C5 CRC64;
     MPSASFTSSR TYVRRSRRKG ANRIAMPNRP SGNIMDPMLQ QNVSAAAGAG SGPSTSGASG
     SSNATSSSSS SSSSAAAGTA AAAPPAPAVA SGSSEYFDSG QGSSSNASAG AAAGASSSGL
     AAIVYNALQM MDTTENSGAG SSGAASSTPP VSSSSKSTCA TATAGSSTAS TSAAAAAAAA
     AASSAVSASS SHQSPYDLRR KISSSSHEQW GSSSSTAVLV GPSSSSPPLV NPGASPSSSS
     SSSSTSSSSS GSSSSSSSSS SASSANVQAP STSATFPVNN APTTGATLAQ PPNVHSSVPQ
     QHCGALPVGA AIEDNNYMLP ARKRSRRLYT QSGEMGATAG GASGEASGAG TSAAGSAGCA
     PTAAQYLQYE LPDEVLLAIF SYLMEQDLCR LALVCKRFNT IANDTELWKR LYQSVFEYDL
     PLFNPELCKF VFEKPEESEY ANPWKESFRQ LYRGVHVRPG YQERRSSGRS IVFFNTIQAA
     LDYPEDRAAA GAFASAGAGA GNVSAGLSNT SASAGSNGSG GGASVNALVN IYEEQVAPTE
     HPGPLIFLHA GHYKGEYLFI DSDVALVGAA PGNVAESVIL EREAGSTVMF VEGAKYAYVG
     YLTLKFSPEV TSTVSHHKHY CLDIGENCSP TVDNCIIRST SVVGAAVCVG GVNANPVIRN
     CDISDCENVG LYVTDYAQGT YEHNEISRNA LAGIWVKNFA SPIMRENHIH HGRDVGIFTF
     ENGMGYFEKN DIHNNRIAGF EVKAGANPTV VKCEIHHGQT GGIYVHENGL GQFIENRIHS
     NNFAGVWITS NSNPTIRKNE IYNGHQGGVY IFGEGRGLIE HNNIYGNALA GIQIRTNSDP
     IVRHNKIHHG QHGGIYVHEK GQGLIEENEV YSNTLAGVWI TTGSTPVLRR NRIHSGKQVG
     VYFYDNGHGK LEDNDIFNHL YSGVQIRTGS NPVIRGNKIW GGQNGGVLVY NGGLGLLEQN
     EIFDNAMAGV WIKTDSNPTL KRNKIYDGRD GGICIFNGGK GILEENDIFR NTQAGVLIST
     QSHPILRRNR IYDGQAAGVE ITNNATATLE HNQIFKNKFG GLCLASGVQP ITRGNNIFNN
     EDEVEKAVSS GQCLYKISSY TSFPMHDFYR CQTCNTTDRN AICVNCIKNC HAGHDVEFIR
     HDRFFCDCGA GTLSNQCQLQ GEPTQDTDTL YDSAAPMESH TLMVN
//
DBGET integrated database retrieval system