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Database: UniProt
Entry: B4JQT0_DROGR
LinkDB: B4JQT0_DROGR
Original site: B4JQT0_DROGR 
ID   B4JQT0_DROGR            Unreviewed;       990 AA.
AC   B4JQT0;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   24-JAN-2024, entry version 80.
DE   SubName: Full=GH13125 {ECO:0000313|EMBL:EDV99260.1};
GN   Name=Dgri\GH13125 {ECO:0000313|EMBL:EDV99260.1};
GN   ORFNames=Dgri_GH13125 {ECO:0000313|EMBL:EDV99260.1};
OS   Drosophila grimshawi (Hawaiian fruit fly) (Idiomyia grimshawi).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Hawaiian Drosophila.
OX   NCBI_TaxID=7222 {ECO:0000313|Proteomes:UP000001070};
RN   [1] {ECO:0000313|EMBL:EDV99260.1, ECO:0000313|Proteomes:UP000001070}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 15287-2541.00 {ECO:0000313|Proteomes:UP000001070};
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   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906}.
CC   -!- SIMILARITY: Belongs to the cullin family.
CC       {ECO:0000256|ARBA:ARBA00006019, ECO:0000256|PROSITE-ProRule:PRU00330,
CC       ECO:0000256|RuleBase:RU003829}.
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DR   EMBL; CH916372; EDV99260.1; -; Genomic_DNA.
DR   RefSeq; XP_001993335.1; XM_001993299.1.
DR   AlphaFoldDB; B4JQT0; -.
DR   SMR; B4JQT0; -.
DR   STRING; 7222.B4JQT0; -.
DR   eggNOG; KOG2166; Eukaryota.
DR   HOGENOM; CLU_004747_7_1_1; -.
DR   InParanoid; B4JQT0; -.
DR   OMA; MFKDMTI; -.
DR   PhylomeDB; B4JQT0; -.
DR   Proteomes; UP000001070; Unassembled WGS sequence.
DR   GO; GO:0031463; C:Cul3-RING ubiquitin ligase complex; IEA:EnsemblMetazoa.
DR   GO; GO:0005829; C:cytosol; IEA:EnsemblMetazoa.
DR   GO; GO:0035324; C:female germline ring canal; IEA:EnsemblMetazoa.
DR   GO; GO:0060090; F:molecular adaptor activity; IEA:EnsemblMetazoa.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:EnsemblMetazoa.
DR   GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IEA:EnsemblMetazoa.
DR   GO; GO:0007409; P:axonogenesis; IEA:EnsemblMetazoa.
DR   GO; GO:0048813; P:dendrite morphogenesis; IEA:EnsemblMetazoa.
DR   GO; GO:0007476; P:imaginal disc-derived wing morphogenesis; IEA:EnsemblMetazoa.
DR   GO; GO:0045475; P:locomotor rhythm; IEA:EnsemblMetazoa.
DR   GO; GO:0045879; P:negative regulation of smoothened signaling pathway; IEA:EnsemblMetazoa.
DR   GO; GO:0120177; P:negative regulation of torso signaling pathway; IEA:EnsemblMetazoa.
DR   GO; GO:0007278; P:pole cell fate determination; IEA:EnsemblMetazoa.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:EnsemblMetazoa.
DR   GO; GO:0070936; P:protein K48-linked ubiquitination; IEA:EnsemblMetazoa.
DR   GO; GO:2000495; P:regulation of cell proliferation involved in compound eye morphogenesis; IEA:EnsemblMetazoa.
DR   GO; GO:0045187; P:regulation of circadian sleep/wake cycle, sleep; IEA:EnsemblMetazoa.
DR   GO; GO:0007423; P:sensory organ development; IEA:EnsemblMetazoa.
DR   GO; GO:0030431; P:sleep; IEA:EnsemblMetazoa.
DR   GO; GO:0007291; P:sperm individualization; IEA:EnsemblMetazoa.
DR   Gene3D; 1.20.1310.10; Cullin Repeats; 4.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR045093; Cullin.
DR   InterPro; IPR016157; Cullin_CS.
DR   InterPro; IPR016158; Cullin_homology.
DR   InterPro; IPR036317; Cullin_homology_sf.
DR   InterPro; IPR001373; Cullin_N.
DR   InterPro; IPR019559; Cullin_neddylation_domain.
DR   InterPro; IPR016159; Cullin_repeat-like_dom_sf.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR11932; CULLIN; 1.
DR   PANTHER; PTHR11932:SF168; CULLIN-3; 1.
DR   Pfam; PF00888; Cullin; 1.
DR   Pfam; PF10557; Cullin_Nedd8; 1.
DR   SMART; SM00182; CULLIN; 1.
DR   SMART; SM00884; Cullin_Nedd8; 1.
DR   SUPFAM; SSF75632; Cullin homology domain; 1.
DR   SUPFAM; SSF74788; Cullin repeat-like; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR   PROSITE; PS01256; CULLIN_1; 1.
DR   PROSITE; PS50069; CULLIN_2; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000001070};
KW   Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT   DOMAIN          598..856
FT                   /note="Cullin family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50069"
FT   REGION          1..38
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          122..159
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        22..38
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   990 AA;  113510 MW;  80D5E621CA428F91 CRC64;
     MNLRGNPQKK EGKMRIRAFP AAGQDQQQQQ QQPPEEEQQL AICQAQYIIG EHRYSWERAL
     GSHRGACGAR VPGSLQSSQM YSYDPRISLF GAAAAPHATP SSNSQPINTS SPTQPLYHYY
     PQQSTSPHSR IVGGSNNFNQ RPRSARNALG QQPQQHHHLR SQHLNVPLNV EATQPVSRFS
     ACPTPGTSAN GPPHHCEQSL RSTLSVVSVA GPVRLREIGR KYPLWLPEYK RRAFNASMDE
     KYVDDIWATL KNAIQEIQKK NNSGLSFEQL YRNAYNMVLH KHGNRLYNGL SNVVSEHLEQ
     KVRQDVLESL NSTFLSKLNQ AWTDHQTSMV MIRDILMYMD RVYVHQRGLD NVYNLGLNLF
     RDQIVRFPEI QKALRDRLLG MVIEERRGEP INHLAIKNAC TMLITLGINS RTVYEEDFEK
     PFLAQSASFY RNESQKFLEE NNAGVYIKKV EARITEESSR ATLYLDKDTE PRIVRVVEEE
     LIKKHMRTIV EMENSGVVHM IKNSKTEDLA CTYKLFSRLK DEGLKVIADT MSAYLREQGS
     MLVKEEENGT TNPITFVQNL LDLKDRFDQF LLHSFSNDRL FKNVISADFE HFLNLNNKSP
     EYLSLFIDDK LKKGGKGMSE QEIETILDKT MVLFRFLLEK DVFERYYKTH LAKRLLLNKS
     VSDDFEKNMI SKLKASTECG CQFTSKLEGM FKDMSVSNTI MDEFKNYVNN NSFSLSGVEL
     TVRILTTGFW PTQTATPNCN IPSAPREAFE VFKKFYLDKH SGRQLTLQPQ MGTAYINAVF
     YGRKANDSDK DKDGPSSSSS GCAVPTTTRK HILQVSTYQM CVLLLYNNRD VLTYDDIHQE
     TDIPERELVR ALQSLSMGKP AQRLLVRNSK TKTKDIEPSD EFYVNDAFVS KFHRVKIQTV
     AAKGESEPER KETRGKVDED RKHEIEAAIV RIMKARKRMA HNLLVSDVTS QLKSRFLPSP
     VFIKKRIEGL IEREYLARTP EDRKVYIYLA
//
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