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Database: UniProt
Entry: B4GX25_DROPE
LinkDB: B4GX25_DROPE
Original site: B4GX25_DROPE 
ID   B4GX25_DROPE            Unreviewed;       903 AA.
AC   B4GX25;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   24-JAN-2024, entry version 99.
DE   SubName: Full=GL21243 {ECO:0000313|EMBL:EDW27352.1};
GN   Name=Dper\GL21243 {ECO:0000313|EMBL:EDW27352.1};
GN   ORFNames=Dper_GL21243 {ECO:0000313|EMBL:EDW27352.1};
OS   Drosophila persimilis (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7234 {ECO:0000313|Proteomes:UP000008744};
RN   [1] {ECO:0000313|EMBL:EDW27352.1, ECO:0000313|Proteomes:UP000008744}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MSH-3 / Tucson 14011-0111.49
RC   {ECO:0000313|Proteomes:UP000008744};
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   -!- SIMILARITY: Belongs to the centaurin gamma-like family.
CC       {ECO:0000256|ARBA:ARBA00005430}.
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DR   EMBL; CH479195; EDW27352.1; -; Genomic_DNA.
DR   RefSeq; XP_002023224.1; XM_002023188.1.
DR   AlphaFoldDB; B4GX25; -.
DR   SMR; B4GX25; -.
DR   EnsemblMetazoa; FBtr0186858; FBpp0185350; FBgn0158836.
DR   eggNOG; KOG0705; Eukaryota.
DR   HOGENOM; CLU_007326_1_0_1; -.
DR   OMA; WYGANIK; -.
DR   PhylomeDB; B4GX25; -.
DR   Proteomes; UP000008744; Unassembled WGS sequence.
DR   GO; GO:0005525; F:GTP binding; IEA:InterPro.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd08836; ArfGap_AGAP; 1.
DR   CDD; cd04103; Centaurin_gamma; 1.
DR   CDD; cd01250; PH_AGAP; 1.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR   Gene3D; 1.10.220.150; Arf GTPase activating protein; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 2.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR037278; ARFGAP/RecO.
DR   InterPro; IPR001164; ArfGAP_dom.
DR   InterPro; IPR038508; ArfGAP_dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR001806; Small_GTPase.
DR   PANTHER; PTHR45819; CENTAURIN-GAMMA-1A; 1.
DR   PANTHER; PTHR45819:SF5; CENTAURIN-GAMMA-1A; 1.
DR   Pfam; PF01412; ArfGap; 1.
DR   Pfam; PF00071; Ras; 1.
DR   PRINTS; PR00405; REVINTRACTNG.
DR   SMART; SM00105; ArfGap; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00175; RAB; 1.
DR   SMART; SM00173; RAS; 1.
DR   SMART; SM00174; RHO; 1.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   SUPFAM; SSF57863; ArfGap/RecO-like zinc finger; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 1.
DR   PROSITE; PS50115; ARFGAP; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS51419; RAB; 1.
DR   PROSITE; PS51421; RAS; 1.
PE   3: Inferred from homology;
KW   ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW   GTPase activation {ECO:0000256|ARBA:ARBA00022468};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008744};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00288}.
FT   DOMAIN          357..590
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          610..730
FT                   /note="Arf-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50115"
FT   REPEAT          774..806
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REGION          298..356
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          476..503
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          522..547
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          835..854
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          878..903
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        315..336
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        483..503
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   903 AA;  98103 MW;  5740CF182DABB038 CRC64;
     MLAVKNFFLP ERTKAPETPQ RFSRMPEAFL RSIRRRSLRV KRAKSLVVPD RSEKRKSDSF
     VNSQEWTISR SVPDLRLGIV GSLNSGKSAL VHRYLTGSYM QEESPEGGRF KKEVFIDGQS
     YLLLIRDEGG APEMQFAGWV DAVIFVFSLE NEGSFNTVYN YYTKMAHFRN GQDIPMILVG
     TQDSISERNP RVIDDTRARK LASDLKRCSY YETCATYGLN VERVFQDACQ KILSQQQLPL
     RISADFAPGG AEAVSLQASS SSLASCTTVA TNENNNITKY NPGTAANSLQ GDCSQVQLRD
     PRDLAPPPGK ELPTPTSTPT TSRKSRRRSN LFIPSSSKKA DKDKEPKGSE LGSGRSIPIK
     QGYLYKRSSK SLNKEWKKKY VTLCDDGRLT YHPSLHDYMD DVHGKEIPLQ YVTVKVPGQK
     PRGSKSIITN SALTSSLLAN GHRAQNTLSD GIGCLTLAKD NQRKLSEKLS LLGAGSGAAA
     GGTEPLKSNS SQQTSGDEGI AMSNSNSQTF IAGEAAATAT ATASKLEAQT PNVKKWHRRM
     KSSSVKASEA DDNDGYEFYI VSLDSKQWHF EAANSEERDE WVAAVEQEIF KSLQSIESSK
     TKQATSTDLA AMLTIRQRVP GNGHCVDCGA PNPEWASLNL GVLMCIECSG IHRNLGSHIS
     KVRSLGLDDW PSPHLSVMLA IGNSLANSVW ESNTRQRAKP TAQASREEKE RWIRSKYEAK
     EFLTSLGGGS STHASPSPGQ QLIEAVIRAD IKSIVSILAN CPAEVTNANV SARDVRTPLL
     LACAIGNLAI AQLLIWYGAN IKHTDHEGRT CLAYARAAQS LATAKSMKAA AAAQAGTTVP
     PPAPPANGGI PAPQYNVEDT TALVELLEGL GCPEAAPLTA SGTLPRRRDT LGTPYEKSVS
     GVI
//
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