GenomeNet

Database: UniProt
Entry: A0A0Q9X3X4_DROMO
LinkDB: A0A0Q9X3X4_DROMO
Original site: A0A0Q9X3X4_DROMO 
ID   A0A0Q9X3X4_DROMO        Unreviewed;      1306 AA.
AC   A0A0Q9X3X4;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=Uncharacterized protein, isoform E {ECO:0000313|EMBL:KRG02573.1};
DE   SubName: Full=Uncharacterized protein, isoform F {ECO:0000313|EMBL:KRG02574.1};
GN   Name=Dmoj\GI15288 {ECO:0000313|EMBL:KRG02573.1};
GN   ORFNames=Dmoj_GI15288 {ECO:0000313|EMBL:KRG02573.1};
OS   Drosophila mojavensis (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila.
OX   NCBI_TaxID=7230 {ECO:0000313|EMBL:KRG02573.1, ECO:0000313|Proteomes:UP000009192};
RN   [1] {ECO:0000313|EMBL:KRG02573.1, ECO:0000313|Proteomes:UP000009192}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TSC#15081-1352.22 {ECO:0000313|EMBL:KRG02573.1}, and Tucson
RC   15081-1352.22 {ECO:0000313|Proteomes:UP000009192};
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).
RN   [2] {ECO:0000313|EMBL:KRG02573.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=TSC#15081-1352.22 {ECO:0000313|EMBL:KRG02573.1};
RX   PubMed=18057021; DOI=10.1093/bioinformatics/btm542;
RA   Zimin A.V., Smith D.R., Sutton G., Yorke J.A.;
RT   "Assembly reconciliation.";
RL   Bioinformatics 24:42-45(2008).
RN   [3] {ECO:0000313|EMBL:KRG02573.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=TSC#15081-1352.22 {ECO:0000313|EMBL:KRG02573.1};
RG   FlyBase;
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the formin homology family. Cappuccino
CC       subfamily. {ECO:0000256|ARBA:ARBA00005271}.
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DR   EMBL; CH933807; KRG02573.1; -; Genomic_DNA.
DR   EMBL; CH933807; KRG02574.1; -; Genomic_DNA.
DR   RefSeq; XP_015020280.1; XM_015164794.1.
DR   RefSeq; XP_015020281.1; XM_015164795.1.
DR   SMR; A0A0Q9X3X4; -.
DR   EnsemblMetazoa; FBtr0429345; FBpp0386812; FBgn0138037.
DR   EnsemblMetazoa; FBtr0430948; FBpp0388274; FBgn0138037.
DR   InParanoid; A0A0Q9X3X4; -.
DR   Proteomes; UP000009192; Unassembled WGS sequence.
DR   GO; GO:0005884; C:actin filament; IEA:InterPro.
DR   GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR   GO; GO:0045010; P:actin nucleation; IEA:InterPro.
DR   Gene3D; 1.20.58.2220; Formin, FH2 domain; 1.
DR   InterPro; IPR015425; FH2_Formin.
DR   InterPro; IPR042201; FH2_Formin_sf.
DR   InterPro; IPR001265; Formin_Cappuccino_subfam.
DR   PANTHER; PTHR45920; FORMIN HOMOLOGY 2 DOMAIN CONTAINING, ISOFORM I; 1.
DR   PANTHER; PTHR45920:SF8; FORMIN-C; 1.
DR   Pfam; PF02181; FH2; 1.
DR   PRINTS; PR00828; FORMIN.
DR   SMART; SM00498; FH2; 1.
DR   SUPFAM; SSF101447; Formin homology 2 domain (FH2 domain); 1.
DR   PROSITE; PS51444; FH2; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009192}.
FT   DOMAIN          843..1285
FT                   /note="FH2"
FT                   /evidence="ECO:0000259|PROSITE:PS51444"
FT   REGION          1..57
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          144..186
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          351..382
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          396..416
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          748..827
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          866..897
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1282..1306
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1151..1178
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1..22
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        396..415
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        753..815
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        874..890
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1282..1297
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1306 AA;  140372 MW;  F44BA591D7A1B9BC CRC64;
     MGNAHGQNRA AGSGSSPQAT GSLLRLAAGG RHGPGCMPPL AALEDRRSSS NSSHQQARVF
     SRFVKQKRDV FLQATPPVSP ASLPASPLAD WTPPDVGHGQ LNASAEQMDF HDVVSLDYNS
     DSTEFHNCSS DDCCYASTNT LTQPEEQSAS QSAAQQQHRQ RLHSLSMTSS TSASTSSSSS
     NDSDSLFDLN NKELIELKRR CRADKIAGLS LSRITYLSIA HESEPDPEQA LEAGLLHTEL
     LITPESSPDE RMALQLGKKL AQVLGSSSAS PTPTPPGSIT EANMMPVGVA AGSVAISTPR
     VDSPLGNGGE LFNISKAKKV ELQNLSSRFT AAVSPASTPT NLTDVGVAAT AAATTSTPTP
     TPTPTSTPTP TPTPTLISTA STPLETQSTV IISFKSSQTP ASAQRSASPT DSSAAGEALL
     QGDEAKQLDA DAASLVPPPP GYGTPTNPLL SSNVLKKVAS FSVERSTSTS SSCNSSSAPI
     VQSPALAMAA PAPSGDERET TLTAAQLEQS LAAGAGSRRG SSFVPEKLSF AAYEKFEGQM
     LIKWLISTLQ SSAALGTLSQ ESLNAMTLQF CQNLKYVGVL KQISNEQQQQ QDAPSGFSPY
     EMYQWTHTEQ PTTSLPLTPG KLDKVTAWPF SSTPAVQKGH YEGSSAQTDS QKTLQQILRK
     RLLNCATLAE VHAVVNELLS SVDEPPRRPS KRCINLTELL NASEATIYEY NRPAESKSYA
     DAGSQTEELT CQGSCKCGGI SAGAATGATE ATAAAPPPPP PPPPPPPPPL PGNAGGAAPP
     PPPPPPPGSA GPPPPPPPGA PCPGNMPPPP PPLSTSKSGS SLAPAPLPDP AEGNWFLRTC
     VQRKSAVNPP KPMRPLYWTR IVTSAPPVPR PPSVANSTDS ADNSTSSPED LPVPAAMPPV
     PPPCKEIWTE IDETPLDNID EFTELFSRQA IAPVSKPKEL KPKREKSIKV LDPKRSRNVG
     IFSRSLHVPA SEIEHAIYHV DTSVISLETL QQISFMRATD EELQRIREAD GGDIPLDHPE
     QFLRDISLIS MASERISCIV FQAEFEESVT LLVRKLETVS QLSQQLIESE DLKLVFSIIL
     TLGNYMNGGN RQRGQADGFN LDILGKLKDV KSKESHTTLL HFIVRTYIAQ RRKEMTLHEI
     TLPIPEPSDV ERAAQLDFDE VQQQINDLNR KLTACKQTTA LVLSASSEHR EPFKSKMEEF
     TASAEKSVAK LHQLIQECRE LFLETMRFYH FSPKGCTLTL SQCTPDQFFG YWTNFTNDFK
     DIWKKEITIL KNEIIKKPKQ LAVENRRDSS TRDRTSCKAR VRRSKN
//
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