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Database: UniProt
Entry: A0A0Q9VZW6_DROVI
LinkDB: A0A0Q9VZW6_DROVI
Original site: A0A0Q9VZW6_DROVI 
ID   A0A0Q9VZW6_DROVI        Unreviewed;      1059 AA.
AC   A0A0Q9VZW6;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   SubName: Full=Uncharacterized protein, isoform O {ECO:0000313|EMBL:KRF78102.1};
GN   Name=Dvir\GJ15244 {ECO:0000313|EMBL:KRF78102.1};
GN   ORFNames=Dvir_GJ15244 {ECO:0000313|EMBL:KRF78102.1};
OS   Drosophila virilis (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila.
OX   NCBI_TaxID=7244 {ECO:0000313|EMBL:KRF78102.1, ECO:0000313|Proteomes:UP000008792};
RN   [1] {ECO:0000313|EMBL:KRF78102.1, ECO:0000313|Proteomes:UP000008792}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 15010-1051.87 {ECO:0000313|Proteomes:UP000008792};
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 MAGUK family.
CC       {ECO:0000256|ARBA:ARBA00007014}.
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DR   EMBL; CH940660; KRF78102.1; -; Genomic_DNA.
DR   RefSeq; XP_015024591.1; XM_015169105.1.
DR   AlphaFoldDB; A0A0Q9VZW6; -.
DR   SMR; A0A0Q9VZW6; -.
DR   EnsemblMetazoa; FBtr0437489; FBpp0394312; FBgn0202440.
DR   GeneID; 6635443; -.
DR   OrthoDB; 2879721at2759; -.
DR   Proteomes; UP000008792; Unassembled WGS sequence.
DR   GO; GO:0030054; C:cell junction; IEA:UniProt.
DR   CDD; cd00071; GMPK; 1.
DR   CDD; cd00992; PDZ_signaling; 3.
DR   CDD; cd11861; SH3_DLG-like; 1.
DR   Gene3D; 2.30.42.10; -; 3.
DR   Gene3D; 3.30.63.10; Guanylate Kinase phosphate binding domain; 1.
DR   Gene3D; 1.10.287.470; Helix hairpin bin; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 2.
DR   InterPro; IPR008145; GK/Ca_channel_bsu.
DR   InterPro; IPR008144; Guanylate_kin-like_dom.
DR   InterPro; IPR020590; Guanylate_kinase_CS.
DR   InterPro; IPR015143; L27_1.
DR   InterPro; IPR004172; L27_dom.
DR   InterPro; IPR036892; L27_dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR036034; PDZ_sf.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   PANTHER; PTHR23119; DISCS LARGE; 1.
DR   PANTHER; PTHR23119:SF51; DISKS LARGE 1 TUMOR SUPPRESSOR PROTEIN; 1.
DR   Pfam; PF00625; Guanylate_kin; 1.
DR   Pfam; PF09058; L27_1; 1.
DR   Pfam; PF00595; PDZ; 3.
DR   Pfam; PF00018; SH3_1; 1.
DR   SMART; SM00072; GuKc; 1.
DR   SMART; SM00569; L27; 1.
DR   SMART; SM00228; PDZ; 3.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF101288; L27 domain; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF50156; PDZ domain-like; 3.
DR   SUPFAM; SSF50044; SH3-domain; 1.
DR   PROSITE; PS00856; GUANYLATE_KINASE_1; 1.
DR   PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
DR   PROSITE; PS51022; L27; 1.
DR   PROSITE; PS50106; PDZ; 3.
DR   PROSITE; PS50002; SH3; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008792};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}.
FT   DOMAIN          4..64
FT                   /note="L27"
FT                   /evidence="ECO:0000259|PROSITE:PS51022"
FT   DOMAIN          241..328
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          369..460
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          543..624
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          657..727
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   DOMAIN          869..1044
FT                   /note="Guanylate kinase-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50052"
FT   REGION          204..228
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          466..540
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          767..792
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        466..515
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1059 AA;  116896 MW;  92BEBEEE0000337D CRC64;
     MPVKKQEAHR ALELLEDYHA RLSEPQDRAL RIAIERVIRI FKSRLFQALL DIQEFYELTL
     LDDSKSIQQK TAETLQIATK WEKDGQATKI ADFIKTTNLN RNCVYEINND ATNPNPSSNL
     NQNANANVAA HAEALSRTFK NELEEILNQR MRIESDYENA KDATADDAAI QQVRNSRSPQ
     QQQQQQVVQQ LQQQQQQQQQ QQQQQQHLAQ SQPTTARSGT QILHKASSTK VNGDDSWYYE
     DIQLERGNSG LGFSIAGGTD NPHIGTDTSI YITKLIPGGA AAADGRLSIN DIIVSVNDVS
     VVDVPHASAV DALKKAGNIV KLHVKRKRVA SATAAAPTTA DVQDSVSGTA VSASASASAS
     APAGPKVIEI DLVKGGKGLG FSIAGGIGNQ HIPGDNGIYV TKLMDGGAAQ VDGRLSIGDK
     LIAVRTNGSE KNLENVTHEL AVGTLKSITD KVTLIVGKTQ HLTSSASQSG SAQLGQQSQA
     HSQSQTQLAA ATRQQQQQQQ QQPANSESAE PGSRYASTNV LAAVPPGTPR AVSTEDITRE
     PRTITIQKGP QGLGFNIVGG EDGQGIYVSF ILAGGPADLG SELKRGDQLL SVNNVNLTHA
     THEEAAQALK TSGGVVTLVA QYRPEDYNRF EARIQELKQQ AALSAGGSGT LLRTTQKRSL
     YVRALFDYDP NRDDGLPSRG LPFKHGDILH VTNASDDEWW QARRVLGDNE DEQIGIVPSK
     RRWERKMRAR DRSVKFQGHA AANNNLDKQS TLDRKKKNFT FSRKFPFMKS RDEKNEDGSD
     QEPNGFVNSN SEIDVNNVNN NQANEPQPFM LCYTQDDANA EGGEIIYRVE LPDMEQITLI
     YLENNDADYP SEENVLSYEA VQRLSISYTR PVIILGPLKD RINDDLISEY PDKFGSCVPH
     TTRPKREYEV DGRDYHFVSS REQMERDIQN HLFIEAGQYN DNLYGTSVAS VREVAERGKH
     CILDVSGNAI KRLQVAQLYP VAVFIKPKSV DSVMEMNRRM TEEQAKKTYE RAIKMEQEFG
     EYFTGVVQGD TIEEIYSKVK SMIWSQSGPT IWVPSKESL
//
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