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Database: UniProt
Entry: B4QPP0_DROSI
LinkDB: B4QPP0_DROSI
Original site: B4QPP0_DROSI 
ID   B4QPP0_DROSI            Unreviewed;      1209 AA.
AC   B4QPP0;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 91.
DE   SubName: Full=GD12830 {ECO:0000313|EMBL:EDX10031.1};
GN   Name=Dsim\GD12830 {ECO:0000313|EMBL:EDX10031.1};
GN   ORFNames=Dsim_GD12830 {ECO:0000313|EMBL:EDX10031.1}, Dsimw501_GD12830
GN   {ECO:0000313|EMBL:KMY98920.1};
OS   Drosophila simulans (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7240 {ECO:0000313|EMBL:EDX10031.1, ECO:0000313|Proteomes:UP000000304};
RN   [1] {ECO:0000313|EMBL:EDX10031.1, ECO:0000313|Proteomes:UP000000304}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mixed {ECO:0000313|EMBL:EDX10031.1}, and mosaic
RC   {ECO:0000313|Proteomes:UP000000304};
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:EDX10031.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed {ECO:0000313|EMBL:EDX10031.1}, and W501
RC   {ECO:0000313|EMBL:KMY98920.1};
RG   FlyBase;
RL   Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:KMY98920.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=W501 {ECO:0000313|EMBL:KMY98920.1};
RX   PubMed=22936249; DOI=10.1101/gr.141689.112;
RA   Hu T.T., Eisen M.B., Thornton K.R., Andolfatto P.;
RT   "A second-generation assembly of the Drosophila simulans genome provides
RT   new insights into patterns of lineage-specific divergence.";
RL   Genome Res. 23:89-98(2013).
RN   [4] {ECO:0000313|EMBL:KMY98920.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=W501 {ECO:0000313|EMBL:KMY98920.1};
RA   Hu T., Eisen M.B., Thornton K.R., Andolfatto P.;
RL   Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CM000363; EDX10031.1; -; Genomic_DNA.
DR   EMBL; CM002912; KMY98920.1; -; Genomic_DNA.
DR   RefSeq; XP_016031391.1; XM_016169785.1.
DR   AlphaFoldDB; B4QPP0; -.
DR   STRING; 7240.B4QPP0; -.
DR   EnsemblMetazoa; FBtr0212740; FBpp0211232; FBgn0184555.
DR   KEGG; dsi:Dsimw501_GD12830; -.
DR   HOGENOM; CLU_003357_0_0_1; -.
DR   OMA; RRDNHCQ; -.
DR   OrthoDB; 5489497at2759; -.
DR   Proteomes; UP000000304; Chromosome 3l.
DR   Proteomes; UP000035880; Chromosome 3L.
DR   Bgee; FBgn0184555; Expressed in embryo and 3 other cell types or tissues.
DR   GO; GO:0000228; C:nuclear chromosome; IEA:EnsemblMetazoa.
DR   GO; GO:0005705; C:polytene chromosome interband; IEA:EnsemblMetazoa.
DR   GO; GO:0005703; C:polytene chromosome puff; IEA:EnsemblMetazoa.
DR   GO; GO:0016456; C:X chromosome located dosage compensation complex, transcription activating; IEA:EnsemblMetazoa.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0035175; F:histone H3S10 kinase activity; IEA:EnsemblMetazoa.
DR   GO; GO:0033696; P:heterochromatin boundary formation; IEA:EnsemblMetazoa.
DR   GO; GO:0048477; P:oogenesis; IEA:EnsemblMetazoa.
DR   GO; GO:0043687; P:post-translational protein modification; IEA:EnsemblMetazoa.
DR   GO; GO:0046777; P:protein autophosphorylation; IEA:EnsemblMetazoa.
DR   GO; GO:0000723; P:telomere maintenance; IEA:EnsemblMetazoa.
DR   CDD; cd00180; PKc; 1.
DR   CDD; cd05583; STKc_MSK_N; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 2.
DR   InterPro; IPR000961; AGC-kinase_C.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR017892; Pkinase_C.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR24351:SF175; CHROMOSOMAL SERINE_THREONINE-PROTEIN KINASE JIL-1; 1.
DR   PANTHER; PTHR24351; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR   Pfam; PF00069; Pkinase; 2.
DR   Pfam; PF00433; Pkinase_C; 1.
DR   SMART; SM00133; S_TK_X; 1.
DR   SMART; SM00220; S_TKc; 2.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 2.
DR   PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 2.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 2.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000304};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KMY98920.1}.
FT   DOMAIN          261..530
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          531..599
FT                   /note="AGC-kinase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51285"
FT   DOMAIN          623..886
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1..118
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          163..184
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          210..230
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1022..1046
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1168..1196
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..20
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        21..37
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        53..118
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        210..229
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1177..1193
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         293
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   1209 AA;  136935 MW;  24DF99006CEB301D CRC64;
     MSRLQKQNYE ILSGTSTSRL KNHQHPRESE SLAYDEPDQM VRNHLNGQLV ANGKGKTLKN
     SNSETLTNGK KSKLNAEGSG SGSGKTLNYN NNNNNNNSIS ATNGQYTNSN SKTTSASARD
     YTYRETISPP TPPSPPTTNV ADIVCISDAE SDDGRYPERE YYDQDMEEDE PNGMEIDESS
     SSLSKAKSNN AAAAAAAAAA AAAAAASKAS SSTTPSYAMP TSNSTPLDLD NEAHQRDLEA
     VTDLKYYVKL YSDEAVSLND FKIIRVLGTG AYGRVFLVRK LTRHDAGKLY AMKVLNKITV
     VQKRKTAEHT KTERVVLEAI QRNPFLVSLH YAFQSSSKLY LVLDFANGGE LFTHLYHSEN
     FEESRVRVYI AEVVLALEQL HQLGIIYRDI KLENILLDGE GHIVLSDFGL SKILTAENEY
     RAHSFCGTLE YMAPEIIRTG PPGHDSAVDW WSVGVLTFEL LTGASPFATS DGQAQQSEIS
     RRIQKEQPLI PSSFSANARD FVLKMLEKNP KRRLGGNHRD ASEIKEHPFF NGINWQELRT
     KRRKAPYKPT LTAEDDVQNF SNEFTDQVPE DPECDAPPSR IRLFRGYTYV APEHLEQMRR
     DNHCQIQYCN TGLQNIPCRP DDLELGTRTS SGAYGTCHFV VDSSTDLVFL AKIIPLSKFR
     PSEVDALISC ALDTTNHKNI VSYHGTFREK CETWIVMEYL SGPELTASLG MDEDSCREIF
     LQLVMAVRHI HSKHFIHGDL KPENIMFENG EDRTVKVIDF GSACYNNRFK SWKDKPRYTL
     DYAPPEMLAD ANLVTYSPAV DIYGLGATLY TMLVGHRPYR QNEDDVDHSA AAHHELRKRM
     RRETFNQRSV RWESASPAFR HLVSWCLQRD PADRPTVSDI LDSEWLQYGS NDPDVDIIMP
     QQMVVDLSED TMEQPMAGMI DDQEQMEFTH DKSTEDEGIT LVSEPMEATV ATQESWKNAA
     AFSSAVAPTD DEIVHERFDP AFEVQADFYG FDEYEPPLPL PEEYYSELPL PEEDRQYMPP
     PAAPIPVEPE TTFRRPRTRQ QRRTESQIIQ PVSLATHEDS KASLRVLMQQ LPPPGDNTVN
     TVARIPKRTQ RVVRTLPPSF GTTKRDENFN GFSKTAISWR KTRASWRHFC LLINGVQQVL
     KIRFKKARRV YCLPHIKEEK LDHAYEKPLT FPRPKAQLKR TKREPKVPRP PTRVQPERAR
     ALRQLYQFQ
//
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