ID   DAPKR_DROME             Reviewed;         674 AA.
AC   Q0KHT7; E1JJH9; Q86P19;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-JAN-2014, sequence version 2.
DT   04-NOV-2026, entry version 131.
DE   RecName: Full=Death-associated protein kinase related;
DE            EC=2.7.11.1;
GN   Name=Drak; ORFNames=CG32666;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Altocrustacea; Allotriocarida;
OC   Hexapoda; Insecta; Pterygota; Neoptera; Eumetabola; Endopterygota;
OC   Aparaglossata; Panorpida; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley; TISSUE=Embryo;
RA   Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA   Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA   Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA   Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA   Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL   Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-384; SER-387; SER-435;
RP   SER-437 AND SER-521, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Embryo;
RX   PubMed=18327897; DOI=10.1021/pr700696a;
RA   Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT   "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL   J. Proteome Res. 7:1675-1682(2008).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP +
CC         H(+); Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] +
CC         ADP + H(+); Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC         COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR   EMBL; AE014298; ACZ95258.1; -; Genomic_DNA.
DR   EMBL; AE014298; ACZ95259.1; -; Genomic_DNA.
DR   EMBL; BT003530; AAO39534.1; -; mRNA.
DR   RefSeq; NP_001162723.1; NM_001169252.2.
DR   RefSeq; NP_001162724.1; NM_001169253.2.
DR   RefSeq; NP_996411.2; NM_206688.2.
DR   AlphaFoldDB; Q0KHT7; -.
DR   SMR; Q0KHT7; -.
DR   BioGRID; 58507; 6.
DR   FunCoup; Q0KHT7; 323.
DR   STRING; 7227.FBpp0290243; -.
DR   iPTMnet; Q0KHT7; -.
DR   PaxDb; 7227-FBpp0290243; -.
DR   PeptideAtlas; Q0KHT7; -.
DR   DNASU; 32097; -.
DR   EnsemblMetazoa; FBtr0301020; FBpp0290242; FBgn0052666.
DR   EnsemblMetazoa; FBtr0301021; FBpp0290243; FBgn0052666.
DR   EnsemblMetazoa; FBtr0340295; FBpp0309256; FBgn0052666.
DR   GeneID; 32097; -.
DR   KEGG; dme:Dmel_CG32666; -.
DR   UCSC; CG32666-RA; d. melanogaster.
DR   UCSC; CG32666-RB; d. melanogaster.
DR   AGR; FB:FBgn0052666; -.
DR   CTD; 32097; -.
DR   FlyBase; FBgn0052666; Drak.
DR   VEuPathDB; VectorBase:FBgn0052666; -.
DR   eggNOG; KOG0032; Eukaryota.
DR   HOGENOM; CLU_023542_0_0_1; -.
DR   InParanoid; Q0KHT7; -.
DR   OMA; AAHNYKT; -.
DR   OrthoDB; 74764at2759; -.
DR   BioGRID-ORCS; 32097; 0 hits in 3 CRISPR screens.
DR   GenomeRNAi; 32097; -.
DR   PRO; PR:Q0KHT7; -.
DR   Proteomes; UP000000803; Chromosome X.
DR   Bgee; FBgn0052666; Expressed in dorsal appendage forming follicle cell in ovary and 264 other cell types or tissues.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR   GO; GO:0007480; P:imaginal disc-derived leg morphogenesis; IMP:FlyBase.
DR   GO; GO:0007476; P:imaginal disc-derived wing morphogenesis; IMP:FlyBase.
DR   GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR   GO; GO:0002009; P:morphogenesis of an epithelium; IGI:FlyBase.
DR   CDD; cd14106; STKc_DRAK; 1.
DR   FunFam; 3.30.200.20:FF:000175; Serine/threonine-protein kinase 17B; 1.
DR   FunFam; 1.10.510.10:FF:001311; Uncharacterized protein, isoform A; 1.
DR   Gene3D; 3.30.200.20; Phosphorylase Kinase, domain 1; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR24342:SF12; DEATH-ASSOCIATED PROTEIN KINASE RELATED; 1.
DR   PANTHER; PTHR24342; SERINE/THREONINE-PROTEIN KINASE 17; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome; Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..674
FT                   /note="Death-associated protein kinase related"
FT                   /id="PRO_0000355636"
FT   DOMAIN          37..295
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          308..388
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          412..440
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          511..583
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          614..650
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        312..343
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        352..363
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        373..382
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        512..525
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        526..541
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        555..564
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        565..583
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        614..631
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        632..650
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        160
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         43..51
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         66
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         384
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         387
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         435
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         437
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         521
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
SQ   SEQUENCE   674 AA;  73001 MW;  BB94555F5161DBF5 CRC64;
     MFTEKGIFPI GDGLLDVDAD RLKGLLVSCP DINEIYEVEQ TPFARGKFAA VRRAIHKNTG
     SHFAAKFLKR RRRAQSSDKE IKHEIAVLML CEGEDNIVNL NAVHETRSDT ALLLELATGG
     ELQTILDNEE CLTEAQARHC MREVLKALKF LHDRSIAHLD LKPQNILLAG ERIEDGLKLC
     DFGISRVVCE GINVREMAGT PDYVAPEVLQ YEPLSLLTDI WSVGVLTYVL LSGFSPFGGD
     TKQETFLNIS QCALTFPDNL FGGVSPVAID FIRRALRIKP NDRMNATGCL DHIWLKDDCS
     LDRQIYLQPQ SDAEEEEEED VDDDVEDEEE EEQVEEEEEE TQNVEEPTTE APQQQQQPVQ
     QHQLAKSGQI HSKPTHNGHH RANSGGSISK IPIATSKLQS TPSSETTTAI HTLTSNSNGH
     VHKPTQIVTP TRRASDSDKE NTYTATFVKK PVATIQLGSS NGIEDATVVA TLTLFPDAPT
     TPKVIRKTPT GESNGSATSV KALVKKFQLE DSSGSAVARR SGGAVTSSSG LHSPTTTSVR
     LNSIRRASEP LTTVYKKQTS QNGCSSTSNP SSSPGSSPTT SGSTATLLIH SQRLGNSTAP
     ASHCVAVPAT ATATSSASSS NSSSGKSTSA AHHLHHHHMH HHHHHHHHHV VIAAKNAAAV
     AATNNLSLDQ GIIC
//