DCLK_DROPS
ID DCLK_DROPS Reviewed; 755 AA.
AC B5DK35;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Serine/threonine-protein kinase GA29083 {ECO:0000250|UniProtKB:Q7PLI7, ECO:0000312|EMBL:EDY70661.1};
DE EC=2.7.11.1;
DE AltName: Full=Doublecortin-like and CAM kinase-like protein;
GN ORFNames=GA29083;
OS Drosophila pseudoobscura pseudoobscura (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=46245;
RN [1] {ECO:0000312|EMBL:EDY70661.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MV2-25 / Tucson 14011-0121.94;
RX PubMed=15632085; DOI=10.1101/gr.3059305;
RA Richards S., Liu Y., Bettencourt B.R., Hradecky P., Letovsky S.,
RA Nielsen R., Thornton K., Hubisz M.J., Chen R., Meisel R.P., Couronne O.,
RA Hua S., Smith M.A., Zhang P., Liu J., Bussemaker H.J., van Batenburg M.F.,
RA Howells S.L., Scherer S.E., Sodergren E., Matthews B.B., Crosby M.A.,
RA Schroeder A.J., Ortiz-Barrientos D., Rives C.M., Metzker M.L., Muzny D.M.,
RA Scott G., Steffen D., Wheeler D.A., Worley K.C., Havlak P., Durbin K.J.,
RA Egan A., Gill R., Hume J., Morgan M.B., Miner G., Hamilton C., Huang Y.,
RA Waldron L., Verduzco D., Clerc-Blankenburg K.P., Dubchak I., Noor M.A.F.,
RA Anderson W., White K.P., Clark A.G., Schaeffer S.W., Gelbart W.M.,
RA Weinstock G.M., Gibbs R.A.;
RT "Comparative genome sequencing of Drosophila pseudoobscura: chromosomal,
RT gene, and cis-element evolution.";
RL Genome Res. 15:1-18(2005).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; 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 Evidence={ECO:0000250|UniProtKB:P28523};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:P28523};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. CaMK subfamily. {ECO:0000255}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CH379061; EDY70661.1; -; Genomic_DNA.
DR RefSeq; XP_015036868.1; XM_015181382.1.
DR RefSeq; XP_015036869.1; XM_015181383.1.
DR AlphaFoldDB; B5DK35; -.
DR SMR; B5DK35; -.
DR STRING; 7237.FBpp0288024; -.
DR EnsemblMetazoa; FBtr0368464; FBpp0331227; FBgn0250441.
DR EnsemblMetazoa; FBtr0376757; FBpp0337913; FBgn0250441.
DR GeneID; 6902745; -.
DR KEGG; dpo:Dpse_GA29083; -.
DR eggNOG; KOG0032; Eukaryota.
DR eggNOG; KOG3757; Eukaryota.
DR HOGENOM; CLU_000288_94_1_1; -.
DR InParanoid; B5DK35; -.
DR OMA; LMTECKV; -.
DR Proteomes; UP000001819; Chromosome 4.
DR Bgee; FBgn0250441; Expressed in female reproductive system and 2 other tissues.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
DR Gene3D; 3.10.20.230; -; 2.
DR InterPro; IPR003533; Doublecortin_dom.
DR InterPro; IPR036572; Doublecortin_dom_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF03607; DCX; 2.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00537; DCX; 2.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR SUPFAM; SSF89837; SSF89837; 2.
DR PROSITE; PS50309; DC; 2.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Repeat; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..755
FT /note="Serine/threonine-protein kinase GA29083"
FT /id="PRO_0000392569"
FT DOMAIN 157..243
FT /note="Doublecortin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00072"
FT DOMAIN 314..397
FT /note="Doublecortin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00072"
FT DOMAIN 484..742
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 18..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..54
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..84
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..128
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 605
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-
FT ProRule:PRU10027"
FT BINDING 490..498
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 513
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 755 AA; 82257 MW; A3C4A040A78EF806 CRC64;
MEVHNSLHCT APVLSSLQAS ASGSGTPKKT AASSAAAQNS KQLLDQLSQQ QKAQEEAETH
SRRDCDSPAS SNSEPEKDLD ELRDLNGSLT GSGSVGKSNG SLSGASSTTS APAGTSTPGS
ANTNGSASGA ASLSVVSATA HLKKRITSSR TPTRKAHRIK FYRNGDRFYP GITIPVSNER
YRSFESLYED LTRLLEENVK IPGAVRTIYD MVGKKITALE ELEDGQSYVC SCNNENFKKV
DYNTSSQPLA NLTLANNSRT SSHRLAKLQR PASPLKNGVL NSIAPVPVGG GAAANGSPLN
TSRFSERDSV VHPRIVTLIR NGTKPRRIIR LLLNKRNSPS FDHVLTAITQ VVRLDTGYVR
KVFTLSGVSV LQLSDFFGSD DVFFAYGTER VNTVEDFKLE SEEQRAINAI RKTLRTAGTA
CKGPKPKMPV KSKKAYPPGE LKAQAEAQLQ ASAAPANEDE EQAALLKSTG VEVAELPAAI
RDNYTLSQII GDGNFAIVLK IKDRQTGIPH ALKIIDKSKC KGKEHYIDAE VRVMKKLHHP
HIISLIMDVD QDTNMYLVLE YVSGGDLFDA ITQVTRFSES QSRIMIRHLG SAMSYLHSMG
IVHRDIKPEN LLVELDDFGN VVQLKLADFG LACEVTEPLY AVCGTPTYVA PEILLEVGYG
LKIDVWAAGI ILYILLCGFP PFVAPDNQQE PLFDAIISGV YEFPDPYWSD IGDGVRDLIA
NMLQSDPDVR FTSEDILDHY WTMGNEEIGC GDYSR
