DCLK_DROPE
ID DCLK_DROPE Reviewed; 755 AA.
AC B4GXC2;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Serine/threonine-protein kinase GL21140 {ECO:0000250|UniProtKB:Q7PLI7, ECO:0000312|EMBL:EDW27233.1};
DE EC=2.7.11.1;
DE AltName: Full=Doublecortin-like and CAM kinase-like protein;
GN ORFNames=GL21140;
OS Drosophila persimilis (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7234;
RN [1] {ECO:0000312|EMBL:EDW27233.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MSH-3 / Tucson 14011-0111.49;
RX PubMed=17994087; DOI=10.1038/nature06341;
RG Drosophila 12 genomes consortium;
RT "Evolution of genes and genomes on the Drosophila phylogeny.";
RL Nature 450:203-218(2007).
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}.
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DR EMBL; CH479195; EDW27233.1; -; Genomic_DNA.
DR RefSeq; XP_002023105.1; XM_002023069.1.
DR AlphaFoldDB; B4GXC2; -.
DR SMR; B4GXC2; -.
DR STRING; 7234.FBpp0185247; -.
DR EnsemblMetazoa; FBtr0186755; FBpp0185247; FBgn0158734.
DR GeneID; 6597935; -.
DR KEGG; dpe:6597935; -.
DR eggNOG; KOG0032; Eukaryota.
DR eggNOG; KOG3757; Eukaryota.
DR HOGENOM; CLU_000288_94_1_1; -.
DR OMA; LMTECKV; -.
DR PhylomeDB; B4GXC2; -.
DR Proteomes; UP000008744; Unassembled WGS sequence.
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 GL21140"
FT /id="PRO_0000392568"
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; 82227 MW; A4EE8C25E997D48E 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 PASPLKNGVP NSIAPVPVGG GAAANGSPLN
TSRFSERDSV VHPRIVTLIR NGTKPRRIIR LLLNKRNSPS FDHVLTAITQ VVRLDTGYVR
KVFTLSGVSV LQLSDFFGSD DVFFAYGTER VNTVDDFKLE 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
