DCLK_DROSI
ID DCLK_DROSI Reviewed; 743 AA.
AC B4NSS9;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Serine/threonine-protein kinase GD17699 {ECO:0000250|UniProtKB:Q7PLI7, ECO:0000312|EMBL:EDX15261.1};
DE EC=2.7.11.1;
DE AltName: Full=Doublecortin-like and CAM kinase-like protein;
GN ORFNames=GD17699;
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;
RN [1] {ECO:0000312|EMBL:EDX15261.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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; CH982438; EDX15261.1; -; Genomic_DNA.
DR AlphaFoldDB; B4NSS9; -.
DR SMR; B4NSS9; -.
DR STRING; 7240.B4NSS9; -.
DR HOGENOM; CLU_000288_94_1_1; -.
DR OMA; LMTECKV; -.
DR PhylomeDB; B4NSS9; -.
DR Proteomes; UP000000304; 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; IPR017441; Protein_kinase_ATP_BS.
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; PS00107; PROTEIN_KINASE_ATP; 1.
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..743
FT /note="Serine/threonine-protein kinase GD17699"
FT /id="PRO_0000392571"
FT DOMAIN 154..240
FT /note="Doublecortin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00072"
FT DOMAIN 309..392
FT /note="Doublecortin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00072"
FT DOMAIN 473..731
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 54..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..69
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 594
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-
FT ProRule:PRU10027"
FT BINDING 479..487
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 502
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 743 AA; 82376 MW; 153777245D200F80 CRC64;
MELEKVKINS LHCNDAVLSS LQASPSATHP QSVPSKANAV TEASIIEKTN LQHNVQEDNS
YNRDCDSPVS SSSEPEKELD DLRYLHSSSL TNSVVVGKST GSLNGAYSIT SVTSKTKTLE
PNSASGSACL TIAPTADHIK KRIPSSRTPT RKALRIKFYR NGDRFYPGIT IPVSNERYRS
FERLFEDLTR LLEENVKIPG AVRTIYNMCG KKITSLDELE DGQSYVCSCN NENFKKVEYN
TGSQPLSNLT LTSSRSNSHR LDKCRPSSPL KNGLLAGSSP LPTCGGGTGN GSPHIASRSS
DRVTVVHPRI VTLIRSGTKP RRIMRLLLNK RNSPSFDHVL TAITQVVRLD TGYVRKVFTL
SGVSVVRLSD FFGSDDVFFA YGTERINTAE DFKLEAEEHR AINVIRKTMR TTGTTCKGPK
PKMPIKSKKV YPPVVDSEAF KAATTPEDDS HAALLTSTGM EINELPSNIR NTYTLGRIIG
DGNFAIVFKI KHRQTGHSYA LKIIDKNKCK GKEHYIDAEV RVMKKLNHPH IISLILSVDQ
NTNMYLVLEY VSGGDLFDAI TQVTRFSESQ SRIMIRHLGA AMTYLHSMGI VHRDIKPENL
LVKLDEHGHV LELKLADFGL ACEVNDLLYA VCGTPTYVAP EILLEVGYGL KIDVWAAGII
LYILLCGFPP FVAPDNQQEP LFDAIISGIY EFPDPYWSDI GDGVRDLIAN MLQADPDVRF
TSEDILDHPW TIGNQNECTT YKR
