ID DCLK_DROSE Reviewed; 744 AA.
AC B4IMC3;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE RecName: Full=Serine/threonine-protein kinase GM11705 {ECO:0000250|UniProtKB:Q7PLI7, ECO:0000312|EMBL:EDW45601.1};
DE EC=2.7.11.1;
DE AltName: Full=Doublecortin-like and CAM kinase-like protein;
GN ORFNames=GM11705;
OS Drosophila sechellia (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7238;
RN [1] {ECO:0000312|EMBL:EDW45601.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Rob3c / Tucson 14021-0248.25 {ECO:0000312|EMBL:EDW45601.1};
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}.
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; CH480967; EDW45601.1; -; Genomic_DNA.
DR RefSeq; XP_002044883.1; XM_002044847.1.
DR AlphaFoldDB; B4IMC3; -.
DR SMR; B4IMC3; -.
DR STRING; 7238.B4IMC3; -.
DR EnsemblMetazoa; FBtr0194690; FBpp0193182; FBgn0166648.
DR HOGENOM; CLU_000288_94_1_1; -.
DR OMA; LMTECKV; -.
DR OrthoDB; 2956627at2759; -.
DR PhylomeDB; B4IMC3; -.
DR Proteomes; UP000001292; 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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd16109; DCX1; 1.
DR Gene3D; 3.10.20.230; Doublecortin domain; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
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 PANTHER; PTHR24347:SF446; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR24347; SERINE/THREONINE-PROTEIN KINASE; 1.
DR Pfam; PF03607; DCX; 2.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00537; DCX; 2.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF89837; Doublecortin (DC); 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
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..744
FT /note="Serine/threonine-protein kinase GM11705"
FT /id="PRO_0000392570"
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 17..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 744 AA; 82562 MW; DEA9B5B1FF3482C1 CRC64;
MELEKVKINS LHCNDAVLSS HQPSPSATHP QSVPSKANAV TEASIIEKTN LQHNVQEDNS
YNRDCDSPVS SSSEPEKELD DLRYLHSSSL TNSVVVGKST GSLNGAYSIT SVTSKTKTLE
PNSASGSACL TIAPTADHIK KRIPSSRTPT RKALRIKFYR NGDRFYPGIT IPVSNERYRS
FERLFEDLTR LLEENVKIPG AVRTIYNMCG KKITSLDELE DGQSYVCSCN NENFKKVEYN
TGSQPLSNLT LTNSRSNSHR LAKCRPSSPL KNGLLAGSNP LPTCGGGTGN GSPHIASRSS
DRVTVVHPRI VTLIRSGTKP RRIMRLLLNK RNSPSFDHVL TAITQVVRLD TGYVRKVFTL
SGVSVVRLSD FFGSDDVFFA YGTERINTAE DFKLEAEEHR AINVIRKTMR TTGTTCKGPK
PKMPIKSKKV YPPVVDSEAF KAATTPEDDR 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 TIGNQGNECT TYKR
//
