DCLK_DROER
ID DCLK_DROER Reviewed; 745 AA.
AC B3NKK1;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Serine/threonine-protein kinase GG21441 {ECO:0000250|UniProtKB:Q7PLI7, ECO:0000312|EMBL:EDV54305.1};
DE EC=2.7.11.1;
DE AltName: Full=Doublecortin-like and CAM kinase-like protein;
GN ORFNames=GG21441;
OS Drosophila erecta (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7220;
RN [1] {ECO:0000312|EMBL:EDV54305.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 14021-0224.01 {ECO:0000312|EMBL:EDV54305.1};
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; CH954179; EDV54305.1; -; Genomic_DNA.
DR RefSeq; XP_001973905.1; XM_001973869.2.
DR AlphaFoldDB; B3NKK1; -.
DR SMR; B3NKK1; -.
DR STRING; 7220.FBpp0139987; -.
DR EnsemblMetazoa; FBtr0141495; FBpp0139987; FBgn0113620.
DR GeneID; 6548606; -.
DR KEGG; der:6548606; -.
DR eggNOG; KOG0032; Eukaryota.
DR eggNOG; KOG3757; Eukaryota.
DR HOGENOM; CLU_000288_94_1_1; -.
DR OMA; LMTECKV; -.
DR OrthoDB; 330091at2759; -.
DR PhylomeDB; B3NKK1; -.
DR Proteomes; UP000008711; 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; Repeat;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..745
FT /note="Serine/threonine-protein kinase GG21441"
FT /id="PRO_0000392566"
FT DOMAIN 159..245
FT /note="Doublecortin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00072"
FT DOMAIN 315..398
FT /note="Doublecortin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00072"
FT DOMAIN 479..737
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 49..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..73
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 600
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-
FT ProRule:PRU10027"
FT BINDING 485..493
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 508
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 745 AA; 82753 MW; 53150365F0336CFB CRC64;
MEFDEIKKHS LNCNADVLSS LQASAPASSP HTVTLKVNAV AEATITEKRN QQQNVQKDFD
SHNRDCDSPV SSTSELEKEF DDLRNLHTSS LTNSVVLGKS IGSLNGDYSV TSASSRTKTL
ENVVTIDSAS GSTCLAIASP VDHIKKRIPN SRTPTRKALR IKFYRNGDRF YPGITIPVSN
ERYRSFERLY EDLTRLLEEN VKIPGAVRTI YNMCGKKITS LDELEDGQSY VCSCNNENFK
KVEYNTGSQP LSNLTLTNNS RSNNQRLAKC RPASPLKNGL LTGISPLPAS GGGTGNGSPL
IASRLSDRVS VVHPRIVTLI RSGTKPRRIM RLLLNKRNSP SFDHVLTAIT QVVRLDTGYV
RKVFTLSGIS VVQLSDFFGS DDVFFAYGTE RINYAEDFKL EAEEYRAINV IRKTMRTAGT
TCKGPKPKMP IKSKKVYPPL VDSEVLKAAT SPEDDSHATL LTSTGIEINE LPLNIRNTYT
LGRIIGDGNF AIVFKIKHRQ TGDSYALKII DKNKCKGKEH YIDAEVRVMK KLNHPHIISL
ILSVDQNTNM YLVLEYVSGG DLFDAITQVT RFSESQSRIM IRHLGAAMTY LHSMGIVHRD
IKPENLLVKL DEHGNVLELK LADFGLACEV NDLLYAVCGT PTYVAPEILL EVGYGLKIDV
WAAGIILYIL LCGFPPFVAP DNQQEPLFDA IISGIYEFPD PYWSDIGDGV RDLIANMLQS
DPDVRFTSED ILDHYWTIGN KGNDL
