DCLK_DROYA
ID DCLK_DROYA Reviewed; 750 AA.
AC B4IT27;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-MAR-2010, sequence version 2.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Serine/threonine-protein kinase GE16371 {ECO:0000250|UniProtKB:Q7PLI7, ECO:0000312|EMBL:EDW99417.1};
DE EC=2.7.11.1;
DE AltName: Full=Doublecortin-like and CAM kinase-like protein;
GN ORFNames=GE16371;
OS Drosophila yakuba (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7245;
RN [1] {ECO:0000312|EMBL:EDW99417.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tai18E2 / Tucson 14021-0261.01 {ECO:0000312|EMBL:EDW99417.1};
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 -!- SEQUENCE CAUTION:
CC Sequence=EDW99417.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; CH891639; EDW99417.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_002086139.2; XM_002086103.2.
DR RefSeq; XP_015045238.1; XM_015189752.1.
DR RefSeq; XP_015045239.1; XM_015189753.1.
DR AlphaFoldDB; B4IT27; -.
DR SMR; B4IT27; -.
DR STRING; 7245.FBpp0261381; -.
DR EnsemblMetazoa; FBtr0399882; FBpp0358887; FBgn0233900.
DR EnsemblMetazoa; FBtr0402347; FBpp0361201; FBgn0233900.
DR EnsemblMetazoa; FBtr0404589; FBpp0363290; FBgn0233900.
DR GeneID; 6539240; -.
DR eggNOG; KOG0032; Eukaryota.
DR eggNOG; KOG3757; Eukaryota.
DR OrthoDB; 330091at2759; -.
DR Proteomes; UP000002282; 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..750
FT /note="Serine/threonine-protein kinase GE16371"
FT /id="PRO_0000392572"
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 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 750 AA; 83076 MW; 38010C123262CB5D CRC64;
MELDKVKTHS LHCNAAVLSS LQAPTSATSP QSFTSKANAV AEAAFIENSN QQQNVQKDLN
SHNRDCDSPV SSTSELEKEF DDLRKLHTSS LTNSVVVGKS TGSLNGDYSI TSATSKTKTL
ESVVTINSAT GSACLTIAST ADHIKKRIPN SRTPTRKALR IKFYRNGDRF YPGVTIPVSN
ERYRSFERLF EDLTRLLEEN VKIPGAVRTI YNMCGKKITS LDELEDGQSY VCSCNNENFK
KVEYNPGSQP LSNLTLTNNS RPYNQRLAKH RPASPLKNGL LVGSSPLAVC GGGTGNGSPL
IASKSSDRVT VVHPRIVTLI RSGTKPRRIM RLLLNKRNSP SFDHVLTAIT QVVRLDTGYV
RKVFTLSGIS VVQLSDFFES DDVFFAYGTE RINTAEDFKL EPEELKAINV IRKTMRTAGT
TCKGPKPKMP IKSKKVYPPS VNSEAFKAAT APEDDRHATL LTSTGIEINE LPSNIRSTYT
LGKIIGDGNF AIVFKIKHRQ TGDSYALKII DKNKCKGKEH YIDAEVRVMK KLNHPHIISL
ILSVDQNTNM YLVLEYVSGG DLFDAITQVT RFAESQSRIM IRHLGAAMTY LHSMGIVHRD
IKPENLLVKL DEHGNVLELK LADFGLACEV NDLLYAVCGT PTYVAPEILL EVGYGLKIDV
WAAGIILYIL LCGFPPFVAP DNQQEPLFDA IISGIYEFPD PYWSDIGDGV RDLIANMLQS
DPDVRFTSED ILDHYWTIGN EGNECTTYKR
