ID U3JLN1_FICAL Unreviewed; 1430 AA.
AC U3JLN1;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN Name=DAPK1 {ECO:0000313|Ensembl:ENSFALP00000003685.1};
OS Ficedula albicollis (Collared flycatcher) (Muscicapa albicollis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Muscicapidae; Ficedula.
OX NCBI_TaxID=59894 {ECO:0000313|Ensembl:ENSFALP00000003685.1, ECO:0000313|Proteomes:UP000016665};
RN [1] {ECO:0000313|Ensembl:ENSFALP00000003685.1, ECO:0000313|Proteomes:UP000016665}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23103876; DOI=10.1038/nature11584;
RA Ellegren H., Smeds L., Burri R., Olason P.I., Backstrom N., Kawakami T.,
RA Kunstner A., Makinen H., Nadachowska-Brzyska K., Qvarnstrom A., Uebbing S.,
RA Wolf J.B.;
RT "The genomic landscape of species divergence in Ficedula flycatchers.";
RL Nature 491:756-760(2012).
RN [2] {ECO:0000313|Ensembl:ENSFALP00000003685.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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:0000256|ARBA:ARBA00001433};
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:0000256|ARBA:ARBA00000775};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
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DR RefSeq; XP_005061001.1; XM_005060944.1.
DR SMR; U3JLN1; -.
DR STRING; 59894.ENSFALP00000003685; -.
DR Ensembl; ENSFALT00000003699.2; ENSFALP00000003685.1; ENSFALG00000003534.2.
DR GeneID; 101814976; -.
DR KEGG; fab:101814976; -.
DR CTD; 1612; -.
DR eggNOG; KOG0032; Eukaryota.
DR GeneTree; ENSGT00940000153424; -.
DR HOGENOM; CLU_002849_2_0_1; -.
DR OMA; RSMHDFQ; -.
DR OrthoDB; 4580305at2759; -.
DR Proteomes; UP000016665; Chromosome Z.
DR GO; GO:0015629; C:actin cytoskeleton; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:1990722; C:DAPK1-calmodulin complex; IEA:Ensembl.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0014069; C:postsynaptic density; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005516; F:calmodulin binding; IEA:Ensembl.
DR GO; GO:0004683; F:calmodulin-dependent protein kinase activity; IEA:Ensembl.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0017075; F:syntaxin-1 binding; IEA:Ensembl.
DR GO; GO:0071447; P:cellular response to hydroperoxide; IEA:Ensembl.
DR GO; GO:0071346; P:cellular response to type II interferon; IEA:Ensembl.
DR GO; GO:0002357; P:defense response to tumor cell; IEA:Ensembl.
DR GO; GO:0008625; P:extrinsic apoptotic signaling pathway via death domain receptors; IEA:Ensembl.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:Ensembl.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:0017148; P:negative regulation of translation; IEA:Ensembl.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:1904094; P:positive regulation of autophagic cell death; IEA:Ensembl.
DR GO; GO:0010508; P:positive regulation of autophagy; IEA:Ensembl.
DR GO; GO:0002834; P:regulation of response to tumor cell; IEA:Ensembl.
DR CDD; cd08782; Death_DAPK1; 1.
DR CDD; cd14194; STKc_DAPK1; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 3.
DR Gene3D; 1.10.533.10; Death Domain, Fas; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 1.20.5.460; Single helix bin; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR020676; DAPK1_cat.
DR InterPro; IPR011029; DEATH-like_dom_sf.
DR InterPro; IPR000488; Death_domain.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR020859; ROC_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24342:SF17; DEATH-ASSOCIATED PROTEIN KINASE 1; 1.
DR PANTHER; PTHR24342; SERINE/THREONINE-PROTEIN KINASE 17; 1.
DR Pfam; PF00023; Ank; 1.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF13637; Ank_4; 1.
DR Pfam; PF00531; Death; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 9.
DR SMART; SM00005; DEATH; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF47986; DEATH domain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50297; ANK_REP_REGION; 7.
DR PROSITE; PS50088; ANK_REPEAT; 7.
DR PROSITE; PS50017; DEATH_DOMAIN; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS51424; ROC; 1.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000016665};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 13..275
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REPEAT 378..410
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 444..476
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 477..509
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 510..542
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 543..575
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 576..608
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 609..641
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 681..955
FT /note="Roc"
FT /evidence="ECO:0000259|PROSITE:PS51424"
FT DOMAIN 1312..1396
FT /note="Death"
FT /evidence="ECO:0000259|PROSITE:PS50017"
FT BINDING 46
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1430 AA; 160316 MW; 01C7A1CF9E7BEDCF CRC64;
MTVFRQENLE EHYETGEDLG SGQFAVVKKC REKSTGQQFA AKFIKKRRTK SSRRGVSRED
IEREVGILKE IRHPNVITLH DVYENKTDVI LILELVAGGE LFDFLAEKES LTEEEATEFL
KQILNGVQYL HSLQIAHFDL KPENIMLLDR NVPKPRIKII DFGLAHKIDF GNEFKNIFGT
PEFVAPEIVN YEPLGLEADM WSIGVITYIL LSGASPFLGE TKQETLANVS AVNYEFEEEF
FSNTSALAKD FIRRLLVKDP KKRMTIQDSL LHPWIKPKDT QQALSRKASA VNMEKFKKFA
ARRKWKQSVR LISLCQRLSR SFLSRSSMSV ARSDDTLDEE DSFVMKAIIH AINDDNVPGL
QHLLGSLTNY DVNQPNKHGT PPLLIAAGCG NIQMLQLLLK RGSRIDVQDK AGSNAIYWAS
RHGHVETLKF LNDNKCPLDV KDKSGETALH VAARYGHVDV VQFLCSIGSN PNFQDKEEET
PLHCAAWHGY YSVAKALCEA GCNVDVKNKE GETPLLTASA RGYHDIVECL AEHRADLHAT
DKDGHIALHL AVRRCQIEVV KTLISQGCFV DFQDRHGNTP LHVACKDGNV PIVMALCEAG
CSLDVTNKYG RTPLHLAANN GILDVVRFLC LTGANVEALT SDGKTAEDLA RAEQHEHVAS
LLTRLKKDTH RVIFIQQLRH TQNPQPRIKL KLFGYSGSGK TTLVESLKCG LIRSFFRRRR
PRLSSTNSSR FPPSPLSSKP SVSVSITNLY PGCENVSVRS RSMMFEPGLT KGVLETFVSP
AHHSHFSSDD QSTKAVDIQN AFLHGVGDFS IWEFSGNPVY FCCYDYFAAN DHTAIHIVLF
SLEEPYEIQL NQVTFWLNFL KSLVPVEEPI AFGGKLKSPL RVVLVGTHAD IVNLPRPVGG
EFWYDKDISL LKEIRNRFGN DLQISEKLFV LDAGASGSKD MKLLRNHLQE IRSQIISTCP
PMTHLCEKII STLPSWRKIN GPNQLMSLQQ FVYDVQEHLN PLASENDLRH IAQQLHSIGE
INIMQSETVQ DVVLLDPRWL CSNVLGRILS VENPKALHHY RGRYTIEDIQ RLVTDSDVEE
LIQVLDAMDI CARDLSSGAM VDIPALIKTD NLHRSWTDEE DEVLIYGGVR IVPVEHLTPF
PCGIFHKVQV NLCRWIHQQS TEGDADIRLW VNGSKIMNRG AELLVLLVNH GQGIEVQVRG
LETEKIKCCL LLDSVCSTID NLIATTLPGL LTGKHYLSPQ QLREHHEPVM VYQPRDFFRA
QSQKETSLTN TMGGYKESFS SILCFGCLDV YSQGSLGMDI HVSDLNLLTR RKLSRLLDPP
DPMGKDWCLL AMNLGLPDLV AKYNTNNGTQ NCFLSSPVHA LLQEWSNASD STVGILMSKL
RELGRRDAAD FLLKASSVFK INLDANGQEA YASSCNSGTS YNSISSVVSR
//
