ID H2UU72_TAKRU Unreviewed; 1437 AA.
AC H2UU72;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 3.
DT 27-MAR-2024, entry version 80.
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:ENSTRUP00000040496.3};
OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000040496.3, ECO:0000313|Proteomes:UP000005226};
RN [1] {ECO:0000313|Ensembl:ENSTRUP00000040496.3, ECO:0000313|Proteomes:UP000005226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21551351;
RA Kai W., Kikuchi K., Tohari S., Chew A.K., Tay A., Fujiwara A., Hosoya S.,
RA Suetake H., Naruse K., Brenner S., Suzuki Y., Venkatesh B.;
RT "Integration of the genetic map and genome assembly of fugu facilitates
RT insights into distinct features of genome evolution in teleosts and
RT mammals.";
RL Genome Biol. Evol. 3:424-442(2011).
RN [2] {ECO:0000313|Ensembl:ENSTRUP00000040496.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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 Ensembl; ENSTRUT00000040638.3; ENSTRUP00000040496.3; ENSTRUG00000015844.3.
DR eggNOG; KOG0032; Eukaryota.
DR GeneTree; ENSGT00940000153424; -.
DR HOGENOM; CLU_002849_2_0_1; -.
DR TreeFam; TF314166; -.
DR Proteomes; UP000005226; Chromosome 21.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0070887; P:cellular response to chemical stimulus; IEA:UniProt.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0048583; P:regulation of response to stimulus; IEA:UniProt.
DR GO; GO:0010033; P:response to organic substance; IEA:UniProt.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd08782; Death_DAPK1; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
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; 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; 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; PF12796; Ank_2; 2.
DR Pfam; PF00531; Death; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 10.
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; 8.
DR PROSITE; PS50017; DEATH_DOMAIN; 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 GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000005226};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 15..268
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REPEAT 371..403
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 404..436
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 437..469
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 470..502
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 503..535
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 536..568
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 569..601
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 602..634
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 674..945
FT /note="Roc"
FT /evidence="ECO:0000259|PROSITE:PS51424"
FT DOMAIN 1319..1401
FT /note="Death"
FT /evidence="ECO:0000259|PROSITE:PS50017"
FT REGION 1342..1362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1437 AA; 159913 MW; 9B0E7AB885B6AA53 CRC64;
MYVRVSLLFR DTPSAVSPLP LSSGQFAVVR RCRHRSTGVE YAAKFIKKRR SKSSRRGVSR
EDIEREVSIL KEIQHPNIIT LHEVFENKAE VILILELVAG GELFDFLAEK ESLSEEEATQ
FLKQILDGVF YLHSKQIAHF DLKPENIMLL NRSVPHPRIK IIDFGLAHKI DFSNDFKNIF
GTPEFVAPEV VNYEPLGLEA DMCLSGASPF LGDNKQETLA NVSAVDYTFD EEFFSNTSIL
AKDFIARLLI KDPKKRMTIQ DSLQHPWIKP KDTQQALSRK ESAVNMEKFK KFAARRKWKQ
SVRLISLCNR LSRSFLSRSN ISVARSDDTL DEEDSFVMKA IIHAINDDNV PGLTHLLGSL
NSYDVNQPNK HGTPPLLIAA GCGNIQIIEV LMRKGAEIQA GDKSGANAIY YAARHGHVET
LKFLHEKKCP LDIQDKSGET ALHVAARYGN VDVVSYLCSI RANPDLADRE QETPLHCAAW
HGYSTVARAL CQAGCHVNAK NREGESPLLT ASARGFVDIV ECLVEHRATL EASDKDGHTA
LHLAVRRCQV DVVRCLLRHH CHLDQQDRHG NTPLHIACKD GNLAIVMAIC SAKANLDLPN
KYGRTSLHLA ASNGSLEVVR HLCLAGVNID AVTNDGKTAE ELASVDHHDH IVSLLVRLKK
DNHKLSYIQQ LRPTQTIQPR IKLKLFGHSG AGKSTLLESL KCGILRSFFR RRRTRMTNTA
RHPNSPINSK PPVSVSISNL YPGCENVSVR SRSMMFEPSL TKGVLEVFSP VHSALSTADE
QATKAIDIQH ANIHSVGDFS VWEFSGNPVY HCSYDYFAAN DSTAIHLVLF SLEEPYETQL
SHVTYWLNLL KALTLPQDNI AFGGRIQQPL VVVLVATHAD LADIPRAFSG EFTYDKEKVL
LKEVRNRFGV DLQISEKLFV MDAGASNSKD VKLLRNHLQE LRSSIISKCS PMTQLTERLL
TTLPSWRKLS GPNQLTSWQQ FVSDVQEHIN PLVSQDHLRT LTMQLHSMGE INIMQSETVQ
DVVLLEPRWL CSGILGKLLS VEAPKAIHHY RGRYRLEEVQ ALVPESDVEE LLQILDAMDI
CARDASNPFM VDVPALIKTS GLHRSWTEED EEDEVLIYGG IRLVPAEHLT PFPCGLFHKL
QVNLCRWSHQ QKSEEEGGED FDGDIHLWTN GAKVSQAGVE AIILLVNHGQ GVEVQVRGHD
SERAKCYTLL DTICSITENL LTSTLPGLLT AKYYLSPQQL REHHAPIMIY QPKDFFRAQA
QRESSLTNTM GGYRESFSSI LSFGCAEVYQ QGTLGTDIHI SDVPLLARRK LCRMLDPPDA
MGKDWCLLAM NLGLTDLVAK HSSGTNGAAE PDSPQAAQQP SPTAALLQEW SSRADSTVGV
LMAKLRELGR RDAADFLLKA SPVFRVNAEA VGGAANGYPA ICNGGTSYNS ISSVVSR
//
