ID A0A0V0VXN0_9BILA Unreviewed; 1459 AA.
AC A0A0V0VXN0;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
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=dapk-1 {ECO:0000313|EMBL:KRX68077.1};
GN ORFNames=T09_3597 {ECO:0000313|EMBL:KRX68077.1};
OS Trichinella sp. T9.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=181606 {ECO:0000313|EMBL:KRX68077.1, ECO:0000313|Proteomes:UP000054681};
RN [1] {ECO:0000313|EMBL:KRX68077.1, ECO:0000313|Proteomes:UP000054681}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS409 {ECO:0000313|EMBL:KRX68077.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRX68077.1}.
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DR EMBL; JYDN01000003; KRX68077.1; -; Genomic_DNA.
DR STRING; 181606.A0A0V0VXN0; -.
DR Proteomes; UP000054681; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; 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:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd08782; Death_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; 1.10.510.10; 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; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR020859; ROC_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24342:SF14; DEATH-ASSOCIATED PROTEIN KINASE DAPK-1; 1.
DR PANTHER; PTHR24342; SERINE/THREONINE-PROTEIN KINASE 17; 1.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF13637; Ank_4; 1.
DR Pfam; PF00531; Death; 1.
DR Pfam; PF00069; Pkinase; 1.
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; 5.
DR PROSITE; PS50088; ANK_REPEAT; 6.
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};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KRX68077.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000054681};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 12..296
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REPEAT 412..444
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 445..468
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 511..543
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 544..576
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 632..664
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 665..697
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 738..973
FT /note="Roc"
FT /evidence="ECO:0000259|PROSITE:PS51424"
FT DOMAIN 1342..1415
FT /note="Death"
FT /evidence="ECO:0000259|PROSITE:PS50017"
FT BINDING 45
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1459 AA; 162533 MW; 1E24550E762ABBCE CRC64;
MLVPDASFEQ LYIVHEELGS GQFAVVKRCE EKATGCQFAG KFIKKRLFNS SQRGAKRSDI
QREIDVLREI GGHPNVISLH QVFETELEII LILELVAGGE LFEHLSKKEC LEEAEASAFV
RQILLGLDHI HSKHIAHLDL KPENVMLKAA NSTCVQLIDF GLSRRIPPDT CVKKLLGTEE
FVGKDLIVEI SHFISSFKFD YFHLSAPETI NYDGLTLAAD MWALGVVTYI LLTGSSPFLG
SSQIETFRNI TAVRYQFDGE YFARTSTLAK DFIRRLLVRD PRQRLTAKQC LKHPWIEPQE
AEHVALLRQS MVNTRQTRTL LARRRWKIAG RIVLGCVRLV RSYCYQTVQT ATLHSAMLAD
NNSPTKNTAY LNSENLIEKA VMCACEMGNL IDLVNICSVA NINFNDISNN ELGALPTHVA
AVAGQLDILK FLESRGCDFS LPDKRGDNPL HLAAQNGHIK IVNYLISRVD VGATNNFKEN
ALHIAVRYGF LDIAGSLVMS GKVDLNAQDK HGETALHIAC WHGYTLIASL LCNCKPDLGI
KNKDGETPLI CAAVRGNLDC VFLLKSAGAD LEQRDKVEIL SPKGNVHFCR ASCVLVFQDM
QTALHLSIRR QHSDIALPLL ESMSNFHLSD KDGNTPLHVA CKEGLTDVVQ RLCQKGCQID
SVNEAGQTPL HIACKEGHLE IVKILCLCEC NVHLKNKDGL TGEMIAAARN HHTICETLKK
VKQDVVLQSY IKQFIPCDGQ PLRRIKLKVF GHSGVGKTKL IDSLRQFGLL DNFLRRFSES
NASVEDDLLK NNKPLSSRRP VDQPSHPGYT RGIEVHNIAI ASGIEFSTWE FSGYSPYCAV
YDRFIGNGDC IHVVVFNVTD PTEVQYRGVI FWMNFIKSCF SPDSTIGPMG VSNNRPIVVL
VATHVDQVEQ PISLSADGEW TSSDADALLS TIKLRFCTDF EIHDSIIVLD ANAPNCVGMK
TLRAVLTHHR KRIVELLPNG CGLLEACVNL LGQLRRTFAT FPALRWSEFF RHLQDNANPL
ASEFHCRVIV ELLQLLGEVV YVRCSPTEQG GDWIVINPNW LCQAIIGRLL SAEFLQTCQR
DGCYTADEML LLFPQLLPNV TEMMRLLDAI GLGTVCEFED DVTFEFPCMN FEQCPPNYWD
PSPKRLVYGG LRFLPRRGMD HLMRASFLRV QKHLRHCSQF FPNHLKLELS QWHGGCKLTK
NSIEAVVVNF GKDQGIELRV RGPREFDVEC FCFFDDLISL IEQTVAEAAP GLLLERHFLS
ARDLAQHNSV IQTYPPGQIF AMQLAEGVLL SDSCGVEEPF LDVVCFGSKS IALSLTLGID
MKIISVPTGA RRELASLLDP MDTMGRDWSI LAAKLGLGPW LAEIESACEP GVSKTDRVLG
EWFARRPSDA TVGALLRCLK EMGRDDAIDL LCRSAPLYAF SPTNVNLQTF ATDSGLGSNN
SRTAFDTPTS LSYANLAAH
//
