ID A0A158Q9R0_ENTVE Unreviewed; 1453 AA.
AC A0A158Q9R0;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN ORFNames=EVEC_LOCUS2527 {ECO:0000313|EMBL:VDD87384.1};
OS Enterobius vermicularis (Human pinworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Oxyuridomorpha; Oxyuroidea; Oxyuridae; Enterobius.
OX NCBI_TaxID=51028 {ECO:0000313|Proteomes:UP000038041, ECO:0000313|WBParaSite:EVEC_0000281901-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:EVEC_0000281901-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (APR-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDD87384.1, ECO:0000313|Proteomes:UP000274131}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (OCT-2018) 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};
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DR EMBL; UXUI01007397; VDD87384.1; -; Genomic_DNA.
DR STRING; 51028.A0A158Q9R0; -.
DR WBParaSite; EVEC_0000281901-mRNA-1; EVEC_0000281901-mRNA-1; EVEC_0000281901.
DR Proteomes; UP000038041; Unplaced.
DR Proteomes; UP000274131; 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; 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; 1.10.510.10; 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; PF00023; Ank; 2.
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; 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; 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}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000274131};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 25..286
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REPEAT 398..430
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 431..463
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 464..496
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 530..562
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 563..595
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 596..628
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 656..688
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 726..977
FT /note="Roc"
FT /evidence="ECO:0000259|PROSITE:PS51424"
FT DOMAIN 1332..1413
FT /note="Death"
FT /evidence="ECO:0000259|PROSITE:PS50017"
FT REGION 770..813
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 770..797
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 58
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1453 AA; 161744 MW; 17EEB6C0614633E2 CRC64;
MRQVSGPSNS GASMHFNEEP FDQRFEIAEE LGNGQFACVR RVIDRNSGIQ YAAKFIKKRR
YATSRRGVTR ANIEREVDVL RTVGGHDNTV QLFEVYESLT DVILVLELVP GGELFDHVSS
KECLDEPEAA AFIRQILNGV KHLHERHIAH LDIKPENIML QKKGETKVKL IDFGLSRRIL
PGTVVKDMIG TPEFVAPEVV NYEPLSTATD MWAVGVVAFI LLSGGSPFLG DTREETFVNI
SAVNYHFNER YFDHISANAK DFISRLFVRD VRKRATVDDC LRHPWIRIVG FSDVDPEESG
PWNIKELAGL SLAETRSYKI RLKWKKAIDV IIACNKLTSK TRLALRKASE NGRTIDSRFD
PEELILSAVL IACEEGNLAG LDQLLTLHRF NLNVANRLGE TAMHVSAGAG QYEVVRYLHL
KGASSGSVDR RGDTPLFWAA RHGHAQVVRY ILEEKADVNF VNKSKETALH VATRYAQLET
ALLLLEYGAD VSLQDEQGET ALHVASWHGY GKLLAALCRY SPRFDAKNQD GETALHCAAA
RGHTECVQSL LEAGAPVDDL DQDGQTALHL ALRRSHIDIA LLLITKGCKL DLQDENGETP
LHIASRLGLL SVVQTLCHLG AAIDIPNTVR LLPSFWQGNV RGIRTPTNSQ LPIRFGSLTA
LHIAAKEGFI EIVRCLCFFG ANVLKKNKDG LTAEIIALAQ EHTNIGTLLA KMKTAKELYV
EQLCSLETPL RRIKLKVFGH SGVGKSRLIC ALQSSSVIGT LIGAVSRRFS DNPSPSSSTA
SSSKDEGLSS TDESVESNNN HRTAKRRGPP HLQYTRGIDV QNVTLQGCGE FSVWEFGGYK
PYHMAYDHFV GNTDCIHMVV FRSTDPTEVQ YKQVLYWMNF LKGRVTPSEP IGHCGIVSRR
SKVVIIGTHA SASLFPQRGV DGEYISSDGE AMLKTIKLRF ETHFDIHDQL ILLDSTHTSC
PGMKSLRNYL SKAREGILSK LQKPMGLVDA CMQCLVTLRK QYCHFPVLTW PNFTEILRDD
INPLAGDNHC RQLIQQLQLI GEVVYLRDET SELDYVVLSP EWLGTHIIGY LLSAEFLSRC
RANGCYSVDD FSQIYPEIAE PADLIRILDT LQFCAPLDGN GEADCEFPAF DVLEVPRDIW
LRDRPSYVYG GVRVLPMRGM ERSLQSTFPR IQVALRRSMR DFQDPMDADL SQWLDCSKMS
SGQMEALIRL HRDAVEVQVR GPCELATSCF YFLEDVTNLV EQTAQEVAPG ISLERHFLSP
KHLREHHPNP AVYAPETIMA MQQAESLTIK NNQEGEEYFT DVVCFGSRDV AAILTLGIDV
SVAQLQLASR CELASLLDPA DAMGRDWSIL AVKLSLMDQL PEVDSTGQSL SRTDQLLAEW
ALQCPETATV GRLCSVLEEL GRQDARDALY RTVPLYLFAP LDEQPSANLI DCRDSGVVSS
TQSTTDPSQS SPS
//
