ID A0A085N8A0_9BILA Unreviewed; 1374 AA.
AC A0A085N8A0;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN ORFNames=M514_22173 {ECO:0000313|EMBL:KFD65696.1};
OS Trichuris suis (pig whipworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichuridae; Trichuris.
OX NCBI_TaxID=68888 {ECO:0000313|EMBL:KFD65696.1};
RN [1] {ECO:0000313|EMBL:KFD65696.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DCEP-RM93F {ECO:0000313|EMBL:KFD65696.1};
RX PubMed=24929829; DOI=10.1038/ng.3012;
RA Jex A.R., Nejsum P., Schwarz E.M., Hu L., Young N.D., Hall R.S.,
RA Korhonen P.K., Liao S., Thamsborg S., Xia J., Xu P., Wang S.,
RA Scheerlinck J.P., Hofmann A., Sternberg P.W., Wang J., Gasser R.B.;
RT "Genome and transcriptome of the porcine whipworm Trichuris suis.";
RL Nat. Genet. 46:701-706(2014).
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=2.7.11.25;
CC Evidence={ECO:0000256|ARBA:ARBA00000478};
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=2.7.11.25; Evidence={ECO:0000256|ARBA:ARBA00000106};
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DR EMBL; KL367534; KFD65696.1; -; Genomic_DNA.
DR Proteomes; UP000030758; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0000165; P:MAPK cascade; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR046872; DRHyd-ASK.
DR InterPro; IPR046873; HisK-N-like.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR043969; MAP3K_PH.
DR InterPro; IPR025136; MAP3K_TRAF-bd.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR11584:SF369; APOPTOTIC SIGNAL-REGULATING KINASE 1, ISOFORM C; 1.
DR PANTHER; PTHR11584; SERINE/THREONINE PROTEIN KINASE; 1.
DR Pfam; PF19039; ASK_PH; 1.
DR Pfam; PF20309; DRHyd-ASK; 1.
DR Pfam; PF20302; HisK-N-like; 1.
DR Pfam; PF13281; MAP3K_TRAF_bd; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}.
FT DOMAIN 692..962
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1352..1374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1217..1244
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 721
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1374 AA; 155597 MW; 9222BFCE20EB5BF2 CRC64;
MRPLDTVTFC TCVSAKLPRW NHHNEGASLV FVRCWVMLAG QPGFRQGIVS VVFLSRTAVG
QSVWLQLVSD VSMAAATGRK LTPAGGSAVN VEASSANSEK FSRPLEIAVV IDLLVKDGLS
LRQSVWNEIE KLAETMFINA NLIQFEKLDF GETCSLDLFY NADVAVVDLS VSCQRTSLFY
HLGVRESMDQ KCNVVLYTME EVREPSISLL LKFPFINYKT LLYALKDGHL VAFDCNQVVP
NIVGTLQSGM SVSPQAGCTF CSKMKKFLKE VQIEASAHSR EKFLCDLRQA RQESQSSRLK
EILAKLRARL DDPDVLSVDT VVNMLLSYRD IQDYAAMVSL VEDIRSIPNN KIYESPAIQF
NYAFALNRRN IDDDRARALE LILDILKSQD NEVPDFLCLA GRIYKDRFSD SRFLDIEARD
QAICWYRKGF ETQPNEYAGI NLATLLVIAG HSFQTSSELQ QIAVILSGLL GRKGSLSNMQ
DYWDVATFFE ISVLAENYFN ACQAAQRMFI LKPPAWFLKS TIGNIGLIEK FRRSLQQYSR
ENQMEYRRFL FWMDFFVEST KADDLHCDLR FPVLSMEPSK AYTPSYVSVN KDDKTIFLWH
VTYSLPKSNF SQWIFPAESI RAVSAAKRDD RAVYLYVYLN SDDFMLFFPT DSHRHRFLDL
VDEITSNVDG TKLLGDYSES QTIDFEFELD ASGQRVVLGK GTFGAVYAGR DRTSQRTIAI
KEVQIKNHEE VQPLMEEIQL HSTLAHTNIV QYLGCEVSDD NKVFRIFMEQ VPGGSLSLLL
RNKWGPLIDS ENTMAYYAKQ ILEGLAYLHS QKIVHRDIKG DNVLVNTYSG LCKIVDFGTC
KRLAGLNPVT DTFTGLHWWS QLLCRTLQYM APEVIDHGQR GYGAPADVWS FGCTMIEMAT
GKPPFVELGS PQAAIFKVGM FKVHPPIPEK LSSCAKSFIS RCFVANPKQR PSAAVLLNDH
FFDQTQMKRK SKVDINFREN YRPPVRSASY INTASSVQKE QPVSASSSVQ SLNELTEIAT
PSEKLTANSG QDGQLSTRFF MMRKDYERRD TLSSIMLEFE DELVDLWLTS LKSDVQDYQC
SISKDVFKSL LGAMRSYVME KDRTSARNFV LQLKEHLDND ESTLSQLCFA LFVFQDVMHY
VLRQQKIKPH WMFSLDNLTQ SCSKCFIELL SPAVQSANGE QEADGGDSSS YASMEQAKSP
SVPVFSYEVF HSIGLLGSQV KRDMKEVKEE NQRLLEEVKS LCRICEDVRS KLTLKCRLPF
RRRSSSSAPC LQDCPTATII ADSTPEHSDA LVKWLRELNI DEETIDILKF ENYSLEDLLC
CVKSRKELVR VGIRAGVSCR LWKHIKEKRK QNGDNGLAEP LATESCCSEA GSDS
//
