ID A0A0N4ZV04_PARTI Unreviewed; 697 AA.
AC A0A0N4ZV04;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Protein kinase domain-containing protein {ECO:0000313|WBParaSite:PTRK_0001241500.1};
OS Parastrongyloides trichosuri (Possum-specific nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC Parastrongyloides.
OX NCBI_TaxID=131310 {ECO:0000313|Proteomes:UP000038045, ECO:0000313|WBParaSite:PTRK_0001241500.1};
RN [1] {ECO:0000313|WBParaSite:PTRK_0001241500.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
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DR AlphaFoldDB; A0A0N4ZV04; -.
DR STRING; 131310.A0A0N4ZV04; -.
DR WBParaSite; PTRK_0001241500.1; PTRK_0001241500.1; PTRK_0001241500.
DR Proteomes; UP000038045; Unplaced.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; IEA:UniProt.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR PANTHER; PTHR23257:SF780; AT08303P; 1.
DR PANTHER; PTHR23257; SERINE-THREONINE PROTEIN KINASE; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SMART; SM00109; C1; 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 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; PS00109; PROTEIN_KINASE_TYR; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 111..162
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 410..687
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 42..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 188..245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 281..300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..73
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..245
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 436
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 697 AA; 78484 MW; F684FC082109980E CRC64;
MTINNPRFSN NELLKTYQDA SKKGAYLRNT SSLHAIAETI ETANQSSDTT SSLTVSNPSK
TLPISRSTHF QFPNPPPDSI PNRPSPFSPI SKTTNAKPSQ GTFNSTPHSI PHVWVSKRLP
TICSDICIGC NKTLGFVSFW EKCKSCKKKV HSDCKKRIGN TCGLTPEFFK AVFKELYMAR
GQEIWDPYRT SGGESSSSTN STAPSTPAPN LIHSVITKQE QGSSSMTSSI NTTSEHFTFS
ESNNTASHSQ IFPRSQMVDS NTKNNNCYDV PSIILTDTNV LSESPNKTGP SASDSSICTT
SSNNESFLTT DQVNTLVKKE VPVITTTSTT LTGTNGTNDS DKTLKNVTFE DVSGLDGLNF
GGDENSDRQG IYYRLNFKTA SMREKNQKKG KKKYENIPED SETNINHCAI EVLELIGYGR
FGEVRRGHYF GDVAIKLLNM DHVPEAKQYE TFLMDTDSFV KARHENIILF LGYTYEKGNL
GIVMNDCKGK TLYQLIHESL PNESLEFSQI INFSLQICQG MTYLHTKGIL HKDLRTKNIF
IEKNNRIVIT DFGIFNMARL RHPPRKNGFY VSENWLCYLA PELIRAITPS AKPLRFTEKS
DVYSFGTCCF EMFFGKFPFS GYSWEVKMFF IEQGMKAPFC GNEVSREMKN ILMNCWSYNP
RNRPAFEDIF GNFGKLPKKK VMRSPSFPIQ RSYESFF
//