ID W2ILJ7_PHYPR Unreviewed; 1774 AA.
AC W2ILJ7;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE SubName: Full=TKL protein kinase {ECO:0000313|EMBL:ETL34243.1};
GN ORFNames=L916_13501 {ECO:0000313|EMBL:ETL34243.1};
OS Phytophthora parasitica (Potato buckeye rot agent).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=4792 {ECO:0000313|EMBL:ETL34243.1};
RN [1] {ECO:0000313|EMBL:ETL34243.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CJ05E6 {ECO:0000313|EMBL:ETL34243.1};
RG The Broad Institute Genomics Platform;
RA Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA Machado M., Johnson C.S., Arredondo F., Hong C., Coffey M., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Phytophthora parasitica CJ05E6.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KI674376; ETL34243.1; -; Genomic_DNA.
DR EnsemblProtists; ETL34243; ETL34243; L916_13501.
DR VEuPathDB; FungiDB:PPTG_14170; -.
DR VEuPathDB; FungiDB:PPTG_14171; -.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0030553; F:cGMP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00038; CAP_ED; 3.
DR CDD; cd13999; STKc_MAP3K-like; 1.
DR Gene3D; 2.60.120.10; Jelly Rolls; 4.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR018488; cNMP-bd_CS.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR018490; cNMP-bd_dom_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR44329; SERINE/THREONINE-PROTEIN KINASE TNNI3K-RELATED; 1.
DR PANTHER; PTHR44329:SF214; ZINC FINGER CONTAINING PROTEIN KINASE-RELATED; 1.
DR Pfam; PF00027; cNMP_binding; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SMART; SM00100; cNMP; 3.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF51206; cAMP-binding domain-like; 4.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00889; CNMP_BINDING_2; 1.
DR PROSITE; PS50042; CNMP_BINDING_3; 3.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW cGMP {ECO:0000256|ARBA:ARBA00022535};
KW cGMP-binding {ECO:0000256|ARBA:ARBA00022992};
KW Kinase {ECO:0000313|EMBL:ETL34243.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022992};
KW Transferase {ECO:0000313|EMBL:ETL34243.1}.
FT DOMAIN 450..716
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 759..894
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 911..1036
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 1198..1291
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT REGION 1420..1450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1579..1637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1712..1774
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1432..1447
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1583..1600
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1616..1637
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1739..1755
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1774 AA; 195216 MW; 2D3497EE9C84AEF1 CRC64;
MVPVRRRGAF FLLSRYRRRR RVPVCTALCL VCVLLLWGDC QAAGDLVGRL YDLETSGSSA
TKLSLSSSAL PSAVAARLSS YSLTWSELSG LMQRALLWDS GFVFASPVSS SSSSNEADDV
KLVQIYTSCS QGMGDLLPGL AEVRTLQSTG NSSNCDVQDC GIIGHFLPTN CPVESVIPLT
RCAVHASDMD GQNQFTGVFW AEDGRSNTVP EPVLRRHTPV DTEPSEALFA VHLSETSFTG
TESCQPHTNF ILPCRGVADD VVITSSSGSV SFTANGSGFT EVDLCPASHG AAMNAWLELQ
STPSPETFST TAIVLLSVAM LVCIGLGASV WWLSRSRAWL QDAYDRVILE GSYDDGCWSP
TSHLLGGPLA PSLAVAGATD EERLTPMEVF FGARPRSRRS PGIHGTSALV ATTRAEITLS
NDQLCRKSSI LRAFVSDPAI VTKRISFAQL HFLRLLAKGG SGEVWLGQYE ARYVAMKCLL
PAKREDPEAL EQFAEEIRMA SLLAHPRIVA FCGVAWQSLL HLCAVTEYMA RGDLESLLAN
PVAQKELSWS REKLTLSSDI VEALVYLHSL VPVVIHRDLK SKNVLLDRRL RAKLSDFGLS
RERSVEDTMT NGIGTILWSA PEVLEGKRYD EKSDLFSFGV VLSEIDTCAL PYGFSRHAKM
RSMQIVHLVS EGKLLPNFRD DCPPAIRDLA QRCLSLDPAA RPTAMELVVD FCCHFINAME
TTSDENESST LDTVRKARLI RRVPILAHVV KQGLCSEGQL LRALELVTFV DGEYIYCQGQ
PGRDVLFIEE GKVLITQRRR SRAMSTVRPV GFIPMDSSGG VVFTRRSTLK RSQVEAEMEI
QLHKHEELEY FGEESLLQGF VARVLNAVAS GAVTCFMLPE AAFARLLAPV HELMLHRHLL
RMHGVLAKQR IFQHFSARQR QFLLDHCTVE HYEEGARIIQ QGDKDDDRYF ILAEGEADVV
LDEQVREFRR PQSALLSNGE LQDVQEQEET GIRTSVVCRK TLYQGFGEMG ILCRPRATHV
VAAGSVICVA ISRKTYIGAS QLLGVGGVDT DAEALLAMSL MEEWALVVKT RNLHLANPLV
SRYLETFVKK FKAAYMQKFE GKTLYLDLLR RMHADPTLAD EFPFVSDRVA WDQPTSSLSI
TRAETRRVLS LLPADRSPFE ISFVARLLES TAFVDKFDRP SHVDKLALAR GVGRYANFLT
VQKDKFLFRQ GKIESRAFLI LRGNISIVNE DVNTLQPGLT VKQYDVLATL SAGDSFGELS
LVTRLQRSAS ALAACEADLL VLERAHLHAL MDLLPGVSVQ HAMVQRAEFL ASLSFLRDSD
FAQCIRVAHD LQDQFYEPRH IFLQEPVHLR SLYIVKSGEV VVYLRRMVPI ADITVTSGTN
ESATTKEVLV RVATIGPQEF FGVAVASASM LISSTSVNGG IASTATSPSP STNAPPSSPP
SPKRPASPPN AQHYVAATLA SVTATGPTSP TTNTDFAKTV FMCSTRVQML ELSERGWRRL
PLSSLHSIRN SLLERHRWNL ETVEKQQQQN NPTYFVVDKP WQPIIRPNIS TTPKKPNGDN
VDPQTRVLEA APATKLARRI QDKKQQQQQQ GHNNAVSRLF SPSPLAPINK PRQPGRLAIS
PTTTVSSRGS PIYGTSPLKS TSTGLAAFTQ NKTLASPLGS PSLLSPTRAA QFGPSLSGSF
QPKNGTLASL ASPSHAYFTQ PSTSIAPIVL SPRPPLKMPI PNGNPSPRQV REDDTQQRRS
STTPLQDTAR NVQTARESDC KAMWKLQRSP SLKQ
//