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Database: UniProt
Entry: W2LSW0_PHYPR
LinkDB: W2LSW0_PHYPR
Original site: W2LSW0_PHYPR 
ID   W2LSW0_PHYPR            Unreviewed;      1557 AA.
AC   W2LSW0;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   SubName: Full=TKL/TKL-CCIN protein kinase {ECO:0000313|EMBL:ETM00573.1, ECO:0000313|EMBL:ETM00574.1};
GN   ORFNames=L917_02720 {ECO:0000313|EMBL:ETM00574.1};
OS   Phytophthora parasitica (Potato buckeye rot agent).
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=4792 {ECO:0000313|EMBL:ETM00574.1};
RN   [1] {ECO:0000313|EMBL:ETM00574.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CHvinca01 {ECO:0000313|EMBL:ETM00574.1};
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 CHvinca01.";
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KI677977; ETM00573.1; -; Genomic_DNA.
DR   EMBL; KI677977; ETM00574.1; -; Genomic_DNA.
DR   EnsemblProtists; ETM00573; ETM00573; L917_02720.
DR   EnsemblProtists; ETM00574; ETM00574; L917_02720.
DR   VEuPathDB; FungiDB:PPTG_07601; -.
DR   Proteomes; UP000054423; Unassembled WGS sequence.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd00180; PKc; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 4.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR44329:SF214; ANKYRIN REPEAT-CONTAINING PROTEIN KINASE A-RELATED; 1.
DR   PANTHER; PTHR44329; SERINE/THREONINE-PROTEIN KINASE TNNI3K-RELATED; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 3.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 3.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 2.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Kinase {ECO:0000313|EMBL:ETM00574.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000313|EMBL:ETM00574.1}.
FT   DOMAIN          646..938
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          1227..1530
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1324..1356
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1326..1356
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         1255
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   1557 AA;  177315 MW;  1AA2D9E8CB995CF9 CRC64;
     MCVLSPPTER ELYALLPICA SSVHVVFRSL VPRLQALDTF LQAHSVDLTG EESEIVDFLE
     ALSHHRHQET VFNALVQQLK LLTDFNALQQ DSNEDAPNNI LQMLLEAPRK SREVHWMHLQ
     IDALMSHEET EEESCDWQEH WKEDYKQQIE FFEEFLDSKK LQEELQILET SEKLELLTAL
     QYERKKLSGS DEELMPVQEQ KLLDRAIDKV SEAAHDEVLT VPEWFVPRYE VQIREDTGSF
     ECCVEGEWNG LNVTLEYGED MDTVINGAEK WCGVKDPYIV TLHGACHVGK TPFIIYESIR
     DFISLLDYAN NVQNSRKVWK RLLEAARGLQ YLHGLGIAHG NITAACVVVG ADKKAKIKSN
     TWEDLPTESS KEDDVYAFAS IILEATSSIE NPDDILPSIE NEQQYPCGMN YAAWLIEEMT
     SSNPHDRPDM NAVVRMLLNV TERERPWSDV QFPELLLHAP DVWTALRTAS QRHETGVGMC
     ARVLRRLEQV LVRLWDEGIV FGDGEDVEYN WQTRTEYLLR SMRYLTRHYL PSNGRELLKI
     AQARRFSNEI QQMHHQLDAL LAEFDSENVY AEIDPTSESI SRSAEEWELE WEYDCGDLMA
     TFHEYLDGLE QSDGVRTDVA MEAMTVMKHE LDNFRYAFTD AQQDLVVRAF DICVRQVGTV
     VTCTPEWFIS PYEVRDGSWW EGVRVTIQKP QQDANACEIV QRQADIWSEL VHPHVVELFG
     ACHVGSAPFF VFERARGGSL MEYLSRYQNT TQLWRLLYET GLGLQYLHER DIVHNELSSD
     NIVVVVEKSS AVRRKLHGRK AKRSLRYDNS MQEVAKLNGL QFAPLNDSRL FQTYRSFTDE
     DSGRWLSPER RGDDMVPGLP SLASDIYSFG MIIIEAVLHG TDSCDEFLND IQDEDQSIFE
     HILDQFEHEA WELVKKMCAW QPELRPSISY VVQKLGELAS RQRTADQLGA YREFGEMNAA
     SVTADDEHFS IPREPKTAVD CMIHVPDEAP STISQALQTL KSQIQNSTDN GIDLEASNDD
     LNVQILRRMD DIYQRLCDIE ANIGEDPDIK DFSTIVANFV DILTQFIAHV NVSSTGNCLT
     QIVAIRQRTN DKFSFHKDLD ELLNELHSYE CLSSEKEEIH DWKCQWYLHR ARQTLSHTWT
     LMSPNAANAA DLLLDELKDA NDREEILAFL RFEVTRHRSS YTSAQVKAMG AACTDISRRL
     SATTTIPEHF HLWQPPRWFI PPYEVEFNPR ESLGHGAFAS VHMGTWLGTP VVIKKLTSGS
     INPLGSPPSA VFYRELSIWY RLNHPYVVKL YGGCHVGGQP FFVCEPASNG RLDTYLHRFD
     PPGPSVGTSS LRSTSTISGH TSGFSRSTSN GSSTGFSADS IGCHRRCEAW KKLRQSALGL
     QYLHQHSIVH GDLKCDNILV AADGTAKLTD FGLSTICRYV DSEQEQSSNV SEVGAQRWKA
     PECLAGAQPS FESDVYSFGM CILQAISGEF PWGSRMPDAA VRFHVRRGVL PPRPKGFEDD
     AHWELVKQMC CFDPQQRLKL PVVVQRLARF ADLEARRQRG GVSVHMRELL FGGSATS
//
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