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
//