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Database: UniProt
Entry: W2P3C3_PHYPR
LinkDB: W2P3C3_PHYPR
Original site: W2P3C3_PHYPR 
ID   W2P3C3_PHYPR            Unreviewed;      1237 AA.
AC   W2P3C3;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   SubName: Full=TKL protein kinase {ECO:0000313|EMBL:ETM55286.1};
GN   ORFNames=L914_01483 {ECO:0000313|EMBL:ETM55286.1};
OS   Phytophthora parasitica (Potato buckeye rot agent).
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=4792 {ECO:0000313|EMBL:ETM55286.1};
RN   [1] {ECO:0000313|EMBL:ETM55286.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IAC_01/95 {ECO:0000313|EMBL:ETM55286.1};
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 IAC_01/95.";
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC       protein kinase family. {ECO:0000256|ARBA:ARBA00005843}.
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DR   EMBL; KI690752; ETM55286.1; -; Genomic_DNA.
DR   AlphaFoldDB; W2P3C3; -.
DR   EnsemblProtists; ETM55286; ETM55286; L914_01483.
DR   VEuPathDB; FungiDB:PPTG_06717; -.
DR   GO; GO:0043229; C:intracellular organelle; IEA:UniProt.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 2.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR000306; Znf_FYVE.
DR   InterPro; IPR017455; Znf_FYVE-rel.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR44329; SERINE/THREONINE-PROTEIN KINASE TNNI3K-RELATED; 1.
DR   PANTHER; PTHR44329:SF214; ZINC FINGER CONTAINING PROTEIN KINASE-RELATED; 1.
DR   Pfam; PF12796; Ank_2; 1.
DR   Pfam; PF01363; FYVE; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00248; ANK; 3.
DR   SMART; SM00064; FYVE; 1.
DR   SMART; SM00220; S_TKc; 2.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 2.
DR   PROSITE; PS50297; ANK_REP_REGION; 2.
DR   PROSITE; PS50088; ANK_REPEAT; 3.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 2.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS50178; ZF_FYVE; 1.
PE   3: Inferred from homology;
KW   ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW   Kinase {ECO:0000313|EMBL:ETM55286.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Transferase {ECO:0000313|EMBL:ETM55286.1};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00091}.
FT   REPEAT          32..65
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          66..98
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          99..131
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   DOMAIN          416..667
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          840..891
FT                   /note="FYVE-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50178"
FT   DOMAIN          970..1233
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
SQ   SEQUENCE   1237 AA;  138807 MW;  7820E54A00A82886 CRC64;
     MGHLIEAVRE GSSEAVQIAL TARADVNLRD EEGWTALTLA AADGSVDLLE QLLVEPNVDI
     DYPNHWGETA LSRAVFIGNE RIAKLLLDEG AKVDLADEDG DTPLHVSVIS GRLDLAYLLL
     ENGADVMVKN KSGNTVQDLA HKYGRKDFVA ILGDYRRDSM WTTVLEAGIR VSSYFGGMIN
     AGIIEGKKGV ECTVQVCVEQ NNQHDEDKSK QSELSFTTLL PELLVLCAGM VETQDMCEDI
     LERLQRVQNY FAENEEIAAI PAKDSFPLVT ARFHAFLEQH SNHSAVERLA STRTILGLLR
     GFHDDIDGIV TQSDLADSTS IAFNWKEKWE KDVLAVENRL INSWKANSSE LSRELPDAAS
     QTGALLLLNS EAMRHKNGYS ARSQHLLESA SKKIARMSGA PIPEIPEWFI PCHEVQRHSK
     PFASGSYGSI YRGIWRGSKV VIKCMTVNTP FEKRAFLREA KIWHKARHPH IINFFGACCS
     SHPCFFVCEE AVNGNLAEYL DKKKSRGREL VWSKLHEAAL GLEYLHQNGI VHGDLKCNQI
     LINGEGTAKL TDFGFSFVLS ESKPKGAGGA TRWRAPECLG YKEQMPTFES DVYSFGMCVV
     EAMTYDVPWG VYLPDVAVVD HLRHRQFIPR PSVFSDAEWD FVLALCAFEP SKRIKLRDAI
     EQLASFASEE TECCISLRAG NHNNQSMIRF SKKSSQQLLE DKNMEQEREA KSKVYCAMIS
     LRCRRNYLRF RYAVQTIQIA FRYKKSVHLK RESMMRNVSA DIIVGLFRMI NERRKYLRFV
     CALRVLQCCY RYREKLRVKA AEPTTATLLS TESPSSPGHT IDLPQQLQAD HSFTPQWVND
     EERLSCVVCY KDFTVFRRKH HCRVCLEIIC GNCSLTRKRM RVCVMCAGLR PPRYPTATQP
     QTDRRGRILS NAGGFLTGLG TLFQSRRNEL EPQSVVSYGP IVLASTELNG QDGLWQDDDI
     TAVRIPRDEV TILETLSRGA YGSVHLGTWN DKQVAIKTLL PESRKNIFDI NQFLMEVKLI
     AAMEHPCIVN LFGVAWSSLA DMCMILEYMD GGDLRSLLDK YKEDQHPLGF DANKLSIALN
     VVSALTYLHS LSPRVIHRDL KSLNILLNSA LEAKVTDFGV SRSYEDRTMT AGVGTGLWMA
     PEVMSGEAYN EKADMFSFGI VLSELDTHNV PHAENSNVPP VRLMQSILMG EIRAQFSQAG
     PQAVVELGNA CLSLDPADRP TAAEAMYKLH CILRDLS
//
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