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
//