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Database: UniProt
Entry: A0A225WSV1_9STRA
LinkDB: A0A225WSV1_9STRA
Original site: A0A225WSV1_9STRA 
ID   A0A225WSV1_9STRA        Unreviewed;      1280 AA.
AC   A0A225WSV1;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=TKL protein kinase {ECO:0000313|EMBL:OWZ20655.1};
GN   ORFNames=PHMEG_0004903 {ECO:0000313|EMBL:OWZ20655.1};
OS   Phytophthora megakarya.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=4795 {ECO:0000313|EMBL:OWZ20655.1, ECO:0000313|Proteomes:UP000198211};
RN   [1] {ECO:0000313|Proteomes:UP000198211}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=zdho120 {ECO:0000313|Proteomes:UP000198211};
RA   Ali S., Shao J., Larry D.J., Kronmiller B., Shen D., Strem M.D.,
RA   Melnick R.L., Guiltinan M.J., Tyler B.M., Meinhardt L.W., Bailey B.A.;
RT   "Phytopthora megakarya and P. palmivora, two closely related causual agents
RT   of cacao black pod achieved similar genome size and gene model numbers by
RT   different mechanisms.";
RL   Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OWZ20655.1}.
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DR   EMBL; NBNE01000302; OWZ20655.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A225WSV1; -.
DR   STRING; 4795.A0A225WSV1; -.
DR   EnsemblProtists; OWZ20655; OWZ20655; PHMEG_0004903.
DR   OrthoDB; 70541at2759; -.
DR   Proteomes; UP000198211; Unassembled WGS sequence.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 7.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR001969; Aspartic_peptidase_AS.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR001995; Peptidase_A2_cat.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   PANTHER; PTHR24123; ANKYRIN REPEAT-CONTAINING; 1.
DR   Pfam; PF00023; Ank; 1.
DR   Pfam; PF12796; Ank_2; 6.
DR   Pfam; PF13637; Ank_4; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   PRINTS; PR01415; ANKYRIN.
DR   SMART; SM00248; ANK; 25.
DR   SUPFAM; SSF48403; Ankyrin repeat; 3.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 18.
DR   PROSITE; PS50088; ANK_REPEAT; 20.
DR   PROSITE; PS50175; ASP_PROT_RETROV; 1.
DR   PROSITE; PS00141; ASP_PROTEASE; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   4: Predicted;
KW   ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW   ProRule:PRU00023}; Kinase {ECO:0000313|EMBL:OWZ20655.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198211};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000313|EMBL:OWZ20655.1}.
FT   REPEAT          35..67
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          68..101
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          102..134
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          135..167
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          201..233
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          234..266
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          267..299
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          357..389
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          390..422
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          423..455
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          456..488
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          490..522
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          523..555
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          589..621
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          622..654
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          655..687
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          701..733
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          734..766
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          767..799
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          802..834
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   DOMAIN          819..836
FT                   /note="Peptidase A2"
FT                   /evidence="ECO:0000259|PROSITE:PS50175"
FT   DOMAIN          884..1130
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
SQ   SEQUENCE   1280 AA;  140534 MW;  E4E1663F5AB24F46 CRC64;
     MAEVTPFLVA VGEGDVERIS ALVEGGEDVN QLGSRQETAL MRAAGDGNLA VVRFLIDAGA
     DVEAVHWMGN TALINAVWRK GNLNVVKILV ECGADVNVSD SWGDTPLIYA ARNGDLEVIK
     FLVEVGAQVN ALGSKQRTAL LCAIRNGHLN TARFLLENGA EIEAADYNGW TSLFHAVWIE
     NEAIVQLLVE EKAIVDTMDR SNLTPLMYAV LKDNLKISKF LVKNGANIQI VNNEGSTALI
     YAARNNNLEI IKILVECGAY VNAVNSAKMT PLVYVLECGD MTAVRFLIES GADTKAVNLN
     NTVENKKLDD FRSLVDSVDD TKTKNVTMLI NAIENGDLDF VQQHFGKDSD RNAANMFGRS
     LLICAAEIGI LDIVRILIDH GADVNTRDRH SRTPLLHASK NRNWDLVRIF VSRGADVNAA
     DNDGLISLMV AAQNGNMDIV QYLVERGADV NTVDQRERTA VLYASMGGYW DVVRFLVSSG
     ADVNAVNIDD RSTALIYAAK QGQLETIRIL VANGADVNAA DCQNLTSVMI AAETENLRVV
     CFLIDSGAEI ASLENKKIKL LMRTAESCDL KGVRLLLGDG SETNIVEVFG RTLLMCAAKT
     GRSDILQFLL ESGADVNAVD RRYRTPVLHA SENRHWDVVR FLVGKGANVN AIGKSGWTSL
     LYAVQENHLD IIQFLVDAGA DINTSTTNWP TSLLNAASGN NKRIPLIVAT DKGVLEVVQF
     LVQRGADVNS VGSDGQTALM QAAEKGNFKT IKFLSQSGAE FDVADKNGKT VLMCAVMSGD
     LDALQFIYEK NSDVDVNAVD HNGWTSLMYG AQSGNLDVVK FLLDSGADVS IVNNNHRTAI
     FIASSRGYTD VQHLLMEYLP YTQATMGNPI SQMPDNCFIP ALDVELQEFI GSENVGRKYR
     ALWLDAEVVV KLFVPELYVT TFSHEVAAWH RLRHPHVLQL YGACDIGHNF FVCEWASNGS
     LVEYLSACKK RGERQTPWKF LHEAALGLAY LHERKIMHGN LCNNSILVGG DGMVKLANFQ
     VSGSATWEQS DVGCWQAPER LRGDATSIAS DIYSLGLCII ATVTRETPWR GCLDDISKVR
     KANWNATADP VKYGPVDDMT DDLTLLASKM CGNDPASRLS SIEAQGHSMT AIYRRIETIW
     YAIDVTNAEE YKKRQEEKRI KLQESFISGV SKTLIVLDEL ETAEARETFV AFLKAEIDSH
     GSSYSAKTLS VLEKAYVDFY TGLKSDAVTV MPKWFLPWYE LAFDGMNYLG EGGFGEVYRA
     KWLESEGVVK QVKLTNSTKL
//
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