PKZ1_PHYIT
ID PKZ1_PHYIT Reviewed; 399 AA.
AC D0N4E2;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2009, sequence version 1.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=Serine/threonine-protein kinase PKZ1 {ECO:0000250|UniProtKB:Q8GVC7};
DE EC=2.7.11.1;
DE AltName: Full=Cleavage-induced protein kinase {ECO:0000312|EMBL:EEY69750.1};
GN Name=PKZ1 {ECO:0000250|UniProtKB:Q8GVC7}; ORFNames=PITG_06236;
OS Phytophthora infestans (strain T30-4) (Potato late blight agent).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=403677;
RN [1] {ECO:0000312|EMBL:EEY69750.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T30-4 {ECO:0000312|EMBL:EEY69750.1};
RX PubMed=19741609; DOI=10.1038/nature08358;
RG The Broad Institute Genome Sequencing Platform;
RA Haas B.J., Kamoun S., Zody M.C., Jiang R.H., Handsaker R.E., Cano L.M.,
RA Grabherr M., Kodira C.D., Raffaele S., Torto-Alalibo T., Bozkurt T.O.,
RA Ah-Fong A.M., Alvarado L., Anderson V.L., Armstrong M.R., Avrova A.,
RA Baxter L., Beynon J., Boevink P.C., Bollmann S.R., Bos J.I., Bulone V.,
RA Cai G., Cakir C., Carrington J.C., Chawner M., Conti L., Costanzo S.,
RA Ewan R., Fahlgren N., Fischbach M.A., Fugelstad J., Gilroy E.M., Gnerre S.,
RA Green P.J., Grenville-Briggs L.J., Griffith J., Grunwald N.J., Horn K.,
RA Horner N.R., Hu C.H., Huitema E., Jeong D.H., Jones A.M., Jones J.D.,
RA Jones R.W., Karlsson E.K., Kunjeti S.G., Lamour K., Liu Z., Ma L.,
RA Maclean D., Chibucos M.C., McDonald H., McWalters J., Meijer H.J.,
RA Morgan W., Morris P.F., Munro C.A., O'Neill K., Ospina-Giraldo M.,
RA Pinzon A., Pritchard L., Ramsahoye B., Ren Q., Restrepo S., Roy S.,
RA Sadanandom A., Savidor A., Schornack S., Schwartz D.C., Schumann U.D.,
RA Schwessinger B., Seyer L., Sharpe T., Silvar C., Song J., Studholme D.J.,
RA Sykes S., Thines M., van de Vondervoort P.J., Phuntumart V., Wawra S.,
RA Weide R., Win J., Young C., Zhou S., Fry W., Meyers B.C., van West P.,
RA Ristaino J., Govers F., Birch P.R., Whisson S.C., Judelson H.S.,
RA Nusbaum C.;
RT "Genome sequence and analysis of the Irish potato famine pathogen
RT Phytophthora infestans.";
RL Nature 461:393-398(2009).
CC -!- FUNCTION: May regulate an early stage of the zoospore pathway.
CC {ECO:0000250|UniProtKB:Q8GVC7}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000250|UniProtKB:P31749};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:P31749};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. {ECO:0000305}.
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DR EMBL; DS028125; EEY69750.1; -; Genomic_DNA.
DR RefSeq; XP_002998397.1; XM_002998351.1.
DR AlphaFoldDB; D0N4E2; -.
DR SMR; D0N4E2; -.
DR STRING; 4787.PITG_06236T0; -.
DR EnsemblProtists; PITG_06236T0; PITG_06236T0; PITG_06236.
DR GeneID; 9465934; -.
DR KEGG; pif:PITG_06236; -.
DR VEuPathDB; FungiDB:PITG_06236; -.
DR eggNOG; KOG0032; Eukaryota.
DR HOGENOM; CLU_000288_63_0_1; -.
DR InParanoid; D0N4E2; -.
DR OMA; SACDMWA; -.
DR OrthoDB; 1164875at2759; -.
DR Proteomes; UP000006643; Partially assembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ATP-binding; Kinase; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..399
FT /note="Serine/threonine-protein kinase PKZ1"
FT /id="PRO_0000408774"
FT DOMAIN 92..371
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 30..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 219
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-
FT ProRule:PRU10027"
FT BINDING 98..106
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 121
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 399 AA; 43158 MW; 26D22B165A28B5BF CRC64;
MLRLGRSAAS EVSSIRNSLQ LQLEQRGARP MQCAYQTQSH SNPEGAKRGR SPMSLAVMGA
AALSVGLELQ TDGIAQARAA MEPGTQLQRH KWQLFDQIGA GAFGVVRLGM HEESGEVAAV
KIVPLENPND QRSYPALERE IAALKLVKAL GGHNSIVDLR DVYVEGRKLF LVTELARGGE
LFEQIVAYGS FPELKARDVA REMASALSFM HRHGLVHKDV KPENILMSAR VVDHNSGVYR
KSNRHESSSL VKLADFGSAG PASVNTNLED IGTAAYLPPE VLNSGLCTSA CDMWALGCVL
YIMLSGSHPY DLDGMSADSV VEHRVKSEPV TFDFSAWDNV SPHAKDLISK LLVKDPTLRL
TADQMLQHPW MNASAEAAAA GLRRPSPLLA GQPIPISPA
