PKZ1_PHYIN
ID PKZ1_PHYIN Reviewed; 399 AA.
AC Q8GVC7;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Serine/threonine-protein kinase PKZ1 {ECO:0000303|PubMed:15819621};
DE Short=Pipkz1 {ECO:0000303|PubMed:15819621};
DE EC=2.7.11.1;
DE AltName: Full=Cleavage-associated kinase {ECO:0000312|EMBL:AAM21157.1};
GN Name=PKZ1 {ECO:0000303|PubMed:15819621};
OS Phytophthora infestans (Potato late blight agent) (Botrytis infestans).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=4787;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAM21157.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DEVELOPMENTAL STAGE, AND
RP INDUCTION.
RC STRAIN=2.20 {ECO:0000312|EMBL:AAM21157.1},
RC Isolate 1306 {ECO:0000269|PubMed:12455688}, and
RC Isolate 88069 {ECO:0000269|PubMed:12455688};
RX PubMed=12455688; DOI=10.1128/ec.1.5.687-695.2002;
RA Judelson H.S., Roberts S.;
RT "Novel protein kinase induced during sporangial cleavage in the oomycete
RT Phytophthora infestans.";
RL Eukaryot. Cell 1:687-695(2002).
RN [2] {ECO:0000305}
RP INTERACTION WITH BZP1.
RC STRAIN=Isolate 1306 {ECO:0000269|PubMed:15819621}, and
RC Isolate 88069 {ECO:0000269|PubMed:15819621};
RX PubMed=15819621; DOI=10.1111/j.1365-2958.2005.04575.x;
RA Blanco F.A., Judelson H.S.;
RT "A bZIP transcription factor from Phytophthora interacts with a protein
RT kinase and is required for zoospore motility and plant infection.";
RL Mol. Microbiol. 56:638-648(2005).
CC -!- FUNCTION: May regulate an early stage of the zoospore pathway.
CC {ECO:0000269|PubMed:12455688}.
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 -!- SUBUNIT: Interacts with BZP1. {ECO:0000269|PubMed:15819621}.
CC -!- DEVELOPMENTAL STAGE: Expressed in zoospores. Not detected in non-
CC sporulating hyphae, hyphae decorated with sporangia, ungerminated
CC sporangia and directly germinating sporangia.
CC {ECO:0000269|PubMed:12455688}.
CC -!- INDUCTION: Up-regulated by exposure of sporangia to cool water, which
CC initiates the cleavage of sporangial cytoplasm into individual
CC zoospores. {ECO:0000269|PubMed:12455688}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. {ECO:0000305}.
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DR EMBL; AY093611; AAM21157.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8GVC7; -.
DR SMR; Q8GVC7; -.
DR VEuPathDB; FungiDB:PITG_06236; -.
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 1: Evidence at protein level;
KW ATP-binding; Kinase; Nucleotide-binding; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..399
FT /note="Serine/threonine-protein kinase PKZ1"
FT /id="PRO_0000408773"
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; 43173 MW; 36CC1EC14D1CC6E7 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 VLNSGMCTSA CDMWALGCVL
YIMLSGSHPF DLDGMSADSV VEHRVKSEPV TFDFSAWDNV SPHAKDLISK LLVKDPTLRL
TADQMLQHPW MNASAEAAAA GLRRPSPLLA GQPIPRGPA
