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Database: UniProt
Entry: A0A420J7Z6_9PEZI
LinkDB: A0A420J7Z6_9PEZI
Original site: A0A420J7Z6_9PEZI 
ID   A0A420J7Z6_9PEZI        Unreviewed;       854 AA.
AC   A0A420J7Z6;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN   ORFNames=GcM3_019009 {ECO:0000313|EMBL:RKF82920.1};
OS   Golovinomyces cichoracearum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Erysiphales; Erysiphaceae; Golovinomyces.
OX   NCBI_TaxID=62708 {ECO:0000313|EMBL:RKF82920.1, ECO:0000313|Proteomes:UP000283383};
RN   [1] {ECO:0000313|EMBL:RKF82920.1, ECO:0000313|Proteomes:UP000283383}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UMSG3 {ECO:0000313|EMBL:RKF82920.1};
RX   PubMed=30253736; DOI=10.1186/s12864-018-5069-z;
RA   Wu Y., Ma X., Pan Z., Kale S.D., Song Y., King H., Zhang Q., Presley C.,
RA   Deng X., Wei C.I., Xiao S.;
RT   "Comparative genome analyses reveal sequence features reflecting distinct
RT   modes of host-adaptation between dicot and monocot powdery mildew.";
RL   BMC Genomics 19:705-705(2018).
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:0000256|ARBA:ARBA00001433};
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:0000256|ARBA:ARBA00000775};
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC       protein kinase family. STE20 subfamily.
CC       {ECO:0000256|ARBA:ARBA00008874}.
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:RKF82920.1}.
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DR   EMBL; MCBQ01001951; RKF82920.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A420J7Z6; -.
DR   STRING; 62708.A0A420J7Z6; -.
DR   Proteomes; UP000283383; Unassembled 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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0019236; P:response to pheromone; IEA:UniProtKB-KW.
DR   CDD; cd01093; CRIB_PAK_like; 1.
DR   CDD; cd06614; STKc_PAK; 1.
DR   Gene3D; 3.90.810.10; CRIB domain; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR000095; CRIB_dom.
DR   InterPro; IPR036936; CRIB_dom_sf.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR033923; PAK_BD.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR48015; SERINE/THREONINE-PROTEIN KINASE TAO; 1.
DR   PANTHER; PTHR48015:SF6; SERINE_THREONINE-PROTEIN KINASE CLA4-RELATED; 1.
DR   Pfam; PF00786; PBD; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00285; PBD; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50108; CRIB; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   3: Inferred from homology;
KW   Kinase {ECO:0000313|EMBL:RKF82920.1};
KW   Pheromone response {ECO:0000256|ARBA:ARBA00022507};
KW   Reference proteome {ECO:0000313|Proteomes:UP000283383};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000313|EMBL:RKF82920.1}.
FT   DOMAIN          79..187
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          192..205
FT                   /note="CRIB"
FT                   /evidence="ECO:0000259|PROSITE:PS50108"
FT   DOMAIN          565..834
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1..39
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          256..496
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        256..279
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        288..305
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        315..331
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        332..352
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        397..496
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   854 AA;  93879 MW;  3D2823678454C516 CRC64;
     MAFQNSTITA GQFMNPGPAP RPPINSPRTN LPHPNTGLSE NLAQMNMFPT VSRGSTSSAT
     GSLVSLPLQR QPELQGGLAV IKQGPAYVKE GKTFLTPWKQ KFLVLRKEAL DFHKNEGGKI
     SYTIVLKDVL AVSRVEAAGT IFEIKRAIIG SSSNPGDDEG PSRSIQIKVK GDDDLYEWID
     FIYARCPGMG GVSNPTNFSH SVHVGFDSQT GEFVGLPPEW SKLLNSSAIT KEDYERNPQA
     VFEVLEFYSD ITKQAQNPNQ YSPMPPSASS LNKQVVPTGY GGGSSIAPPR QVPNSVLNNS
     NTTPVVPRRP TPPEAVQRQQ IQAIKSSSID QARESQRQRE REAAEEQNRK DMEAYNASLP
     KTRVPTAQKE LGGFGGGSIS NSDRYNPSRA APLTPVAARQ PQNQVSSARS PRQVPSTQSS
     NNGARPRISK QTTSPSLRED LTSASRADQN TQRRSISRYQ NGTNGQLQQP RPLINGQNQQ
     SSPRLPPNTN QVKPLNYGIK QTTPVTTNGI KQNDAVRAAE AALTAKPTLA EKERKQDARM
     STMSESEVMA KLKEAVSKDD PNMSYSKQKK IGQGASGSVY VAKVKENPLS LIAREVLRQQ
     GPKAQVAIKQ MDLAHQPRKE LIVNEIMVMK DSRHRNIVNF LDAFLRNNSS ELWVVMEYME
     GGALTDVIDN NPSITEEQIS TICLETCSGL AHLHAQDIIH RDIKSDNVLL DARGNVKITD
     FGFCAKLTES KKKRATMVGT PYWMAPEVVK QKEYGPKVDI WSLGIMAIEM IESEPPYLNE
     EPLKALYLIA TNGTPRLKKP EKLSKELKAF LSVCLCVDIR SRASADELLA HDFLKYGCPP
     GSLSELLAFR KSGK
//
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