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
//