ID A0A420H6T7_9PEZI Unreviewed; 898 AA.
AC A0A420H6T7;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
DE AltName: Full=Autophagy-related protein 1 {ECO:0000256|ARBA:ARBA00030237};
GN ORFNames=OnM2_108001 {ECO:0000313|EMBL:RKF53145.1};
OS Erysiphe neolycopersici.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Erysiphales; Erysiphaceae; Erysiphe.
OX NCBI_TaxID=212602 {ECO:0000313|EMBL:RKF53145.1, ECO:0000313|Proteomes:UP000286134};
RN [1] {ECO:0000313|EMBL:RKF53145.1, ECO:0000313|Proteomes:UP000286134}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UMSG2 {ECO:0000313|EMBL:RKF53145.1};
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004170};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004170}.
CC Preautophagosomal structure membrane {ECO:0000256|ARBA:ARBA00004623};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004623}.
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:RKF53145.1}.
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DR EMBL; MCFK01010847; RKF53145.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A420H6T7; -.
DR STRING; 212602.A0A420H6T7; -.
DR Proteomes; UP000286134; Unassembled WGS sequence.
DR GO; GO:0034045; C:phagophore assembly site membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0010506; P:regulation of autophagy; IEA:InterPro.
DR CDD; cd14009; STKc_ATG1_ULK_like; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR045269; Atg1-like.
DR InterPro; IPR048941; ATG1-like_MIT2.
DR InterPro; IPR022708; Atg1-like_tMIT.
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 PANTHER; PTHR24348:SF22; NON-SPECIFIC SERINE_THREONINE PROTEIN KINASE; 1.
DR PANTHER; PTHR24348; SERINE/THREONINE-PROTEIN KINASE UNC-51-RELATED; 1.
DR Pfam; PF12063; ATG1-like_MIT1; 1.
DR Pfam; PF21127; ATG1-like_MIT2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Autophagy {ECO:0000256|ARBA:ARBA00023006};
KW Kinase {ECO:0000313|EMBL:RKF53145.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Protein transport {ECO:0000256|ARBA:ARBA00022927};
KW Reference proteome {ECO:0000313|Proteomes:UP000286134};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transport {ECO:0000256|ARBA:ARBA00022927}.
FT DOMAIN 33..338
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 376..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 507..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 384..412
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 509..524
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 62
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 898 AA; 100097 MW; 2F44BA6FE80D765B CRC64;
MTTPSSAPPS PSFLPSSKPR RKRAMVDKNV GCFSIEDEIG RGSFATVYRG QHKATGALVA
VKSVNLSKLN KKLKENLYTE IEILKGLHHP HAVALIDCRE SSTHIYLVME YCELGDLSYF
IRKRDSLGEH EALRDMVRRY PMPSVGGLPE VIVRHFLKQL ASAMEFLRAR NFIHRDVKPQ
NLLIIPSPEF LANARGRPVA MNGSVSSLEP IVGLSSLPML KIADFGFARS LPSASLAETL
CGSPLYMAPE ILRFEKYDAK ADLWSVGAVL FEMMTAKPPF RASNHVELLR KIEQGDDFIR
FPKDVKISPQ MKDIIKALLK RTPTMRMSFE RFFEHPAVID TIPELVREDY QKDIPVQTKK
VEAVSHQNAI IKVEKRHSQK IPNISSSRER NTPPPGIVTV DSERNSSTDT RHLTQQVRTG
FMDHKRPIII SSTTTPNMET NSKNQAQLLK NDVVKDKLPF SNGPEDVNIG DVIAEAEQAV
RDAREYVLVE KRAVEVNAFA DEMAANPSTA DGLNISSPRV GQTSEGKPRQ ERIPRRSNSQ
GKLSSSPSVT SAISRALNSA SLRVFGVSYP DVKTKGISPN LYTLHNFSAY PTSPSAITFS
GDGRSGKNLD EDQRCLNDIE ESATRSDVVF GFAEVKYKQL VPSTPSIDYG FGGSGNYRDG
YHIHEDEGLT IEAIVSLSEE ALVLYIKALS LLAKSMDIAR TWWSRKSRSE FQHCQNYNIR
SDASSNMGTI NRINQAIQWV RDRFNEVFEK AELISLKLLD AQKQLPEDHP AYLNPTSLGP
KNVSHNIILT SGVTAEKLMY DRAIDMSRSA AISELANEDI DGCERSYVTA VRMLEAVLEY
DAEPSSPLFI KEPGTSKDTI AERQVELMNG IDLADQQAVL KGRYGPEISL NKIMLTKK
//
