ATG1_MAGO7
ID ATG1_MAGO7 Reviewed; 982 AA.
AC Q52EB3; G4N7K2; Q2Q439;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Serine/threonine-protein kinase ATG1 {ECO:0000303|PubMed:17416896};
DE EC=2.7.11.1 {ECO:0000250|UniProtKB:P53104};
DE AltName: Full=Autophagy-related protein 1 {ECO:0000250|UniProtKB:P53104};
GN Name=ATG1 {ECO:0000303|PubMed:17416896};
GN ORFNames=MGG_06393 {ECO:0000303|PubMed:15846337};
OS Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS fungus) (Pyricularia oryzae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX NCBI_TaxID=242507;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP FUNCTION.
RC STRAIN=Guyane 11;
RX PubMed=17416896; DOI=10.1128/ec.00011-07;
RA Liu X.-H., Lu J.-P., Zhang L., Dong B., Min H., Lin F.-C.;
RT "Involvement of a Magnaporthe grisea serine/threonine kinase gene, MgATG1,
RT in appressorium turgor and pathogenesis.";
RL Eukaryot. Cell 6:997-1005(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX PubMed=15846337; DOI=10.1038/nature03449;
RA Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL Nature 434:980-986(2005).
CC -!- FUNCTION: Serine/threonine protein kinase involved in the cytoplasm to
CC vacuole transport (Cvt) and found to be essential in autophagy, where
CC it is required for the formation of autophagosomes. Involved in the
CC clearance of protein aggregates which cannot be efficiently cleared by
CC the proteasome. Required for selective autophagic degradation of the
CC nucleus (nucleophagy) as well as for mitophagy which contributes to
CC regulate mitochondrial quantity and quality by eliminating the
CC mitochondria to a basal level to fulfill cellular energy requirements
CC and preventing excess ROS production. Also involved in endoplasmic
CC reticulum-specific autophagic process, in selective removal of ER-
CC associated degradation (ERAD) substrates. Plays a key role in ATG9 and
CC ATG23 cycling through the pre-autophagosomal structure and is necessary
CC to promote ATG18 binding to ATG9 through phosphorylation of ATG9.
CC Catalyzes phosphorylation of ATG4, decreasing the interaction between
CC ATG4 and ATG8 and impairing deconjugation of PE-conjugated forms of
CC ATG8 (By similarity). Autophagy is essential to fungal development,
CC production of appressorium turgor, and pathogenicity in rice blast
CC disease (PubMed:17416896). {ECO:0000250|UniProtKB:P53104,
CC ECO:0000269|PubMed:17416896}.
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:P53104};
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:P53104};
CC -!- SUBUNIT: Homodimer. Forms a ternary complex with ATG13 and ATG17.
CC {ECO:0000250|UniProtKB:P53104}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17416896}.
CC Preautophagosomal structure membrane {ECO:0000250|UniProtKB:P53104};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:P53104}.
CC -!- TISSUE SPECIFICITY: Uniformly detected in conidia, mycelia and
CC appressoria (at protein level). {ECO:0000269|PubMed:17416896}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. APG1/unc-51/ULK1 subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00159}.
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DR EMBL; DQ224381; ABB46201.1; -; mRNA.
DR EMBL; CM001234; EHA50859.1; -; Genomic_DNA.
DR RefSeq; XP_003717178.1; XM_003717130.1.
DR AlphaFoldDB; Q52EB3; -.
DR SMR; Q52EB3; -.
DR STRING; 318829.MGG_06393T0; -.
DR EnsemblFungi; MGG_06393T0; MGG_06393T0; MGG_06393.
DR GeneID; 2684548; -.
DR KEGG; mgr:MGG_06393; -.
DR VEuPathDB; FungiDB:MGG_06393; -.
DR eggNOG; KOG0595; Eukaryota.
DR HOGENOM; CLU_006447_0_0_1; -.
DR InParanoid; Q52EB3; -.
DR OMA; INNVVQW; -.
DR OrthoDB; 1084750at2759; -.
DR PHI-base; PHI:2035; -.
DR PHI-base; PHI:2069; -.
DR PHI-base; PHI:8612; -.
DR Proteomes; UP000009058; Chromosome 4.
DR GO; GO:1990316; C:Atg1/ULK1 kinase complex; IEA:EnsemblFungi.
DR GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
DR GO; GO:0097635; C:extrinsic component of autophagosome membrane; IEA:EnsemblFungi.
DR GO; GO:0061908; C:phagophore; IEA:EnsemblFungi.
DR GO; GO:0034045; C:phagophore assembly site membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0120095; C:vacuole-isolation membrane contact site; IEA:EnsemblFungi.
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; IMP:PAMGO_MGG.
DR GO; GO:0075016; P:appressorium formation; IMP:PAMGO_MGG.
DR GO; GO:0048102; P:autophagic cell death; IMP:PAMGO_MGG.
DR GO; GO:0000045; P:autophagosome assembly; IEA:EnsemblFungi.
DR GO; GO:0000422; P:autophagy of mitochondrion; IEA:EnsemblFungi.
DR GO; GO:0120164; P:conidium germination; IMP:UniProtKB.
DR GO; GO:0044805; P:late nucleophagy; IEA:EnsemblFungi.
DR GO; GO:0034727; P:piecemeal microautophagy of the nucleus; IEA:EnsemblFungi.
DR GO; GO:0075307; P:positive regulation of conidium formation; IMP:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0061709; P:reticulophagy; IEA:EnsemblFungi.
DR GO; GO:0009847; P:spore germination; IMP:PAMGO_MGG.
DR InterPro; IPR045269; Atg1-like.
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 InterPro; IPR022708; Ser/Thr_kinase_C.
DR PANTHER; PTHR24348; PTHR24348; 1.
DR Pfam; PF12063; DUF3543; 1.
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; Autophagy; Cytoplasm; Kinase; Membrane; Nucleotide-binding;
KW Protein transport; Reference proteome; Serine/threonine-protein kinase;
KW Transferase; Transport.
FT CHAIN 1..982
FT /note="Serine/threonine-protein kinase ATG1"
FT /id="PRO_0000085648"
FT DOMAIN 19..324
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 334..506
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 813..834
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 898..918
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 947..982
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 336..356
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 363..384
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 393..407
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 464..496
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 162
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 25..33
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 48
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 982 AA; 107443 MW; 9811E0BC78307638 CRC64;
MADRSARRAR PGDDSVGQFV IGAEIGKGSF AQVYMGKHKV SGAAVAIKSV ELARLNKKLK
ENLYGEINIL KTLRHPHIVA LHDCVESATH INLMMEYCEL GDLSLFIKKR EKLSTNPATH
DMARKYPNVP NSGLNEVVIR HFLKQLSSAL KFLRESNLVH RDVKPQNLLL LPSPEFREVN
KLARPILTAS QDSLVPVAGL ASLPMLKLAD FGFARVLPST SLAETLCGSP LYMAPEILRY
ERYDAKADLW SVGTVLFEMI VGRPPFRASN HVELLRKIEA AEDVIKFPRE TTISSEMKGL
TRALLKRNPV ERISFENFFA HPVIISSIPG LVEDDIPKPE ASEQRSSSKD TRAASKSDDP
IASPRKYSFR RHPTDNDQIR DQFRRVEPPS SAAESAPSRQ TSAFSGIAAE ARKQAAAEAS
ARTGQSSRNE PGDNLVPRRP QAQPSTSAPS KPGLYEERRR GISNASLNRS NRESSSPTSA
ALANDSARAP PQQTSRRVQA EEREKAAQDV AFERDYVVVE KKHVEVNAFA DEMAANPRLG
GQGTPLSPKS GQIVRRATQQ GNPTSTTGAI PAAPSRTMQI AQGTQRHYHE RGTSLSASPG
STASFITKAI QDASLRLLGI KYPAGLTKGA SPPELYNPYP AYPTPSPPVG LISSGKQSTP
VDEDARVAQL IEEHATRSDV VYGFAEVKYK QLVPLAPSAE HGLGGTTLED MPTGEEDVLT
VEAIVSLSEE ALVLYVKALT LLAKSMDIAS LWWARKNRGD QANNALSSTR DSVNTQTLSL
RINSAVQWVR SRFNEVLEKA EVVRLRLMDA QKRLPDDHPS HPSNHPQGSE SVNGASAEGV
FLTVGVTAEK LMYDRALEMS RTAAINEITN EDLAGCEISY VTAIRMLEAV LDNDEDAPKR
RLSANMDDSG GDGEDGHAEI NADDQQAVQK MIHMIRSRLT SVRSKVRMIS NASKAQQQSQ
PQSLIRRRSG DVTPRSVPSY SS
