ATG1_GIBZE
ID ATG1_GIBZE Reviewed; 944 AA.
AC I1RNG8; A0A098E0U2; A0A1C3YJQ0;
DT 25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=Serine/threonine-protein kinase ATG1 {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000250|UniProtKB:P53104};
DE AltName: Full=Autophagy-related protein 1 {ECO:0000303|PubMed:28894236};
GN Name=ATG1 {ECO:0000303|PubMed:28894236};
GN ORFNames=FG05547, FGRAMPH1_01T18179;
OS Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084
OS / PH-1) (Wheat head blight fungus) (Fusarium graminearum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=229533;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=17823352; DOI=10.1126/science.1143708;
RA Cuomo C.A., Gueldener U., Xu J.-R., Trail F., Turgeon B.G., Di Pietro A.,
RA Walton J.D., Ma L.-J., Baker S.E., Rep M., Adam G., Antoniw J., Baldwin T.,
RA Calvo S.E., Chang Y.-L., DeCaprio D., Gale L.R., Gnerre S., Goswami R.S.,
RA Hammond-Kosack K., Harris L.J., Hilburn K., Kennell J.C., Kroken S.,
RA Magnuson J.K., Mannhaupt G., Mauceli E.W., Mewes H.-W., Mitterbauer R.,
RA Muehlbauer G., Muensterkoetter M., Nelson D., O'Donnell K., Ouellet T.,
RA Qi W., Quesneville H., Roncero M.I.G., Seong K.-Y., Tetko I.V., Urban M.,
RA Waalwijk C., Ward T.J., Yao J., Birren B.W., Kistler H.C.;
RT "The Fusarium graminearum genome reveals a link between localized
RT polymorphism and pathogen specialization.";
RL Science 317:1400-1402(2007).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=20237561; DOI=10.1038/nature08850;
RA Ma L.-J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.-J.,
RA Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA Houterman P.M., Kang S., Shim W.-B., Woloshuk C., Xie X., Xu J.-R.,
RA Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA Butchko R.A.E., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.J.,
RA Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA Kumar L., Lee Y.-H., Li L., Manners J.M., Miranda-Saavedra D.,
RA Mukherjee M., Park G., Park J., Park S.-Y., Proctor R.H., Regev A.,
RA Ruiz-Roldan M.C., Sain D., Sakthikumar S., Sykes S., Schwartz D.C.,
RA Turgeon B.G., Wapinski I., Yoder O., Young S., Zeng Q., Zhou S.,
RA Galagan J., Cuomo C.A., Kistler H.C., Rep M.;
RT "Comparative genomics reveals mobile pathogenicity chromosomes in
RT Fusarium.";
RL Nature 464:367-373(2010).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=26198851; DOI=10.1186/s12864-015-1756-1;
RA King R., Urban M., Hammond-Kosack M.C.U., Hassani-Pak K.,
RA Hammond-Kosack K.E.;
RT "The completed genome sequence of the pathogenic ascomycete fungus Fusarium
RT graminearum.";
RL BMC Genomics 16:544-544(2015).
RN [4]
RP IDENTIFICATION, FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=28894236; DOI=10.1038/s41598-017-11640-z;
RA Lv W., Wang C., Yang N., Que Y., Talbot N.J., Wang Z.;
RT "Genome-wide functional analysis reveals that autophagy is necessary for
RT growth, sporulation, deoxynivalenol production and virulence in Fusarium
RT graminearum.";
RL Sci. Rep. 7:11062-11062(2017).
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 (By similarity).
CC Involved in the clearance of protein aggregates which cannot be
CC efficiently cleared by the proteasome (By similarity). Required for
CC selective autophagic degradation of the nucleus (nucleophagy) as well
CC as for mitophagy which contributes to regulate mitochondrial quantity
CC and quality by eliminating the mitochondria to a basal level to fulfill
CC cellular energy requirements and preventing excess ROS production (By
CC similarity). Also involved in endoplasmic reticulum-specific autophagic
CC process, in selective removal of ER-associated degradation (ERAD)
CC substrates (By similarity). Plays a key role in ATG9 and ATG23 cycling
CC through the pre-autophagosomal structure and is necessary to promote
CC ATG18 binding to ATG9 through phosphorylation of ATG9. Catalyzes
CC phosphorylation of ATG4, decreasing the interaction between ATG4 and
CC ATG8 and impairing deconjugation of PE-conjugated forms of ATG8 (By
CC similarity). Autophagy is required for proper vegetative growth,
CC asexual/sexual reproduction, and full virulence (PubMed:28894236).
CC Autophagy is particularly involved in the biosynthesis of
CC deoxynivalenol (DON), an important virulence determinant
CC (PubMed:28894236). {ECO:0000250|UniProtKB:P53104,
CC ECO:0000269|PubMed:28894236}.
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 (By similarity). Dimerization requires the presence
CC of ATG13 (By similarity). Forms a ternary complex with ATG13 and ATG17
CC (By similarity). {ECO:0000250|UniProtKB:P53104}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P53104}.
CC Preautophagosomal structure membrane {ECO:0000250|UniProtKB:P53104};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:P53104}.
CC -!- DOMAIN: The LIR motif is required for the interaction with ATG8 and for
CC the association of ATG1 with autophagosomes (By similarity).
CC {ECO:0000250|UniProtKB:P53104}.
CC -!- DOMAIN: The C-terminal region of ATG1 responsible for ATG13-binding
CC comprises six alpha-helices which fold into two antiparallel three-
CC helix bundles resembling each other (By similarity).
CC {ECO:0000250|UniProtKB:W0T9X4}.
CC -!- DISRUPTION PHENOTYPE: Blocks autophagy (PubMed:28894236). Significantly
CC decreases the radial growth of colonies under nutrient-rich conditions
CC (PubMed:28894236). Strongly reduces conidiation and completely fails to
CC form any perithecia (PubMed:28894236). Causes only mild infection in
CC point-inoculated spikelets of flowering wheat heads and impairs the
CC spreading to nearby spikelets (PubMed:28894236).
CC {ECO:0000269|PubMed:28894236}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. APG1/unc-51/ULK1 subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=SCB64773.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; HG970334; SCB64773.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_011324096.1; XM_011325794.1.
DR AlphaFoldDB; I1RNG8; -.
DR SMR; I1RNG8; -.
DR STRING; 5518.FGSG_05547P0; -.
DR GeneID; 23552726; -.
DR KEGG; fgr:FGSG_05547; -.
DR eggNOG; KOG0595; Eukaryota.
DR HOGENOM; CLU_006447_0_0_1; -.
DR InParanoid; I1RNG8; -.
DR PHI-base; PHI:1176; -.
DR Proteomes; UP000070720; Chromosome 3.
DR GO; GO:0034045; C:phagophore assembly site membrane; IEA:UniProtKB-SubCell.
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:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
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 3: Inferred from homology;
KW ATP-binding; Autophagy; Cytoplasm; Kinase; Membrane; Nucleotide-binding;
KW Protein transport; Reference proteome; Serine/threonine-protein kinase;
KW Transferase; Transport.
FT CHAIN 1..944
FT /note="Serine/threonine-protein kinase ATG1"
FT /id="PRO_0000443863"
FT DOMAIN 24..327
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 344..423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 443..475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 512..572
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 777..801
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 860..895
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 924..930
FT /note="Required for Cvt trafficking"
FT /evidence="ECO:0000250|UniProtKB:P53104"
FT REGION 925..944
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 428..431
FT /note="LIR"
FT /evidence="ECO:0000250|UniProtKB:P53104"
FT COMPBIAS 349..416
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 443..468
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 520..548
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 167
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 30..38
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 53
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 944 AA; 103814 MW; CE0B2ED06EF32824 CRC64;
MAGPQESSTS SGSRKSGSRA VGQFNIGSEI GKGSFAQVYL GWHKETKAAV AIKSVELERL
NKKLRENLYS EIQILKTLRH PHIVALHDCI ESTSHINLIM EYCELGDLSL FIKKREKLAT
HPATHDMARK YPSMPNSGLH EVVIRHFLKQ LTSALEFLRS KNYVHRDVKP QNLLLLPSQP
FRDQRSRPVM QASQDSLIPI SGLASLPMLK LADFGFARVL PSTSLADTLC GSPLYMAPEI
LRYERYDAKA DLWSVGTVLY EMSTGRPPFR ARNHVELLRK IEAAEDVIKF PREVSITPEL
KALIRSLLKR SPVERLSFEN FFTHQVVTSE IPGLVEDDIP KSLRQESRDP RSAFQSGSPS
LSSRSPRQTG HQSPTEALVS RSPRDQQPRS PQVGSPGGSR YARRSNESQR TTGNSPREGG
EGLGIRRPVA QHAMTAPVQQ VAYDSVTGRN RASPPTSLLD QVRRNRALSN PPITEEERAA
QDVALEREYV VVERRHVEVN ALADELAANE KLGDASQRSG PITRRYTQQG APTSTTGAIS
TPYSRNALAT QPRHDRKSSY EKSLSASPGS ASSAISKAIQ DASLRLFGFK VPPLRASPKG
PSPPLYQAFP TYPTPQAPVG LLGDGRNVQG TDEDGKAAQT IEELATRSDC VYGFAEVKYK
QLVPLAPSAD HILGGLEPEQ LVNEEDGLTV EAIVALSEEA LVLYVKSLTL LARAMDIASL
WWSKKSRGDT GTGLSAAAAQ TVVQRINAVV QWVRQRFNEV LEKSEIVRLK LTEAQKQLPD
DHPSHPSNHG TESIASSAGS PTKQVYLTPG ISAEKLMYDR ALEMSRAAAI DEVTNENLSG
CEISYITAIR MLEAVLDNDE GSGSETRRLS TGKEAEREAV KEVSGGELDS DEEAHVRKRR
LAAVRKKQQM IAEANSKTNL VYQQAVRRRS GDMTPRSVPS HASS
