ID   ATG7_GIBZE              Reviewed;         694 AA.
AC   I1S0J7;
DT   25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2012, sequence version 1.
DT   25-MAY-2022, entry version 55.
DE   RecName: Full=Ubiquitin-like modifier-activating enzyme ATG7 {ECO:0000250|UniProtKB:P38862};
DE   AltName: Full=ATG12-activating enzyme E1 ATG7 {ECO:0000250|UniProtKB:P38862};
DE   AltName: Full=Autophagy-related protein 7 {ECO:0000303|PubMed:28894236};
GN   Name=ATG7 {ECO:0000303|PubMed:28894236};
GN   ORFNames=FG10226, FGRAMPH1_01T07585;
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: E1-like activating enzyme involved in the 2 ubiquitin-like
CC       systems required for cytoplasm to vacuole transport (Cvt) and autophagy
CC       (By similarity). Activates ATG12 for its conjugation with ATG5 and ATG8
CC       for its conjugation with phosphatidylethanolamine (By similarity). Both
CC       systems are needed for the ATG8 association to Cvt vesicles and
CC       autophagosomes membranes (By similarity). Autophagy is essential for
CC       maintenance of amino acid levels and protein synthesis under nitrogen
CC       starvation (By similarity). Required for selective autophagic
CC       degradation of the nucleus (nucleophagy) as well as for mitophagy which
CC       contributes to regulate mitochondrial quantity and quality by
CC       eliminating the mitochondria to a basal level to fulfill cellular
CC       energy requirements and preventing excess ROS production (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:P38862,
CC       ECO:0000269|PubMed:28894236}.
CC   -!- SUBUNIT: Homodimer (By similarity). Interacts with ATG8 through a
CC       thioester bond between Cys-550 and the C-terminal 'Gly-116' of ATG8 and
CC       with ATG12 through a thioester bond between Cys-550 and the C-terminal
CC       'Gly-160' of ATG12 (By similarity). Interacts also with ATG3 (By
CC       similarity). {ECO:0000250|UniProtKB:P38862}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P38862}.
CC       Preautophagosomal structure {ECO:0000250|UniProtKB:P38862}.
CC   -!- DOMAIN: The C-terminal residues 650 to 689 are required for
CC       homodimerization, as well as the interactions with ATG3, ATG8 and
CC       ATG12; and the C-terminal 17 residues are required for the ATG8
CC       lipidation (By similarity). {ECO:0000250|UniProtKB:P38862}.
CC   -!- DOMAIN: The GxGxxG motif is important for the function, possibly
CC       through binding with ATP (By similarity).
CC       {ECO:0000250|UniProtKB:P38862}.
CC   -!- DISRUPTION PHENOTYPE: Significantly decreases the radial growth of
CC       colonies under nutrient-rich conditions (PubMed:28894236). Causes only
CC       mild infection in point-inoculated spikelets of flowering wheat heads
CC       and impairs the spreading to nearby spikelets (PubMed:28894236).
CC       Reduces strongly the production of deoxynivalenol (DON), an important
CC       virulence determinant (PubMed:28894236). {ECO:0000269|PubMed:28894236}.
CC   -!- SIMILARITY: Belongs to the ATG7 family. {ECO:0000305}.
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DR   EMBL; HG970332; CEF75596.1; -; Genomic_DNA.
DR   RefSeq; XP_011319173.1; XM_011320871.1.
DR   AlphaFoldDB; I1S0J7; -.
DR   SMR; I1S0J7; -.
DR   STRING; 5518.FGSG_10226P0; -.
DR   GeneID; 23557142; -.
DR   KEGG; fgr:FGSG_10226; -.
DR   VEuPathDB; FungiDB:FGRAMPH1_01G07585; -.
DR   eggNOG; KOG2337; Eukaryota.
DR   HOGENOM; CLU_012998_2_1_1; -.
DR   InParanoid; I1S0J7; -.
DR   Proteomes; UP000070720; Chromosome 1.
DR   GO; GO:0000407; C:phagophore assembly site; IEA:UniProtKB-SubCell.
DR   GO; GO:0008641; F:ubiquitin-like modifier activating enzyme activity; IEA:InterPro.
DR   GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.140.100; -; 1.
DR   Gene3D; 3.40.140.70; -; 1.
DR   InterPro; IPR006285; Atg7.
DR   InterPro; IPR032197; Atg7_N.
DR   InterPro; IPR042522; Atg7_N_1.
DR   InterPro; IPR042523; Atg7_N_2.
DR   InterPro; IPR045886; ThiF/MoeB/HesA.
DR   InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR   InterPro; IPR035985; Ubiquitin-activating_enz.
DR   PANTHER; PTHR10953; PTHR10953; 1.
DR   Pfam; PF16420; ATG7_N; 1.
DR   Pfam; PF00899; ThiF; 1.
DR   SUPFAM; SSF69572; SSF69572; 1.
DR   TIGRFAMs; TIGR01381; E1_like_apg7; 1.
PE   3: Inferred from homology;
KW   Autophagy; Cytoplasm; Protein transport; Reference proteome; Transport;
KW   Ubl conjugation pathway.
FT   CHAIN           1..694
FT                   /note="Ubiquitin-like modifier-activating enzyme ATG7"
FT                   /id="PRO_0000443880"
FT   REGION          650..689
FT                   /note="Homodimerization"
FT                   /evidence="ECO:0000250|UniProtKB:P38862"
FT   MOTIF           370..375
FT                   /note="GXGXXG motif"
FT                   /evidence="ECO:0000250|UniProtKB:P38862"
FT   ACT_SITE        550
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:P38862"
SQ   SEQUENCE   694 AA;  77814 MW;  7E1227B40AA7C78E CRC64;
     MAKPLQFAPF ISEIELPFYS ALFASKLDHD KLDDSARSVL GLYEPRSEEP ESSCRLQILG
     NALTSGKTNE PSSPLATMRA EGIIRNVNTL EDFKNTDKPA MLRTAGRQVW DAIKDGSIYS
     VPSLLSSFII LSYADLKKYK FTYWFAFPAL HSDPVWKRSG PAERLTSQET TALVDRVGTW
     RYSVDARERG FFLAKKVPGR RETDDPDTPQ ELPFHWEIGS LRDFETGFFD QVPEEDRYVA
     FTDPSTYPEA PGWPLRNFLI LIRHRFRLTK TKVICYRDTW AKRHEAKSVI LTIEMDPVEN
     LDITEMPKVT GWARSSNGKL QAQQVNLGEY MDPARLADSS VDLNLKLMKW RIAPNLNLET
     IKNTKCLLLG AGTLGSYVSR NLMGWGVRKI TFVDYGRVSF SNPVRQPLFN FNDCLEGGKP
     KALRAAEALK EIYPGVDSEG HALSVPMLGH PFTDETKTKE DYQKLEKLIN EHDAIFLLMD
     SRESRWLPTV MGKAAGKIVM NAALGFDSYV VMRHGAETSP EGQTPLGCYF CNDVVAPADS
     QKDQTLDQQC TVTRPGVAPI ASALLVELLT SLLQHPLGKD APAPQPTSGV IPERDPPDHA
     LGLVPHQIRG YTSTFQQIVI RGQSYDCCSA CSPKILNAYR HDGWGFVKRA LQEKEYVAEL
     SGLAEVQRRA EEMAAHVDWE EDDDLVDDGE GELI