ID   ATG7_MAGO7              Reviewed;         714 AA.
AC   Q52CS0; A4RIA9; G4MUY4;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 2.
DT   25-MAY-2022, entry version 103.
DE   RecName: Full=Ubiquitin-like modifier-activating enzyme ATG7;
DE   AltName: Full=ATG12-activating enzyme E1 ATG7;
DE   AltName: Full=Autophagy-related protein 7;
GN   Name=ATG7; ORFNames=MGG_07297;
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 [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: E1-like activating enzyme involved in the 2 ubiquitin-like
CC       systems required for cytoplasm to vacuole transport (Cvt) and
CC       autophagy. Activates ATG12 for its conjugation with ATG5 and ATG8 for
CC       its conjugation with phosphatidylethanolamine. Both systems are needed
CC       for the ATG8 association to Cvt vesicles and autophagosomes membranes.
CC       Autophagy is essential for maintenance of amino acid levels and protein
CC       synthesis under nitrogen starvation. 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. Plays a role
CC       in the regulation of filamentous growth and chronological longevity (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Preautophagosomal
CC       structure {ECO:0000250}.
CC   -!- DOMAIN: The GxGxxG motif is important for the function, possibly
CC       through binding with ATP. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ATG7 family. {ECO:0000305}.
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DR   EMBL; CM001232; EHA55718.1; -; Genomic_DNA.
DR   RefSeq; XP_003715525.1; XM_003715477.1.
DR   AlphaFoldDB; Q52CS0; -.
DR   SMR; Q52CS0; -.
DR   STRING; 318829.MGG_07297T0; -.
DR   EnsemblFungi; MGG_07297T0; MGG_07297T0; MGG_07297.
DR   GeneID; 2683193; -.
DR   KEGG; mgr:MGG_07297; -.
DR   VEuPathDB; FungiDB:MGG_07297; -.
DR   eggNOG; KOG2337; Eukaryota.
DR   HOGENOM; CLU_012998_2_1_1; -.
DR   InParanoid; Q52CS0; -.
DR   OMA; VQTWRYS; -.
DR   OrthoDB; 549762at2759; -.
DR   PHI-base; PHI:2075; -.
DR   Proteomes; UP000009058; Chromosome 2.
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..714
FT                   /note="Ubiquitin-like modifier-activating enzyme ATG7"
FT                   /id="PRO_0000212817"
FT   REGION          591..616
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          691..714
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           380..390
FT                   /note="GXGXXG motif"
FT   COMPBIAS        694..714
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        565
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   714 AA;  79179 MW;  6942F8858D46030B CRC64;
     MSGNDEAAAA GVAPPQTLQF APFESQIEMP FYSALFSRKL DHDKLDDSVR PVIGLYQPMS
     ERPPAESTRM QIQGGALSSS HVPMGYTRAD GSIRNFNTIE DFKKADKGAI LRQAGAQIWD
     AIKDGSIYEI PSLLSSFAIL SYADLKKYRF TYWFAYPTLH SVPAWRRDGP LARFSSKETT
     ALVNEVGTFR YAHDTRQHGF FLAKKVPYRS GPFRRGLPRD DSDGDDIGFT WSIGALGEFE
     KGFFKGIKEE DQYIAFVDSS SYAENPSWPL RNLLVLIRQR FQLQKANILC YRDTQARRDE
     PRSIVLPLAS EGPATPQTSE MPKVTGWERH PSSKLQARVI SLAEYMDPTR IADQAVDLNL
     KLMKWRISPK LDLEAMRSLK CLLLGAGTLG SYVSRNLMGW GVRKITFVDY GNVSFSNPVR
     QPLFEFEDCL SGGVPKAPKA AEALKKINPG VEAEGHVLSV PMLGHPVLNE AQTKEDFEKL
     QQLIKAHDVV FLLMDTRESR WLPTVMGKAE GKIVMNAALG FDTYVVMRHG AAPKDGTEST
     LGCYFCNDVV APSDSMKDQT LDQQCTVTRP GVAAIASAML VEMLTSVLQH PQREHAPAPK
     ATGPPGNPEY QRDPPDHALG IVPHQVRGFL ANFQNMIISG ESYPNCSACS SPIVGAYKSD
     GWEFVKKALS DKDYVLELSG LAEVQRQAEA MQNEVDWDED EDVAAAEEGD GEML