ID   ATG7_BOTF1              Reviewed;         765 AA.
AC   M7U9B9;
DT   25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2013, sequence version 1.
DT   25-MAY-2022, entry version 31.
DE   RecName: Full=Ubiquitin-like modifier-activating enzyme atg7 {ECO:0000303|PubMed:29417220};
DE   AltName: Full=ATG12-activating enzyme E1 atg7 {ECO:0000303|PubMed:29417220};
DE   AltName: Full=Autophagy-related protein 7 {ECO:0000303|PubMed:29417220};
GN   Name=atg7 {ECO:0000303|PubMed:29417220}; ORFNames=BcDW1_1144;
OS   Botryotinia fuckeliana (strain BcDW1) (Noble rot fungus) (Botrytis
OS   cinerea).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Sclerotiniaceae; Botrytis.
OX   NCBI_TaxID=1290391;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BcDW1;
RX   PubMed=23704180; DOI=10.1128/genomea.00252-13;
RA   Blanco-Ulate B., Allen G., Powell A.L., Cantu D.;
RT   "Draft genome sequence of Botrytis cinerea BcDW1, inoculum for noble rot of
RT   grape berries.";
RL   Genome Announc. 1:E0025213-E0025213(2013).
RN   [2]
RP   FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH ATG7, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=29417220; DOI=10.1007/s00294-018-0810-3;
RA   Ren W., Sang C., Shi D., Song X., Zhou M., Chen C.;
RT   "Ubiquitin-like activating enzymes BcAtg3 and BcAtg7 participate in
RT   development and pathogenesis of Botrytis cinerea.";
RL   Curr. Genet. 64:919-930(2018).
CC   -!- FUNCTION: E1-like activating enzyme involved in the 2 ubiquitin-like
CC       systems required for cytoplasm to vacuole transport (Cvt) and autophagy
CC       (PubMed:29417220). Activates ATG12 for its conjugation with ATG5 and
CC       ATG8 for its conjugation with phosphatidylethanolamine (By similarity).
CC       Both 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. 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 (By similarity). Required for
CC       normal mycelial growth and conidiogenesis, and regulates sclerotial
CC       formation (PubMed:29417220). Plays an essential role in pathogenesis
CC       (PubMed:29417220). {ECO:0000250|UniProtKB:P38862,
CC       ECO:0000269|PubMed:29417220}.
CC   -!- SUBUNIT: Homodimer (By similarity). Interacts with ATG8 through a
CC       thioester bond between Cys-616 and the C-terminal Gly of ATG8 and with
CC       ATG12 through a thioester bond between Cys-616 and the C-terminal Gly
CC       of ATG12 (By similarity). Interacts also with ATG3 (PubMed:29417220).
CC       {ECO:0000250|UniProtKB:P38862, ECO:0000269|PubMed:29417220}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:29417220}.
CC       Preautophagosomal structure {ECO:0000269|PubMed:29417220}.
CC   -!- DOMAIN: The C-terminal residues 721 to 760 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: Blocks the autophagic process (PubMed:29417220).
CC       Leads to fewer aerial hyphae and slower mycelial growth rate and fails
CC       to produce any conidia (PubMed:29417220). Reduces also the production
CC       of sclerotia in cold environment (PubMed:29417220). Fails to infect
CC       wounded cucumber leaves and shows only slight virulence on wounded
CC       tomato and grape fruits (PubMed:29417220).
CC       {ECO:0000269|PubMed:29417220}.
CC   -!- SIMILARITY: Belongs to the ATG7 family. {ECO:0000305}.
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DR   EMBL; KB707707; EMR90329.1; -; Genomic_DNA.
DR   AlphaFoldDB; M7U9B9; -.
DR   SMR; M7U9B9; -.
DR   STRING; 1290391.M7U9B9; -.
DR   EnsemblFungi; EMR90329; EMR90329; BcDW1_1144.
DR   HOGENOM; CLU_012998_2_1_1; -.
DR   Proteomes; UP000012045; Unassembled WGS sequence.
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   1: Evidence at protein level;
KW   Autophagy; Cytoplasm; Protein transport; Reference proteome; Transport;
KW   Ubl conjugation pathway.
FT   CHAIN           1..765
FT                   /note="Ubiquitin-like modifier-activating enzyme atg7"
FT                   /id="PRO_0000443881"
FT   REGION          646..670
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          721..760
FT                   /note="Homodimerization"
FT                   /evidence="ECO:0000250|UniProtKB:P38862"
FT   REGION          744..765
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           436..441
FT                   /note="GXGXXG motif"
FT                   /evidence="ECO:0000250|UniProtKB:P38862"
FT   COMPBIAS        748..765
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        616
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:P38862"
SQ   SEQUENCE   765 AA;  85721 MW;  C4DF7F842EF28D65 CRC64;
     MNLPEYHRLA AYITSDHSQD YTQDTNVAFI EEGPWDGEEE ELITSFSTVE DLYTAICVRE
     DNNQLDMALK FAPFASEIEL PFYTALSQLK IDHDKLDDSA RPVLGLYEPR ATQSPDQSSR
     MRVLGNALSS NEVPSGHIRA EGKIKNVNTI EDFKNMDKQA MLQTSAKQIW DAINDGTIYS
     IPSLLSSFTI LSFANLKKYT FTYWFAFPAL HSEPAWRKVE QPPKFSAEET TALTEELGTW
     RYSHDNREHG FFLAKRVYPS SEHPQDPESE STSDLPFKWV IGSLREFESG FFNGVDAKNQ
     YVSFVDPSTY HENPGWMLRN LLVLVRRRYK LDKVQILCYR DNHAKRHVPQ SLILILESIY
     DPEYQSTAPD QIPKVTGWER NSLGKLTAKV TNLAQYMDPA QLADQAVDLN LKLMKWRIAP
     ELNLDAIKNT KCLLLGAGTL GTYVSRLLMG WGVRKITFVD NASVSFSNPV RQPLFDFKDC
     IDGGAKKAYR ASEALQEIYP GVDSTGHVMA VPMLGHPITD EAATKMNFEL LQKLIEDHDA
     IFLLMDTRES RWLPTVMGKA AGKIVMNAAL GFDTYVVMRH GVTPEDGGPA ALGCYFCNDV
     VAPSDSVKDQ TLDQQCTVTR PGVAPEASSK LVELLASVLQ HPLKGAAPAP KLSSNHQSGQ
     LEFDRDPPNH PLGLVPHQIR GFLAAYKTML ISGPSYDCCS ACSPKIVNAY KEDGWEFIKR
     ALTEKDYITE LSGLAEVQRK AEAAANDVEW DSDEEGMEDE EPELL