ID   ATG7_SCLS1              Reviewed;         683 AA.
AC   A7EI75;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   25-MAY-2022, entry version 79.
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=SS1G_05017;
OS   Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold)
OS   (Whetzelinia sclerotiorum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Sclerotiniaceae; Sclerotinia.
OX   NCBI_TaxID=665079;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 18683 / 1980 / Ss-1;
RX   PubMed=21876677; DOI=10.1371/journal.pgen.1002230;
RA   Amselem J., Cuomo C.A., van Kan J.A.L., Viaud M., Benito E.P., Couloux A.,
RA   Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA   Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.-M.,
RA   Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA   Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA   Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA   Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA   Grossetete S., Gueldener U., Henrissat B., Howlett B.J., Kodira C.,
RA   Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA   Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA   Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA   Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA   Zeng Q., Rollins J.A., Lebrun M.-H., Dickman M.;
RT   "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT   sclerotiorum and Botrytis cinerea.";
RL   PLoS Genet. 7:E1002230-E1002230(2011).
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; CH476626; EDO02541.1; -; Genomic_DNA.
DR   RefSeq; XP_001593590.1; XM_001593540.1.
DR   AlphaFoldDB; A7EI75; -.
DR   SMR; A7EI75; -.
DR   STRING; 665079.A7EI75; -.
DR   EnsemblFungi; EDO02541; EDO02541; SS1G_05017.
DR   GeneID; 5490255; -.
DR   KEGG; ssl:SS1G_05017; -.
DR   eggNOG; KOG2337; Eukaryota.
DR   HOGENOM; CLU_012998_2_1_1; -.
DR   InParanoid; A7EI75; -.
DR   OMA; VQTWRYS; -.
DR   Proteomes; UP000001312; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0000407; C:phagophore assembly site; IBA:GO_Central.
DR   GO; GO:0019778; F:Atg12 activating enzyme activity; IBA:GO_Central.
DR   GO; GO:0019779; F:Atg8 activating enzyme activity; IBA:GO_Central.
DR   GO; GO:0000045; P:autophagosome assembly; IBA:GO_Central.
DR   GO; GO:0000422; P:autophagy of mitochondrion; IBA:GO_Central.
DR   GO; GO:0006501; P:C-terminal protein lipidation; IBA:GO_Central.
DR   GO; GO:0006995; P:cellular response to nitrogen starvation; IBA:GO_Central.
DR   GO; GO:0044805; P:late nucleophagy; IBA:GO_Central.
DR   GO; GO:0034727; P:piecemeal microautophagy of the nucleus; IBA:GO_Central.
DR   GO; GO:0032446; P:protein modification by small protein conjugation; IBA:GO_Central.
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..683
FT                   /note="Ubiquitin-like modifier-activating enzyme atg7"
FT                   /id="PRO_0000317871"
FT   REGION          566..587
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          663..683
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           354..359
FT                   /note="GXGXXG motif"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        665..683
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        534
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   683 AA;  76121 MW;  FB2057015B39E5CC CRC64;
     MALKFAPFAS EIELPFYTAL SQLKIDHDKL DDSARPVLGL YEPRATQSPD QSSRMRVLGN
     ALSSTEVPLG HIRAEGIIKN VNTIEDFKNT DKQAMLQTSA KQIWDAINDG TIYSIPSLLS
     SFTILSFANL KKYTFTYWFA FPALHSEPAW KKVEQPPKFS AEETTALTEE LAKRVYPSLE
     QPQDPENESN SDLPFKWVIG SLREFEDGFF NGVDAKDQYV SFVDPSTYLE NPGWMLRNLL
     VLIRRRYKLD KVQILCYRDN HAKRHVPQSL ILVLESIYDP EYQSTGPDET PKVTGWERNS
     LGKLTAKVTN LAQYMDPAQL ADQAVDLNLK LMKWRIAPEL DLDAIKNTKC LLLGAGTLGT
     YVSRLLMGWG VRKITFIDNA SVSFSNPVRQ PLFDFKDCID GGAKKAYRAA EALQEIYPGV
     DSTGHVMSVP MLGHPITDEA ATKMDFELLQ KLVEDHDAIF LLMDTRESRW LPTVMGKAAG
     KIVMNAALGF DTYVVMRHGV TPEDGGPAAL GCYFCNDVVA PSDSVKDQTL DQQCTVTRPG
     VAPEASSKLV ELLASVLQHP LRGAAPAPKL SANQQSGQME FDRDPPNHPL GLVPHQIRGF
     LSAYKTMLIS GPSYDCCSAC SPKIVNAYKE DGWEFIKRAL TEKDYITELS GLAEVQRKAE
     EAANDVEWDS EEEGVEDEEA ELL