ID   ATG7_CANGA              Reviewed;         623 AA.
AC   Q6FQY7;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 107.
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; OrderedLocusNames=CAGL0I02420g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS   Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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; CR380955; CAG60294.1; -; Genomic_DNA.
DR   RefSeq; XP_447357.1; XM_447357.1.
DR   AlphaFoldDB; Q6FQY7; -.
DR   SMR; Q6FQY7; -.
DR   STRING; 5478.XP_447357.1; -.
DR   EnsemblFungi; CAG60294; CAG60294; CAGL0I02420g.
DR   GeneID; 2889381; -.
DR   KEGG; cgr:CAGL0I02420g; -.
DR   CGD; CAL0132204; CAGL0I02420g.
DR   VEuPathDB; FungiDB:CAGL0I02420g; -.
DR   eggNOG; KOG2337; Eukaryota.
DR   HOGENOM; CLU_012998_2_1_1; -.
DR   InParanoid; Q6FQY7; -.
DR   OMA; VQTWRYS; -.
DR   Proteomes; UP000002428; Chromosome I.
DR   GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
DR   GO; GO:0097632; C:extrinsic component of phagophore assembly site membrane; IEA:EnsemblFungi.
DR   GO; GO:0019778; F:Atg12 activating enzyme activity; IEA:EnsemblFungi.
DR   GO; GO:0019779; F:Atg8 activating enzyme activity; IEA:EnsemblFungi.
DR   GO; GO:0042802; F:identical protein binding; IEA:EnsemblFungi.
DR   GO; GO:0000422; P:autophagy of mitochondrion; IEA:EnsemblFungi.
DR   GO; GO:0006501; P:C-terminal protein lipidation; IEA:EnsemblFungi.
DR   GO; GO:0032258; P:cytoplasm to vacuole transport by the Cvt pathway; IEA:EnsemblFungi.
DR   GO; GO:0044805; P:late nucleophagy; IEA:EnsemblFungi.
DR   GO; GO:0016236; P:macroautophagy; IEA:EnsemblFungi.
DR   GO; GO:0034727; P:piecemeal microautophagy of the nucleus; IEA:EnsemblFungi.
DR   GO; GO:0032446; P:protein modification by small protein conjugation; IEA:EnsemblFungi.
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..623
FT                   /note="Ubiquitin-like modifier-activating enzyme ATG7"
FT                   /id="PRO_0000212812"
FT   MOTIF           327..332
FT                   /note="GXGXXG motif"
FT   ACT_SITE        499
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   623 AA;  70746 MW;  721C110E203E1F41 CRC64;
     MTQKLLYVSP VESFVDTSFF QELSRLKLDI HGLSTSQITI HSYLDLKNIP SVSSACHLFL
     DQQSFNSEDI CASSERVRLE GKLYNCNSLE EFKSLDKQQY LAEQGQKIYT KALEDINSAI
     GFSIISFADL KKYVFYYWVC TPLFQHENQQ ISILDGPEDI DASFNDKAKV WFTNHYSNWV
     AIVLENGDIN EYTKGLNTSS IRGLLIRDTS NKQDMPSAFL RNFITIFSLD YPEAKELDVF
     LMRSSTIKSI KLRIRLSETE HTKLKFSGWE RNSLSKLMPR AVDLSALIDP LKVAEQSVDL
     NLKLMKWRIA PELDLDCIRN NKVLILGSGT LGCYTARSLM AWGCRNITLV DNGRVSYSNP
     VRQPLFEFSD VGKEKAVAAA ASLKRVFPLI NAKGVQLDIP MIGHPVKDEN NERKHFDALV
     DLIKSHDTMF LLLDSRETRW LPTLLGKFYD KIVMNAALGF DSYLIMKHGN IDDNFGCYFC
     NDVVVPTDSL TGRTLDQMCT VTRPGVAMLA ASQAVELFVS NLQSRGQENV LGECPHQIRG
     FVNNFTTLKL QSPAYDNCSA CSRHILNEYN KRGWDFVKQA LNDNNYIEEL SGLRRIKEEV
     ENMELEGGEI KIIDSEDDGF EII