ID   ATG7_PICGU              Reviewed;         646 AA.
AC   A5DLC6;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 2.
DT   03-AUG-2022, entry version 76.
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=PGUG_04077;
OS   Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539
OS   / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX   NCBI_TaxID=294746;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL Y-324;
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA   Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA   Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA   Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA   Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA   Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA   Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA   Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA   Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA   Birren B.W., Kellis M., Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(2009).
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; CH408159; EDK39979.2; -; Genomic_DNA.
DR   RefSeq; XP_001483348.1; XM_001483298.1.
DR   AlphaFoldDB; A5DLC6; -.
DR   SMR; A5DLC6; -.
DR   STRING; 4929.XP_001483348.1; -.
DR   EnsemblFungi; EDK39979; EDK39979; PGUG_04077.
DR   GeneID; 5125358; -.
DR   KEGG; pgu:PGUG_04077; -.
DR   VEuPathDB; FungiDB:PGUG_04077; -.
DR   eggNOG; KOG2337; Eukaryota.
DR   HOGENOM; CLU_012998_2_1_1; -.
DR   InParanoid; A5DLC6; -.
DR   OMA; VQTWRYS; -.
DR   OrthoDB; 549762at2759; -.
DR   Proteomes; UP000001997; 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   3: Inferred from homology;
KW   Autophagy; Cytoplasm; Protein transport; Reference proteome; Transport;
KW   Ubl conjugation pathway.
FT   CHAIN           1..646
FT                   /note="Ubiquitin-like modifier-activating enzyme ATG7"
FT                   /id="PRO_0000317869"
FT   MOTIF           338..343
FT                   /note="GXGXXG motif"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        516
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   646 AA;  73318 MW;  B9FE5891CB1F3F2F CRC64;
     MIMTELRDLV GKPLKYVPTR SFVESSFFKA LSDLKLNQLK LNTDTVSISG FMNHPKNLTK
     FQDYPILNLD FSSFELASSA SSAASDENVE YKGTLLNVNT IEEFKAINKS DLLKQWGSLI
     YKSITEGDTT YRSVNQFFVL TFSDLKKYKF YYWFAYPSLQ SQWTVKECKE APSFEDETRK
     YLDTQEELEF FFAREQEEFC GLSKFLNGSK KVNEHSTFVF VDSCRHPGLY PGWQLKNFLY
     ILARQGMREI RLFVYRYDGT SIMMKLQLDS IPNDIKFMGW ERTKDDKLGP KLADLGSLID
     PIQLADQAVD LNLKLMKWRI SPQLNLEKVA QQKVLLLGSG TLGSYVARAL MGWGVRHITF
     VDNGRVSYSN PVRQPLFGFN DCFSDEGLGR WKAPRAAEAL KEIFPGVNSS AYNLEVPMIG
     HPVENEQSAK ANYETLERLV DENDAIFLLM DSRESRWLPT LLGMAKNKLV INAALGFDSF
     LVMRHGTTTN NLGCYYCNDV VAPSDSLSDR TLDQMCTVTR PGGALMASAL AVELLVSVLQ
     HPEGAEADAK EHSFFGEVPH QIRGFLHNFS QTKLYAPKYT HCSACSQPVV DSFRSQGWDF
     VKNCLNDTKH LERVCGLEEV QREAERASEA LLEQAAGLDL SDEEWL