ID   ATG7_PICST              Reviewed;         652 AA.
AC   A3LPA1;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 2.
DT   25-MAY-2022, entry version 83.
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=PICST_42095;
OS   Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS   Y-11545) (Yeast) (Pichia stipitis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX   NCBI_TaxID=322104;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545;
RX   PubMed=17334359; DOI=10.1038/nbt1290;
RA   Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA   Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.-S.,
RA   Passoth V., Richardson P.M.;
RT   "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT   yeast Pichia stipitis.";
RL   Nat. Biotechnol. 25:319-326(2007).
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; CP000496; ABN65006.2; -; Genomic_DNA.
DR   RefSeq; XP_001383035.2; XM_001382998.1.
DR   AlphaFoldDB; A3LPA1; -.
DR   SMR; A3LPA1; -.
DR   STRING; 4924.XP_001383035.2; -.
DR   EnsemblFungi; ABN65006; ABN65006; PICST_42095.
DR   GeneID; 4836974; -.
DR   KEGG; pic:PICST_42095; -.
DR   eggNOG; KOG2337; Eukaryota.
DR   HOGENOM; CLU_012998_2_1_1; -.
DR   InParanoid; A3LPA1; -.
DR   OMA; VQTWRYS; -.
DR   OrthoDB; 549762at2759; -.
DR   Proteomes; UP000002258; 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..652
FT                   /note="Ubiquitin-like modifier-activating enzyme ATG7"
FT                   /id="PRO_0000317870"
FT   MOTIF           340..345
FT                   /note="GXGXXG motif"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        522
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   652 AA;  73894 MW;  0B1104FBFB56DE35 CRC64;
     MSDSDKTAAR VAPKYVPISS FVESSFFTKL SELKLNEFKL DSSKRDIHGF ITSPRRLNKF
     NDQPTLNLDL QSFDIAEKEA NNLHISGELY NVNTIEEFKN INKSDLLNDW GKEVYTRLIQ
     TESLDYKAFN WFFILTFSDL KKYKFYYWVA FPTLNAPWFV TSTRDDSLVE KHTKNITRLL
     ENDGDSENLA FSQLYQVVGE SYLDLNSIRS SRNGVFVFLD GCLNKETKPS VQLKNYLYFL
     AYKGFEDVDV IVYRNDGSSF QVHYELDTDS FNKNVQPKIT GWERTSQGKL GPKLADLGSL
     INPHQLADQA VDLNLKLMKW RIAPELNLDI VKEQRVLLLG AGTLGSYVAR ALMGWGVRKI
     TFVDNGRISY SNPVRQPLFS FKDCFSDNGQ GEMKAARAAE ALKEIFPGVS SEGISLEVPM
     IGHPVSDEAK SKSNFGTLSQ LFDDHDIIYL LMDSRESRWL PTVLGYAKNK IVINAALGFD
     SYLVMRHGNL SQPEESRLGC YYCNDVVAPN DSLTDRTLDQ MCTVTRPGVA LMASALAVEL
     LVSILQHPDG SKAAQDESTK FGGVPHQIRG FLHNFQQTKL YAPNYKHCSA CSHTVISKFE
     EEGWEFVKKC LNDSGYLEEI CGLKQVQEEA EKATEDLMKD MDLDDEDSEW LD