ID   ATG7_VANPO              Reviewed;         626 AA.
AC   A7TEY0;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   25-MAY-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=Kpol_1050p86;
OS   Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS
OS   2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Vanderwaltozyma.
OX   NCBI_TaxID=436907;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 / NRRL
RC   Y-8283 / UCD 57-17;
RX   PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA   Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.;
RT   "Independent sorting-out of thousands of duplicated gene pairs in two yeast
RT   species descended from a whole-genome duplication.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(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; DS480381; EDO19226.1; -; Genomic_DNA.
DR   RefSeq; XP_001647084.1; XM_001647034.1.
DR   AlphaFoldDB; A7TEY0; -.
DR   SMR; A7TEY0; -.
DR   STRING; 436907.A7TEY0; -.
DR   EnsemblFungi; EDO19226; EDO19226; Kpol_1050p86.
DR   GeneID; 5547560; -.
DR   KEGG; vpo:Kpol_1050p86; -.
DR   eggNOG; KOG2337; Eukaryota.
DR   HOGENOM; CLU_012998_2_1_1; -.
DR   InParanoid; A7TEY0; -.
DR   OMA; VQTWRYS; -.
DR   OrthoDB; 549762at2759; -.
DR   PhylomeDB; A7TEY0; -.
DR   Proteomes; UP000000267; 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..626
FT                   /note="Ubiquitin-like modifier-activating enzyme ATG7"
FT                   /id="PRO_0000317872"
FT   MOTIF           322..327
FT                   /note="GXGXXG motif"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        498
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   626 AA;  70885 MW;  DF38FE7C96126605 CRC64;
     MNESTVKYST AFRSFFDTSF FQELSRLKLE VFKLSSEAQK LYSKVEPSKS SESSHLFFNG
     NSFNPDSISD ANSTSVIGSI FNFNKIEGFK DLDKHQFLQD RAIESWEAGL DDINKAVSFH
     VISFADLKKY KFIYWVCFPY FQLESLEISC TNVTEIENCA KYQDWFNNNR SQWVSIVDSN
     CEIGSYSKNA FNKNSKLLIR DTSKMKNTPS ALAKNFLSIF KYQNLEVKEI SVYFVREDDS
     SFQMSLKLSS IDNEVTPKLK TSGWEKNLLG RLAPLSIDLS TLIDPLKVAG QSVDLNLKLM
     KWRIAPDIDL DVIKERKVLI LGAGTLGCYV SRSLMAWGVR KLTLVDNGTV SFSNPVRQPL
     FEFNDEGKSK AEAAAASLKR IFPLMDATGV TLNIPMIGHV VSNEENIKKD YEKLLELIKE
     HDTIFLLMDS RETRWLPTVL GNIENKIVIN AALGFDSYLV MRHGNYYGNA EKRLGCYFCN
     DVVAPTDSLS DRTLDQMCTV TRPGVALMAS SLAVEVFVSI LQDEKRNNIS TEEKTVLGEV
     PHQLRGFLNN FTTLKLETPA YEHCSACSKP IIEVCQEQGW EFLKQALADP LLVERVSGLE
     KVKQEVEELA AKSFDWVSDD EELVEL