ID   ATG7_CANAL              Reviewed;         639 AA.
AC   Q59PZ3; A0A1D8PTA1; Q59Q11;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2017, sequence version 2.
DT   25-MAY-2022, entry version 96.
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=APG7; Synonyms=ATG7; OrderedLocusNames=CAALFM_CR06730WA;
GN   ORFNames=CaO19.707, CaO19.8326;
OS   Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=237561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA   Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA   Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA   Scherer S.;
RT   "The diploid genome sequence of Candida albicans.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA   van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA   Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA   Chibana H., Nantel A., Magee P.T.;
RT   "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT   on the eight chromosomes.";
RL   Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA   Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT   "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT   specific measurements and provides a simple model for repeat and indel
RT   structure.";
RL   Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
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; CP017630; AOW31370.1; -; Genomic_DNA.
DR   RefSeq; XP_711780.2; XM_706688.2.
DR   AlphaFoldDB; Q59PZ3; -.
DR   SMR; Q59PZ3; -.
DR   STRING; 237561.Q59PZ3; -.
DR   GeneID; 3646615; -.
DR   KEGG; cal:CAALFM_CR06730WA; -.
DR   CGD; CAL0000178896; APG7.
DR   VEuPathDB; FungiDB:CR_06730W_A; -.
DR   eggNOG; KOG2337; Eukaryota.
DR   HOGENOM; CLU_012998_2_1_1; -.
DR   InParanoid; Q59PZ3; -.
DR   OMA; VQTWRYS; -.
DR   OrthoDB; 549762at2759; -.
DR   PRO; PR:Q59PZ3; -.
DR   Proteomes; UP000000559; Chromosome R.
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..639
FT                   /note="Ubiquitin-like modifier-activating enzyme ATG7"
FT                   /id="PRO_0000212811"
FT   MOTIF           322..327
FT                   /note="GXGXXG motif"
FT   ACT_SITE        502
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   639 AA;  72863 MW;  56429D133303DB63 CRC64;
     MSNHSDQIVK KYILNQSFVE SSFFTKLSEL KLEKYKLDSS YIAIHGFQTH PTKLNKFNDT
     PVLNLDQSSF DDTLNDSRIN IPGELFNVNT IEEFKSLDKL KLLNTWGQNV YSEVTNATSF
     DYKLFNKFYI LTYSDLKKYK FYYWVAYPTL SNTWTVESES QETDTTITQL VETELDNEYG
     QFFQYYGGKL HKSVQADKEH TFVFIDTCLS KDRKPSSQLK NYLYFIAYKG IKEIDLVTYR
     NNNLSFTQHL KLDAFTDSPK ISGWERTNQG KLGPKLADLG SLINPLQLAE QAVELNLKLM
     KWRIAPDIDL EIIKKQKVLL LGAGTLGSYV ARALLGWGVR SITFVDSGRI SFSNPVRQPL
     FNFEDCFSDS GQGEYKALRA AENLKRVFPG VDAKGICLAV PMVGHPVTDE HKERENYETL
     VKLFEEHDVI FLLMDSRESR WLPTLIGAAN EKIVINAALG FDSYLVMRHG VTNQKDRLGC
     YYCNDVVAPN DSLSDRTLDQ MCTVTRPGGA LMASSLAVEL LVAILQHPER NLAPHDAETK
     FGNIPHQIRG FLHNFQQTKL FAPSYVHCSA CSPRVITEFK QEGWEFVRKC LDDSQYLEDI
     SGLTKVQQEA ELAAKQLLED LSLDDDVSND IDEDSEWLS