ID   ATG7_PICAN              Reviewed;         628 AA.
AC   A7KAI6;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   25-MAY-2022, entry version 50.
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;
OS   Pichia angusta (Yeast) (Hansenula polymorpha).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Pichiaceae; Ogataea.
OX   NCBI_TaxID=870730;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=ATCC 34438 / CBS 4732 / DSM 70277 / JCM 3621 / NBRC 1476 / NRRL
RC   Y-5445;
RX   PubMed=17204848; DOI=10.4161/auto.3595;
RA   Meijer W.H., van der Klei I.J., Veenhuis M., Kiel J.A.K.W.;
RT   "ATG genes involved in non-selective autophagy are conserved from yeast to
RT   man, but the selective Cvt and pexophagy pathways also require organism-
RT   specific genes.";
RL   Autophagy 3:106-116(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, ECO:0000269|PubMed:17204848}.
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; EF102887; ABO31291.1; -; Genomic_DNA.
DR   AlphaFoldDB; A7KAI6; -.
DR   SMR; A7KAI6; -.
DR   PhylomeDB; A7KAI6; -.
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; 3.40.140.70; -; 1.
DR   InterPro; IPR006285; Atg7.
DR   InterPro; IPR032197; Atg7_N.
DR   InterPro; IPR042522; Atg7_N_1.
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; 2.
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; Transport;
KW   Ubl conjugation pathway.
FT   CHAIN           1..628
FT                   /note="Ubiquitin-like modifier-activating enzyme ATG7"
FT                   /id="PRO_0000317868"
FT   MOTIF           315..320
FT                   /note="GXGXXG motif"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        500
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   628 AA;  70004 MW;  38F053AFA688F5BD CRC64;
     MEPKYINTQS FVDSSFFVKL SQLKLDVLKL DQSSRPIHGY YNYKRLAPGQ APAINLNDIS
     FASGQELESQ LPARSAFIVS GEITNVNTLE EFKSQSKLEF LTRAGGKIID SIKNKAALQD
     PSLLAHFAVF SFADLKKYKF YYWFAFPTLH SEWHITSEGP LGGDAPDSQF SLIRDGKPVP
     LAQLNAVPTH SPLHVAFVDT SAVPDAYSYV LRNFLTMLAI YGYRDVVVDV HRDNQSSSRQ
     IALKLQSAVD SPKISGWERT SQGKLGPKLA DLGALIDPSQ LADQAIDLNL KLMKWRIVPT
     LDLDRIKATK CLLLGSGTLG SYVGRALLAW GVRKITFVDN GKVSFSNPVR QPLFNFIDCL
     DGGSPKAETA AENMKRIFPL VDAQGFTLEV PMAGHPITDE TKQKLDFDRL GELVQNHDVI
     FLLMDSRETR WLPTVMGNVN NKLVINAALG FESYLVMRHG CINPEKLPEE QQESRLGCYF
     CNDVYAPSDS TTDRTLDQMC TVTRPGVALM AASLAVELMV SVLQHPDRQY APHSAQDSCT
     VLGSLPHQLR GFLHNFEMLK LSAKNFRYCS ACSVSVVQEF KSRGWEFVKQ ALENPKYLEQ
     LTGLTQVHQQ AEEAELNFDI SDSEGEFD