ID   ATG7_PENRW              Reviewed;         702 AA.
AC   A7KAL8; B6HK58;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 80.
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=Pc21g11380;
OS   Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin
OS   54-1255) (Penicillium chrysogenum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC   Penicillium chrysogenum species complex.
OX   NCBI_TaxID=500485;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
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).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255;
RX   PubMed=18820685; DOI=10.1038/nbt.1498;
RA   van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA   Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA   Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA   Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A., van der Klei I.J.,
RA   van Peij N.N.M.E., Veenhuis M., von Doehren H., Wagner C., Wortman J.R.,
RA   Bovenberg R.A.L.;
RT   "Genome sequencing and analysis of the filamentous fungus Penicillium
RT   chrysogenum.";
RL   Nat. Biotechnol. 26:1161-1168(2008).
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; EF107740; ABO31078.1; -; Genomic_DNA.
DR   EMBL; AM920436; CAP96035.1; -; Genomic_DNA.
DR   RefSeq; XP_002568170.1; XM_002568124.1.
DR   AlphaFoldDB; A7KAL8; -.
DR   SMR; A7KAL8; -.
DR   STRING; 1108849.XP_002568170.1; -.
DR   PRIDE; A7KAL8; -.
DR   EnsemblFungi; CAP96035; CAP96035; PCH_Pc21g11380.
DR   GeneID; 8309771; -.
DR   KEGG; pcs:Pc21g11380; -.
DR   VEuPathDB; FungiDB:PCH_Pc21g11380; -.
DR   eggNOG; KOG2337; Eukaryota.
DR   HOGENOM; CLU_012998_2_1_1; -.
DR   OMA; VQTWRYS; -.
DR   OrthoDB; 549762at2759; -.
DR   BioCyc; PCHR:PC21G11380-MON; -.
DR   Proteomes; UP000000724; Contig Pc00c21.
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..702
FT                   /note="Ubiquitin-like modifier-activating enzyme atg7"
FT                   /id="PRO_0000317867"
FT   REGION          143..167
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          201..222
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          295..319
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           387..392
FT                   /note="GXGXXG motif"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        205..222
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        298..319
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        566
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   702 AA;  78616 MW;  9493BBBD8097D540 CRC64;
     MQYAPFASDI ELPFYTSLAS HKINHDKLDD SARPVLGLYE IRPSDPEAAS CRIQIHGNAL
     TSSEAEGMIK NVNTVEEYRN MDRPHLLHQA GQMIWDAIHD GTILSCPSLL CSFVIVSFAD
     LKKYKFHYWF AFPAIHSDPQ WVPVQPTDQV SQSHQDHDID NLKGSHLSPH ESTALVEAVQ
     TWSYIVDHRQ RGFFLARKSR LRPDASSGDP QTKSAQQDTS NSNWQIASLS EYENGFFKNV
     ADEDCYFCFS DPSNYEQAPG WMLRNLLVLI KQRWGIERVQ LIRYRDVHAK RDQGRSTVIR
     LESSPKQEPQ TPKSLQTRES LPLPKVTGWE RNSTGKLAGR IVNLTEYMDP KRLADQSVDL
     NLKLIKWRIS PTLDLEKIKH TKCLLLGAGT LGSYVSRNLL GWGVKKITFV DNGTVSFSNP
     VRQPLFNFQD CLNGGARKAH RASEALTEIY PGVETTGHAL SVPMAGHPIV DERVTRADFD
     RLQTLIDGHD AIFLLMDTRE SRWLPTVMGK AAGKIVMNAA LGFDSFVVMR HGITEDEKPA
     ELGCYFCNDV VAPANSTKDQ TLDQQCTVTR PGVAPIASAL LVELFVSLLQ HPKGAGAPAP
     IARNTERDDH PLGAVPHQIR GFLSNFENLS VTGKSYPSCS ACSDKVVSAY REQGWDFVRR
     ALNEHGYVEE LSGLKEVHEK AEEALADIDW DEASDNEEIE IL