ATG7_ASHGO
ID ATG7_ASHGO Reviewed; 625 AA.
AC Q756G8;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 109.
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; OrderedLocusNames=AER298C;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(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; AE016818; AAS52979.1; -; Genomic_DNA.
DR RefSeq; NP_985155.1; NM_210509.1.
DR AlphaFoldDB; Q756G8; -.
DR SMR; Q756G8; -.
DR STRING; 33169.AAS52979; -.
DR PRIDE; Q756G8; -.
DR EnsemblFungi; AAS52979; AAS52979; AGOS_AER298C.
DR GeneID; 4621368; -.
DR KEGG; ago:AGOS_AER298C; -.
DR eggNOG; KOG2337; Eukaryota.
DR HOGENOM; CLU_012998_2_1_1; -.
DR InParanoid; Q756G8; -.
DR OMA; VQTWRYS; -.
DR Proteomes; UP000000591; Chromosome V.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
DR GO; GO:0097632; C:extrinsic component of phagophore assembly site membrane; IEA:EnsemblFungi.
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:0042802; F:identical protein binding; IEA:EnsemblFungi.
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:0032258; P:cytoplasm to vacuole transport by the Cvt pathway; IEA:EnsemblFungi.
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 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..625
FT /note="Ubiquitin-like modifier-activating enzyme ATG7"
FT /id="PRO_0000212810"
FT MOTIF 322..327
FT /note="GXGXXG motif"
FT ACT_SITE 498
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 625 AA; 70069 MW; 645041C6FD9ABFDC CRC64;
MSQSLKFAPP FQSFVDASFF QVFSRLKLDV LRLDSHELPL HAKVDLAGLA RGSSISHVFL
DSQSFDEATA SLPGISLRGS FFNFNTLEEF KRLDKGRFLS EQAQLLWEAG VNGYLDEAAG
FFVICFADLK KYRFYYWFAT PCFQPETLEL KVVKREALTE IDKFSNFIEQ NKILCGVLNE
ETGEVIRASR HELERYSTLV VRDTSNIEHC PTSLVKNFVA VWRHHNPNRS ECRVLLLRET
CSFSLELSVT GDAMSTSQLK ASGWERNVRG LLTPKISELG AIIDPTKLAE QSIDLNLKLM
KWRLVPDINL DIVKNCKVLL LGAGTLGCYV ARSLLAWGVR KITFVDNGSV SYSNPVRQPL
FNFTDCGQPK ATSAAAAMKA IFPLVDATGF QLEVPMIGHP LTDEARQKKD YEELRQLIRD
HDIVFLLMDS RETRWLPTIL GNLESKLVIN AALGFDSYLV MRHGNYEQPE SSRLGCYFCH
DVVAPSDSLT DRTLDEMCTV TRPGVALIAA AYATELAVSV LQHPQGNNAP ETSESVLGSV
PHQLRGFLPQ LSTVKLRTPA YKHCSACSSV IVDAVRENGW EFLREALVDH RIVERLSGLA
QVQQETETFL ATMEISDDDC FDEIS
