ATG7_DEBHA
ID ATG7_DEBHA Reviewed; 652 AA.
AC Q6BGV9;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 25-MAY-2022, entry version 101.
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=DEHA2G23518g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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; CR382139; CAG91073.2; -; Genomic_DNA.
DR RefSeq; XP_462562.2; XM_462562.1.
DR AlphaFoldDB; Q6BGV9; -.
DR SMR; Q6BGV9; -.
DR STRING; 4959.XP_462562.2; -.
DR PRIDE; Q6BGV9; -.
DR EnsemblFungi; CAG91073; CAG91073; DEHA2G23518g.
DR GeneID; 2905518; -.
DR KEGG; dha:DEHA2G23518g; -.
DR VEuPathDB; FungiDB:DEHA2G23518g; -.
DR eggNOG; KOG2337; Eukaryota.
DR HOGENOM; CLU_012998_2_1_1; -.
DR InParanoid; Q6BGV9; -.
DR OMA; VQTWRYS; -.
DR OrthoDB; 549762at2759; -.
DR Proteomes; UP000000599; Chromosome G.
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..652
FT /note="Ubiquitin-like modifier-activating enzyme ATG7"
FT /id="PRO_0000212814"
FT MOTIF 335..340
FT /note="GXGXXG motif"
FT ACT_SITE 519
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 652 AA; 74515 MW; 414804B0F85B2534 CRC64;
MSSVSASTER KHIKFTPIQS FVESSFFTKL SELKLDEFKL DSTKKEIKGF LTHPKRLNKF
NDYPTINFDY SSFDKGPDVN EDNNISWKGY IYNVNTIEEF KDIDKQAILK RWGTEIYNEI
QDGSVDLSYE CFNKVHVLAF CDLKKYKFYY WFAFPTLHSP WNIIGADGDS LKKFIPSIKE
FVETSKFVQF FQINDGNIIE RVSEFQESKI FVFIDTCLSQ ACTPSVQLKN YLYVLARKGF
ENIDLIIYRN NGNSFYWKLQ LDKDKLGINE VPRISGWERL SNGKLGPRLA DLGSLIDPQE
LAKQAVDLNL KLMKWRIAPN LDLDIIKNQR VLLLGAGTLG SYVSRALMGW GVRNITFVDN
GRISYSNPVR QPLFSFKDCF SDEGQGEWKA IRAANTLKEI FPDVQSKGYN LEVPMIGHPV
NNETKQKSSF DKLSDLFDDH DVVFLLMDSR ESRWLPTVLG LAKNKIVLNA ALGFDSFLVM
RHGNISNANN DDTRVGCYYC NDVVAPNDSL SDRTLDQMCT VTRPGVALMA SSLAVELFIS
MLQHPNKQYA EPGPSNNLIL GEVPHQIRGF LHNYSQSKLQ TPNYKHCSAC SKYVIDKFNE
LGWEFVKNCL NDVTYLEETC GLLKVQQEAD LASSELLKDL ELSDDDDSEW LD
