ID   ATG7_LODEL              Reviewed;         664 AA.
AC   A5E0T7;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 79.
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=LELG_03224;
OS   Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC
OS   1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade;
OC   Lodderomyces.
OX   NCBI_TaxID=379508;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11503 / BCRC 21390 / CBS 2605 / JCM 1781 / NBRC 1676 / NRRL
RC   YB-4239;
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA   Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA   Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA   Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA   Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA   Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA   Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA   Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA   Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA   Birren B.W., Kellis M., Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(2009).
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; CH981527; EDK45045.1; -; Genomic_DNA.
DR   RefSeq; XP_001525296.1; XM_001525246.1.
DR   AlphaFoldDB; A5E0T7; -.
DR   SMR; A5E0T7; -.
DR   STRING; 379508.A5E0T7; -.
DR   PRIDE; A5E0T7; -.
DR   EnsemblFungi; EDK45045; EDK45045; LELG_03224.
DR   GeneID; 5232875; -.
DR   KEGG; lel:LELG_03224; -.
DR   VEuPathDB; FungiDB:LELG_03224; -.
DR   eggNOG; KOG2337; Eukaryota.
DR   HOGENOM; CLU_012998_2_1_1; -.
DR   InParanoid; A5E0T7; -.
DR   OMA; VQTWRYS; -.
DR   OrthoDB; 549762at2759; -.
DR   Proteomes; UP000001996; Unassembled WGS sequence.
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..664
FT                   /note="Ubiquitin-like modifier-activating enzyme ATG7"
FT                   /id="PRO_0000317866"
FT   MOTIF           331..336
FT                   /note="GXGXXG motif"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        514
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   664 AA;  75132 MW;  1B1A2B0F36210FA0 CRC64;
     MGSDLNTLRF TPIQSFVDSS FFAKLARLKL EKFKLDSSTQ YICGFQTRPS KLNKFDDIPT
     LALDEQSFVE EEIGKDSIAN DRLITSGSIT NLNTIEEFKA ISKQDLLHSW GEDLYQQIMA
     NDTFEYKIFQ SFKVLSYSDL KKYKFYYWVS FPTLQSSWTI LERNDVINSG IQQDIDSQTK
     YLNGQFYQLR EGRLDTQIED SSNTELVPTF VFLDSCLSQS KRPSAQLKNY LFYLAKKKGY
     SEIKVIVYRN NAASFLLKLK LQECPDPWKV VGWERTSQGK LGPKLADLGL LSDPTQLASQ
     AVDLNLKLMK WRVAPELDLD IIKQQKVLLL GAGTLGCYVA RALLGWGVCN IKFVDSGRVS
     YSNPVRQPLF NFEDCFSDNG RGMPKASAAA NALKKIFPGV NAQGYEIEVP MIGHPITDEQ
     KQGSQYGVLD DLFNQSDVVF LLMDSREARW LPTVMGVAKG KIVINAALGF DSYLVMRHGN
     ISSLKDKLRL GCYFCNDIVA PEDSLSDRTL DQMCTVTRPG AALMASSLAV ELLVSILQHP
     DKSFANAVEN NDDRKKHEEK VEKFSKFGAC PHQIRGFLNT FSQNKFHIPN YEHCSACSQK
     VVDQYIQNGW EFVKDCLNNQ GYLEELCGLS KVQEEAELAA QQLLEELSFE EKGEIDSEDL
     DWIN