ID   ATG7_AJECN              Reviewed;         695 AA.
AC   A6QXC6;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   25-MAY-2022, entry version 67.
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=HCAG_02033;
OS   Ajellomyces capsulatus (strain NAm1 / WU24) (Darling's disease fungus)
OS   (Histoplasma capsulatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma;
OC   unclassified Histoplasma.
OX   NCBI_TaxID=2059318;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NAm1 / WU24;
RX   PubMed=19717792; DOI=10.1101/gr.087551.108;
RA   Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA   Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA   McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA   Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA   Henn M.R., Birren B.W., Taylor J.W.;
RT   "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT   and their relatives.";
RL   Genome Res. 19:1722-1731(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; CH476655; EDN04168.1; -; Genomic_DNA.
DR   RefSeq; XP_001544986.1; XM_001544936.1.
DR   AlphaFoldDB; A6QXC6; -.
DR   SMR; A6QXC6; -.
DR   STRING; 339724.A6QXC6; -.
DR   EnsemblFungi; EDN04168; EDN04168; HCAG_02033.
DR   GeneID; 5450897; -.
DR   KEGG; aje:HCAG_02033; -.
DR   VEuPathDB; FungiDB:HCAG_02033; -.
DR   HOGENOM; CLU_012998_2_1_1; -.
DR   OMA; VQTWRYS; -.
DR   OrthoDB; 549762at2759; -.
DR   Proteomes; UP000009297; 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..695
FT                   /note="Ubiquitin-like modifier-activating enzyme ATG7"
FT                   /id="PRO_0000317865"
FT   MOTIF           385..390
FT                   /note="GXGXXG motif"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        565
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   695 AA;  77535 MW;  6820EA0F53FB8540 CRC64;
     MQYTPFASDI ELPFYTSLAS LKINHDKLDD SARKLLGLYE IRSTDRPEAS CRMQIHGTAL
     TRDEVPFGYY RAEGMIKNVN TIEEYHNIDR NALLLQTGKM IWDAINDETI YSCPSLLVSF
     IVLSFADLKK YKFSYWFAFP AIHSAPSWTS VMDPKPLTGN ESSTLVDAVQ TWRYGVDARQ
     HGFFLARKDW HVVNSPSDGT VLNKAHVDNQ QSLSPIAKEL GFSWKISSIS DFETGFFHDA
     LPEDCFVCFA DPSNYPDAPG WMLRNLLVLV RQRWKLNEVY ILRYRDVQSK RDQGRSVVLK
     LRSDTAHLDP NDSRLGSQMP MPKVTGWERN AAGKLTGRVT NLTEYMDPRR LADQSVDLNL
     KLMKWRISPN LNLENIKNTK CLLLGAGTLG SYVARNLLGW GVRKITFVDN GTVSFSNPVR
     QPLFGFNDCL GGGAKKALRA AAALEEIYPG VDASGYVLSV PMPGHPITDA SKAELEFKEL
     KKLVDEHDAI FVLLDTREAR WLPTVMGKAT GKIVMNAALG FDTYVVMRHG VENCSAPETE
     LGCYFCNDVV APADSIKDQT LDQQCTVTRP GIAAIASALL VELFVSVLQH PDGPAAPASI
     PKQESRTDHP LGIVPHQIRG FLSNFSNVIV SGKSYNCCSA CSGNIMDAYK NHGWDFVRKA
     VNERNYVEEL SGLKEVSLSL KKRVVIGTKF HRSSV