ID A0A091PFH0_APAVI Unreviewed; 699 AA.
AC A0A091PFH0;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=Ubiquitin-like modifier-activating enzyme ATG7 {ECO:0000256|ARBA:ARBA00017647, ECO:0000256|RuleBase:RU366022};
DE AltName: Full=Autophagy-related protein 7 {ECO:0000256|RuleBase:RU366022};
DE Flags: Fragment;
GN ORFNames=N311_01101 {ECO:0000313|EMBL:KFP90235.1};
OS Apaloderma vittatum (Bar-tailed trogon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Trogoniformes; Trogonidae; Apaloderma.
OX NCBI_TaxID=57397 {ECO:0000313|EMBL:KFP90235.1, ECO:0000313|Proteomes:UP000054244};
RN [1] {ECO:0000313|EMBL:KFP90235.1, ECO:0000313|Proteomes:UP000054244}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N311 {ECO:0000313|EMBL:KFP90235.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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 as well as the
CC ATG8 family proteins for their conjugation with
CC phosphatidylethanolamine. Both systems are needed for the ATG8
CC association to Cvt vesicles and autophagosomes membranes. Required for
CC autophagic death induced by caspase-8 inhibition. Required for
CC mitophagy which contributes to regulate mitochondrial quantity and
CC quality by eliminating the mitochondria to a basal level to fulfill
CC cellular energy requirements and preventing excess ROS production.
CC Modulates p53/TP53 activity to regulate cell cycle and survival during
CC metabolic stress. {ECO:0000256|RuleBase:RU366022}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|RuleBase:RU366022}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU366022}.
CC Preautophagosomal structure {ECO:0000256|RuleBase:RU366022}.
CC -!- SIMILARITY: Belongs to the ATG7 family. {ECO:0000256|ARBA:ARBA00010931,
CC ECO:0000256|RuleBase:RU366022}.
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DR EMBL; KL386900; KFP90235.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091PFH0; -.
DR Proteomes; UP000054244; 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-UniRule.
DR CDD; cd01486; Apg7; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.40.140.100; Ubiquitin-like modifier-activating enzyme ATG7 C-terminal domain; 1.
DR Gene3D; 3.40.140.70; Ubiquitin-like modifier-activating enzyme ATG7 N-terminal domain; 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 NCBIfam; TIGR01381; E1_like_apg7; 1.
DR PANTHER; PTHR10953; UBIQUITIN-ACTIVATING ENZYME E1; 1.
DR PANTHER; PTHR10953:SF3; UBIQUITIN-LIKE MODIFIER-ACTIVATING ENZYME ATG7; 1.
DR Pfam; PF16420; ATG7_N; 1.
DR Pfam; PF00899; ThiF; 1.
DR SUPFAM; SSF69572; Activating enzymes of the ubiquitin-like proteins; 1.
PE 3: Inferred from homology;
KW Autophagy {ECO:0000256|ARBA:ARBA00023006, ECO:0000256|RuleBase:RU366022};
KW Cytoplasm {ECO:0000256|RuleBase:RU366022};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927,
KW ECO:0000256|RuleBase:RU366022};
KW Reference proteome {ECO:0000313|Proteomes:UP000054244};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU366022};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU366022}.
FT DOMAIN 19..329
FT /note="Ubiquitin-like modifier-activating enzyme Atg7 N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF16420"
FT DOMAIN 345..605
FT /note="THIF-type NAD/FAD binding fold"
FT /evidence="ECO:0000259|Pfam:PF00899"
FT ACT_SITE 578
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR606285-1"
FT NON_TER 699
FT /evidence="ECO:0000313|EMBL:KFP90235.1"
SQ SEQUENCE 699 AA; 77767 MW; 4F16718946033C47 CRC64;
MATASSEVHH PVDPGIPKLQ FAPFSSALDA GFWHELTQKK LNEYRLDETP KVIKGYYYNG
DPLGLPARLT LEFSAFDMNA SIPARCCPAF GTLYNTNTFE TFKSCDKKSL LEKEANEIWE
SIKSGAALEN PMLLNRFLLL TFADLKKYNF YYWFCYPALC FPDGIHIIQK PVCLGDRFPL
NQIQALQKAY DELCQKESVT ALPYFLIKYH DNSVEISLLK KWENFFQDQG GKVTVGVYDP
CNLSHYPGWP LRNFLILAAH KWGSILQSIE VLCFRDRTMQ GVRDITHSII FEIKLPERAL
GPDCPKAVGW EKNQKGGMGP RMVNLSECMD PKRLAESSVD LNLKLMCWRL VPTLDLEKIV
SAKCLLLGAG TLGCSVARTL MGWGVRKITF VDNAKISYSN PVRQPLYEFE DCLSGGKPKA
LAAADRLQKI FPGVSSEGYN MSIPMPGHPV NFSEVTMAQA RKDVAKLEEL IDSHDVVFLL
MDTRESRWLP AVIAASKRKL VINAALGFDT FVVMRHGLKK PKQQESGDSC SNNASGSSDL
LGSSLFSNIP GYKLGCYFCN DVVAPGDSTR DRTLDQQCTV SRPGLAMVAG ALAVELMVSV
LQHPEGGYAV ASSSDDRMNE PPTSLGLVPH QIRGFLSRFD NVLPVSLAFD KCTACSTKVL
DQYEREGFNF LAKVFNSSHS FLEDLTGLTL LHQETQAAE
//