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Database: UniProt
Entry: A0A091PFH0_APAVI
LinkDB: A0A091PFH0_APAVI
Original site: A0A091PFH0_APAVI 
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
//
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