ID   A0A0K0D0P3_ANGCA        Unreviewed;       648 AA.
AC   A0A0K0D0P3;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 24.
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};
OS   Angiostrongylus cantonensis (Rat lungworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Strongyloidea; Metastrongylidae;
OC   Angiostrongylus.
OX   NCBI_TaxID=6313 {ECO:0000313|Proteomes:UP000035642, ECO:0000313|WBParaSite:ACAC_0000363501-mRNA-1};
RN   [1] {ECO:0000313|Proteomes:UP000035642}
RP   NUCLEOTIDE SEQUENCE.
RA   Martin A.A.;
RL   Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|WBParaSite:ACAC_0000363501-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
CC   -!- FUNCTION: E1-like activating enzyme involved in the 2 ubiquitin-like
CC       systems required for autophagy. {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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   AlphaFoldDB; A0A0K0D0P3; -.
DR   STRING; 6313.A0A0K0D0P3; -.
DR   WBParaSite; ACAC_0000363501-mRNA-1; ACAC_0000363501-mRNA-1; ACAC_0000363501.
DR   Proteomes; UP000035642; 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   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:UP000035642};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU366022};
KW   Ubl conjugation pathway {ECO:0000256|RuleBase:RU366022}.
FT   DOMAIN          5..291
FT                   /note="Ubiquitin-like modifier-activating enzyme Atg7 N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16420"
FT   DOMAIN          310..558
FT                   /note="THIF-type NAD/FAD binding fold"
FT                   /evidence="ECO:0000259|Pfam:PF00899"
FT   ACT_SITE        530
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606285-1"
SQ   SEQUENCE   648 AA;  73163 MW;  D74AF892DE69C60B CRC64;
     MSHFTFVPFC TFVDTVFWAE LNRRKLNEWR LDETPRELGG MISLCEFEAL HLSLLKGVEC
     GLQSKKKKIC YFKVDCTGDM CRLSLSHESF EPSIPGAYSG RLLLMNTLDS FKRLDRKALL
     FDEAMKVWEN IKSGIWLEEP ICLMPFTFTV FADLKKFQYH YWNCYPAICY PTNIRQEDSH
     AIENDKLMYY FDHTKAHAFL VDRVGECLPL LNLINICDPA EVKVVFADPS PVPGCAGWPL
     RNLLAAVAYF KRTWRWCSFI SLRGVNQLPA SVGWERNSEG KLLSQFVDMR QQFDPKKLME
     QSVELNLSLI KWRLVPEMQL VRCTSLKVLI FGAGTLGSNI ARCLMGWGVK KITFLDNSSV
     SYSNPVRQSL SEFEDARRSR SKAETAATAL QRVYPSIDSS AVCLTVPMPG HTTSQNEEDA
     LERDVTIIDE LVANHDVVFL ALDSREARWL PTVLATRHGK MAFSVALGFD NYVVIRHGVR
     SYLQDVKAGS GDLSAQEGTV VPYSDLACYF CSDVTAPGNS STDRTLDQQC TVSRAGLSMI
     ASGIAVEVMA SVLQYRDPLA APANIGEPDD TSSLLGATPH QVRGYLSRFT QMTPCVRRFE
     KCVACGCTVV NEYVTRGVEF VKEVCYTTVY DLQLWPYCFV LFSWETIY
//