ID   A0A0K0FXN7_STRVS        Unreviewed;       661 AA.
AC   A0A0K0FXN7;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   24-JAN-2024, entry version 29.
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   Strongyloides venezuelensis (Threadworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC   Strongyloides.
OX   NCBI_TaxID=75913 {ECO:0000313|Proteomes:UP000035680, ECO:0000313|WBParaSite:SVE_1721300.1};
RN   [1] {ECO:0000313|Proteomes:UP000035680}
RP   NUCLEOTIDE SEQUENCE.
RA   Martin A.A, De Silva N.;
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|WBParaSite:SVE_1721300.1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (AUG-2015) 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}.
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DR   AlphaFoldDB; A0A0K0FXN7; -.
DR   STRING; 75913.A0A0K0FXN7; -.
DR   WBParaSite; SVE_1721300.1; SVE_1721300.1; SVE_1721300.
DR   Proteomes; UP000035680; 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:UP000035680};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU366022};
KW   Ubl conjugation pathway {ECO:0000256|RuleBase:RU366022}.
FT   DOMAIN          4..293
FT                   /note="Ubiquitin-like modifier-activating enzyme Atg7 N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16420"
FT   DOMAIN          310..555
FT                   /note="THIF-type NAD/FAD binding fold"
FT                   /evidence="ECO:0000259|Pfam:PF00899"
FT   ACT_SITE        525
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606285-1"
SQ   SEQUENCE   661 AA;  75054 MW;  32313C5AB229B608 CRC64;
     MIFQVQPFVT SCDPIFFSNW SDKKLNEWKL NENPIKITAT FSNAGQKRVE PELRFSESSF
     SDHEPRSFKE CVIEGIMYPL NKIENLMSFN KKGALEKISE ELYLKITESW DWMNNPKSIL
     NFILLTYGDL KSHEYHYVSC IPSFVFLKNL RIVGEIKTID NLPFSFKEIP KDWAFVLDSE
     GTICSLDILK ELEIKGESFD DITLVYKCPC TKINLFGWPL RNLLCAIATT IKPINKIKVL
     CYRCGNIPST IATIQWDEID FNNENEIFKK VVGWEKKGDG SINIHSVNLR RQMDPLSIAE
     QANSLNVSLI KWRLVPELDI DVFTKNRVLL LGSGTLGCNI ARGLIGWGVK HITFVDNGNV
     SYSNPIRQSL YTIEDAILRK SKAVAAAESL KKIIPNCITE GVNLNIPMPG HIISESQSEK
     YFEDFSKLDN LIQNHDTIFL LLDSKEARWL PTLMSAVYNK LVITVGIGFD SYVILRHGVN
     LSPYIDNSMI NTLTEVPCEK LGCYFCNDIT SPGNSVDDRT LDMKCTVTRS GNSMTAAGNA
     VELYASLQQH QLKSSAPHIS KDDHKNASLL GSVPHQLRGN LFGFSQSVWF HQRNKNCVAC
     GDNVIEMYKS CDLLKEKWQH IKEIINNREK LEMLTGLSLI QKNAERNEED VISLESEDDL
     E
//