GenomeNet

Database: UniProt
Entry: V4AQA5_LOTGI
LinkDB: V4AQA5_LOTGI
Original site: V4AQA5_LOTGI 
ID   V4AQA5_LOTGI            Unreviewed;       660 AA.
AC   V4AQA5;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   24-JAN-2024, entry version 40.
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};
GN   ORFNames=LOTGIDRAFT_116619 {ECO:0000313|EMBL:ESO95826.1};
OS   Lottia gigantea (Giant owl limpet).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Patellogastropoda; Lottioidea; Lottiidae; Lottia.
OX   NCBI_TaxID=225164 {ECO:0000313|EMBL:ESO95826.1, ECO:0000313|Proteomes:UP000030746};
RN   [1] {ECO:0000313|EMBL:ESO95826.1, ECO:0000313|Proteomes:UP000030746}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23254933; DOI=10.1038/nature11696;
RA   Simakov O., Marletaz F., Cho S.J., Edsinger-Gonzales E., Havlak P.,
RA   Hellsten U., Kuo D.H., Larsson T., Lv J., Arendt D., Savage R.,
RA   Osoegawa K., de Jong P., Grimwood J., Chapman J.A., Shapiro H., Aerts A.,
RA   Otillar R.P., Terry A.Y., Boore J.L., Grigoriev I.V., Lindberg D.R.,
RA   Seaver E.C., Weisblat D.A., Putnam N.H., Rokhsar D.S.;
RT   "Insights into bilaterian evolution from three spiralian genomes.";
RL   Nature 493:526-531(2013).
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   EMBL; KB201611; ESO95826.1; -; Genomic_DNA.
DR   RefSeq; XP_009053668.1; XM_009055420.1.
DR   AlphaFoldDB; V4AQA5; -.
DR   STRING; 225164.V4AQA5; -.
DR   EnsemblMetazoa; LotgiT116619; LotgiP116619; LotgiG116619.
DR   GeneID; 20231371; -.
DR   KEGG; lgi:LOTGIDRAFT_116619; -.
DR   CTD; 20231371; -.
DR   HOGENOM; CLU_012998_2_1_1; -.
DR   OMA; RQIWDAI; -.
DR   OrthoDB; 1128973at2759; -.
DR   Proteomes; UP000030746; 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:UP000030746};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU366022};
KW   Ubl conjugation pathway {ECO:0000256|RuleBase:RU366022}.
FT   DOMAIN          4..305
FT                   /note="Ubiquitin-like modifier-activating enzyme Atg7 N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16420"
FT   DOMAIN          322..599
FT                   /note="THIF-type NAD/FAD binding fold"
FT                   /evidence="ECO:0000259|Pfam:PF00899"
FT   ACT_SITE        544
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606285-1"
SQ   SEQUENCE   660 AA;  74659 MW;  1C8A0B0FCC70DAA0 CRC64;
     MESLQFAPFS SGLDAGFWPK LSEKKLNEYA LDESSKDISG FYYNGDIRNQ NPILNVDYTC
     FDRLFKTPAR SFISHGVLYL KNTIEGFKEC DKKLLLEEKA NQIWQDIKTG KAVEDPTLLS
     RFILLAYADL KKYHYYYWFA FPALIYNEHS ADNYREQGLF MKFIMINVKL GKKLLTSFLN
     IYKKFQRNLT LNSIVNKFSK FSGVFFMVII AFSFCDPCTL ENHPGWPLRN FLLLIAYTWA
     DKLETCNILC FRDKSRDGKR EISHSLMLNV QLPKLDKETC PKCVGWEKNE KQKLGPRMVN
     LSATMDPSRL CASAVDLNLK LMRWRLLPDL DLDKISSTKC LLLGSGTLGC NVARCLMGWG
     VKNITLVDNS KVSYSNPVRQ SLFIFQDCLN GGKAKAEAAA NSMRQIFPGV NALGLSLSIP
     MPGHAITGIF YFSPAVLVQT KKDIETLEDL IDKHDAVFLL MDTRESRWLP TLLGAVKQKI
     VINAALGFDT YLVLRHGYKS DTGVDGTKIK LGEVIPGDQL GCYFCNDVVA PGDSTRDRSL
     DQQCTVTRPG ISMIGSALAV ELLMSVLQHP LGFNFFQIRG FLSRFSSVLP ASHAFDKCTA
     CSQIVMETYK KEGFEFLVKV FNEPSYLENL TGLTAMHEGT FDVEVWDLSD EEDFSNKEEL
//
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