ID A0A2N3N038_9PEZI Unreviewed; 763 AA.
AC A0A2N3N038;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
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=jhhlp_007609 {ECO:0000313|EMBL:PKS05780.1};
OS Lomentospora prolificans.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Microascales; Microascaceae; Lomentospora.
OX NCBI_TaxID=41688 {ECO:0000313|EMBL:PKS05780.1, ECO:0000313|Proteomes:UP000233524};
RN [1] {ECO:0000313|EMBL:PKS05780.1, ECO:0000313|Proteomes:UP000233524}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JHH-5317 {ECO:0000313|EMBL:PKS05780.1,
RC ECO:0000313|Proteomes:UP000233524};
RX PubMed=28963165; DOI=10.1534/g3.117.300107;
RA Luo R., Zimin A., Workman R., Fan Y., Pertea G., Grossman N., Wear M.P.,
RA Jia B., Miller H., Casadevall A., Timp W., Zhang S.X., Salzberg S.L.;
RT "First Draft Genome Sequence of the Pathogenic Fungus Lomentospora
RT prolificans (Formerly Scedosporium prolificans).";
RL G3 (Bethesda) 7:3831-3836(2017).
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 and ATG8 for
CC its conjugation with phosphatidylethanolamine. Both systems are needed
CC for the ATG8 association to Cvt vesicles and autophagosomes membranes.
CC Autophagy is essential for maintenance of amino acid levels and protein
CC synthesis under nitrogen starvation. Required for selective autophagic
CC degradation of the nucleus (nucleophagy) as well as for mitophagy which
CC contributes to regulate mitochondrial quantity and quality by
CC eliminating the mitochondria to a basal level to fulfill cellular
CC energy requirements and preventing excess ROS production.
CC {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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PKS05780.1}.
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DR EMBL; NLAX01001139; PKS05780.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N3N038; -.
DR STRING; 41688.A0A2N3N038; -.
DR VEuPathDB; FungiDB:jhhlp_007609; -.
DR InParanoid; A0A2N3N038; -.
DR OrthoDB; 1128973at2759; -.
DR Proteomes; UP000233524; 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:UP000233524};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU366022};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU366022}.
FT DOMAIN 15..340
FT /note="Ubiquitin-like modifier-activating enzyme Atg7 N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF16420"
FT DOMAIN 357..587
FT /note="THIF-type NAD/FAD binding fold"
FT /evidence="ECO:0000259|Pfam:PF00899"
FT REGION 590..609
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 687..719
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 744..763
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 687..714
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 560
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR606285-1"
SQ SEQUENCE 763 AA; 84301 MW; E1B03B6D4438B13C CRC64;
MAEAAGGASI IGKSIQFVPN SSEIELPFYS ALFALKLDHD KLDDSARQVL GLYEPRAVDP
EDSCKLQVLG NALTSTHGSL GTIRADGIIK NTNTMEEFKN LDKPAMIRTA GRQIWDAIKD
GSIYSIPSLL SSFTIISYAD LKKYQFTYWF AFPALHSSWV HTAEPSYLTP DESTALVDNV
GTWRYSVDNR EHGYFLAKKV AHSADESSED KNDNLDFVWK IASLREFEAA NSERAFFDGV
PKKDRYVCFV DPSTYAHNPG WQLRNLLVLI QQRFKLDEVQ ILCYRDVQSR RHEARSVILP
IKQAEGSVTG SVEGDMPKVT GWERNGKALR AKQANLAEYM DPARLADQSV DLNLKLMKWR
IAPDLNLDAI KNTKCLLLGS GTLGSYVSRN LMGWGVRKIT FVDYGKVSFS NPVRQPLFEF
KDCLGGGVPK APRAAEALKE IYPGVESEGH VLTVPMLGHP FADDGKQAKA DFDKLQSLID
EHDAIFLLMD TRESRWLPTV MGKAGKKIVL TAALGFDSYV VMRHGAEDNV EGETPLGCYF
CNDVVSPANS MKDQTLDQQC TVTRPGVAAI ASALAVELLT SILQHPLAHR APAPHVTPGS
TPERDPPDHP LGLVPHQIRG YVSTFQTLNI RGHAYPNCSA CSAPVLDAYR KEGWEFVQRA
LLEKDYISEL SGLAEIQRQA ELAAADLEWD DEEGGGEDEG EEVENDEDGE DDEAISAQPW
GSRAVVFSCF SPSIRGLEAI SLGELEDYDE EDVEGDDEQA AVL
//
