ATG7_BOTF4
ID ATG7_BOTF4 Reviewed; 704 AA.
AC G2XR75;
DT 25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 1.
DT 25-MAY-2022, entry version 43.
DE RecName: Full=Ubiquitin-like modifier-activating enzyme atg7 {ECO:0000303|PubMed:29417220};
DE AltName: Full=ATG12-activating enzyme E1 atg7 {ECO:0000303|PubMed:29417220};
DE AltName: Full=Autophagy-related protein 7 {ECO:0000303|PubMed:29417220};
GN Name=atg7 {ECO:0000303|PubMed:29417220}; ORFNames=BofuT4_P013520.1;
OS Botryotinia fuckeliana (strain T4) (Noble rot fungus) (Botrytis cinerea).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Botrytis.
OX NCBI_TaxID=999810;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T4;
RX PubMed=21876677; DOI=10.1371/journal.pgen.1002230;
RA Amselem J., Cuomo C.A., van Kan J.A.L., Viaud M., Benito E.P., Couloux A.,
RA Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.-M.,
RA Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA Grossetete S., Gueldener U., Henrissat B., Howlett B.J., Kodira C.,
RA Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA Zeng Q., Rollins J.A., Lebrun M.-H., Dickman M.;
RT "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT sclerotiorum and Botrytis cinerea.";
RL PLoS Genet. 7:E1002230-E1002230(2011).
RN [2]
RP FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH ATG7, AND SUBCELLULAR
RP LOCATION.
RX PubMed=29417220; DOI=10.1007/s00294-018-0810-3;
RA Ren W., Sang C., Shi D., Song X., Zhou M., Chen C.;
RT "Ubiquitin-like activating enzymes BcAtg3 and BcAtg7 participate in
RT development and pathogenesis of Botrytis cinerea.";
RL Curr. Genet. 64:919-930(2018).
CC -!- FUNCTION: E1-like activating enzyme involved in the 2 ubiquitin-like
CC systems required for cytoplasm to vacuole transport (Cvt) and autophagy
CC (PubMed:29417220). Activates ATG12 for its conjugation with ATG5 and
CC ATG8 for its conjugation with phosphatidylethanolamine (By similarity).
CC Both systems are needed for the ATG8 association to Cvt vesicles and
CC autophagosomes membranes (By similarity). Autophagy is essential for
CC maintenance of amino acid levels and protein synthesis under nitrogen
CC starvation. Required for selective autophagic degradation of the
CC nucleus (nucleophagy) as well as for mitophagy which contributes to
CC regulate mitochondrial quantity and quality by eliminating the
CC mitochondria to a basal level to fulfill cellular energy requirements
CC and preventing excess ROS production (By similarity). Required for
CC normal mycelial growth and conidiogenesis, and regulates sclerotial
CC formation (PubMed:29417220). Plays an essential role in pathogenesis
CC (PubMed:29417220). {ECO:0000250|UniProtKB:P38862,
CC ECO:0000269|PubMed:29417220}.
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with ATG8 through a
CC thioester bond between Cys-555 and the C-terminal Gly of ATG8 and with
CC ATG12 through a thioester bond between Cys-555 and the C-terminal Gly
CC of ATG12 (By similarity). Interacts also with ATG3 (PubMed:29417220).
CC {ECO:0000250|UniProtKB:P38862, ECO:0000269|PubMed:29417220}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:29417220}.
CC Preautophagosomal structure {ECO:0000269|PubMed:29417220}.
CC -!- DOMAIN: The C-terminal residues 660 to 699 are required for
CC homodimerization, as well as the interactions with ATG3, ATG8 and
CC ATG12; and the C-terminal 17 residues are required for the ATG8
CC lipidation (By similarity). {ECO:0000250|UniProtKB:P38862}.
CC -!- DOMAIN: The GxGxxG motif is important for the function, possibly
CC through binding with ATP (By similarity).
CC {ECO:0000250|UniProtKB:P38862}.
CC -!- DISRUPTION PHENOTYPE: Blocks the autophagic process (PubMed:29417220).
CC Leads to fewer aerial hyphae and slower mycelial growth rate and fails
CC to produce any conidia (PubMed:29417220). Reduces also the production
CC of sclerotia in cold environment (PubMed:29417220). Fails to infect
CC wounded cucumber leaves and shows only slight virulence on wounded
CC tomato and grape fruits (PubMed:29417220).
CC {ECO:0000269|PubMed:29417220}.
CC -!- SIMILARITY: Belongs to the ATG7 family. {ECO:0000305}.
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DR EMBL; FQ790255; CCD43243.1; -; Genomic_DNA.
DR AlphaFoldDB; G2XR75; -.
DR SMR; G2XR75; -.
DR STRING; 999810.G2XR75; -.
DR EnsemblFungi; CCD43243; CCD43243; BofuT4_P013520.1.
DR eggNOG; KOG2337; Eukaryota.
DR HOGENOM; CLU_012998_2_1_1; -.
DR InParanoid; G2XR75; -.
DR PHI-base; PHI:7878; -.
DR Proteomes; UP000008177; Unplaced contigs.
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-KW.
DR Gene3D; 3.40.140.100; -; 1.
DR Gene3D; 3.40.140.70; -; 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 PANTHER; PTHR10953; PTHR10953; 1.
DR Pfam; PF16420; ATG7_N; 1.
DR Pfam; PF00899; ThiF; 1.
DR SUPFAM; SSF69572; SSF69572; 1.
DR TIGRFAMs; TIGR01381; E1_like_apg7; 1.
PE 1: Evidence at protein level;
KW Autophagy; Cytoplasm; Protein transport; Reference proteome; Transport;
KW Ubl conjugation pathway.
FT CHAIN 1..704
FT /note="Ubiquitin-like modifier-activating enzyme atg7"
FT /id="PRO_0000443882"
FT REGION 660..699
FT /note="Homodimerization"
FT /evidence="ECO:0000250|UniProtKB:P38862"
FT REGION 682..704
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 372..377
FT /note="GXGXXG motif"
FT /evidence="ECO:0000250|UniProtKB:P38862"
FT COMPBIAS 687..704
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 555
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000250|UniProtKB:P38862"
SQ SEQUENCE 704 AA; 78634 MW; 0ECAF4B9395DD9D0 CRC64;
MALKFAPFAS EIELPFYTAL SQLKIDHDKL DDSARPVLGL YEPRATQSPD QSSRMRVLGN
ALSSNEVPSG HIRAEGKIKN VNTIEDFKNM DKQAMLQTSA KQGQIWDAIN DGTIYSIPSL
LSSFTILSFA NLKKYTFTYW FAFPALHSEP AWRKVEQPPK FSAEETTALT EELGTWRYSH
DNREHGFFLA KRVYPSSEHP QDPESESTSD LPFKWVIGSL REFESGFFNG VDAKNQYVSF
VDPSTYHENP GWMLRNLLVL VRRRYKLDKV QILCYRDNHA KRHVPQSLIL ILESIYDPEY
QSTAPDQIPK VTGWERNSLG KLTAKVTNLA QYMDPAQLAD QAVDLNLKLM KWRIAPELNL
DAIKNTKCLL LGAGTLGTYV SRLLMGWGVR KITFVDNASV SFSNPVRQPL FDFKDCIDGG
AKKAYRASEA LQEIYPGVDS TGHVMAVPML GHPITDEAAT KMNFELLQKL IEDHDAIFLL
MDTRESRWLP TVMGKAAGKI VMNAALGFDT YVVMRHGVTP EDGGPAALGC YFCNDVVAPS
DLLQSVKDQT LDQQCTVTRP GVAPEASSKL VELLASVLQH PLKGAAPAPK LSSNHQSGQL
EFDRDPPNHP LGLVPHQIRG FLAAYKTMLI SGPSYDCCSA CSPKIVNAYK EDGWEFIKRA
LTEKDYITEL SGLAEVQRKA EAAANDVEWD SDEEGMEDEE PELL
