ID   ATG5_MAGO7              Reviewed;         314 AA.
AC   Q525E4; A4R0W4; A4UTN9; G4MQ90;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2005, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Autophagy protein 5;
GN   Name=ATG5; ORFNames=MGG_09262;
OS   Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS   fungus) (Pyricularia oryzae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX   NCBI_TaxID=242507;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC   STRAIN=Guyane 11;
RX   PubMed=19629489; DOI=10.1007/s00294-009-0259-5;
RA   Lu J.-P., Liu X.-H., Feng X.-X., Min H., Lin F.-C.;
RT   "An autophagy gene, MgATG5, is required for cell differentiation and
RT   pathogenesis in Magnaporthe oryzae.";
RL   Curr. Genet. 55:461-473(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX   PubMed=15846337; DOI=10.1038/nature03449;
RA   Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA   Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA   Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA   Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA   Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA   Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT   "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL   Nature 434:980-986(2005).
CC   -!- FUNCTION: Involved in cytoplasm to vacuole transport (Cvt) and
CC       autophagic vesicle formation. Autophagy is essential for maintenance of
CC       amino acid levels and protein synthesis under nitrogen starvation.
CC       Required for selective autophagic degradation of the nucleus
CC       (nucleophagy). Also required for mitophagy, which eliminates defective
CC       or superfluous mitochondria in order to fulfill cellular energy
CC       requirements and prevent excess ROS production. Conjugation with ATG12,
CC       through a ubiquitin-like conjugating system involving ATG7 as an E1-
CC       like activating enzyme and ATG10 as an E2-like conjugating enzyme, is
CC       essential for its function. The ATG12-ATG5 conjugate acts as an E3-like
CC       enzyme which is required for lipidation of ATG8 and ATG8 association to
CC       the vesicle membranes (By similarity). Required for cell
CC       differentiation and pathogenesis. {ECO:0000250,
CC       ECO:0000269|PubMed:19629489}.
CC   -!- SUBUNIT: Conjugated with ATG12. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Preautophagosomal structure membrane
CC       {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
CC   -!- PTM: Conjugated to ATG12; which is essential for autophagy.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ATG5 family. {ECO:0000305}.
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DR   EMBL; EF486490; ABO93146.1; -; mRNA.
DR   EMBL; CM001231; EHA57283.1; -; Genomic_DNA.
DR   RefSeq; XP_003709895.1; XM_003709847.1.
DR   AlphaFoldDB; Q525E4; -.
DR   SMR; Q525E4; -.
DR   STRING; 318829.MGG_09262T0; -.
DR   PRIDE; Q525E4; -.
DR   EnsemblFungi; MGG_09262T0; MGG_09262T0; MGG_09262.
DR   GeneID; 2680280; -.
DR   KEGG; mgr:MGG_09262; -.
DR   VEuPathDB; FungiDB:MGG_09262; -.
DR   eggNOG; KOG2976; Eukaryota.
DR   HOGENOM; CLU_051894_2_0_1; -.
DR   InParanoid; Q525E4; -.
DR   OMA; KWHYPLG; -.
DR   OrthoDB; 457861at2759; -.
DR   PHI-base; PHI:2073; -.
DR   PHI-base; PHI:2091; -.
DR   Proteomes; UP000009058; Chromosome 1.
DR   GO; GO:0034045; C:phagophore assembly site membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.246.190; -; 1.
DR   Gene3D; 3.10.20.620; -; 1.
DR   InterPro; IPR007239; Atg5.
DR   InterPro; IPR042526; Atg5_HR.
DR   InterPro; IPR042527; Atg5_UblA_dom.
DR   PANTHER; PTHR13040; PTHR13040; 1.
DR   Pfam; PF04106; APG5; 1.
PE   2: Evidence at transcript level;
KW   Autophagy; Isopeptide bond; Membrane; Protein transport;
KW   Reference proteome; Transport; Ubl conjugation.
FT   CHAIN           1..314
FT                   /note="Autophagy protein 5"
FT                   /id="PRO_0000219006"
FT   REGION          1..59
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        18..32
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CROSSLNK        162
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ATG12)"
FT                   /evidence="ECO:0000250"
FT   VARIANT         152
FT                   /note="H -> R (in strain: Guyane 11)"
FT   VARIANT         263
FT                   /note="D -> G (in strain: Guyane 11)"
SQ   SEQUENCE   314 AA;  33637 MW;  4145059D651C29BA CRC64;
     MASPRRSEAD LASPARGPGS GPPSPPHPGP DSARPLSRIT SAAASPPPPG QRTAEPPTTI
     SIPRTLWRLS IPLYITHPSL PNTPFITSLP RVSYLSLLLP RIRAFLPPSI PAPTSFHHEG
     IALRALPLGL LVDLYQPTLP WRLTVDQGDD WHVGDTFLNG VKEADFVRNG HAKQIMGMSK
     ADTTALWNAV RDADYPAWAR INARLLNPST PIKHVPLRIY IPSSGGGGAG GATPAGSFRV
     MQTLVPPRTA NRIPQTLGPT LRDLLPVLFP SSRDPVLANV VLHGAPVPFS APLEGLMREA
     AYPDGWLCLT VVPL