ID   ATG5_AJECN              Reviewed;         333 AA.
AC   A6RE26;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   25-MAY-2022, entry version 59.
DE   RecName: Full=Autophagy protein 5;
GN   Name=ATG5; ORFNames=HCAG_07891;
OS   Ajellomyces capsulatus (strain NAm1 / WU24) (Darling's disease fungus)
OS   (Histoplasma capsulatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma;
OC   unclassified Histoplasma.
OX   NCBI_TaxID=2059318;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NAm1 / WU24;
RX   PubMed=19717792; DOI=10.1101/gr.087551.108;
RA   Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA   Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA   McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA   Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA   Henn M.R., Birren B.W., Taylor J.W.;
RT   "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT   and their relatives.";
RL   Genome Res. 19:1722-1731(2009).
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). {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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CH476663; EDN11431.1; -; Genomic_DNA.
DR   RefSeq; XP_001537575.1; XM_001537525.1.
DR   AlphaFoldDB; A6RE26; -.
DR   SMR; A6RE26; -.
DR   STRING; 339724.A6RE26; -.
DR   EnsemblFungi; EDN11431; EDN11431; HCAG_07891.
DR   GeneID; 5443832; -.
DR   KEGG; aje:HCAG_07891; -.
DR   VEuPathDB; FungiDB:HCAG_07891; -.
DR   HOGENOM; CLU_051894_2_0_1; -.
DR   OMA; KWHYPLG; -.
DR   OrthoDB; 457861at2759; -.
DR   Proteomes; UP000009297; Unassembled WGS sequence.
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   3: Inferred from homology;
KW   Autophagy; Isopeptide bond; Membrane; Protein transport;
KW   Reference proteome; Transport; Ubl conjugation.
FT   CHAIN           1..333
FT                   /note="Autophagy protein 5"
FT                   /id="PRO_0000317848"
FT   REGION          107..133
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          256..275
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        107..124
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        260..275
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CROSSLNK        172
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ATG12)"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   333 AA;  36887 MW;  6C49DB4D6C6EEBE9 CRC64;
     MASPTPAPSA IQRRVWEGRI PLEITLSPAE CRTYDKADPY LICYPRVSYL PFLLPRLRAF
     FATSLIDIEA QDYQGWFSFE GVPLKWHYPL GLLYDLYSGA DPVTSKSTVG EHLSHTTSPR
     QPNDPEPHNV HEPGDPIPWQ LQVHFSDWPD QELVRLDADG RVIHDAFINS VKEADFVRNG
     TAKRIMTLSK EDSSGLWQAV QEHDFTNFQR ISNILIPGGP NHFRNIPLRI FLPSPPNSAT
     PSLKVIQSLF PPTIPPAANQ TGAPGRQTQP QPQTIGSSLN SLLPSLFPSK RIPVLAKPVL
     QGAVVPMTAP LEEVVRVAGY ADGWLAIVVS MVG