ID   ATG5_COCIM              Reviewed;         351 AA.
AC   Q1DP17; J0HFW6;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   25-MAY-2022, entry version 69.
DE   RecName: Full=Autophagy protein 5;
GN   Name=ATG5; ORFNames=CIMG_07946;
OS   Coccidioides immitis (strain RS) (Valley fever fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX   NCBI_TaxID=246410;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RS;
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).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=RS;
RX   PubMed=20516208; DOI=10.1101/gr.103911.109;
RA   Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA   Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA   Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA   FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA   Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA   Taylor J.W., Rounsley S.D.;
RT   "Population genomic sequencing of Coccidioides fungi reveals recent
RT   hybridization and transposon control.";
RL   Genome Res. 20:938-946(2010).
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   -!- 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; GG704913; EAS29200.3; -; Genomic_DNA.
DR   RefSeq; XP_001240783.1; XM_001240782.2.
DR   AlphaFoldDB; Q1DP17; -.
DR   SMR; Q1DP17; -.
DR   STRING; 246410.Q1DP17; -.
DR   EnsemblFungi; EAS29200; EAS29200; CIMG_07946.
DR   GeneID; 4559549; -.
DR   KEGG; cim:CIMG_07946; -.
DR   VEuPathDB; FungiDB:CIMG_07946; -.
DR   InParanoid; Q1DP17; -.
DR   OMA; KWHYPLG; -.
DR   OrthoDB; 457861at2759; -.
DR   Proteomes; UP000001261; 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..351
FT                   /note="Autophagy protein 5"
FT                   /id="PRO_0000317854"
FT   REGION          106..143
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        117..143
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CROSSLNK        186
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ATG12)"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   351 AA;  38802 MW;  B013D6453D6FF9AE CRC64;
     MAASSASTSA IQQRVWQGRI PLQIVLSPSE CRIYDQSDPY IISIPRLSYL PFILPRLFSF
     FSSSLIDPDV QAHDGWFSFE GVPLKWHYPV GLLYDLYAGA EPITSKSLSS PGSEREHYVR
     GGTRENISES GAEGEKDDNH GHDHEFKRDA LPWRLMVHFH DWPEQDLIRL DPEGKILHDA
     FINSVKEADC LRNGTAKRIM ALSKEDSSGL WKSVEEHNLP AYHRIHNTLL LPTPPTPFRN
     IPIRIFLPAP PDSPSPSLKV IQSPIPPLIQ PTASPSSSIS SASRQMQPQV QTIGTALNSL
     LPSLFPSKRT PMLAKPVLHG AVVPMSAPVE EVVKCAGYAD GWLGVVVSMV G