ID A0A319AS93_9EURO Unreviewed; 553 AA.
AC A0A319AS93;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Autophagy-related protein 17 {ECO:0000256|ARBA:ARBA00013806, ECO:0000256|RuleBase:RU368080};
GN ORFNames=BP01DRAFT_287656 {ECO:0000313|EMBL:PYH49152.1};
OS Aspergillus saccharolyticus JOP 1030-1.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1450539 {ECO:0000313|EMBL:PYH49152.1, ECO:0000313|Proteomes:UP000248349};
RN [1] {ECO:0000313|EMBL:PYH49152.1, ECO:0000313|Proteomes:UP000248349}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JOP 1030-1 {ECO:0000313|EMBL:PYH49152.1,
RC ECO:0000313|Proteomes:UP000248349};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Autophagy-specific protein that functions in response to
CC autophagy-inducing signals as a scaffold to recruit other ATG proteins
CC to organize pre-autophagosomal structure (PAS) formation. Modulates the
CC timing and magnitude of the autophagy response, such as the size of the
CC sequestering vesicles. Plays particularly a role in pexophagy and
CC nucleophagy. {ECO:0000256|ARBA:ARBA00024948}.
CC -!- FUNCTION: Autophagy-specific protein that functions in response to
CC autophagy-inducing signals as a scaffold to recruit other ATG proteins
CC to organize preautophagosomal structure (PAS) formation. Modulates the
CC timing and magnitude of the autophagy response, such as the size of the
CC sequestering vesicles. Plays particularly a role in pexophagy and
CC nucleophagy. {ECO:0000256|RuleBase:RU368080}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU368080}.
CC Preautophagosomal structure membrane {ECO:0000256|RuleBase:RU368080};
CC Peripheral membrane protein {ECO:0000256|RuleBase:RU368080}. Membrane
CC {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004170}.
CC -!- SIMILARITY: Belongs to the ATG17 family.
CC {ECO:0000256|ARBA:ARBA00006259, ECO:0000256|RuleBase:RU368080}.
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DR EMBL; KZ821219; PYH49152.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A319AS93; -.
DR STRING; 1450539.A0A319AS93; -.
DR OrthoDB; 1940609at2759; -.
DR Proteomes; UP000248349; Unassembled WGS sequence.
DR GO; GO:0034045; C:phagophore assembly site membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR InterPro; IPR007240; Atg17.
DR InterPro; IPR045326; ATG17-like_dom.
DR PANTHER; PTHR28005; AUTOPHAGY-RELATED PROTEIN 17; 1.
DR PANTHER; PTHR28005:SF1; AUTOPHAGY-RELATED PROTEIN 17; 1.
DR Pfam; PF04108; ATG17_like; 1.
PE 3: Inferred from homology;
KW Autophagy {ECO:0000256|RuleBase:RU368080};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|RuleBase:RU368080};
KW Kinase {ECO:0000313|EMBL:PYH49152.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000248349};
KW Transferase {ECO:0000313|EMBL:PYH49152.1}.
FT DOMAIN 44..467
FT /note="Autophagy protein ATG17-like"
FT /evidence="ECO:0000259|Pfam:PF04108"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 205..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 492..527
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 431..458
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 496..527
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 553 AA; 60598 MW; 507854E31ACB5F36 CRC64;
MSSALESSAV SNDVHHPGEA SKDQESSIPQ LDTLISHLVA AKRSLSSINH VWRANEIVTA
ARSALEESVI VSARTGFLRR GLNNQLRLLY SVRSEVEEIS LRGRSEFAGV LKDLDAAGAR
LRKTLGLLQG TIVHPSFRPD GEDQKSLHDF VDERGVDELH AALKASIDRT NAAQLDLDSS
NYAFDNELQA IKKALGNYRE VTKLASSRSS SSSSPSASNS SLPNLSSMPS MLHSLEMHAQ
EMANLLESLV RHFDLCVTAV KHTEGGGAAA QTITGDMPAG VNVNGRGGPN IEEEINAHLN
APLDPLSESG YLEMVSVLMK DAAEAEDVVM EIQDRIGEME SVLESIICSR DNLLSVYNAT
TEIFGHISSL ASVRLPSYIA QAHNFTRVWN EEHDRINGGL ADLSDLSSLY DGFLEAYDSL
ILEVSRRRHV RQRVEKVLRD AKHKLDQLYE EDVNAREAFR VEQGDYLPSD IWPGIGCEPM
RIEFQRIFGG SLKPEDGEPS EAHAESTVRT SDEQHPPAAA EELVADDEVI PDLPKSLVEQ
ALARLQARSK QVA
//
