ID   ATG13_SCLS1             Reviewed;         905 AA.
AC   A7F7B2;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   25-MAY-2022, entry version 69.
DE   RecName: Full=Autophagy-related protein 13;
GN   Name=atg13; ORFNames=SS1G_13492;
OS   Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold)
OS   (Whetzelinia sclerotiorum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Sclerotiniaceae; Sclerotinia.
OX   NCBI_TaxID=665079;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 18683 / 1980 / Ss-1;
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).
CC   -!- FUNCTION: Activates the atg1 kinase in a nutritional condition
CC       dependent manner through the TOR pathway, leading to autophagy. Also
CC       involved in cytoplasm to vacuole transport (Cvt) and more specifically
CC       in Cvt vesicle formation. Seems to play a role in the switching
CC       machinery regulating the conversion between the Cvt pathway and
CC       autophagy. Finally, atg13 is also required for glycogen storage during
CC       stationary phase (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with atg1 to form the atg1-atg13 kinase complex.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q06628}.
CC       Preautophagosomal structure {ECO:0000250|UniProtKB:Q06628}.
CC   -!- SIMILARITY: Belongs to the ATG13 family. Fungi subfamily.
CC       {ECO:0000305}.
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DR   EMBL; CH476645; EDN98633.1; -; Genomic_DNA.
DR   RefSeq; XP_001585608.1; XM_001585558.1.
DR   AlphaFoldDB; A7F7B2; -.
DR   SMR; A7F7B2; -.
DR   STRING; 665079.A7F7B2; -.
DR   PRIDE; A7F7B2; -.
DR   EnsemblFungi; EDN98633; EDN98633; SS1G_13492.
DR   GeneID; 5481606; -.
DR   KEGG; ssl:SS1G_13492; -.
DR   eggNOG; KOG4573; Eukaryota.
DR   HOGENOM; CLU_007151_1_0_1; -.
DR   InParanoid; A7F7B2; -.
DR   OMA; MHQHPRS; -.
DR   Proteomes; UP000001312; Unassembled WGS sequence.
DR   GO; GO:1990316; C:Atg1/ULK1 kinase complex; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0019898; C:extrinsic component of membrane; IBA:GO_Central.
DR   GO; GO:0000407; C:phagophore assembly site; IBA:GO_Central.
DR   GO; GO:0000423; P:mitophagy; IBA:GO_Central.
DR   GO; GO:0034727; P:piecemeal microautophagy of the nucleus; IBA:GO_Central.
DR   GO; GO:0034497; P:protein localization to phagophore assembly site; IBA:GO_Central.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.900.10; -; 1.
DR   InterPro; IPR040182; ATG13.
DR   InterPro; IPR018731; Atg13_N.
DR   InterPro; IPR036570; HORMA_dom_sf.
DR   PANTHER; PTHR13430; PTHR13430; 1.
DR   Pfam; PF10033; ATG13; 1.
PE   3: Inferred from homology;
KW   Autophagy; Cytoplasm; Protein transport; Reference proteome; Transport.
FT   CHAIN           1..905
FT                   /note="Autophagy-related protein 13"
FT                   /id="PRO_0000317952"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          295..377
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          398..425
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          444..535
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          554..704
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          747..850
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          871..905
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        322..339
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        352..377
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        398..413
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        456..487
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        500..517
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        554..626
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        650..673
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        747..800
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        817..833
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        871..886
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        890..905
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   905 AA;  96648 MW;  944CFCF5EF4BDF56 CRC64;
     MPHYQEVDDA SGDGGPMAAT GPSREAVKKM DQIIQNFHTK AAIIVLGARV GLPVVFTKEG
     TKKVNKWFQI ETDDTDAYRD ELHTWRMCGG FQNRPPPLII ETYLDTSHLT SSQRLVIVDD
     LGKRWDALDA LSNSCGSNDG RSEVILERWK IELRDIPGEQ PYDFGSTLPT IYKKCIVFFR
     SLYSTAKLVP AWKFKKSLGK NGSPTNSLII NCRITTGDTQ PRRIDGLKQP ILDHSGPVTS
     TYVLGATDTP AGQIFAEVTY RNDCNFRVDD SESILSSRFM GADEHFFTPS LAAKGDLSRR
     RSTKQTEIGS LPAHKHLTDD SGPVQTYGSL STFHGNAPPR GSSPMSALRA QRPIGSDTSS
     PPVGSLPYSR PSLTSKGSLK SFEGMALARR TSLSFQPFKA GSLSSSPSRA TYAGETLPAS
     PGSLPRASGI SALAQARNRS SLTAGMPATL RGGPVTSDNV VPTSVSSSPK PAPIARYSSS
     FTHRRSRPSY GGASKLVDDD QGSSGKQSVS SSVQPGSGIL AEAGAGGSSG SLQTDDDNIS
     DFLKLLDSKK TLQSFEPSGE ASKKRATAQL SKFQSMRDSH NALTDSMASS SMLQRSSSSS
     SRQLSSVPPM VAATSISAAS SPGKPISPHT PHTPAIPSRL SANSIAEYDQ PRRVTRRSRT
     TEARLEDVQD NDHSNDAGTN AIDIPTSPRP YYPHARRSSS VAQQHRALAI DDDLGDLPFG
     VHRSISLGAD DREPPSLSTL LNIGQASDDV ESPTGQSPSL LQPAPRISEG STAMSRQTSS
     SLEAHDSEVP QLSRFSGPGS ANSPYRPRIG KTGGRGVTPP QTGSFSSLLV DRGSASGSER
     AGGGRYSFSR GIGAYEADDE PLLFDMSEIG RDISRRSIDE PRGGYEASRG GDSGSSSRRG
     SRWGR