ID   ATG26_PHANO             Reviewed;        1453 AA.
AC   Q0UY53;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Sterol 3-beta-glucosyltransferase {ECO:0000305};
DE            EC=2.4.1.173 {ECO:0000305};
DE   AltName: Full=Autophagy-related protein 26 {ECO:0000250|UniProtKB:Q06321};
GN   Name=ATG26 {ECO:0000250|UniProtKB:Q06321}; ORFNames=SNOG_03311;
OS   Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS   blotch fungus) (Parastagonospora nodorum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC   Parastagonospora.
OX   NCBI_TaxID=321614;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173;
RX   PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA   Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L.,
RA   Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E.,
RA   Torriani S.F.F., McDonald B.A., Oliver R.P.;
RT   "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT   analysis of the wheat pathogen Stagonospora nodorum.";
RL   Plant Cell 19:3347-3368(2007).
CC   -!- FUNCTION: Probable sterol 3-beta-glucosyltransferase that mediates
CC       autophagic degradation of peroxisomes (pexophagy) (By similarity). Also
CC       required for cytoplasm to vacuole transport (Cvt) and autophagic
CC       degradation of mitochondria (mitophagy) and nuclei (nucleophagy) (By
CC       similarity). {ECO:0000250|UniProtKB:Q2U0C3}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a sterol + UDP-alpha-D-glucose = a sterol 3-beta-D-glucoside +
CC         H(+) + UDP; Xref=Rhea:RHEA:22724, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15889, ChEBI:CHEBI:37424, ChEBI:CHEBI:58223,
CC         ChEBI:CHEBI:58885; EC=2.4.1.173; Evidence={ECO:0000305};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q06321}.
CC       Preautophagosomal structure membrane {ECO:0000250|UniProtKB:Q2U0C3};
CC       Peripheral membrane protein {ECO:0000250|UniProtKB:Q2U0C3}.
CC   -!- DOMAIN: The GRAM and PH domains are required for the localization of
CC       ATG26 to the preautophagosomal structure (PAS) and are involved in
CC       autophagy (By similarity). {ECO:0000250|UniProtKB:Q2U0C3}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 28 family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAT90042.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; CH445328; EAT90042.2; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_001793879.1; XM_001793827.1.
DR   AlphaFoldDB; Q0UY53; -.
DR   SMR; Q0UY53; -.
DR   STRING; 13684.SNOT_03311; -.
DR   GeneID; 5970736; -.
DR   KEGG; pno:SNOG_03311; -.
DR   eggNOG; KOG1192; Eukaryota.
DR   InParanoid; Q0UY53; -.
DR   OMA; YPDWIRI; -.
DR   OrthoDB; 1024049at2759; -.
DR   Proteomes; UP000001055; Unassembled WGS sequence.
DR   GO; GO:0034045; C:phagophore assembly site membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0102203; F:brassicasterol glucosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0102205; F:cholesterol alpha-glucosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0102202; F:soladodine glucosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016906; F:sterol 3-beta-glucosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0030259; P:lipid glycosylation; IEA:InterPro.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0016126; P:sterol biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd03784; GT1_Gtf-like; 1.
DR   Gene3D; 2.30.29.30; -; 3.
DR   InterPro; IPR004276; GlycoTrans_28_N.
DR   InterPro; IPR004182; GRAM.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR002213; UDP_glucos_trans.
DR   Pfam; PF03033; Glyco_transf_28; 1.
DR   Pfam; PF02893; GRAM; 2.
DR   Pfam; PF00169; PH; 1.
DR   SMART; SM00568; GRAM; 2.
DR   SMART; SM00233; PH; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   3: Inferred from homology;
KW   Autophagy; Cytoplasm; Glycosyltransferase; Lipid biosynthesis;
KW   Lipid metabolism; Membrane; Protein transport; Reference proteome; Repeat;
KW   Steroid biosynthesis; Steroid metabolism; Sterol biosynthesis;
KW   Sterol metabolism; Transferase; Transport.
FT   CHAIN           1..1453
FT                   /note="Sterol 3-beta-glucosyltransferase"
FT                   /id="PRO_0000318046"
FT   DOMAIN          235..282
FT                   /note="GRAM 1"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          286..383
FT                   /note="PH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT   DOMAIN          771..837
FT                   /note="GRAM 2"
FT                   /evidence="ECO:0000255"
FT   REGION          1..57
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          81..226
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          500..608
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          624..688
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..49
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        86..106
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        115..141
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        163..180
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        181..215
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        503..527
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        528..568
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        577..608
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        628..688
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1453 AA;  163032 MW;  6778677005A7FD2D CRC64;
     MASQDRGRDR SSRRLTKKRK DIGRDTRGLS LDIPERFKDG DDAQEDVTAP KRSDAMSMNQ
     SIFSIIARAG GQSQVDLGTM QEVDSGDSDD DGKGKTLHDR LDGAARLSRL RTANDFRPPQ
     EDSRAEKIGS GKHRRALSEN KLLRSLPKLK ISSRKDVRSD GQHTDQMSSS QFLPPRPSTE
     TPSETHKRGD ALKGKARATT GDEIHVEKQR KSERRGGQGS SVGLAQSRGP VSLATRIQQI
     FEFEHAEEVI SEYPCWLLQS ILLQGYMYIT QKHICFYAYI PKKHHDVSKT GYLYKRGRSK
     YNRYWFILRG DVLSYYTNPA ELYFPRNRIN LQYAISAEVV ENKKKGEYET IFTVTTDERT
     YQFKADSAAS AKEWVKSIQK VIFRTHNEGN SVKISMPIRN VIEIEESSIL DFADTVKVRV
     VDNGETFAID EYFFSFFNRG QDALNVLRIM INDNEHHQVS TENQVNPTPI TAPLKTSNRH
     SLVVSPIVPD DTPRIKENVR ATLSPLPNPN VGRSSISDIS ARSSTDVPRK SWDVRRSMDA
     SRALRRSSHE VRRSFSGGRS EKLTKSRAPD RSPLSPAADT ESATLSLDPG TESSAAIQSM
     DESSASASQI LNRSDVFRAP AIHSAGVSHS ERPQQAARHS QDTTRSSGAD QHLQLLVRPS
     KQTNTSLLPA STEAEEDTDP SQTLPRLSNS SSALQEIASY PLQKASGIAG FLRMRSKEMG
     SLLATESMGY YEKVSGMLAG GRKHYNTADG LEPHDQIHGI EDDDDAAKAA DNFREHFAFP
     ESEILQSSFF ASLQRMLPNY GKIYISGRYF CFRSLMPTSK TKIILPMKDI ENVNKEKGFR
     MGYHGLAIVI RGHEELFFEF SKAEYRDECA ITVLRILENT KYIEEASSSS GVDSDDEAAK
     AEHDLLQQAR EQSDTHEQID VSEIARAADH DRIPLIFDDP LASFVDFKPP EPLTIVCLTI
     GSRGDVQPYI SLCKELLKEG HKARIATHAE FEPWVRKHGI DFAPVDGDPA ELMRICVEHG
     MFTYGFIKEA NSKFRGWLDD VCSSSWRACQ GADVLIESPS TMAGIHVAEA LEIPYFRAFT
     MPWSRTRAYP HAFSVLENKM GGGYNNMTYQ LFDKLFWTAI SAQVNKWRRR ELGLQNTSQS
     KMQANLRPFL YNFSPHVVPP PLDWPDWIRV TGYWFLDEGD TYQPPADLAA FITQARKDEK
     KLVYVGFGSI VIDDPAALTK TVVDSVLKAD VRCVLSKGWS DRLATKDASK PEIPLPPEIF
     QIQAAPHDWL FKQMDAAVHH GGSGTTGASL RAGIPTIIKP FFGDQFFFAQ RVEDMGVGIW
     LKKVNTSVFS RALWEATNSQ RMIIKAKVLG QKIRKDNGPQ VAIQTIYREL DRARTLVKKH
     VKQDDEQTDE FEEDWTMIEE GQDVDVSAHH FEAQSPLVGM NQDAPRTGGG SLVLGSMVMK
     GAQKRNSESA YRD