ID A0A1L9TBS0_9EURO Unreviewed; 1380 AA.
AC A0A1L9TBS0;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Sterol 3-beta-glucosyltransferase {ECO:0000256|ARBA:ARBA00017894};
DE EC=2.4.1.173 {ECO:0000256|ARBA:ARBA00012650};
DE AltName: Full=Autophagy-related protein 26 {ECO:0000256|ARBA:ARBA00029843};
GN ORFNames=ASPSYDRAFT_33013 {ECO:0000313|EMBL:OJJ56851.1};
OS Aspergillus sydowii CBS 593.65.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=1036612 {ECO:0000313|EMBL:OJJ56851.1, ECO:0000313|Proteomes:UP000184356};
RN [1] {ECO:0000313|Proteomes:UP000184356}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 593.65 {ECO:0000313|Proteomes:UP000184356};
RX PubMed=28196534; DOI=10.1186/s13059-017-1151-0;
RA de Vries R.P., Riley R., Wiebenga A., Aguilar-Osorio G., Amillis S.,
RA Uchima C.A., Anderluh G., Asadollahi M., Askin M., Barry K., Battaglia E.,
RA Bayram O., Benocci T., Braus-Stromeyer S.A., Caldana C., Canovas D.,
RA Cerqueira G.C., Chen F., Chen W., Choi C., Clum A., Dos Santos R.A.,
RA Damasio A.R., Diallinas G., Emri T., Fekete E., Flipphi M., Freyberg S.,
RA Gallo A., Gournas C., Habgood R., Hainaut M., Harispe M.L., Henrissat B.,
RA Hilden K.S., Hope R., Hossain A., Karabika E., Karaffa L., Karanyi Z.,
RA Krasevec N., Kuo A., Kusch H., LaButti K., Lagendijk E.L., Lapidus A.,
RA Levasseur A., Lindquist E., Lipzen A., Logrieco A.F., MacCabe A.,
RA Maekelae M.R., Malavazi I., Melin P., Meyer V., Mielnichuk N., Miskei M.,
RA Molnar A.P., Mule G., Ngan C.Y., Orejas M., Orosz E., Ouedraogo J.P.,
RA Overkamp K.M., Park H.-S., Perrone G., Piumi F., Punt P.J., Ram A.F.,
RA Ramon A., Rauscher S., Record E., Riano-Pachon D.M., Robert V., Roehrig J.,
RA Ruller R., Salamov A., Salih N.S., Samson R.A., Sandor E., Sanguinetti M.,
RA Schuetze T., Sepcic K., Shelest E., Sherlock G., Sophianopoulou V.,
RA Squina F.M., Sun H., Susca A., Todd R.B., Tsang A., Unkles S.E.,
RA van de Wiele N., van Rossen-Uffink D., Oliveira J.V., Vesth T.C.,
RA Visser J., Yu J.-H., Zhou M., Andersen M.R., Archer D.B., Baker S.E.,
RA Benoit I., Brakhage A.A., Braus G.H., Fischer R., Frisvad J.C.,
RA Goldman G.H., Houbraken J., Oakley B., Pocsi I., Scazzocchio C.,
RA Seiboth B., vanKuyk P.A., Wortman J., Dyer P.S., Grigoriev I.V.;
RT "Comparative genomics reveals high biological diversity and specific
RT adaptations in the industrially and medically important fungal genus
RT Aspergillus.";
RL Genome Biol. 18:RESEARCH28.1-RESEARCH28.45(2017).
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;
CC Evidence={ECO:0000256|ARBA:ARBA00035583};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22725;
CC Evidence={ECO:0000256|ARBA:ARBA00035583};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ergosterol + UDP-alpha-D-glucose = ergosteryl 3-beta-D-
CC glucoside + H(+) + UDP; Xref=Rhea:RHEA:61836, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16933, ChEBI:CHEBI:52973, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:58885; Evidence={ECO:0000256|ARBA:ARBA00035586};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61837;
CC Evidence={ECO:0000256|ARBA:ARBA00035586};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Membrane {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004170}. Preautophagosomal structure membrane
CC {ECO:0000256|ARBA:ARBA00004623}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004623}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 28 family.
CC {ECO:0000256|ARBA:ARBA00006962}.
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DR EMBL; KV878589; OJJ56851.1; -; Genomic_DNA.
DR STRING; 1036612.A0A1L9TBS0; -.
DR VEuPathDB; FungiDB:ASPSYDRAFT_33013; -.
DR OrthoDB; 76239at2759; -.
DR Proteomes; UP000184356; 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:0051506; F:ergosterol UDP-glucosyltransferase activity; IEA:RHEA.
DR GO; GO:0102202; F:soladodine 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 CDD; cd03784; GT1_Gtf-like; 1.
DR CDD; cd13215; PH-GRAM1_AGT26; 1.
DR CDD; cd13216; PH-GRAM2_AGT26; 1.
DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 2.
DR InterPro; IPR048066; ATG26_PH_GRAM1.
DR InterPro; IPR048065; ATG26_PH_GRAM2.
DR InterPro; IPR010610; EryCIII-like_C.
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 PANTHER; PTHR48050; STEROL 3-BETA-GLUCOSYLTRANSFERASE; 1.
DR PANTHER; PTHR48050:SF25; STEROL 3-BETA-GLUCOSYLTRANSFERASE; 1.
DR Pfam; PF06722; EryCIII-like_C; 1.
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 SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 3: Inferred from homology;
KW Autophagy {ECO:0000256|ARBA:ARBA00023006};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927};
KW Reference proteome {ECO:0000313|Proteomes:UP000184356};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 286..385
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 1..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 76..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 202..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 455..531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 567..587
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1316..1336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..102
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..129
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..146
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..225
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 458..510
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1316..1331
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1380 AA; 154817 MW; B21FA414170B2463 CRC64;
MRPFKDDAKR RVERKLSGNK QSISRSMFSS PFPERLKEDY DDSQMDYTAP PGGGKSGDGL
QYMHQSVLSL IAAVGSRTES GARFDSSSDS EEHTDKKSPQ LSDKPSGEQN TAPSETGGTK
QVPSAPETRT SSKKRGRRHR RSISDHKLFR PFKSGTINQD KERDEPSISG RLSPLPVLPR
PRSATPRAAP ILSRMVEARA LLDTEESPEE SSPSSSQEGK NVNFSQQSSA SPLSLRLMEM
FHFATPEKVV VEYSCYLLQS MLLQGYMYVT EGHICFYAYL PRKSTIAIKS GYIYKRGRKN
PKYSRYWFSL KKDVLSYYAD SSNLYFPSGQ IDLRYGISAS LTESKEKGRD SRDFQVTTDH
RTYYFRADSS TDAREWVKSL QKVIFRTHNE GESIKVSFPI EKVLDIEESP MAEIAETFKL
RVVDEESFAI DEYYFTFFDS GRDAFNLLKG LIRDTPTKDP SPSKSPLPGN TANHNRSRGS
QSRWSVTSGG KPQGTPPRRR SASTGVLSAD TGIEKSPRMK QQDSSTSFVN PIDQITESSA
VLQSMTDTTE SASQILNRSD VFHSPTIQTW QRRASDAAKP NRRSSDEMAR SIIEHAPDGL
SQEREDLYAA YSSEQGSKDA SKLYSPAAFN DLVRAGSYPL QRAAGFAEYL KSRSREMSTL
LATESMGYIE KVSGMWAGGR RHYGDLEGVL PDDRALYPET TEESVRDGNR FRAHFALPPT
EKLGAAYFAY LHRALPLYGK IYISQNRVCF RSLLPGTRTK MILPLRDIEN VEKEKGFQFG
YHGLVVVVRG YEELFFEFNA SDARDDCAVT IIQQLEPIKL MAESGLLSQQ ESDESEAAQT
EHRMLEEARL NASTEQTLRS PLSESSELPS IFDDPRASIV DFKPPEPLTI TCLTIGSRGD
VQPYIALCKG LLAEGHKPRI ATHAEFEPWI REHGIDFALV DGEPAELMRL CVENGMFTIS
FLREATARFR GWIDDLLVSA WTACQGSDLI IESPSAMAGI HIAEALRIPY FRGFTMPWSR
TRAYPHAFTV PEHRMGGAYN YFTYVMFDNV FWGTTSGQVN RWRMNTLGLK ATNLDKMQPN
KVPFIYNFSP SVVPPPLDFP DWVRITGYWF LDENPDWTPP KELAEFMQRA REDGKKIVYI
GFGSIVVSDP PALTRSVVES VLKADVRCIL SKGWSSRLGD PNSSKSEIPL PPEIHQIQSI
PHEWLFPQMD AAVHHGGAGT TGASLRAGVP TIVRPFFGDQ FFFGNRVQDL GVGMCVKKIN
VSTFSRLLWT VTHDERLIVR ARRLGERIRS EDGVATAIQA IYRDLEYATT LTRQRSSISS
TPFSPTPTTK TADENVDDDI GDIEEWTLVS DGDDIDFTKL MRDRAVSGAD NLAERLSLGD
//
