ID A0A0H1BT99_9EURO Unreviewed; 1501 AA.
AC A0A0H1BT99;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 43.
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=EMPG_12602 {ECO:0000313|EMBL:KLJ12336.1};
OS Blastomyces silverae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Blastomyces.
OX NCBI_TaxID=2060906 {ECO:0000313|EMBL:KLJ12336.1, ECO:0000313|Proteomes:UP000053573};
RN [1] {ECO:0000313|Proteomes:UP000053573}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 139 {ECO:0000313|Proteomes:UP000053573};
RX PubMed=26439490; DOI=10.1371/journal.pgen.1005493;
RA Munoz J.F., Gauthier G.M., Desjardins C.A., Gallo J.E., Holder J.,
RA Sullivan T.D., Marty A.J., Carmen J.C., Chen Z., Ding L., Gujja S.,
RA Magrini V., Misas E., Mitreva M., Priest M., Saif S., Whiston E.A.,
RA Young S., Zeng Q., Goldman W.E., Mardis E.R., Taylor J.W., McEwen J.G.,
RA Clay O.K., Klein B.S., Cuomo C.A.;
RT "The dynamic genome and transcriptome of the human fungal pathogen
RT Blastomyces and close relative Emmonsia.";
RL PLoS Genet. 11:E1005493-E1005493(2015).
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}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 28 family.
CC {ECO:0000256|ARBA:ARBA00006962}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KLJ12336.1}.
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DR EMBL; LDEV01000981; KLJ12336.1; -; Genomic_DNA.
DR STRING; 2060906.A0A0H1BT99; -.
DR OrthoDB; 76239at2759; -.
DR Proteomes; UP000053573; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C: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 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); 3.
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 Reference proteome {ECO:0000313|Proteomes:UP000053573};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KLJ12336.1}.
FT DOMAIN 301..402
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 1..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 78..193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 219..245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 485..593
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 642..710
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1418..1501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 127..149
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 227..244
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 540..563
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 564..593
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 644..659
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 670..686
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 687..701
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1431..1445
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1460..1477
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1484..1501
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1501 AA; 166565 MW; ED83B6D5BD104613 CRC64;
MPPDDESRTT GASGRSKPHP TSTYRLSSSH IPDRLRMGDD EQEDMTAPPG GTAGRGGRFQ
YMHQSVFSMI AAASSKKDFH NRFDESSDAE DEDANADADR AFKSRFLSND GVGGRRRAGS
ASTSHLPHLV KRDKTTISST AEERGRSQHR KKLSEHKFLK SLAKLPHRNN KGMEPASEPE
PELEEPTVTG EPSSANAVQL VAATEAPVLS RMLDAQSRFG EYEAPPSSTE RSRKDHHERK
ESSPASLLSA RLMDIFGFDR PEKVISEYQC WLLQSVLLQG YMYITERHIS FYAYLPKKSH
TTIKSGYLSK RGRQNPKYNR YYFELKGDVL SYYLDRSNLY FPSGHVDLRY GISANLAEHK
GKDKDKDVKD FTITTNTRTY QFRADSAMSA REWVKALQKV IFRSHNEGDS VKISLPIENV
IDIEENPVID FADTFKIRVV ESGESYAIDE YFFSFFECGK EAIEVLKKMV SNTPAQQIPQ
TMLAPDAGYT SRRRRSHSVD EISPPSTHGT TLLSEAVKAT LRPHSPLGSR SGSPKQGLDR
PRSPFRRFSR SRGHSRESSG AGLEQRRRSG STNRASVGDN QAETSPGGKL LNSSDSFVQS
LEHATDSSAI LQSTNGTVES ASQILNRSDV FQSPTIHKLR DTLSGAGEAP RRHSEDTARF
APSPADVRIH PPSRTQTTQS LTKPEHQDGG SDSEHDLQHR SVAHSASSPT LQELMKAGSY
PLQRAAGLAG YLKSRSKRMS NLLATESMGY FEKVSGMWIG GKRHYGEGET ILPDDRMVDP
EDEEQGCEHG DRFRAHFALP SSEKLQATYF AYLHRVIPLY GKLYISNRKF CFRSLLPGTR
TKMILPLRDI ENVEKEKGFR FGYHGLVVII SGHEELFFEF NTADARDDCA VTLHQNLESI
RYLVESGLLA QQDREEAEAA RAEHQMLQEA RLEGMEEEHS SQTLSASAPL SPTSSPILFD
DPRVSIVNFK PQEALRITCL TIGSRGDVQP YIALCKGLMA EGHIPKIATH REFEPWIRKH
GIDFAPVEGD PAELMRICVE NGMFTYSFLK EASSKFRGWI DDLLSSAWAS CQNSDILIES
PSAMAGIHIA EALGIPYFRA FTMPWTRTRA YPHAFAVPEH KMGGAYNYIT YVMFDNVFWK
AIAGQVNRWR KRELGLRSTN LDKMQPNKVP FLYNFSPSVV PPPLDFCDWI RVTGYWFLDE
GADWQPPAEL DNFIKQARAD KKKIVYIGFG SIVVSDPAAL TKTVVDSVLR ADVRCILSKG
WSDRLGDPSS AKVEIPLPPE VHQIKSAPHD WLFSHIDAAA HHGGAGTTGA SLRAGIPTII
KPFFGDQFFF GSRVEDLGVG ICMKRLNVGV FTRALWEATH SERIIVKAKA LGEQIRKEDG
VGNAIQAIYR DLEYAKTLVR QRSNATSASQ AGIVPVATEG SGAGISSETG LDEDGDGEGD
ADADAAMEDS WTFVGDEAGT ELARKTRARE RDYDVPVDVV AARVTGSNGS SGSGSHDGRS
G
//
