ID V5F8A7_BYSSN Unreviewed; 1449 AA.
AC V5F8A7;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 49.
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=PVAR5_0726 {ECO:0000313|EMBL:GAD92139.1};
OS Byssochlamys spectabilis (strain No. 5 / NBRC 109023) (Paecilomyces
OS variotii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Thermoascaceae; Paecilomyces.
OX NCBI_TaxID=1356009 {ECO:0000313|EMBL:GAD92139.1, ECO:0000313|Proteomes:UP000018001};
RN [1] {ECO:0000313|Proteomes:UP000018001}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=No. 5 / NBRC 109023 {ECO:0000313|Proteomes:UP000018001};
RX PubMed=24407650; DOI=10.1128/genomeA.01162-13;
RA Oka T., Ekino K., Fukuda K., Nomura Y.;
RT "Draft genome sequence of the formaldehyde-resistant fungus Byssochlamys
RT spectabilis No. 5 (anamorph Paecilomyces variotii No. 5) (NBRC109023).";
RL Genome Announc. 2:E0116213-E0116213(2014).
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}.
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:GAD92139.1}.
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DR EMBL; BAUL01000019; GAD92139.1; -; Genomic_DNA.
DR eggNOG; KOG1192; Eukaryota.
DR HOGENOM; CLU_000537_6_0_1; -.
DR InParanoid; V5F8A7; -.
DR OrthoDB; 76239at2759; -.
DR Proteomes; UP000018001; 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 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 Protein transport {ECO:0000256|ARBA:ARBA00022927};
KW Reference proteome {ECO:0000313|Proteomes:UP000018001};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:GAD92139.1};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 293..392
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 75..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 206..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 466..557
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 596..659
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 886..906
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1396..1433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..46
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..141
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..171
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..230
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 466..484
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 492..514
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 605..622
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 630..649
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1419..1433
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1449 AA; 161587 MW; 08E1A5B672B26BAC CRC64;
MQRLDVEDSI KKRMGRRLSF RSRSIHRMPS HQVPDRFKDG DDAQDDFTAP PKGIGGREYM
HQSIFSMIAA AGSKTDFHGR FDDPSDSDGE GEGIAEESST SKGDKGRDAK SPTKKRETEN
TPSSKDSVKK DLLEDRGRIH RRKLSDHRLL RSVPKLQSRH TKGKESVGKN ELGACDELLP
ASPPRRPRSL TPRAAPVLSR MIEAEARFGD PPSHRQETQK AAEDRSPTRQ RADSAPSSLL
STRLMEIFGF DKPEKVMGEY ACWLLQSVML QGYMYITEGH VCFYAYLPKK SNTTVKSGYL
SKRGRQNPKY NRYWCSLKGD VLSYYADPSN LYFPSGHVDL RYGISAALIE QKDKGKDVKD
FTVTTDQRTY YFRADSAPSA KEWVRTLQKV IFRSHNEGDS VKISLPIENV IDIEENPMIE
FAETVKVRVV ESGDTYAIDE YFFSFFNFGK DAFNVLKDLV KNTATQTNSQ GLPDATSGDA
SVERPQGQTL DAPFHSPRSG RSSPRFNEPV KSTLLSRSPD AGKGHLRSKS MESADPLSPA
RAYLDRSPPD NKASSDSFVH SIEQGTESSA VLQSITGTAE SASQILNRSD VFQSPTINRL
RVPSDADATG RRRSDETARS ASARAKARAG TGVNKEDQEV REAASDSENE VNSRSRYSTS
APTLQELVKA GTYPLQRAAG LAGYLKNRSK RMSTLLATES MGYIEKVSGM WAGGRRHYGE
GEGILPDDQL VDPEDEERGC GHGDRFRAHF ALPPTEKLQA TYFGYLHRLL PLYGKVYISN
RKFCFRSLLP GTRTKMILPL RDIENVEKEK GFRFGYHGLV IIIRGHEELF FEFNASDVRD
DCAVTLHQSL ESIKFLAESG ILAQEDKEEA EAAKAEHQML QEARLDVSAD NEEGSRALSP
PESPEVHPIF DDPRASIINF KPTESLRITC LTIGSRGDVQ PYIALCKGLL AEGHRPRIAT
HAEFGPWVRK HGIDFAPIDG DPAELMRICV ENGMFTYSFL KEASLKFRGW IDDLLSSAWA
SCQDSDLLIE SPSAMAGIHI AEALRIPYFR AFTMPWSRTR AYPHAFAVPE HKMGGAYNYI
TYVMFDNVFW KAIAGQVNRW RKNELGLRGT NLDKMQPNKV PFLYNFSPSV VPPPLDFPDW
IRVTGYWFLN EGDDWQAPRE LTSFIQRARA DGKKLVYIGF GSIVVSDPAA LTRTVVESVQ
KADVRCVLSK GWSDRLGDPA SAKSEIPLPP EIHQIQSAPH DWLFSQMDAV AHHGGAGTTG
ASLRAGVPTI VKPFFGDQFF FGTRIEDLGV GICMKKLNVS VFSRALWEAT HSERMIVKAK
MLGEQIRSED GVSTAIQAIY RDLEYAKTLA RQRSIASATP FSPVAKKEEI TEPPLDDDVA
DSEEWTFVGD DTDIDISKRM RDREDADIDL PPPALCSHGS SSPARTVQSV LDASDASIGW
KRDDMRAQA
//
