ID A0A1Z5TFT7_HORWE Unreviewed; 1416 AA.
AC A0A1Z5TFT7;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=sterol 3beta-glucosyltransferase {ECO:0000256|ARBA:ARBA00012650};
DE EC=2.4.1.173 {ECO:0000256|ARBA:ARBA00012650};
DE AltName: Full=Autophagy-related protein 26 {ECO:0000256|ARBA:ARBA00029843};
GN ORFNames=BTJ68_05383 {ECO:0000313|EMBL:OTA34860.1};
OS Hortaea werneckii EXF-2000.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Hortaea.
OX NCBI_TaxID=1157616 {ECO:0000313|EMBL:OTA34860.1, ECO:0000313|Proteomes:UP000194280};
RN [1] {ECO:0000313|EMBL:OTA34860.1, ECO:0000313|Proteomes:UP000194280}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EXF-2000 {ECO:0000313|EMBL:OTA34860.1,
RC ECO:0000313|Proteomes:UP000194280};
RA Sinha S., Flibotte S., Neira M., Lenassi M., Gostincar C., Stajich J.E.,
RA Nislow C.E.;
RT "The recent genome duplication of the halophilic yeast Hortaea werneckii:
RT insights from long-read sequencing.";
RL Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
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:OTA34860.1}.
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DR EMBL; MUNK01000053; OTA34860.1; -; Genomic_DNA.
DR STRING; 1157616.A0A1Z5TFT7; -.
DR VEuPathDB; FungiDB:BTJ68_05383; -.
DR InParanoid; A0A1Z5TFT7; -.
DR OrthoDB; 76239at2759; -.
DR Proteomes; UP000194280; 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:0051506; F:ergosterol UDP-glucosyltransferase activity; IEA:RHEA.
DR GO; GO:0102202; F:soladodine glucosyltransferase activity; IEA:UniProtKB-EC.
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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Reference proteome {ECO:0000313|Proteomes:UP000194280};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 288..389
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 1..230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 460..579
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 600..658
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1381..1416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..39
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 137..158
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 465..479
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 501..541
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 542..579
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 617..639
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1416 AA; 157752 MW; 10E335DE364FE9F4 CRC64;
MTSVRRSSAS SFRARPGRNS SRSPDRHRMS MQIPARFRVE EEDEEEDVTG RAEPSARSVQ
QSFYGMLGAA GQKQMGRTGF WPDSGSESDG DIELEGGDKA GRASPPGGGR LSSGMPGSDE
EGCPSQPNLI RQSKSKKSDN SQLRRTLKSV RERAGSLEGE DQMSQSQFLP PREPQIEAPE
RPKSATGIRS DAPMLDRKLK AKAKADLDSS TVSSSRNDSD RERNSSSVKQ RAVDLPSALA
EIFQFDEAEE IIAEYACWYL QSVLLQGYMY ITRNHVCFYA YMPKRGSTVV KSGHLGKQGK
RNPRYRRYWC QLKGDTLYYF ADAADLYFPR GTIDLRYGIS AEMMTEKGHE KSKDSPAFMI
TTDSRTYHFR ADSVANAKEW IKQLQKIIFR SHNDGDSVKI SLPLQNVVDV EAIPVIDFAE
TIKLRVIDND ETYAVDEYFF TFFEHGRDAR AKLNSLTQSN EARKLVSSEE GEERIDPLSK
GRGLPFSRRP SSPGLSENND DSGDEQNRPS VEGERNISDE GRRVLLDASH SGSRRRHRDS
QSSISQSANE SGDSFFSASE QTTASPTSPS GAGGIDMSAS QMLTGDGAFQ APTLRMPASR
AGTGEQLHRE PPHASIDQTP TERTADPSSN RTQSRVSMAG KAGGDSKESD KSSTPTPARP
AMQVLAAPLQ PAASLYGHMR NYSKRGLSYL SSSPKDYYGK ISTALAGGKR HYSEADDALA
PDDAVQDPED DMGAEEHEKR FQQHFALPET EKLLAVFYCS LHRVLPLYGK IYIGARNFCF
RSLLYGTRTK IVIPLKNIDN LEKEKGFRWG YPGMVVVIRG HEELFFDFSA GGLRDDCVVT
VFRAVEKAHD LQESTILSEH EKEEAEAAAA ERDLLHGARS AGQTRSPIEN RQDADPVLYE
GPPVLFDDLS ASMLDFKPKQ PLRITCLTIG SRGDVQPYIA LCKGLKAEGH HPRIATHHEF
GSWVKKHGID FVPVEGDPAE LMRICVEYGM FTPSFLLEVN SKFRGWLDTL LNSAWEASKG
SDLLIESPSA MAGIHIAEAL GIPYFRAFTM PWTRTRAYPH AFSVPTKKMG GHYNYYTYTI
FDNLFWRITS GQINRWRWKS LGLQPTSLEK LQQNKVPFLY NFSPSVVVPP LDFSDWVRVT
GYWFLDEGDT WTPPDDLMAF INQARKDKQK LVYIGFGSVT VADSKQLTQQ VVNAVLKADV
RCILSKGWSD RLETKDPGAV EVPLPSSVFQ IRSAPHDWLF RQIDAAVHHG GAGTTGASLR
AGVPTIIKPF FGDQYFFATR VEDVGVGIHL QKVTVNTLGR ALWIATHDER MRTKARVLGE
RIRSEDGVGT AIKAIYRDLD YARSLIKKRP KQTESGLELE EPEEESWTFV ENDGDVTIEE
LQTESESTAQ DSEGRSFGLM GRRPYLGSMG LRGRPT
//
