ID A0A0G4LPZ9_9PEZI Unreviewed; 1458 AA.
AC A0A0G4LPZ9;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
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=BN1708_003732 {ECO:0000313|EMBL:CRK24041.1};
OS Verticillium longisporum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX NCBI_TaxID=100787 {ECO:0000313|EMBL:CRK24041.1, ECO:0000313|Proteomes:UP000044602};
RN [1] {ECO:0000313|EMBL:CRK24041.1, ECO:0000313|Proteomes:UP000044602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VL1 {ECO:0000313|EMBL:CRK24041.1};
RA Wang D.B., Wang M.;
RL Submitted (MAY-2015) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CVQH01016668; CRK24041.1; -; Genomic_DNA.
DR STRING; 100787.A0A0G4LPZ9; -.
DR OrthoDB; 76239at2759; -.
DR Proteomes; UP000044602; 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: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:UP000044602};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 314..410
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 1..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 107..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 506..527
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 545..672
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1220..1240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1370..1458
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..31
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..69
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..87
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..137
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 178..192
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..207
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 545..559
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 562..577
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 578..672
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1390..1405
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1444..1458
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1458 AA; 162223 MW; F50603B64D0645C4 CRC64;
MAPTHPSLPP ISTALSPTTA SPNSAQPTPT PTDEDPKKRV ARKLRRKRRN ETYAMDLPER
LKGGNDSENE EDLMPAGNTQ NGPPMFMNMN QSIFGLIAAA GSRVDFHDRF EGQSSDDDDE
SGHQTAKHDK HKSTSPRPES NLSKTTVMGK ATKERRHRRS GSAGNVIARS LQALPRLGKR
RSKKESSKLE PPSEDASESS VPQSSLHESA EEDQDQYKLA PVMSRMLEAR ADVASRPSFD
LDRLTSEQSR RDSSDLGPSP LALRLAEIFE FTKPEEVIEE YPCWLLQSVL LQGYMYITAR
HICFYAYLPK KAHEVVKSGY LSKSGKRNPK YNRYWFRMKG DVLTYYRDPS NVYFPSGQID
LRYGISASIT DKDKAGLHFS VTTSHRTYHF RADSAPSAKE WISMPIENVI DIEDSQMLQF
ADTCKIRVID NDETYAIDEY FFSFFSFGKE AINVLKIMFE GASAETKDPA DLPKGASART
SIAANRRSIG PDKIGIARLP ENVKATLSPM SPTSPLGPSP RPSADVARPS MDAFRVFGRK
SLDLSSVTRD ASPRRSFSGS RSHSRNRLED SRNTVDKNES SDSYVQSSME DPSFSAMAAS
SNEDASASQI LHRSDVFQSP TMRRSGSRTR QSSKKTVQGT QSPPALATYS GQHAATTGSI
ADDPNRGPSL QSITKMGAYP LQRVGAFAEY LNSSSRRMSS MLATESMGYV EKVSGMWKGN
RKHYDAPPET RTDDEDLYED SEGRVQLSTE RFRAHFALPG TEKLQVTYYG FLFQVLPLYG
KIYISDRFLC FRSLLPGTRT KLILPLKDIE NVDKEKGFRF GYSGLVLVIR GHEEVFFEFS
QRDAREDCFG HLLKSVERSR FLHNSGMLNQ EDKEEAEYAL AEREALKEAR QDEFHDHEVK
LPEQTSCLSD APTILFDDPK ASFLNFKPAQ SLKVTCLTIG SRGDVQPYIA LCKGLIAEGH
RPRIATHAEF QPWIESHGIE FAKVEGDPGE LMRLCIENGT FTFSFIREAN SMFRGWLDEL
LVSAWEACQG SDLLIESPSA MAGIHVAEAL GIPYFRAFTM PWTRTRAYPH AFVVPESKLG
GAYNYMTYIM FDNIFWKATA GQVNRWRNKT LKLPNTNLEK MQPNKVPFLY NFSPSVVAPP
LDFSDWIRVT GYWFLDEATK WKPPKELTDF IAQARADEKK LVYVGFGSII VTDTAKMTQE
VIDAVLKADV RCILSKGWSD RVASSGDAGT DDAAAASKRE EPVMPPEIHV IKSAPHDWLF
SQIDAAAHHG GSGTTGASLR AGIPTIIRPF FGDQFFFGNR VEDIGVGICL KKWGATSFAR
ALWEATHNER MIIKARVLGE QIRKENGVES AIQCIYRDME YATSLVKRKG DKNRKGAQGQ
QADARTGSDP DADADEEEES WTFIGGDEPD PDVVTQRLSA MHASASGGHV PGMGTLRADS
KSLGSKVLGS SPGSQVAA
//
