ID A0A0P7BA50_9HYPO Unreviewed; 1423 AA.
AC A0A0P7BA50;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 41.
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=AK830_g9321 {ECO:0000313|EMBL:KPM37255.1};
OS Neonectria ditissima.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Neonectria.
OX NCBI_TaxID=78410 {ECO:0000313|EMBL:KPM37255.1, ECO:0000313|Proteomes:UP000050424};
RN [1] {ECO:0000313|EMBL:KPM37255.1, ECO:0000313|Proteomes:UP000050424}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R09/05 {ECO:0000313|EMBL:KPM37255.1,
RC ECO:0000313|Proteomes:UP000050424};
RA Gomez-Cortecero A., Harrison R.J., Armitage A.D.;
RT "Draft genome of a European isolate of the apple canker pathogen Neonectria
RT ditissima.";
RL Submitted (SEP-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 -!- 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:KPM37255.1}.
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DR EMBL; LKCW01000172; KPM37255.1; -; Genomic_DNA.
DR STRING; 78410.A0A0P7BA50; -.
DR OrthoDB; 76239at2759; -.
DR Proteomes; UP000050424; 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:UP000050424};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KPM37255.1}.
FT DOMAIN 282..378
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 1..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 85..189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 202..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 455..485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 539..578
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 603..663
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1361..1423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..70
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..103
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..188
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 549..565
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1380..1395
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1403..1417
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1423 AA; 159792 MW; 4744E3CFA3A2B8B9 CRC64;
MAPPSDAGPV RPSVDDEDIK KRVSRRLHKK RREDRTSTVF PEPLRDSDDS AEEEDTPSQG
PPQFMNMNQS IFGLIAAAGS RVDFNDRFDG ISSDEEEGHE TTQQGTPTDD LSKTSVLKVS
SKDKSSRRKR LSGHKLLRSL PTLPKLLPKR RQSSRLSAPK EETEESSEAS ASGTSTPPTF
TLTRHDSRQA PMMSRMLEAK AEMTSRPSFD VERASSDVGR SESTDLPPLA KKLMEIFEFD
TPEQVIEEYP CWLLQSVLLQ GYMYITSKHI CFYAYLPKKA HDIAKTGYLM KSGKRNPKYN
RYWFRLKGDV LAYYRDSTNL YFPHGQIDLR YGISSNITDT DKEGLHFSVV THHRTYNFRA
DSAPSAKEWV KSLQRVIFRS HNDGDSVKIS LPIVNVIDIE DTQMIQFADT CKVRVIDNDE
TYAIDEYFFS FFSFGKEAIN VLRILIEDAS GSRDEDKVLG RQEKASSLPP SRRSPPLAAR
HSIHLDKIRT GKLPEQVKAT LSPMSPHSPG LSPRVSSDVP YRASLDAFRQ IGRKSLDLSG
VIREQSPRRS FSGTRRHRDG NQTPKQEQDS TDSFVQSSIE EPSLSILAAS SNEDPSASQI
LRGSEVFHSP TMRRSASASR AADSKKPTPR NSSAQYVPHR VQHAATTGSL STQPDSVDAQ
RPGTPTLQSI TKIGAFPLQR ANAFAEYLSK TSQRMGSLFA TESMGYVEKV SGMWKGGHRH
YDEPAGLRTD DDDLEEDADG KVQISMDRFR AHFALPETEK LQATYFGHIL RVLPLYGKFY
ISDRSFCFRS LLPGTRTKLI LPLKDIETVH KEKGFRFGYS GLVVVIRGHE ELFFEFGQAE
IRDDCAITLL QSLETTRYLE KSGLLDQEEL EEENFAIEER DALKSARQDE FADHQLELPH
HSSGVSNAPT ILFDDPNCSS LAFKPQTSMK ITCLTIGSRG DVQPYIALCK GLLAEGHKPR
IATHGEFQGW IESHGIEFAR VEGDPAELMR LCIENGTFTW SFLREANSTF RGWLDDLLDS
SFKACEGSEL LIESPSAMAG IHIAEKLGIP YFRAFTMPWT RTRAYPHAFI MPEHKMGGAY
NYMTYVMFDN IFWKATAYQV NRWRNKTLGL PNTSLEKMQP NKVPFLYNFS PSVVAPPLDF
SDWIRVTGYW FLDEGGEWEP PKELQDFITK ARADGKKLVY VGFGSIIVND PAKMTQEVID
AVQKADVRCI LSKGWSDRIS SKEDPSKPRA EEPAMPDAIH VIKSAPHDWL FRQIDAAAHH
GGSGTTGASL RAGIPTIIRP FFGDQFFFAS RVEDLGVGVW VKKWGTNSFG RALWEVTRNE
RMIVKARVLG EQIRSETGVD TAIQCIYRDL EYAKSLIKRK AGKNTEADPA EDDETEESWT
FVGRDEPDPD HVTKKLSDGL MGPATSSEKS LGSQVMTSPA VAI
//
