ID W9Y7X4_9EURO Unreviewed; 1473 AA.
AC W9Y7X4;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
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=A1O1_06108 {ECO:0000313|EMBL:EXJ85740.1};
OS Capronia coronata CBS 617.96.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Capronia.
OX NCBI_TaxID=1182541 {ECO:0000313|EMBL:EXJ85740.1, ECO:0000313|Proteomes:UP000019484};
RN [1] {ECO:0000313|EMBL:EXJ85740.1, ECO:0000313|Proteomes:UP000019484}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 617.96 {ECO:0000313|EMBL:EXJ85740.1,
RC ECO:0000313|Proteomes:UP000019484};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Capronia coronata CBS 617.96.";
RL Submitted (MAR-2013) 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:EXJ85740.1}.
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DR EMBL; AMWN01000005; EXJ85740.1; -; Genomic_DNA.
DR RefSeq; XP_007725178.1; XM_007726988.1.
DR STRING; 1182541.W9Y7X4; -.
DR GeneID; 19160977; -.
DR eggNOG; KOG1192; Eukaryota.
DR HOGENOM; CLU_000537_6_0_1; -.
DR OrthoDB; 76239at2759; -.
DR Proteomes; UP000019484; 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:UP000019484};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EXJ85740.1}.
FT DOMAIN 275..374
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 77..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 190..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 453..684
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1380..1473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..131
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..159
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..177
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..218
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 559..575
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 576..605
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 614..640
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1413..1432
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1473 AA; 163398 MW; 10F48892ED161847 CRC64;
MASLDPPPKK TGGRKLQKRN PNLNRLPSSH IPSRLRLGPD AQDDVTAPSR GRNAPAAYMN
QSIFSMIAAA GSRTDFNARF NDSSESEDEI AEEEQTTAPG DRPEASTSAP VKNEPAKEED
TQSEPTDQRS PGHRIVRSLP RLSARALKRK DKDRPSQQSG SPDSDKTSES SRSNPRDAPV
LSRLLSAEAE FQESGGNDTQ REPGSDAQQP RTRAESSPQT LLAARLMDIF GFDKPETVLA
EYPCWLLQSV LLQGYLYITK QHLCFYAYLP KKSHTVAKNG YLAKKGRTNS KYKRYWFSLK
GDVLSYYTDP SNLYFPSGNI DLTFGISAAL STEKGKRKEC RDFSVTTDHR TYHFRADSPS
SAKEWVQALQ KTIFRSHNDG DSVKISLPVE NIIDFEESPV VDFAETVKIR VIESEDSYAI
DEYFFSFFSF GQDALHVLGE LLTEAPARRR SEDVFSPIRR AESPSSPQSR PAELGPGSPG
RPSTPVLKDS IRATLLPFSP GGDGRMSPRK SGELSRGASP SRSSGELPRE YGRASFERGR
RSGSTSRLEV SASRRNGRSP LARHHDSEDS YVPSIDKETD SSTAPLSPRV EAQMSASQIL
TRSDVFHSRP ANRMETLASV STEPTRTSSD GGTILSSSPH REAASPRAVR GMADVTGHSP
RGARAPVHNE ATFPDNDKKV GKDDPSPALQ DLVKAGTYPL QRAGAFAYYL KNRSVSMRKL
LAEESMSYLE KVSGMWAGGR KHYGENEGIV PEDRGIDPED EEANVGHGDR FRAHFALPPT
ERLQATYFGF LHRVLPLYGK IYISNRKFCF RSLLPGTRTK LVLPLKDIEN VDKEKGFRFG
YHGLVLVIRG HEELFFEFSS AEHRDDCTVT LLHSLETVRY MAESGLLGQQ DEDDAEAARE
EHRMLQEARR NSGGEHQLVL PDTAEAIYSH AETSAASMGD PGASIINFRP SAPMRITCLT
IGSRGDVQPY IALCKGLLAE GHRPRIATHA EFGPWVQKHG IDFRPVEGDP AELMRICVEN
GMFTYSFLRE ASVKFRSWID QLLTSAWRAC QDSDLLIESP SAMAGIHIAE ALGIPYFRAF
TMPWTRTRAY PHAFAVPEHK IGGAYNYYSY VMFDNVFWKA IAGQVNRWRK KELGLRSTNL
DKMQPNKVPF LYNFSPHVVV PPLDYSDWVR VTGYWFLDEA QDWQPTEELT AFIRKARDDG
KKLVYIGFGS IVVSDPAALT KTVVESVMKA DVRCILSKGW SDRLGDPTRA VKAEVPLPAE
IFQIKSAPHD WLFRQIDAAV HHGGAGTTGA SLRAGVPTVI KPFFGDQFFF GSRVEDLGVG
ICLKKVNVSL FSRALWEATH SERMIVKARL LGEQIRKENG VQTAIQAIYR DLEYAKSLIK
PRPAGPGTSA SATGEPDDGG DIEENWTFIG DESDPEMQRR IQDWESPRRG RAGPRWSMDS
PAPATTPGPA AAAAAPAAGL RAMQRVEPVR KGR
//
