ID A0A1B8CMA4_9PEZI Unreviewed; 1433 AA.
AC A0A1B8CMA4;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 32.
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=VE00_01706 {ECO:0000313|EMBL:OBT47968.1};
OS Pseudogymnoascus sp. WSF 3629.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1622147 {ECO:0000313|EMBL:OBT47968.1, ECO:0000313|Proteomes:UP000091997};
RN [1] {ECO:0000313|EMBL:OBT47968.1, ECO:0000313|Proteomes:UP000091997}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WSF 3629 {ECO:0000313|EMBL:OBT47968.1,
RC ECO:0000313|Proteomes:UP000091997};
RA Palmer J.M., Drees K.P., Foster J.T., Lindner D.L.;
RT "Comparative genomics of Pseudogymnoascus destructans, the fungus causing
RT white-nose syndrome of bats.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000091997}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WSF 3629 {ECO:0000313|Proteomes:UP000091997};
RX PubMed=29295979; DOI=10.1038/s41467-017-02441-z;
RA Palmer J.M., Drees K.P., Foster J.T., Lindner D.L.;
RT "Extreme sensitivity to ultraviolet light in the fungal pathogen causing
RT white-nose syndrome of bats.";
RL Nat. Commun. 9:35-35(2018).
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}.
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DR EMBL; KV454572; OBT47968.1; -; Genomic_DNA.
DR STRING; 1622147.A0A1B8CMA4; -.
DR OrthoDB; 76239at2759; -.
DR Proteomes; UP000091997; 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; 1.
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 Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Reference proteome {ECO:0000313|Proteomes:UP000091997};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 274..368
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 74..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 140..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 447..491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 506..601
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 619..647
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 723..744
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1398..1433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 94..109
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..156
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..171
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 449..491
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 520..540
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 559..579
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 580..601
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1433 AA; 159740 MW; E185F4DABE63C87B CRC64;
MIRSHEDVKK RIGRKLTKKR REDRRVTMEI PQRFEDGDDA DEDCTAPKGQ NGLINQSVFG
MIAAAGSQAD FHARFDGQDS DDEEDETAEP EDASRPSEAS SSPATTKAPT DERISRHRFH
RRNLSDNKLL RSLSQLGIKN RSKHAHLSSA SSDPVTPEKI KDTERDHITR SPFKGPPIMS
QMLEAKAAAV QRASFDSRRS DYISGQSDGG ADGVEGLPSD LAIRLMEIFE FESPELVIDE
YPCWLMKSVL LQGYMYLTEK HICFYAYLPK KSNEIVKSGY LSKRGLKNPK YNRYWFNLQG
DVLSYYTDPS DKYFPSGNID LRYGISASVV DKEKTFFEVT TNHRKYQFHA DSVPSAKEWV
KALQKIIFRS HNDGDSVKIS LPIENVIDVE DSPVIEFAET CKIRVIDNDE TYAIDEYFFS
FFSFGKQALS VLRTLVSDSA AKQIPEGLLV QPQGNSGSNS PKAGSSRPSL AISTRETKPF
PNLGKATSSG LEESVKATLT PLISSPLHVH SPRASGDFSR ASFDITQRSA SQTRASRRSM
DVSRFNLDGQ GPSTDRRSFS RNRASEKKNS EKQDSSDSYV HSMEESSAAA QSASEDVEGS
ASQILRGSEG FFQPTIHRSA SASRRRDDAQ LPASPLVPHA LTAPPRAATI DAYERPKLTE
ADNASSPSLQ TLAKAGAYPL QRAAGFANYL NRHSKRMSTL LATESMGYVE KVSGMWKGGK
KHYDEPLGQG LEDDTDDEGG QSDGAEHRFQ AHFALPAGER LHAAYFGYFH RVLPLYGKIY
ISNRSFCFRS LLPGSRTKLI LPLKDIENVD KEKGFRFGYS GLVVVVKGHE ELFFEFGQPD
ARDDCCVTLL QNLETIRYLK ESGLLTQEEE ESAAWAVAEH KALQEARQES RQHIHDLELP
TTAEGASTET APIMFDDPRA SILNFKPTES LRITCLTIGS RGDVQPYIAL CKGFIAEGHR
PKIATHVEFK DWIEGHGIEF APVGGDPAEL MRICVENGMF TYSFLKEAST NFRGWIDDLL
SSSWLACQNS DVLIESPSAM AGIHIAEALG IPYFRAFTMP WTRTRAYPHA FAVPEHKMGG
AYNYITYVMF ENVFWKAIAG QINRWRKKEL SLPRTSLEKM QPNKVPFLYN FSPSVVVPPL
DYSDWIRVTG YWFLDEGADY KPPKEISDFI AKARADGKKL VYIGFGSIVV SDSAALTKTV
VNSVLKADVR CILSKGWSDR LDKIGATEPE VLPEEILQIK SAPHDWLFTQ VDAVTHHGGS
GTTGASLRAG KPTIIKPFFG DQFFYGGRVE DLGVGIYLRK LNVSVFARAL WEATHSERII
AKANLLGEQI RSENGVDTAI QCIYRDMEYA NSLIKRKSGS HEGLAEDIEE SWTFIGDDND
PELMSRIHAW DPRVVLAHSR DLTEPQPKDA AESPVPTPRS ETPLPSEKDA ETK
//