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Database: UniProt
Entry: A0A1B8CMA4_9PEZI
LinkDB: A0A1B8CMA4_9PEZI
Original site: A0A1B8CMA4_9PEZI 
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
//
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