ID F8NKF5_SERL9 Unreviewed; 1323 AA.
AC F8NKF5;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 57.
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=SERLADRAFT_366132 {ECO:0000313|EMBL:EGO28421.1};
OS Serpula lacrymans var. lacrymans (strain S7.9) (Dry rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Boletales; Coniophorineae; Serpulaceae; Serpula.
OX NCBI_TaxID=578457;
RN [1] {ECO:0000313|EMBL:EGO28421.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=S7.9 {ECO:0000313|EMBL:EGO28421.1};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Eastwood D.C., Floudas D., Binder M., Majcherczyk A., Schneider P.,
RA Aerts A., Asiegbu F.O., Baker S.E., Barry K., Bendiksby M., Blumentritt M.,
RA Coutinho P.M., Cullen D., Cullen D., Gathman A., Goodell B., Henrissat B.,
RA Ihrmark K., Kauserud H., Kohler A., LaButti K., Lapidus A., Lavin J.L.,
RA Lee Y.-H., Lindquist E., Lilly W., Lucas S., Morin E., Murat C.,
RA Oguiza J.A., Park J., Pisabarro A.G., Riley R., Rosling A., Salamov A.,
RA Schmidt O., Schmutz J., Skrede I., Stenlid J., Wiebenga A., Xie X.,
RA Kues U., Hibbett D.S., Hoffmeister D., Hogberg N., Martin F.,
RA Grigoriev I.V., Watkinson S.C.;
RT "Evolution of plant cell wall degrading machinery underlies the functional
RT diversity of forest fungi.";
RL Submitted (APR-2011) 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}.
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DR EMBL; GL945430; EGO28421.1; -; Genomic_DNA.
DR RefSeq; XP_007314620.1; XM_007314558.1.
DR GeneID; 18810133; -.
DR KEGG; sla:SERLADRAFT_366132; -.
DR HOGENOM; CLU_000537_6_0_1; -.
DR OrthoDB; 76239at2759; -.
DR Proteomes; UP000008064; 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); 2.
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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 342..434
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 56..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 147..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 567..630
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..36
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..80
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..106
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..132
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 590..630
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1323 AA; 146799 MW; 6E8DFA415B31F613 CRC64;
MSSRVPEPPN TTMLSSGACD NPSQELDPQG QLEDGNDGFS SYRGRIKTAM EKTVDLGRSI
SGKFNPVLSN SPPSGSRRRF SSSNRKGKAK EQSHDRHTHQ EAFNDDSPFI RPRSPSSVPS
RPSLQSFRGV DSMRAGTQTL IQALQALPWT DEPGDEDGSN AAPQLDSDSE EGTSGEYYNR
MASSIHAIYR PVARSRRVDA SAPLAGLRGH LSTRTVQEGP YFSEGMVNSE DDGEVEDFEA
VTPRPAAHRP EYIKSQPPSS SVVSEAFERN AYSRTGSMTT VRVQRRTRLA EKLKEVFDLN
DIDEVVAEMP CWLLRSVLLQ GYMYLTNSHL CFFAHMPARE DQVLKSGSLN KKTQRTKRWI
KYWVVLKNDA ISWYQSSSDP YFPHGIVDLR YAISCDPSGE KDIRMRTTQR SLVLSADSVP
SRDEWVKAIR KVMFKAQNMG DSVKIAIPYS AVLDVEKSSA MDFSETIEVK VIDKEDNISM
DSYFFAYFHD LPAALEQIRD AVRAGRNFVQ RSSPQTVVDT TTLRPLPSVP QAIDRARSLP
IPDTSKITSG FSLSSLLRPF QDTLPLGRIG SAPDRSEGSE DYTHISKRGD TSFIPITTSP
PNISDVSESA KNKHPPSHST SLNVTTTDHT YPPSTLIGDM SDMAIKDSGS SGSSWNVGVP
SWLKGSRKVF SLSSAITSPG DSAAILSTSP VASNVSEVYS SPTPANRSGS GTNDLGYSIL
ETQEATVDLH ATEKFKNAFA FDDKETLLGY FTGYIFRLLP VYGRLYVSTN YFCFKSSGPL
TARTRMVLPL RDVLTVEKTK AARFGHHGLI IIIKGHEELF FEFGVEDRRN AFVTIVEKQL
EDVRKRLHAV EPQPLTQGKR DALILEEFEP RSSSSTDANS IPPPENLADS LPAVMFTSAS
STFLTFKPQK PLHFTFLTIG SRGDVQPYIS LARGLMADGH RVRIATHGEF KVWIEAHGIE
FGYVGGDPAE LMRICVDNGM FTVSFLKEGV QKFRGWLDDL LKTSWDACQG TDVLIESPSA
MGGIHIAEAL QIPYFRAFTM TWTRTRAYPH AFAVPEHKMG GSYNYMSYVM FDQVFWRATS
GQINRWRRNV LHLGSTSLDK MEPHKIPFLY NFSPHVVPPP LDWPEWIRVT GYWFLDDAEV
GAKKWVPPPD LIPFIDSAHQ AGKKVVYIGF GSIVVSNPQA MTRCIIEAIV QSGVYAILSK
GWSDRLHVKT GEAAEPEEPL PKQIYAISSI PHDWLFQRID AACHHGGAGT TGASLRAGIP
TIIRPFFGDQ FFWADRVEAL GIGSGVRKLT VESLTEALRS ATTDVKQIDR AKLVGEHIRA
PLL
//
