ID A0A3D8R263_9HELO Unreviewed; 2034 AA.
AC A0A3D8R263;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
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=BP6252_09407 {ECO:0000313|EMBL:RDW68011.1};
OS Coleophoma cylindrospora.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Dermateaceae; Coleophoma.
OX NCBI_TaxID=1849047 {ECO:0000313|EMBL:RDW68011.1, ECO:0000313|Proteomes:UP000256645};
RN [1] {ECO:0000313|EMBL:RDW68011.1, ECO:0000313|Proteomes:UP000256645}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BP6252 {ECO:0000313|EMBL:RDW68011.1,
RC ECO:0000313|Proteomes:UP000256645};
RX PubMed=30018880; DOI=10.5598/imafungus.2018.09.01.13;
RA Wingfield B.D., Bills G.F., Dong Y., Huang W., Nel W.J.,
RA Swalarsk-Parry B.S., Vaghefi N., Wilken P.M., An Z., de Beer Z.W.,
RA De Vos L., Chen L., Duong T.A., Gao Y., Hammerbacher A., Kikkert J.R.,
RA Li Y., Li H., Li K., Li Q., Liu X., Ma X., Naidoo K., Pethybridge S.J.,
RA Sun J., Steenkamp E.T., van der Nest M.A., van Wyk S., Wingfield M.J.,
RA Xiong C., Yue Q., Zhang X.;
RT "IMA Genome-F 9: Draft genome sequence of Annulohypoxylon stygium,
RT Aspergillus mulundensis, Berkeleyomyces basicola (syn. Thielaviopsis
RT basicola), Ceratocystis smalleyi, two Cercospora beticola strains,
RT Coleophoma cylindrospora, Fusarium fracticaudum, Phialophora cf. hyalina,
RT and Morchella septimelata.";
RL IMA Fungus 9:199-223(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}.
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:RDW68011.1}.
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DR EMBL; PDLM01000010; RDW68011.1; -; Genomic_DNA.
DR STRING; 1849047.A0A3D8R263; -.
DR Proteomes; UP000256645; 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 Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
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 InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR001680; WD40_rpt.
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 Pfam; PF00400; WD40; 2.
DR SMART; SM00568; GRAM; 2.
DR SMART; SM00233; PH; 1.
DR SMART; SM00320; WD40; 4.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Reference proteome {ECO:0000313|Proteomes:UP000256645};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW WD repeat {ECO:0000256|PROSITE-ProRule:PRU00221}.
FT REPEAT 241..282
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT DOMAIN 873..971
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 33..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 666..760
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 778..803
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1054..1123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1141..1278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1333..1352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1488..1515
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2008..2034
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 688..714
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 782..802
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1161..1175
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1176..1240
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1256..1278
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2009..2034
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2034 AA; 225341 MW; 63203842F7EB9611 CRC64;
MAPVKKEKPE MSAFERKRLE NMAANAKMIK ELSTTAEKII PKPAPKPKST STPRKRSAPV
KREAPRPTRT SSRLAGIEAD SETLKRKNEV EAEYAALNSA AKRQRVSGDL NFSDVVVEGK
KWAKGDDFLS GIMRGAQPNL RTFSEDDIKE TTDEGLKALR EKMSGLELYE GFEPNQIKLT
PERIYALGFH PTTEKPLIFA GDKLGNLGLF DASQTPPEVK AEDNDEDEED ADIPEPAITA
FKVHSRTISS FVFPADGNSI YSGSYDSAIR KLDLQKGVAV EVYAPEDKDT DLPISSIAMP
STDQNLLYFS TLEGSFGRHD IRTPSDTEIW QLTDKKIGGF SLHPLHPHLV ATASLDRMLK
IWDLRKITGK GEDRRPTLLG EHESRLSVSH ASWSPAGHVA TASYDDTIKI HSFLDAKSFK
IGHDLDADAM APTATIRHNN QTGRWVTILK PQWQERPDDG IQKFVIGNMN RFVDVYTSEG
EQLAQLGGDG ITAVPAVAQF HPQKSWVAGG TASGKLCLWM LRHEGQQSAS IGAVMIRLLR
RKDANGCLTA KRAVVSVQDP PNLGSEPPKA QEAAARARVD ERNTTLSTTH AMPPEDELKK
RVARKLTKRR KEGHRVTMEI PERFRDGDDA DDDCTAATGS NAFMNQSVFG MIAAAGSQVD
FNARFDQQSS DDDDDPTEPS TATSDLQVNK QRHEKASSSA KPERHRRKFS ESKLMRSIPR
LGARSKSGPS SKLEASPDPK SPTEPEQPDS PSPQLSRTPS RHAPIMSQML EARAELSLRP
SFELPRTSTD GTGTSDTEES GSSSLAKRLK EIFKFETAEE VIEGPFVPYF PGLELTETEY
PCWLLKSVLL QGYMYITTKH ICFYAYLPKK SNQVVKSGYL AKSGRRNPKY SRYWFRLKGD
VLSYYTDPSD LYFPSGNIDL RYGISANVAD KEKGKDASHF TVTTHQRKFH FKADSNPSAK
EWVKALQKII FRSHNDGDSV KISLPIENII DIEHSQIIDF ADTCKIRVID NDETYAIDEY
FFSFFSFGKE ALNVLKILVE DTTAQKIPED LLALAPAQDG THSPKPRSPR QLTRAKPSMP
PPITTNVPPL PNNVGSTLSP LLSPGLGGRS PRASTDLSRG SSDYRQSLEL NKFGRRSVDL
SRKSKVEPAM RSLSTSRRSL SRNRLGDRRV SEKQGSSDSF VHSMEEPGSS AAFQSGSDET
QASASQILRG SDVFLSPTIQ RSPSAGRHQE TGSSRNAEAG PASARTEVDH TDSLQAPHHA
ATTGSVADSN AGSVDPSGSV PTLQSLVKAG SYPLQRAAGF AGYLNKHSKR MSTLLATESM
GYAEKVAGMW KGGKKHYDEQ QGPGTDDEGM DDDENTMSGD RFREHFALPV SEKLQASYFG
YLTRVLPLYG KVYISDRSFC FRSLLPGTRT KLILPLKDIL NAEKEKGFRF GYSGLVVIIK
GHEELFFEFN KTELRDDCAI TLLQNLETAR FLQESGLLST EEKEMAENAS AEHRALQEAR
GDGHTDHEVK MPKSVESSRH ESPAILFDDP RASILNFKPT ESLRITCLTI GSRGDVQPYI
ALCKGLIAEG HRPKIATHNE FKDWVESHGI AFAPVEGDPT ELMRICIENG MFTYSFLKEA
SSKFRGWIDG LLSSSWVACQ DTDILIESPS AMAGIHIAEA LSIPYFRAFS MPWTRTRAYP
HAFAVPEHKM GGAYNYITYV MFDNVFWKGT AGQINRWRKK ELGLQATNLE KMQPNKVPFL
YSFSPSVVIP PLDYSDWIRV TGYWFLDEGT NWSPPQELTD FIAKAREDKK KLIYIGFGSI
VVSDSAALTN TIIKSVLKAD VRCVLSKGWS DRLDKKDANE LEAPLPPEIH QIRSAPHDWL
FSQMDAAVHH GGAGTTGASL RAGIPTIIKP FFGDQFFFGS RVEDLGVGIY LRKLNVSVFS
RALWEASHSE RMIIKARVLG EEIRQENGVN TAIQSIYRDL EYARSLIKHK DGKVVSDDAL
EAGDEESWTF IGDDNDTDLS KRYHDWESTA GNRSTASSAG KSIGAAGPSR TTTL
//
