ID J9VMM9_CRYNH Unreviewed; 1615 AA.
AC J9VMM9;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=sterol 3beta-glucosyltransferase {ECO:0000256|ARBA:ARBA00012650};
DE EC=2.4.1.173 {ECO:0000256|ARBA:ARBA00012650};
GN ORFNames=CNAG_02834 {ECO:0000313|EMBL:AFR93859.1};
OS Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 /
OS CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=235443 {ECO:0000313|EMBL:AFR93859.1, ECO:0000313|Proteomes:UP000010091};
RN [1] {ECO:0000313|EMBL:AFR93859.1, ECO:0000313|Proteomes:UP000010091}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H99 / ATCC 208821 / CBS 10515 / FGSC 9487
RC {ECO:0000313|Proteomes:UP000010091};
RX PubMed=24743168; DOI=10.1371/journal.pgen.1004261;
RA Janbon G., Ormerod K.L., Paulet D., Byrnes E.J.III., Yadav V.,
RA Chatterjee G., Mullapudi N., Hon C.C., Billmyre R.B., Brunel F., Bahn Y.S.,
RA Chen W., Chen Y., Chow E.W., Coppee J.Y., Floyd-Averette A., Gaillardin C.,
RA Gerik K.J., Goldberg J., Gonzalez-Hilarion S., Gujja S., Hamlin J.L.,
RA Hsueh Y.P., Ianiri G., Jones S., Kodira C.D., Kozubowski L., Lam W.,
RA Marra M., Mesner L.D., Mieczkowski P.A., Moyrand F., Nielsen K., Proux C.,
RA Rossignol T., Schein J.E., Sun S., Wollschlaeger C., Wood I.A., Zeng Q.,
RA Neuveglise C., Newlon C.S., Perfect J.R., Lodge J.K., Idnurm A.,
RA Stajich J.E., Kronstad J.W., Sanyal K., Heitman J., Fraser J.A.,
RA Cuomo C.A., Dietrich F.S.;
RT "Analysis of the genome and transcriptome of Cryptococcus neoformans var.
RT grubii reveals complex RNA expression and microevolution leading to
RT virulence attenuation.";
RL PLoS Genet. 10:E1004261-E1004261(2014).
CC -!- SIMILARITY: Belongs to the glycosyltransferase 28 family.
CC {ECO:0000256|ARBA:ARBA00006962}.
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DR EMBL; CP003822; AFR93859.1; -; Genomic_DNA.
DR RefSeq; XP_012048164.1; XM_012192774.1.
DR GeneID; 23886388; -.
DR KEGG; cng:CNAG_02834; -.
DR VEuPathDB; FungiDB:CNAG_02834; -.
DR HOGENOM; CLU_000537_6_0_1; -.
DR OrthoDB; 76239at2759; -.
DR Proteomes; UP000010091; Chromosome 3.
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 Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR048066; ATG26_PH_GRAM1.
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; 1.
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 Coiled coil {ECO:0000256|SAM:Coils};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AFR93859.1}.
FT DOMAIN 496..588
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 1..161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 214..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 298..335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 660..697
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 723..894
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1528..1587
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 368..402
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..30
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..88
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 105..152
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 214..228
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..284
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 307..326
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 666..683
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 723..762
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 802..846
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 849..864
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1615 AA; 179332 MW; 1102F81877EA758A CRC64;
MPPPISPTPH PLQPPFPPTA IAPDPNPPPH HQQAAESLVN TAAQHVAPTC PPTSDESPQM
ADQATHSSDD SLISSRQTPQ QEETESAIIS GTLPDEMEPA KDAQTVRFSS PSPTSYSTHK
YPTEVTAGLN EPLMSSRAPS TASSQTPESS PDFRASRDIG SMNADRSPPF FILAVLRIPV
IHNSSTTPPA SVHVQQIRMG ASALVSALNA LPWEEDDESD DGEDDDEFME PARGSSSAMY
ERKQRPQISR LGSSLSTIRP MSSSSPTHAK APSTSHGSHP THTLHFPFRQ NAIARRARRP
GTTELDYQYA TPETSSRRTN AAGSEASSEG EVPLPKGFVS HPNLIIPSGE GEAAAHADLK
LINDRICKEQ QIADVEEQAE ILRSAEEQRM RLGKEFVRHK NRDSADLNVD AALREGGSEG
DDVIEEQMQT NEAEKRITRK ERLAERLMEV FGLEEREQVL EEMKCWLLRS VMLKGYMYLT
KKHICFFANM PNENNLLVKS GPLSKKASRS KLNTKFWVVL KNDVLSWYES TSDPYFPKGN
ISLQYCHSCD AVDGTRFKVR TSERNYTFTA DTESSRDEWV KAIQKVMFKT QHEGETIKLI
IPLEAVVDVD MSPTLEFTET IEIKCIDAED QMSVDSYFFA SFPNNDHAFS AIQKLVRERP
SPPELPRISS ATTIHANQES LDTSHATIKR HGTDSSAEKL VMASHRPFRK ISSILKPLIL
KSSGEEPHEE HSESPHHDDD DEASHLPHIE AISNRQRPEE ESDNDDFDGY PPRQIGPPPP
SMNDDARNWR PSWIRKPASK LFGNSPSGSF VSHPGRSPTD SPTTVAESGP SLRSRTGRTK
QSSVTEVLEP PIHHEEEGSE DEMSSKPSVV DSNSAETARK RAARLSWTSE TSSGSQMIKS
KSEFSMLGSE SGHSESAETI RKFRSFFALS DKEDLIDHFP GYLYRVLPMI IPIRDLYGLK
AQKAFRFGHS GLTVVIKGHE EIFIEFRSAS RRKACIILLE ERMEAVRLSG ENTTIDSHKV
EVRIMEDLDE SIPVEPKSPW PVSPSPLFGS TTSTSFLEFK PEPMKIACLT IGSRGDVQPY
IALCKGLQAE GHTTKIATHG EYKDWVEGHG IAFENVGGDP AELMQMCVDN GMFTVSFLKE
GLQKFRGWLD DLLNSSWEAC QGSDLLIESP SAMSGIHIAE ALRIPYYRAF TMPWTRTRAY
PHAFAVPEHG RGGPYNYMTY TMFDQVFWRA ISGQVNRWRR NVLGLDATTF DKMEQHKVPF
LYNFSPTVVP PPLDWTEWIH VTGYWFLDKA DEKQGEKSWT PPQGLTDFID KAHGEKKKVV
YIGFGSIVVS DPEEMTRCVV EAVMNSGVCA ILSKGWSDRG SKKGEPKGDS EGADGVKYPP
EIFAIDSIDH GWLFPRIDAA CHHGGAGTTG ASLRAGIPTI IKPFFGDQAF WAERVESLNV
GSAIRRLTSH QLASALIKAT TDEKQISKAR VVGDMIRKEN GIARAIEAIY RDLEYAKSII
KSPPSTDDRT PEKISSLLHP LTTADLSLNR VRSRSRSRSR SSQGRFSPRR YPVDDDGWSV
VSGGSRSRSG SASAVASPER RPLNVGSTLG SHVFKTALLP NPFGKWRNLE EGDDR
//
