ID A0A0F4YWG5_TALEM Unreviewed; 1419 AA.
AC A0A0F4YWG5;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE RecName: Full=Sterol 3-beta-glucosyltransferase {ECO:0000256|ARBA:ARBA00017894};
DE EC=2.4.1.173 {ECO:0000256|ARBA:ARBA00012650};
DE AltName: Full=Autophagy-related protein 26 {ECO:0000256|ARBA:ARBA00029843};
GN ORFNames=T310_3989 {ECO:0000313|EMBL:KKA21978.1};
OS Rasamsonia emersonii CBS 393.64.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Rasamsonia.
OX NCBI_TaxID=1408163 {ECO:0000313|EMBL:KKA21978.1, ECO:0000313|Proteomes:UP000053958};
RN [1] {ECO:0000313|EMBL:KKA21978.1, ECO:0000313|Proteomes:UP000053958}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 393.64 {ECO:0000313|EMBL:KKA21978.1,
RC ECO:0000313|Proteomes:UP000053958};
RA Heijne W.H., Fedorova N.D., Nierman W.C., Vollebregt A.W., Zhao Z., Wu L.,
RA Kumar M., Stam H., van den Berg M.A., Pel H.J.;
RL Submitted (APR-2015) 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}. Preautophagosomal structure membrane
CC {ECO:0000256|ARBA:ARBA00004623}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004623}.
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:KKA21978.1}.
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DR EMBL; LASV01000162; KKA21978.1; -; Genomic_DNA.
DR RefSeq; XP_013328590.1; XM_013473136.1.
DR STRING; 1408163.A0A0F4YWG5; -.
DR GeneID; 25316338; -.
DR OrthoDB; 76239at2759; -.
DR Proteomes; UP000053958; Unassembled WGS sequence.
DR GO; GO:0034045; C:phagophore assembly site 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:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0030259; P:lipid glycosylation; IEA:InterPro.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
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 Autophagy {ECO:0000256|ARBA:ARBA00023006};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW ECO:0000313|EMBL:KKA21978.1};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927};
KW Reference proteome {ECO:0000313|Proteomes:UP000053958};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KKA21978.1};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 291..390
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 1..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 74..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 470..567
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 601..664
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1349..1419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 869..896
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 26..51
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..121
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..171
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..193
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..233
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 523..537
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 601..617
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1366..1382
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1399..1419
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1419 AA; 158139 MW; FC477662C63609F2 CRC64;
MPHPDDAGKS RLGFRLSTPS KSHRRMSSSR MPERLKDGDD AHEDVTAPPR DANGRDVHYM
NQSIFSMIAA AGSKSDFHSR FDDSSDSDGG EAEKPEEESS RRPTSRSKPQ KIEKPTLEVP
DEDDKEEGEG SAEERGRGHR RRISDSKLMR SISKFHAKHS KGKESVDKSQ PAARDKSVSP
SPARLSGSMT PRSAPVLSRM IEAQSRYDPA ASSTGTATST EEGNGEKKSS ESASTSLLAT
RLKEIFGFDR PEQVIGEYPC WLMQSALLQG YMYVTEGHLC FYAYLPQKSN TAVKTGYLAK
RGRKNPKYSR YWFSLKGDVL SYYADPSKLY FPSGHVDLRY GISAALSDQK DKGNEVKDFT
VTTDNRTYHF RADSAASAKE WVRALQKVIF RSHNEGGRVK ISLPIENVID IEENPMIDFA
ETFKIRVVDS GETYAIDEYF FSFFNYGKDA FNVLKNLIND TPAQRISQDP LATFGLKGSP
ESSRHRSRSA DTHQRSSSSG PFVEAGAGDA GGVSVFNGRS AHSRTKSDSR SRRRSDVMSR
ASLAQSQQDR SLQEKQHDSS DSFVQSLGQG TESSVILQST TDTAESASQI LNRSDVFRSP
TIHRLRSTPS ASEDTARSGP RKVSVGDVAP PGYSLDELSS KRDQESQGAI SESDHDAPSS
SKVYATSTPT LQEIVRAGAY PLQRAAGFAE YIKSRSRQMS SLLASESMGY IEKVSGMWTG
GGRHYAEGEG FHSERFLDQE DMEHSSSHGD RFRAHFALPS TEKLQATYYG YLHRVLPLYG
KIYIGSTKFC FRSLLPGTRT KMILPIKEIE NVEKEKGFRF GYQGLVVIIR GHEELFFEFN
TSDARDDCAV TLHQSLEAVR FLVESSVLTQ QENEEADAAK AEHQLLQEAR QDILDEESQE
VHPIFDDPRA SIINFKPAES LRITCLTIGS RGDVQPYIAL CKGLLAEGHR PKIATHAEFE
PWVRKHGIDF APVEGDPAEL MRICVENGMF TYSFLKEASL KFRGWIDDLL SSAWKSCQDS
DVLIESPSAM AGIHIAEALR IPYFRAFTMP WTRTRAYPHA FAVPEHRMGG AYNYITYVMF
DNVFWKAISG QVNRWRKKEL GLRGTNLDKM QPNKVPFLYN FSPSVVPPPL DYPDWIRVTG
YWFLNEGADW TPPPELSEFI QRARQDGKKI VYIGFGSIVV SDPAALTKTV VESVQKADVR
CILSKGWSDR LGDPTSTRPE ITLPPEIHQI QAAPHDWLFT QIDAAAHHGG AGTTGASLRA
GVPTIIKPFF GDQFFFGARV EDLGVGICMK KLNVSVFSRA LWEATHSERM IVKARRLGEQ
IRKENGVANA IQAIYRDLEY ATTLTRQRSA VSSTPFTPSG TDEKTVTEDD LEDIEETWTF
VDDVTDPDLS KKGRGMDHEN SGGQSQDRSQ TRPADTSLA
//
