ID A0A0D1YNN4_9EURO Unreviewed; 1375 AA.
AC A0A0D1YNN4;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KIV84457.1};
GN ORFNames=PV11_00233 {ECO:0000313|EMBL:KIV84457.1};
OS Exophiala sideris.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=1016849 {ECO:0000313|EMBL:KIV84457.1, ECO:0000313|Proteomes:UP000053599};
RN [1] {ECO:0000313|EMBL:KIV84457.1, ECO:0000313|Proteomes:UP000053599}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 121828 {ECO:0000313|EMBL:KIV84457.1,
RC ECO:0000313|Proteomes:UP000053599};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala sideris CBS121828.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KN846951; KIV84457.1; -; Genomic_DNA.
DR STRING; 1016849.A0A0D1YNN4; -.
DR HOGENOM; CLU_000537_1_0_1; -.
DR OrthoDB; 76239at2759; -.
DR Proteomes; UP000053599; Unassembled WGS sequence.
DR GO; GO:0016906; F:sterol 3-beta-glucosyltransferase activity; IEA:UniProt.
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 Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR InterPro; IPR010610; EryCIII-like_C.
DR InterPro; IPR004276; GlycoTrans_28_N.
DR InterPro; IPR002213; UDP_glucos_trans.
DR InterPro; IPR003903; UIM_dom.
DR PANTHER; PTHR48050; STEROL 3-BETA-GLUCOSYLTRANSFERASE; 1.
DR PANTHER; PTHR48050:SF13; UDP-GLUCURONOSYLTRANSFERASE; 1.
DR Pfam; PF06722; EryCIII-like_C; 1.
DR Pfam; PF03033; Glyco_transf_28; 1.
DR SMART; SM00726; UIM; 5.
DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE 4: Predicted;
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Reference proteome {ECO:0000313|Proteomes:UP000053599};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 147..209
FT /note="Glycosyltransferase family 28 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF03033"
FT DOMAIN 479..571
FT /note="Erythromycin biosynthesis protein CIII-like C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF06722"
FT REGION 28..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 698..833
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1070..1091
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1200..1349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 709..725
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 746..798
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 801..824
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1249..1270
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1272..1306
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1317..1349
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1375 AA; 150669 MW; 58A3701290DFAF0B CRC64;
MSASDTPPPN PQPNEVIGLP VQIIQEAEAI AAANQEEGQT TQNPNNASAR HHGGASPHLD
DVPAPAYNSA DYGQLDISQN GLDTGARLGN DGRVNININQ RNSKLTKLLL PALRHQLELQ
RKKADGEPPI PEGLGETEGL PPPPMNIVIQ IVGSRGDVQP FVALGQVLKN KYKHRVRIAT
HPTFRDFVTE NGLEFFSIGG DPAELMAFMV KNPGLMPGMD SLKSGDVGKR RKGIYEIITG
CWRSTIEAGD GTGVQLADDS RSFDSAISFG TDPTMKPFVA DAIIANPPSF AHVHIAEKLG
IPLHLMFTMP WSPTQSFPHP LANIVSSNTD ANMANFVTYA LVDMLTWQGL GDVINRFRER
SLNLEPISIM WAPGMVSRLR IPWTYCWSPA LIPKPADWGN YIDISGFFFL NLSTNYTPAQ
ELADFLAAGP APVYIGFGSI VVDDPNAMTK MIFEAIKKTG QRALVSKGWG GLGADELGIP
EGVFMLGNCP HDWLFKHVSC VVHHGGAGTT AAGILAGRPT VVVPFFGDQP FWGAMTARAG
AGPKPIPYKQ LTADKLAAQI MAALKPESFE RANELSMQIK AEDGTEAGAQ SFHKQLHLPD
VRCSLAPTRT AVWRIKRTDI RLSPLAAVVL GSEGLLDFSD LKLYRAREYE TEDGPWEPIS
GGASALIGTI GNLSMGIADF PVEILKSLKT ASGELKDLHE REQQRKHSAG SETPTPTNLS
TERIPESAIA SPERNSLESK KSLERGRSQS PSGPAGPTYS HERVQSPTSS EPMGGATLVA
TTSSSRPSAM ASVISPDGSK RSHSHHRRWS HHRSHSRSHS GSPKPHHRDH SPACEEVGQI
SLETAISGAK AVGKIVSAGV KSPMDFTLSL AKGFHNAPKL YGDQTVRKSE KITDFQSGLR
AAGKEFTYGF YDGVTGLVTQ PLAGARKEGA AGFFKGAAKG FGGLILKPGA GIWGLPGYTA
KGIYAEVAKH FGSNVQNYII AARTAQGFED WKNSTPEERD AIIQAWKDSK LEEKKRGHLY
GTERKEAIES HILTKTHSDS VELVHGFKNT RHLSWDERKA LAERRDHLKK EQKELERREK
DVKKEEAKRS GGITGKIKSH CNYCPFDHDS SHHLDHTRSV SALELAKTHS PDEDSSMQDY
EHAITTAVTE TSKGNPSGDA IIERALRASL RELHNAGHNG NDHNDEAYKS ALRASLQEFK
RAQADHQQRR ESQETGTVST VAEQDEEDDD EEHRNQLEKV LTKSLEEYKA SQAARSQPTV
TDFAESNDSG IDTDYDNDKD FKRAVEESQR LHDQNQLKHA DLTKREEALG TNVTNGHGAE
EDEELKRAFT ASEQDEKTRQ EHLTKQRTEE EIVLDYIKKQ SLLEEEHRKQ RDAQT
//
