ID M7TR78_BOTF1 Unreviewed; 1210 AA.
AC M7TR78;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=Putative udp-transferase protein {ECO:0000313|EMBL:EMR83765.1};
GN ORFNames=BcDW1_7607 {ECO:0000313|EMBL:EMR83765.1};
OS Botryotinia fuckeliana (strain BcDW1) (Noble rot fungus) (Botrytis
OS cinerea).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Botrytis.
OX NCBI_TaxID=1290391 {ECO:0000313|EMBL:EMR83765.1, ECO:0000313|Proteomes:UP000012045};
RN [1] {ECO:0000313|Proteomes:UP000012045}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BcDW1 {ECO:0000313|Proteomes:UP000012045};
RX PubMed=23704180; DOI=10.1128/genomea.00252-13;
RA Blanco-Ulate B., Allen G., Powell A.L., Cantu D.;
RT "Draft genome sequence of Botrytis cinerea BcDW1, inoculum for noble rot of
RT grape berries.";
RL Genome Announc. 1:E0025213-E0025213(2013).
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DR EMBL; KB707981; EMR83765.1; -; Genomic_DNA.
DR AlphaFoldDB; M7TR78; -.
DR HOGENOM; CLU_000537_2_0_1; -.
DR Proteomes; UP000012045; 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 PANTHER; PTHR48050; STEROL 3-BETA-GLUCOSYLTRANSFERASE; 1.
DR PANTHER; PTHR48050:SF5; UDP-GLUCOSE,STEROL TRANSFERASE; 1.
DR Pfam; PF06722; EryCIII-like_C; 1.
DR Pfam; PF03033; Glyco_transf_28; 1.
DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE 4: Predicted;
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EMR83765.1}.
FT DOMAIN 236..395
FT /note="Glycosyltransferase family 28 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF03033"
FT DOMAIN 554..657
FT /note="Erythromycin biosynthesis protein CIII-like C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF06722"
FT REGION 1..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 96..161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 199..223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 770..897
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1142..1210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..59
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..116
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..133
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 199..218
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 777..804
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 805..824
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 831..850
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 858..897
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1142..1201
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1210 AA; 133141 MW; 697B2DED8ED1DE2E CRC64;
MSGAPAETAA NSGPTLADGP AQIPLQSRSL SATKTDLPAA DITHNVQQEE EKRPDLAPTK
VWQTERPRAT TKSSLLAPAY KRGETNTSLL NEAIWSRGPD YKDDGSTSSS SSSSSEDEED
APAEKKKRNY VPGKKNVVDT GGRKQYNKFQ VGNDDYSTRG RVSKRDGRLN ISFNETNNRG
YLAKALGATF FSKVEHDDMT GETPEANLAR RQRGKLSRPS AEEVVTSNIP RPRLNIVVMV
IGSRGDIQPF LKLGKSLKEY GHRVRIATHP AFRDFVQKDS GLEFFSVGGD PAELMAFMVK
NPGMIPTMET LKKGEVGRRR EQMAEMFEGF WRACINATDE EKDVTNLKMM GDKEPFVADA
IIANPPCFAH IHCAERLGVP LHLMFTFPYT PTQSFPHPLA NIKKTNVDPG YTNFMSYPLV
EMMTWQGLGD LVNNFRVKTL GLEPVSTLWA PGQLYRLKVP YTYLWSPGLV PKPKDWGPEI
DIAGFVFLDL ADTFTPPDDL VKFLDDGEPP VYIGFGSIVV DDPDRFTEMI FEAVKKAGVR
ALVSKGWGGL GGENTPDNVF MLENTPHDWL FPKVKAVVHH GGAGTTAIGL KCGKPTMIVP
FFGDQQFWGS MIGTSGAGAD PVPYKELTAD KLAEGIKQCL TDKAREAVEK IAKDIEAEGD
GAQNAVKSFH RSLKLRGEHS MRCSILEDRV AVWTMKGTNL RLSALAAELL VERKKITWKQ
LRLIRHHEWN DFEGPGEPIS GVTTAVTGTV TGIAAGVGSI PFKVRKTIKR RSVHEEKKKR
KSEDTRKSES GTTLVEKKPD SQEHADNSNA STLNNQTIQE ESRQDENSGP SKEIKNINSA
TETHDTNPEA AANSPCDAGM ANHTTSGEPT RQHSQANREE QQNSQTKNID NQSMLSSDPI
NNEAEAVVKD IGHGFGETAE AVARAPMDLA LALAQGFHNA PRLYGDTTVR RPTRITGMKS
GLKAAGEEFI FGIYDGVTGL VVQPYTGARD HGALGFVKGV GMGLTGFVLK DISAIVGPFG
YTLKGVHKEM VKNKQPTAFI RKARMLQGQR DIYQLNRDSK ERKGVEDRVT HGWNVILEVW
KLMDEKKRDG GLGLKGKLKV MRERRTWRSN GAFEGVGAAE KAVQAKKRGD KGGVKAVFKK
QRKELEKAER PRKGVAAELE DDKIRRQQGV EGNNEGEGEV HPETGHDERQ VVVEEGSAKP
EGKDIPQLIA
//
