ID E4ZK77_LEPMJ Unreviewed; 1293 AA.
AC E4ZK77;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE SubName: Full=Similar to UDP-glucose,sterol transferase {ECO:0000313|EMBL:CBX91672.1};
GN ORFNames=LEMA_P071800.1 {ECO:0000313|EMBL:CBX91672.1};
OS Leptosphaeria maculans (strain JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8)
OS (Blackleg fungus) (Phoma lingam).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Leptosphaeriaceae;
OC Plenodomus; Plenodomus lingam/Leptosphaeria maculans species complex.
OX NCBI_TaxID=985895 {ECO:0000313|Proteomes:UP000002668};
RN [1] {ECO:0000313|Proteomes:UP000002668}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8
RC {ECO:0000313|Proteomes:UP000002668};
RX PubMed=21326234; DOI=10.1038/ncomms1189;
RA Rouxel T., Grandaubert J., Hane J.K., Hoede C., van de Wouw A.P.,
RA Couloux A., Dominguez V., Anthouard V., Bally P., Bourras S.,
RA Cozijnsen A.J., Ciuffetti L.M., Degrave A., Dilmaghani A., Duret L.,
RA Fudal I., Goodwin S.B., Gout L., Glaser N., Linglin J., Kema G.H.J.,
RA Lapalu N., Lawrence C.B., May K., Meyer M., Ollivier B., Poulain J.,
RA Schoch C.L., Simon A., Spatafora J.W., Stachowiak A., Turgeon B.G.,
RA Tyler B.M., Vincent D., Weissenbach J., Amselem J., Quesneville H.,
RA Oliver R.P., Wincker P., Balesdent M.-H., Howlett B.J.;
RT "Effector diversification within compartments of the Leptosphaeria maculans
RT genome affected by Repeat-Induced Point mutations.";
RL Nat. Commun. 2:202-202(2011).
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DR EMBL; FP929072; CBX91672.1; -; Genomic_DNA.
DR RefSeq; XP_003835037.1; XM_003834989.1.
DR STRING; 985895.E4ZK77; -.
DR CAZy; GT1; Glycosyltransferase Family 1.
DR EnsemblFungi; CBX91672; CBX91672; LEMA_P071800.1.
DR GeneID; 13287803; -.
DR eggNOG; KOG1192; Eukaryota.
DR HOGENOM; CLU_000537_2_1_1; -.
DR InParanoid; E4ZK77; -.
DR OMA; YTNFMSY; -.
DR OrthoDB; 76239at2759; -.
DR Proteomes; UP000002668; Genome.
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 Reference proteome {ECO:0000313|Proteomes:UP000002668};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CBX91672.1}.
FT DOMAIN 269..429
FT /note="Glycosyltransferase family 28 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF03033"
FT DOMAIN 589..690
FT /note="Erythromycin biosynthesis protein CIII-like C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF06722"
FT REGION 1..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 799..885
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1079..1170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1184..1293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..74
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..137
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..177
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 807..823
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 843..866
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1097..1118
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1200..1215
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1232..1247
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1248..1282
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1293 AA; 143277 MW; 66CFAE9E3C304FEA CRC64;
MTDRDKVQHR VTPTGMVLHE PTFPNIPIPD HGPYSSQTAG SAAPSNRVAT PMGIATHHAG
TSEDSLTTKP QPIDETHSKP PKTSRPMQQR YATERPKPSV RHSLLGKMHH GGPPKRPSPT
HKGTTVTFDP YSSESDSSSS DSDEEEGEKN YPKKTLSHQR DLTGQENRQR RESHGGPFSR
LKITNDHFRT SAKVSKADGR LKLNILENDM NSGYVAKALG AVLHKHSKND DDEQRGVESY
DARGIQGAKM SPEEDEMENN PSRRVKLNIV IIIIGSRGDI QPFIRIAKIL KEDYGHRVRL
ATHPAFKEFV EKDSGLEFFS VGGNPAELMA FMVKNPGLIP NIDTIKGGEI GRRRAQMYEM
FQGMWRACIN ASDDETDQHN AKMMGNKDPF LADAIIANPP SFAPQHIAEK LGIPLHMMFT
FPYTPTAFFP HPLANIKTSN VEASYGNFMS YPLVEMMMWQ GLGDLINRFR TQILHLEEVS
TLWAPGQLYR MKVPYTYMWS PGLIPKPKDW GPEIDISGFV FLDLASSFTP PDDLKEFLDD
GEPPVYIGFG SIVVDDPDEF TKLIFDAVKM AGCRALVSKG WGGFGSNADC PENVFMIDNC
PHDWLFPRCA AVVHHGGAGT TAIGLKCAIP TMIVPFFGDQ PFWGAMVSKA KAGAHECIPY
KKLNSKRLAE GIKQCLTDEA KENVKKIAES IEKEGDGALN AVRSFHRSLP LVGENSMRCD
FLEDRAAAWK IKNTNVKLSA LAAEILVEKK KLKWNELRLI RHYEWNDFGG PGEPITGIWG
TLMTSVTDAA TGVGGVPVEM GKSIRKREKI RDKKRKIQMR HEHKKATLAR ANANLPKDRL
GKEATNGSTE KVRDKDTDES NDGKRPQASR EPSTLSRISE PDEDLADELT NEAASGFRKT
GGALARFPMN LTLAITKGCH NAPRLYGDET VRRPPRVTGM HSGLRAGRDE LLYGVMDGVT
GIVTQPIRGA KNHGIVGAMK GVGYGIGGFV LKDIAALLGP FAYGMKGLDA QYMKRYQPTA
YLRRARITQG QLELTSLERK SRVARIDEVK EGEGKNTMKR DQVEQNVSAR WQALQDTMAK
ERKNHKSGLA ATLMGRGEKK EGTRVGRKST DVPKEGRSSQ SRARTTPIAE ADKQVRPTDS
MANKDQEAFQ QSSIRKSMDH HGRSAAMLRS TTAPITMVEL EEHGDRDPLE PLPRSPHHQV
ADSNRSREND TQARGNAHLV DDAVNQSDPE LGNHLRVEDE TARISRTKTS DTEPQSGDAS
SQDTRVESET TDWTTTGSKM GGEVRVRSTE VRF
//
