ID A0A139HZ78_9PEZI Unreviewed; 1309 AA.
AC A0A139HZ78;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KXT07774.1};
GN ORFNames=AC579_2785 {ECO:0000313|EMBL:KXT07774.1};
OS Pseudocercospora musae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX NCBI_TaxID=113226 {ECO:0000313|EMBL:KXT07774.1, ECO:0000313|Proteomes:UP000073492};
RN [1] {ECO:0000313|EMBL:KXT07774.1, ECO:0000313|Proteomes:UP000073492}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 116634 {ECO:0000313|EMBL:KXT07774.1,
RC ECO:0000313|Proteomes:UP000073492};
RA Chang T.-C., Salvucci A., Crous P.W., Stergiopoulos I.;
RT "Comparative genomics of the Sigatoka disease complex on banana suggests a
RT link between parallel evolutionary changes in Pseudocercospora fijiensis
RT and Pseudocercospora eumusae and increased virulence on the banana host.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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:KXT07774.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LFZO01000532; KXT07774.1; -; Genomic_DNA.
DR STRING; 113226.A0A139HZ78; -.
DR Proteomes; UP000073492; 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; 3.
DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
DR PROSITE; PS50330; UIM; 2.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000073492};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 157..221
FT /note="Glycosyltransferase family 28 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF03033"
FT DOMAIN 490..592
FT /note="Erythromycin biosynthesis protein CIII-like C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF06722"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 123..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 704..846
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1037..1068
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1147..1309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..148
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 717..846
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1156..1176
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1200..1214
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1220..1243
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1244..1279
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1309 AA; 141898 MW; 43DF0CC9CADB5B39 CRC64;
MAPANDQEPE RAGGRGETDK QVPQVMLDQA NAAVAGENDM SSYTAAERRH MGHDVAVNVP
DYGTTPADYD IPPPAYGDQY GTVNQEQEGF GTKASVADDG RVNIRIDQRN RRLSQLLVPS
LKQLQQAADK QQAPPPPYIP PSLGGAGDEA PPPPLNVVIQ IVGSRGDVQP FVALGKVLKD
TYGHRVRLAT HPNFKDFVTE NDLEFFSIGG DPAALMSFMV KNPGLMPGFD TLRAGDVGKR
RKEVGEYLRG CWRSCFETGD GMGPEATDDT IEDWTSHNPN ETDSLHKPFV ADCIIANPPS
FAHVHCAEKL GIPLHIMFTM PYSPTQAFPH PLANIQSSNA DDHLTNYISY ALVDMLTWQG
LGDIINRFRQ RSLGLDPVSL MWAPGMLQRL QVPHTYCWSP ALIPKPKDWG ANISISGFYF
LDLAKTYTPD PELKAFLDAG SPPIYIGFGS IVLDDPNAMT KLLFEAVKLT GQRALVSKGW
GGMGADELGK PDNVFMLGNC PHDWLFKQVS CVVHHGGAGT TAAGITAGRP TLVVPFFGDQ
PFWGAMVARA GAGPEPIHHK QLTSDNLADA IKKCLEPQTQ ERARELAAKI ATEKGSDVGA
QSFHQFLDVD KLRCSLAPSR PAVWRIKRTQ ARLSAMAACT LAQEGLLDFN DLKLYRPREY
EADEGPWDPI TGGASALVGT MSTMMLGVAD FPIATLKALK IHPDAQTKKE GKKPEGQQRT
VSSSASVKSG ATGTTAGQSE DAAPTTTGSS SPSPAMTPRS NTDHSTMSGE ASRSTSSFNF
EESLQRLNAG PLSPGSQRDT NGKRMNSSLA GALSGQLGNR PRSRSNSRSR TPGQAGSGGT
DWKSSFQNAQ DTAKGVNRIV GAGIKSPLDF TMGLTRGFHN APKLYGDDTV RKSENVTDLK
SGLRAAAKEF GFGMYDGITG LVTQPMKGAA KEGPAGFVKG IGKGIGGIAL KPGAAFFGIP
GYTMKGVYKE LQKHFGSSVQ NYIIASRTAQ GFDECQKASP EECRDVIMRW QVLQSNLKKK
RNPDEMVRDI LKEQMDKKEA RLQGRGEKRS GPGSRFWSRA GTTASSRTAV DPENAMLAMG
TPSKTMDPAE AEQRAVDEAI RLSVLQTSHG DAAEDARVEQ GIRDNMAEIQ RVRTTRIDQH
EDMQLRQAMD VSSAEAARHQ TEREQYEKDL EKALAQSLKE QRGWNDSDSE AGINSPALSE
ATLPPPPPNE KPPQYIPTDT GHLAGTTQTE FERQQSSSKA GASEKTQQER DEERIVMDYV
KKQSLLEEEN KKKMSGKGDD DDEDDEELQM ALKLSMQEHG EASGSASGK
//
