ID A0A010S2H0_9PEZI Unreviewed; 1321 AA.
AC A0A010S2H0;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE SubName: Full=Glycosyltransferase family 28 domain-containing protein {ECO:0000313|EMBL:EXF78768.1};
GN ORFNames=CFIO01_01607 {ECO:0000313|EMBL:EXF78768.1};
OS Colletotrichum fioriniae PJ7.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum acutatum species complex.
OX NCBI_TaxID=1445577 {ECO:0000313|EMBL:EXF78768.1, ECO:0000313|Proteomes:UP000020467};
RN [1] {ECO:0000313|EMBL:EXF78768.1, ECO:0000313|Proteomes:UP000020467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PJ7 {ECO:0000313|EMBL:EXF78768.1,
RC ECO:0000313|Proteomes:UP000020467};
RA Baroncelli R., Thon M.R.;
RT "The genome sequence of Colletotrichum fioriniae PJ7.";
RL Submitted (FEB-2014) 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:EXF78768.1}.
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DR EMBL; JARH01000609; EXF78768.1; -; Genomic_DNA.
DR RefSeq; XP_007597551.1; XM_007597489.1.
DR KEGG; cfj:CFIO01_01607; -.
DR eggNOG; KOG1192; Eukaryota.
DR HOGENOM; CLU_000537_1_0_1; -.
DR OrthoDB; 76239at2759; -.
DR Proteomes; UP000020467; 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; 6.
DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
DR PROSITE; PS50330; UIM; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000020467};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EXF78768.1}.
FT DOMAIN 142..201
FT /note="Glycosyltransferase family 28 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF03033"
FT DOMAIN 476..574
FT /note="Erythromycin biosynthesis protein CIII-like C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF06722"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 247..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 683..816
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1005..1024
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1118..1154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1171..1321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 691..777
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 784..813
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1128..1142
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1203..1290
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1321 AA; 143223 MW; A80E8D2930DF99BC CRC64;
MTVVKNPEAG ASSSAPPPPP RRPSDLNLDR TDSAEVPDAL VSDGFSLPSL EAENEAPPAY
GDLPDQLQFN QAGFEAGANV TGDGRVNINI NQSGNRLAEI LAPTLRNQLL VDKRPQAPLP
PAYIPPSLGG QPGQTPPPQL NVVIQIVGSR GDVQPFVALG KVLKDTYGHR VRIATHATFQ
KFVEENGLEF FCIGGDPAEL MAFMVKNPGL MPGFDTLKSG EVSKRRRGIQ DILLGCWRSC
IEAGNGLGPP PKPHAKDQPL DEHYGIPGDP TQKPFVADAI IANPPSFAHI HIAEKMGVPL
HLMFTMPWTP TRAFPHPLAN IQSTNTDTVM TNYVSYALVE MMTWQGLGDV INRFRDKALD
LEPMSLIWAP GVLTRLRIPY TYCWSPALIP KPNDWGREID ISGFYFLNLA SAFTPEPDLA
AFLAAGPPPV YIGFGSIVVD DPNALTRMIF DAVHQTGVRA LVSKGWGGLG AEDVGLPEGV
FMLGNVPHDW LFKHVSAVCH HGGAGTTAAG IQAGKPTIIV PFFGDQPFWG AMVSRAGAGP
DPIPYKELTG DKLAEAIKFA IKPETQARAQ ELGHKIREEK GTDLGGKSFH DHLDTDELRC
SIEPSRAAAW RVRRTKVRLS PMAAAVLVER GLIKYSDLKL YRPKEYITEG QPWDPISAVS
TSLVADISSI GMAVADFPRE LFKSRSKGDK TPETSTPSLT EASSSKQSLH QSSSKQSLHQ
SDKASIAAPS THASESSTQL GLMEMEGSTP TLPQSPQPDT ASLAQSQTAS TAPSMVFSPP
DGASIARSET TPSEHASTTQ SVRPSNSPAK RSFKESMPAN VGVDAAVAAG TSVSRIVTTG
VKTPMNVCLG LARGFRNAPR LYNDDTVRPP EKVTDLASGI RIAAKEFGYG MFDGIGGLVT
QPLKGAEKEG GIGLIKGFGK GIGGLILKPA SAVWSVPAYT MQGVHATLRN AFSSSVQNYI
IASRMKQGQM DMDSASVAER EDVVVRWNNV KFDLKNFQAM KLKEQREKQR AEGEGPYGQP
EKSLTAPVTG WAHTRKLSFE ERKQLHARKE AWKKGHVEAI VPASRSDLSL SEPSSMSAAE
DEEFERAIRV SVAETSRGNA EEDAAVEQAI RASVNHFRSS GVPDIRAEKA APLDRDAKNQ
DQDPFSSAEL EITDEEYQRL IEEAINQSMS LKAAGVQPGE GSHGDDEEFH RALEQSKIAQ
QQPPAHEDDE ELQRILEESK RQHAEGNTNE EEELRKAIEA SEAAHREQQN KDAAARTEED
VVMEYVKKQS LAEEEFRRNA SKGKGRDVAA DVDDDEDEEL RRAMEESLKM SGRPGGSSSY
Q
//
