ID A0A163E0I9_DIDRA Unreviewed; 1270 AA.
AC A0A163E0I9;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=Transferase {ECO:0000313|EMBL:KZM23443.1};
GN ORFNames=ST47_g5423 {ECO:0000313|EMBL:KZM23443.1};
OS Didymella rabiei (Chickpea ascochyta blight fungus) (Mycosphaerella
OS rabiei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Didymellaceae; Ascochyta.
OX NCBI_TaxID=5454 {ECO:0000313|EMBL:KZM23443.1, ECO:0000313|Proteomes:UP000076837};
RN [1] {ECO:0000313|EMBL:KZM23443.1, ECO:0000313|Proteomes:UP000076837}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ArDII {ECO:0000313|EMBL:KZM23443.1,
RC ECO:0000313|Proteomes:UP000076837};
RX PubMed=27091329; DOI=10.1038/srep24638;
RA Verma S., Gazara R.K., Nizam S., Parween S., Chattopadhyay D., Verma P.K.;
RT "Draft genome sequencing and secretome analysis of fungal phytopathogen
RT Ascochyta rabiei provides insight into the necrotrophic effector
RT repertoire.";
RL Sci. Rep. 6:24638-24638(2016).
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:KZM23443.1}.
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DR EMBL; JYNV01000195; KZM23443.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A163E0I9; -.
DR STRING; 5454.A0A163E0I9; -.
DR Proteomes; UP000076837; 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 Reference proteome {ECO:0000313|Proteomes:UP000076837};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KZM23443.1}.
FT DOMAIN 255..412
FT /note="Glycosyltransferase family 28 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF03033"
FT DOMAIN 575..675
FT /note="Erythromycin biosynthesis protein CIII-like C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF06722"
FT REGION 1..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 793..859
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1068..1247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..79
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..124
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..156
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 794..812
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 825..856
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1094..1110
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1111..1133
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1134..1150
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1154..1206
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1229..1243
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1270 AA; 141587 MW; 1FE04EB607842F61 CRC64;
MANFAREETQ VSPTGMVIEE PTFPDFAGGP SARNRSTALK FPTPEDPTPA HISQHDLTEP
QAREQPSTKQ SQTASAPRRL LDRSATERPK PSTKHSLLRN MPAPRKQRPT PVQRQTTITF
DHSSSESDSS EDEQLPAKST SRDETIQREE SRTRSGNQRR SSTMNPFARF KVSNEHFQTK
GSVKSDGRLK LSILEEDFGS GYIAKALGAV LPKHGKEEEH HSVHSYDDRG VGAEKIAPEE
DEMEHDPSRR MKLNIVIIII GSRGDIQPFI RIGKILKEDY GHRVRIATHP AFKDFVQKDS
GLEFFSVGGN PAELMAFMVK NPGLIPNIDT IKGGEIGRRR AQMYEMFQGM WRACINATDD
ETDHMNAKMM GDKAPFVADA IIANPPSFAP AHIAEKLGIP LHMMFTFPYT PTVQFPHPLA
NIKVSNVEPT YSNFMSYPLV EMMMWQGLGD LINRFRTDVL RLESISTLWA PGQLYRLKVP
YTYMWSPGII PKPKDWGPEI DVTGFVFLDL ASNFTPPDDL KEFLDDGEPP VYIGFGSIVV
DDPDQFTKLI FEAIEMAGVR ALVSKGWGGF GSNADCPDNV FMLENTPHDW LFPRCKAVIH
HGGAGTCAIG LKCAKPTMIV PFFGDQPFWG AMVSKAKAGA HECIPYRNLT AERLAKGIKE
CLTEEAQKNV QKIADSIEAE GDGALNAVRS FHRSLPLHGE GSMRCDFLDN RAATWKIKNT
KVQLSALAAE ILVNKKKLKW NELRLIRHYE WNDFGGPGEP VTGLWGSIYT TLTDAALGVG
SVPVEMGKSL KKREKLWEKK RQHQKKRQKK KETMARANAE LEKSTNNSAE DHVAKKEQEQ
NGRPKPEREE STLSKINEPE ETLNVELAHE AAFGFRKTGH ALARFPMNVT LALTQGFHNA
PRLYGDETVR RPPRVTGLHS GLRAGRDELV YGVTDGVTGI VTQPIRGAKE NGVVGAVRGV
GFGIGGFVLK DIAALLGPTA YLMKGLDAEY MKKYQPTTLI RRGRIAQGQL ELQQLEHKTR
VTNIREAEGK NAEPKENRDD VEDIVAHRWA ALKQAIAEEK KHNKQGIIAS LTGTSEKKAG
TMVPRKGTSV KKPANPPLSK SVTTPIAQTE KDANTKRKTD YDAVKKSFES QHRRSVTLNR
SSTEPLTRRS WDDSNAARPA KPEKKERPQS IHEEPEFEET HVLGNAHLNE EMGSDEDEKR
HDPVPSAPTV DPESKQDFKP DQRLPQEPGR ASADSSSDKT KVGTETMDWV KMRQEAESRE
DAGRTWVVNV
//
