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Database: UniProt
Entry: A0A0G2IGQ3_9PEZI
LinkDB: A0A0G2IGQ3_9PEZI
Original site: A0A0G2IGQ3_9PEZI 
ID   A0A0G2IGQ3_9PEZI        Unreviewed;      1500 AA.
AC   A0A0G2IGQ3;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   SubName: Full=Putative udp-glucose:glycoprotein glucosyltransferase {ECO:0000313|EMBL:KKY39865.1};
GN   ORFNames=UCDDA912_g00181 {ECO:0000313|EMBL:KKY39865.1};
OS   Diaporthe ampelina.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Diaporthales; Diaporthaceae; Diaporthe.
OX   NCBI_TaxID=1214573 {ECO:0000313|EMBL:KKY39865.1, ECO:0000313|Proteomes:UP000034680};
RN   [1] {ECO:0000313|EMBL:KKY39865.1, ECO:0000313|Proteomes:UP000034680}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DA912 {ECO:0000313|EMBL:KKY39865.1};
RA   Lawrence D.P., Travadon R., Rolshausen P.E., Baumgartner K.;
RT   "Distinctive expansion of gene families associated with plant cell wall
RT   degradation and secondary metabolism in the genomes of grapevine trunk
RT   pathogens.";
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KKY39865.1, ECO:0000313|Proteomes:UP000034680}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DA912 {ECO:0000313|EMBL:KKY39865.1};
RA   Morales-Cruz A., Amrine K.C., Cantu D.;
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|ARBA:ARBA00001913};
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC       {ECO:0000256|ARBA:ARBA00004922}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC       {ECO:0000256|ARBA:ARBA00004319}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 8 family.
CC       {ECO:0000256|ARBA:ARBA00006351}.
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:KKY39865.1}.
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DR   EMBL; LCUC01000007; KKY39865.1; -; Genomic_DNA.
DR   STRING; 1214573.A0A0G2IGQ3; -.
DR   OrthoDB; 1734at2759; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000034680; Unassembled WGS sequence.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0003980; F:UDP-glucose:glycoprotein glucosyltransferase activity; IEA:InterPro.
DR   GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR   CDD; cd06432; GT8_HUGT1_C_like; 1.
DR   InterPro; IPR040497; Glyco_transf_24.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   InterPro; IPR009448; UDP-g_GGtrans.
DR   InterPro; IPR040693; UGGT_TRXL_1.
DR   InterPro; IPR040694; UGGT_TRXL_2.
DR   InterPro; IPR040692; UGGT_TRXL_3.
DR   InterPro; IPR040525; UGGT_TRXL_4.
DR   PANTHER; PTHR11226; UDP-GLUCOSE GLYCOPROTEIN:GLUCOSYLTRANSFERASE; 1.
DR   PANTHER; PTHR11226:SF0; UDP-GLUCOSE:GLYCOPROTEIN GLUCOSYLTRANSFERASE; 1.
DR   Pfam; PF18404; Glyco_transf_24; 1.
DR   Pfam; PF18400; Thioredoxin_12; 1.
DR   Pfam; PF18401; Thioredoxin_13; 1.
DR   Pfam; PF18402; Thioredoxin_14; 1.
DR   Pfam; PF18403; Thioredoxin_15; 1.
DR   Pfam; PF06427; UDP-g_GGTase; 1.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Reference proteome {ECO:0000313|Proteomes:UP000034680};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KKY39865.1}.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           29..1500
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002545586"
FT   DOMAIN          42..220
FT                   /note="UGGT thioredoxin-like"
FT                   /evidence="ECO:0000259|Pfam:PF18400"
FT   DOMAIN          273..404
FT                   /note="UGGT thioredoxin-like"
FT                   /evidence="ECO:0000259|Pfam:PF18401"
FT   DOMAIN          412..655
FT                   /note="UGGT thioredoxin-like"
FT                   /evidence="ECO:0000259|Pfam:PF18402"
FT   DOMAIN          667..864
FT                   /note="UDP-glucose:glycoprotein glucosyltransferase
FT                   thioredoxin-like"
FT                   /evidence="ECO:0000259|Pfam:PF18403"
FT   DOMAIN          1179..1445
FT                   /note="Glucosyltransferase 24 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF18404"
FT   REGION          1447..1500
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1500 AA;  168345 MW;  62DF004D4F383563 CRC64;
     MIPLLQLPGS LLASLLAAGL FKAQPTCAGP SVEIAMKAAF PSPPYLIELL ETAAQENASS
     YFPLLDRIAD GYFSELKTDA ELYESFLPLL QEDGHITSDE GLSIFKLALS TRSAVPRIEA
     HYQYYQTGVE PTLQGDQGGC DAWAIWLGQQ HCIPTLDAGQ VRGHVSERQD RDLPFDRSLG
     DGPSCILYAD ITSPRFAPFH RVLSEKALNR ECTYKLRHRR LSYDSLEPLP VSGYGVALQL
     KRTDYIVIDD RKAEEDASQK VITSEVVLDQ EEEVADLKPL STSELSSLGL KASSFIMQSD
     DPFSTLLKLT QDFPKHSSSL AAHDVSDDFY SEHKGNRAEL VPAGTNVLWM NGVQLVERQM
     DAFTLVDLLR SERKLINGVT DLGLTGEEAI ALLTHQSVAA AKATDDVQRF VWHDGPEDGK
     VIVYLNNIEK DKRYEGFPKH LMSLLQGGGM PGSLPQIRRD IFNLVFPVDL SKEEDVALVA
     KQLQEFVKRK LPVRFGIVPL AFTDASERQA KIVYNLVDTY GLGAMMAYLQ AAIEAKKTGE
     ADKGLFEIAV ANRTLREDAI ALSFEDVLAS EHHSEQTRLS KVWADRLRAH GPNPVFFADG
     LPMSRRGNWL QPMSQQIGID LQMLRQALFY GEIEDDQWIP DYFLQNAAKR RNTVIFPSDP
     NDLDVLDVNK LHSEHAELFE MVPVLEAYPE STKENWAVLT LVLDLTNPEG LKLAASALQF
     RVNNPGIRLD IIHNPVDSEE AHKINSALKA SQSDLAAADS EELLKIIIDT TEGLTEDNDL
     YGSALRRFLT TAAIRPGQNM LILNGRVVGP IESAADFNVD DYQLFLDIEQ KLRILPVYNA
     IEDLGLAEKV SSPLAAAKVT SITSLSTMPD LPEGIFESGS PLRISAFNVW NSTHTAFEIG
     DKSKATIQLV AVINPASEQG QRWVPILKVL SELSGVYLKV FINPKEKLEE LPVKRFYRYV
     LDHAPVFDES GKVKSLVAEF KGLPSEALLN VAMDVPPAWL VASKASVHDL DNLKLSSIKS
     DVEVIYELEN ILIEGHSRES TGSLPRGAQL TLSTEKDSKV ADTIIMFNLG YFQFKANPGF
     YNIQLKEGRS SDIYHIESVG AKGYSAVPGD EGTEAALMNF MGTTLYPRIN RKPGMEEADV
     LEESAEGGVF DVVSKGLKFG KDLFGVKTRS SSDVEHAEIN IFSVASGHLY ERMLNIMMLS
     VMKNTNHSVK FWFIEQFLSP AFKDFLPFMA EEYGFKYEMV TYKWPHWLRQ QKEKQREIWG
     YKILFLDVLF PLSLDKVIFV DADQIVRTDM YSLVQHELEG APYGFTPMCD SRVEMEGFRF
     WKQGYWANYL RGQPYHISAL YVVDLRRFRE LAAGDRLRQT YHTLSADPNS LSNLDQDLPN
     HMQFQIPIHS LPQEWLWCET WCSDETFAEA KTIDLCNNPQ TKEPKLDRAR RQVPEWTLYD
     DEIAALDRRR KGRAEGADEK EKVVRGDGEE LKEPREDKNP KSRGFEGEDP EATGHVKDEL
//
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