ID A0A1S8BCD7_9PEZI Unreviewed; 1496 AA.
AC A0A1S8BCD7;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=UDP-glucose:glycoprotein glucosyltransferase {ECO:0000313|EMBL:OMP84981.1};
GN ORFNames=BK809_0000733 {ECO:0000313|EMBL:OMP84981.1};
OS Diplodia seriata.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC Diplodia.
OX NCBI_TaxID=420778 {ECO:0000313|EMBL:OMP84981.1, ECO:0000313|Proteomes:UP000190776};
RN [1] {ECO:0000313|EMBL:OMP84981.1, ECO:0000313|Proteomes:UP000190776}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F98.1 {ECO:0000313|EMBL:OMP84981.1,
RC ECO:0000313|Proteomes:UP000190776};
RA Robert-Siegwald G., Vallet J., Abou-Mansour E., Xu J., Rey P., Bertsch C.,
RA Rego C., Larignon P., Fontaine F., Lebrun M.-H.;
RT "Draft genome sequence of Diplodia seriata F98.1, a fungal species involved
RT in grapevine trunk diseases.";
RL Submitted (JAN-2017) 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:OMP84981.1}.
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DR EMBL; MSZU01000086; OMP84981.1; -; Genomic_DNA.
DR STRING; 420778.A0A1S8BCD7; -.
DR OrthoDB; 1734at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000190776; 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:UP000190776};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:OMP84981.1}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..1496
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013023835"
FT DOMAIN 44..229
FT /note="UGGT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18400"
FT DOMAIN 277..408
FT /note="UGGT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18401"
FT DOMAIN 414..660
FT /note="UGGT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18402"
FT DOMAIN 672..864
FT /note="UDP-glucose:glycoprotein glucosyltransferase
FT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18403"
FT DOMAIN 1184..1450
FT /note="Glucosyltransferase 24 catalytic"
FT /evidence="ECO:0000259|Pfam:PF18404"
FT REGION 1466..1496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1469..1496
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1496 AA; 169175 MW; 3369F5D56D11A67E CRC64;
MRVRHWLPRS QAALLFAALA PPSASASQSH SPPINVALKA RFNSPPYLVE LLETAAFENA
TAYFPLLDRI ADGYFDAKPS EQAQYDAFLQ LLQDDGHITD PDALSSFQFA LSIHTAAPRI
EAHYQFYNTS VEPSLVPDQP DDCESWVLLN GKQYCSPDMD KEHGDVKNPR VKDLPFDRPM
RQEYRSVPSV LYADITSPSF RNFHKTIIKT ARAGETSYTL RHKPPKNTRH DPQDVHGYGV
ELALKRTDYI VIDDRQAEDD AKAPAADAAQ AVLQDEEVAD LKPLSESDLK GLGLKAGSFV
MGSEDPLDTL LKLSQDFPKH SSAIAAHDVS KDFLKEHKAN REAVLPPGYN ILWINGVQVM
PRDVDAFALL EHLRRERQIV NSVRKLGFTP PEAINVLANN NIAKAKDNDE PQRYDWRDST
EGGNVIVFLN NLEKDKRYAE WPESLRALLQ PSYPGTLPSV KRDIQNVVIP VDLTNALDAT
LLVETLQSMV KRKLAVRWGI VPSTKNVRAE RQAHVIYYLL EYHGLSAVMQ YLEQSLKLKE
IFEPSKTAFG TVTADAKIRG NRVAKSFDQL FEEPSVVQRV EAASTWLTRM AADGNSPPFF
VNGVALRRND EWLSSMSMRV SRDLNTIQKA VFENELDEDA DDWLPGVFLA NALVRRNPMI
VPEDEKDVKH VDMAQAYADY GHLIERLPTF KPAEDSEWFQ WAQLIVLGDF DSNAGANLLA
DAYQFAAEHG DLETAFVHTG DVDRHSRLSY LLWKNKGQSF VDDLPEDFVP SSRELKECGE
YWESMKPLMR IFDGDSGRES LVLNGRTVGL IRKRRPFTVD DLENLLTYER QKRIEPANKA
IMDLGLEDKI KSPGASAQFT SLVALSTVSN VPEGIFDTPP TTRRDVFKFW NETHTCIKTG
ELETSPIQIV ASVDPSSETA QRWLPILKVL SELSGVHMRL FLNPKERLSE LPVKRFYRYV
LASKPSFDEN GSTEALQARF DGIPSEALLN LGLDVPPQWV VAAKESVHDL DNIKLSQLKG
QSSIDAVYEL EYILIEGHSR DLTNGMYPRG AQLDLRTTSN PRYADTIIMA NLGYFQFKAN
PGFFDIELQP GRSQEIFTID SAGTLGWEPR PGDRTKEIAL MDFKGVTLYP RLSRRSGKED
EDVLEAPTTM VEDLAAKGAA FADGILSKVG INVKTGGSSR HADINIFSVA SGHLYERMLN
IMMVSVMKHT KHTVKFWFIE QFLSPSFKSF LPTLAAAYGF EYEMVTYKWP HWLRGQKEKQ
REIWGYKILF LDVLFPLDLD KVIFVDADQI VRADMHELVT HDLEGAPYGF TPMCDSRTEM
EGFRFWKQGY WKNFLKGRPY HISALYVVDL NRFRRLAAGD RLRQQYQQLS ADPNSLSNLD
QDLPNNMQVG LPIHSLPQDW LWCETWCSDD ALRSAKTIDL CNNPQTKEPK LDRARRQVPE
WTVYDEEIAA LARKADAAAG IVAENNGAEQ DERLLEKVAE QAEEVEKEKA KKHDEL
//
