ID A0A317VIV7_9EURO Unreviewed; 1362 AA.
AC A0A317VIV7;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=UDP-glucose:glyco protein glucosyltransferase {ECO:0000313|EMBL:PWY73875.1};
GN ORFNames=BO94DRAFT_538924 {ECO:0000313|EMBL:PWY73875.1};
OS Aspergillus sclerotioniger CBS 115572.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1450535 {ECO:0000313|EMBL:PWY73875.1, ECO:0000313|Proteomes:UP000246702};
RN [1] {ECO:0000313|EMBL:PWY73875.1, ECO:0000313|Proteomes:UP000246702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 115572 {ECO:0000313|EMBL:PWY73875.1,
RC ECO:0000313|Proteomes:UP000246702};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (DEC-2016) 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:PWY73875.1}.
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; MSFK01000031; PWY73875.1; -; Genomic_DNA.
DR STRING; 1450535.A0A317VIV7; -.
DR OrthoDB; 1734at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000246702; 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:0048856; P:anatomical structure development; IEA:UniProt.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR GO; GO:0043934; P:sporulation; IEA:UniProt.
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:UP000246702};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:PWY73875.1}.
FT DOMAIN 7..95
FT /note="UGGT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18400"
FT DOMAIN 143..269
FT /note="UGGT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18401"
FT DOMAIN 278..521
FT /note="UGGT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18402"
FT DOMAIN 534..732
FT /note="UDP-glucose:glycoprotein glucosyltransferase
FT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18403"
FT DOMAIN 1054..1320
FT /note="Glucosyltransferase 24 catalytic"
FT /evidence="ECO:0000259|Pfam:PF18404"
FT REGION 123..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1323..1362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1344..1362
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1362 AA; 153684 MW; 34E34BE3D4A1928C CRC64;
MAAQDAACPV WVHSEGKQYC SSAMERAQQD VSGSDDPREL PFDRVFGDPS LPPAILYADV
ASPMFKEFHQ SLSALAKEGQ MSYRVRYRPP QHWSSRPLFV SGYGLELALK RTDYIVIDDR
AAEERGPDGV ESKKPGDAED DLNDLRPLSS SEVSRLGLNT ASYVMDSDDP FDTLVKLSQD
FPKYSARVAA HNISTELLQD IRSSRLRMLP PGLNALWING VQIEPRQVDA FTLLDHLRRE
RKLIEKFRNL GLSAKEAVEL LAHPSLGESL ARDGPQRYNY RDDIEGGGVI MWLNDLEKDA
RYESWSSELA GFMQRTYPGQ LPAVRRDANN IVYPVDLTNS EDADIVVKTI QVFVKNKIPV
RFGLIPVTFS DGAIAQLKVA HYLQETFGLA SFMNYLEVSA SKNKLASPDK ACFQAATKDR
DARAEKQPLS LEEILKNDSS DVTVAKTTAY LNRLGMKHEA SHAFVNGIPV TRNANWAQEM
SSRISRDTQL IQQRIADGEV DEDTWLPELF LSQAFDRRNP AFIPEDPKEI RAVDLVKIAD
SHRDLFGQIP RIASDQDDAL ESAHVIVIGN FDDEPGYELL SAALESRKAH GGIEALFLHN
PKPETPAMAR SSAVYRSLNG GKGTDVTHIL EAITSSDSPS DEEARNVAQF WEAQQSVVEE
FGLAPGMRAL VINGRVIGPI AEDTELTSED FDQLLTYERH KRITPVAKAV KALEFGEKLS
DPLAFAKLTS LTTLSTISDV PEGIFESTSD IRLFLYNRWN NLRSAITVST SEDPAITIVA
SIDPTSEVAQ RWLPILKVLS ELASVRVRLV LNPREEIKEL PTKRFYRYVL NSQPSFNDDG
SVSRPTASFS GVPVEALLTL GMDVPSSWLV APKDSIYDLD NIKLSSVKEG TDVDAIYALE
HILIEGHSRD MTVKSPPKGV QLLLGTENNP HFSDTIVMAN LGYFQFKAQP GLWNINLKPG
RSEQIFTLDS VGGLGYNPQP GDENNEVALL SFQGRTLFPR VSRKKGYETE DVLETGPKPG
SAMDYMSKGF NFASDILSSV GVNTKGTSGK QADINIFSVA SGHLYERMLN IMMVSVMRNT
KHSVKFWFIE QFLSPSFKSL LPHLAQEYKF SYEMVTYKWP HWLRAQQEKQ REIWGYKILF
LDVLFPLDLD KVIFVDADQI VRTDMYDLVS LDLEGAPYGF TPMCDSRHEM EGFRFWKQGY
WKNFLRGQPY HISALYVVDL NRFRALAAGD RLRGQYQMLS ADPESLSNLD QDLPNHMQHY
IPIKSLPQEW LWCETWCSDE SQSQARTIDL CNNPMTKEPK LDRARRQVPE WTEYDDEIAA
LSKRVALQQQ QQQQQQEEEE ERQRQSYPDD EEDEETWNKD EL
//
