ID A0A2J5HTL2_9EURO Unreviewed; 1481 AA.
AC A0A2J5HTL2;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=UDP-glucose:Glyco protein glucosyltransferase-domain-containing protein {ECO:0000313|EMBL:PLN80704.1};
GN ORFNames=BDW42DRAFT_106557 {ECO:0000313|EMBL:PLN80704.1};
OS Aspergillus taichungensis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=482145 {ECO:0000313|EMBL:PLN80704.1, ECO:0000313|Proteomes:UP000235023};
RN [1] {ECO:0000313|Proteomes:UP000235023}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 19404 {ECO:0000313|Proteomes:UP000235023};
RG DOE Joint Genome Institute;
RA Mondo S.J., Kjaerbolling I., Vesth T.C., Frisvad J.C., Nybo J.L.,
RA Theobald S., Kuo A., Bowyer P., Matsuda Y., Lyhne E.K., Kogle M.E.,
RA Clum A., Lipzen A., Salamov A., Ngan C.Y., Daum C., Chiniquy J., Barry K.,
RA LaButti K., Haridas S., Simmons B.A., Magnuson J.K., Mortensen U.H.,
RA Larsen T.O., Grigoriev I.V., Baker S.E., Andersen M.R., Nordberg H.P.,
RA Cantor M.N., Hua S.X.;
RL Submitted (DEC-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}.
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DR EMBL; KZ559544; PLN80704.1; -; Genomic_DNA.
DR OrthoDB; 1734at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000235023; 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 Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:PLN80704.1}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..1481
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014412723"
FT DOMAIN 41..225
FT /note="UGGT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18400"
FT DOMAIN 270..398
FT /note="UGGT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18401"
FT DOMAIN 405..649
FT /note="UGGT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18402"
FT DOMAIN 661..856
FT /note="UDP-glucose:glycoprotein glucosyltransferase
FT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18403"
FT DOMAIN 1177..1443
FT /note="Glucosyltransferase 24 catalytic"
FT /evidence="ECO:0000259|Pfam:PF18404"
FT REGION 252..276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1451..1481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 252..267
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1460..1481
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1481 AA; 165128 MW; C50031D3D433B66A CRC64;
MRLVSGLAAS CQLAAVGVAL LTPLVHASPS VNVALQASFD SPQYLVELLE TAAEENSTAY
FPLLDRIADG AFDDTVTDKE LYDRFLQIVH DDGHLRTSES LSSFKVSLAI RSASPRIAAH
YQYYNASVQQ TLMAAQDAAC PVWVHMDGKQ YCSSAMERAQ QDVSGEMDQR ELPFDRVLGD
LSLPPAVLYA DVSSPMFKDF HLALSALAKE GQISYRIRYR PSQHRSPRPL FVSGYGVELA
LKRTDYIVID DRDAEQREGK SSNAEGDAPD DLKPLSSSEV SRLGVNTVSY VMDSDSPLDT
LIKLSQDFPK YSANVAAHDA SPELLQDIRS SRLQMLPPGT NVMWINGVQV DPREIDAFSL
LDTLRRERKL IEKFRDLGIS ATEAVDLLSH EYLGEALAQD APPRYNYRDE IEGGRVIIWM
NDLEKDARYD SWPSAVRAYL QRSYPGQLPA VRRNANNIVV PVDLSTMEGV QVVINHLKVF
VQNGIPVRFG LVPVASSPGS SAQLKVAHYL QETFGLASLM QFLEETAAKK SAASPDKACF
EVATKDRTAR PDRQVLSFEE VLKDKDLDAL VARTAEYQTR LGIEGQKPPI LVNGAPVSSG
ESWMQQMSVA ISKDIQMIQQ GVVEGVIDDG TVIYEYLLSE AFDRRTSWVV PEDPKDIQVV
DIATVSDSRE EVLRELPHIA SQSDNALDSL HLLVVGDFDS ANGQSLLTAA LESRKKHPEV
EVLFLHNPTT HGSSTGVSTA LYKSLKGDKK GDAAQVLADV ASYDGTEAPE IAQFWEAQRP
LAKDLGFAPG ARGVVINGRT VGPIQEDVAV VFDDLDQLFA YEQKKRIGPV AKAVKELEFG
SKLSEPFAFA KLTSLTTLST ISDVPEGISQ SMSDVRLNLF GKWEDSRSTI TVSSSEDPAI
TIVASIDPTS EVAQRWLPIL KVLSELASVR LRLFLNPREQ ISELPTKRFY RYVLDSEPSF
DDDGALSRPT ASFSSVPVDA LLTLGMDVPS PWLVAPKESI HDLDNIKLSS VRDGADVDAI
YALEHILIEG HSRDTTIRSP PSGVQLVLGT DDNPHFADTI IMANLGYFQF KAQPGLWKIN
LKPGRSERIY NLDSVGSLGY SPQPGDENTE VALLSFQGKT LFPRLSRKKG RENEDVLETG
PQPGSAMDYM SKGLNFASSI LSSVGVGSKS EEKHADINIF SVASGHLYER MLNIMMVSVM
RNTNHSVKFW FIEQFLSPSF KSFLPHLAKE YGFSYEMVTY KWPHWLRAQS EKQRQIWGYK
ILFLDVLFPL SLDKVIFVDA DQIVRTDMYD LVTMDLEGAP YGFTPMCDSR EEMEGFRFWK
QGYWKNFLRG QPYHISALYV VDLNRFRALA AGDRLRGQYQ MLSADKNSLS NLDQDLPNHM
QHHIPIKSLP QEWLWCETWC SDASLTQART IDLCNNPQTK EPKLDRARRQ VPEWTEYDEE
IAALSKKVAL EQEMLQQEQE QMQGEDEDED GDDSGWDKDE L
//