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Database: UniProt
Entry: A0A2J5HTL2_9EURO
LinkDB: A0A2J5HTL2_9EURO
Original site: A0A2J5HTL2_9EURO 
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
//
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