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Database: UniProt
Entry: E3QHX9_COLGM
LinkDB: E3QHX9_COLGM
Original site: E3QHX9_COLGM 
ID   E3QHX9_COLGM            Unreviewed;      1492 AA.
AC   E3QHX9;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   SubName: Full=UDP-glucose:Glycoprotein Glucosyltransferase {ECO:0000313|EMBL:EFQ30467.1};
GN   ORFNames=GLRG_05611 {ECO:0000313|EMBL:EFQ30467.1};
OS   Colletotrichum graminicola (strain M1.001 / M2 / FGSC 10212) (Maize
OS   anthracnose fungus) (Glomerella graminicola).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum graminicola species complex.
OX   NCBI_TaxID=645133 {ECO:0000313|Proteomes:UP000008782};
RN   [1] {ECO:0000313|Proteomes:UP000008782}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M1.001 / M2 / FGSC 10212 {ECO:0000313|Proteomes:UP000008782};
RX   PubMed=22885923; DOI=10.1038/ng.2372;
RA   O'Connell R.J., Thon M.R., Hacquard S., Amyotte S.G., Kleemann J.,
RA   Torres M.F., Damm U., Buiate E.A., Epstein L., Alkan N., Altmueller J.,
RA   Alvarado-Balderrama L., Bauser C.A., Becker C., Birren B.W., Chen Z.,
RA   Choi J., Crouch J.A., Duvick J.P., Farman M.A., Gan P., Heiman D.,
RA   Henrissat B., Howard R.J., Kabbage M., Koch C., Kracher B., Kubo Y.,
RA   Law A.D., Lebrun M.-H., Lee Y.-H., Miyara I., Moore N., Neumann U.,
RA   Nordstroem K., Panaccione D.G., Panstruga R., Place M., Proctor R.H.,
RA   Prusky D., Rech G., Reinhardt R., Rollins J.A., Rounsley S., Schardl C.L.,
RA   Schwartz D.C., Shenoy N., Shirasu K., Sikhakolli U.R., Stueber K.,
RA   Sukno S.A., Sweigard J.A., Takano Y., Takahara H., Trail F.,
RA   van der Does H.C., Voll L.M., Will I., Young S., Zeng Q., Zhang J.,
RA   Zhou S., Dickman M.B., Schulze-Lefert P., Ver Loren van Themaat E.,
RA   Ma L.-J., Vaillancourt L.J.;
RT   "Lifestyle transitions in plant pathogenic Colletotrichum fungi deciphered
RT   by genome and transcriptome analyses.";
RL   Nat. Genet. 44:1060-1065(2012).
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; GG697349; EFQ30467.1; -; Genomic_DNA.
DR   RefSeq; XP_008094487.1; XM_008096296.1.
DR   STRING; 645133.E3QHX9; -.
DR   EnsemblFungi; EFQ30467; EFQ30467; GLRG_05611.
DR   GeneID; 24410976; -.
DR   VEuPathDB; FungiDB:GLRG_05611; -.
DR   eggNOG; KOG1879; Eukaryota.
DR   HOGENOM; CLU_002668_1_0_1; -.
DR   OrthoDB; 1734at2759; -.
DR   UniPathway; UPA00378; -.
DR   PHI-base; PHI:6227; -.
DR   Proteomes; UP000008782; 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:UP000008782};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EFQ30467.1}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..1492
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003178479"
FT   DOMAIN          38..218
FT                   /note="UGGT thioredoxin-like"
FT                   /evidence="ECO:0000259|Pfam:PF18400"
FT   DOMAIN          268..399
FT                   /note="UGGT thioredoxin-like"
FT                   /evidence="ECO:0000259|Pfam:PF18401"
FT   DOMAIN          405..648
FT                   /note="UGGT thioredoxin-like"
FT                   /evidence="ECO:0000259|Pfam:PF18402"
FT   DOMAIN          660..855
FT                   /note="UDP-glucose:glycoprotein glucosyltransferase
FT                   thioredoxin-like"
FT                   /evidence="ECO:0000259|Pfam:PF18403"
FT   DOMAIN          1167..1433
FT                   /note="Glucosyltransferase 24 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF18404"
FT   REGION          1438..1492
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1438..1456
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1463..1492
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1492 AA;  167006 MW;  BB62C31F3F69F6CA CRC64;
     MLRLSRLPMG LALTLSAAVN VLAVPSVTVD MKAAFPSGPY LLELLETAAG ENATAYFPLL
     DRIANGYFSE AKTDKDVYDK FLHVLNEDGH VNTPDALSTF KLALSLRTAA PRIEAHYQYY
     RTAVEPKLGS DAQDGCEAWV ELGGKQYCAP TLDTPKEPES ALDGSKVLPF DRVLGSGGEA
     ILYADPASSA FGPFHSTLAE KARKGEIEYR LRYTKPAGIY EEPLPVSGYG VELALKRTDY
     IVIDDREAQS DDSQKIANAG EVLDAAEDVA DLKPLAKSEL QELGLKAASF IMQSQDPFET
     LLRLTQDFPK FSTSIAAHNV STNFLAEHQL NRQQLVPSGM NVLWMNGVQL IERQIEAFTI
     IDLLRRERKL IDGVRDLGFT GGQAVSLLGH PKVAESKADD EPPRFDWTDD EEKEEVIMFL
     NDLEKDERYK DFPSQLTALL QRVYPGQLPP IRRDIFNLIV PVDFSKIEDL NVVAQLNTFI
     QRKVPIRFGL VPLTPTEDAA KITKVLYYLL DNYGLEVFIE YLDAAMQDAK TEKPDQSVFE
     KAIKDREPLP TAKLLAFDDV LQSQELHNVL ELARSWVKRL NANTPIPPVF INGIPVPREN
     NWLQAMSMKA SSDLQTIQRA VYFGAITEEV WFPDFFLEKA VKRRNTYIYP EDDKSIKILD
     VNKIYTEHDG LFSNIPAIEA YADSTKENWA VLTIVGDFVS DQGASLLLTA LAFRRSNPGV
     RLDIVYNPPT SASASAVNTA LKNSGDKLAE VESISDLKAI FDSAAVEPDG MFTAALSKFL
     SFAAIKPGSN LVILNGRVIG PFTEAEPFQG DDFQFLLEFE QKARILPVYA AVDDLGLTDK
     ISGPLAAAKI TSVTALSTIS DLPADIFESA PSMRVSAHDQ WNSTYTAIEI GNPETSSVHI
     VGVLNPASEQ AQRWAPILKV VSKLDGVYLK LFLNPQEKID ELPVKRFFRY VLESEPSFDE
     AGKVRGLEAS FKGLPSEALL NAGMDVPPSW LVAPKVSVHD PDNIKLSSIK SNVYASYELE
     SILIEGHSRE GGQSQPPRGA QLVLGTEKEP HFADTIIMAN LGYFQFKASP GFYNIQLKSG
     RSSEIYTIDS IGAKGWNPVP GDEGTEVVLM DFQGTTLYPR LSRKPGQEEA DVLAEPEDNS
     IVGRGLKFAE GILGKKKSAS DEEHAEINIF SVASGHLYER MLNIMMVSVM KNTKHTVKFW
     FIEQFLSPSF KDFIPHMAKE YGFKYEMVTF KWPHWLRQQK EKQREIWGYK ILFLDVLFPL
     SLDKVIFVDA DQIVRTDMIS LVNHDLEGKP YGFTPMCDSR TEMEGFRFWK QGYWANYLRG
     QPYHISALYV VDLRRFRELA AGDRLRQTYH SLSADPNSLA NLDQDLPNHM QFQIPIHSLP
     QEWLWCETWC SDESQKDAKT IDLCNNPQTK EPKLDRARRQ VPEWSVYDNE IAALDRKRKG
     LLVEAPKKEE TKAGGGGEGE QQKPVIAEED KNTKSRNWEE PPAENTHVID EL
//
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