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
//