ID A0A1B9IHU1_9TREE Unreviewed; 1635 AA.
AC A0A1B9IHU1;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=UDP-glucose:glycoprotein glucosyltransferase {ECO:0000313|EMBL:OCF55259.1};
GN ORFNames=L486_07372 {ECO:0000313|EMBL:OCF55259.1};
OS Kwoniella mangroviensis CBS 10435.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Kwoniella.
OX NCBI_TaxID=1331196 {ECO:0000313|EMBL:OCF55259.1, ECO:0000313|Proteomes:UP000092583};
RN [1] {ECO:0000313|EMBL:OCF55259.1, ECO:0000313|Proteomes:UP000092583}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 10435 {ECO:0000313|EMBL:OCF55259.1,
RC ECO:0000313|Proteomes:UP000092583};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C., Litvintseva A., Chen Y., Heitman J., Sun S., Springer D.,
RA Dromer F., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A.,
RA Alvarado L., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA Murphy C., Pearson M., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Kwoniella mangroviensis CBS10435.";
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000092583}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 10435 {ECO:0000313|Proteomes:UP000092583};
RA Cuomo C., Litvintseva A., Heitman J., Chen Y., Sun S., Springer D.,
RA Dromer F., Young S., Zeng Q., Chapman S., Gujja S., Saif S., Birren B.;
RT "Evolution of pathogenesis and genome organization in the Tremellales.";
RL Submitted (DEC-2013) 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; KI669467; OCF55259.1; -; Genomic_DNA.
DR STRING; 1331196.A0A1B9IHU1; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000092583; 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:UP000092583};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:OCF55259.1}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..1635
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008628633"
FT DOMAIN 38..234
FT /note="UGGT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18400"
FT DOMAIN 302..429
FT /note="UGGT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18401"
FT DOMAIN 437..693
FT /note="UGGT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18402"
FT DOMAIN 729..973
FT /note="UDP-glucose:glycoprotein glucosyltransferase
FT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18403"
FT DOMAIN 1293..1558
FT /note="Glucosyltransferase 24 catalytic"
FT /evidence="ECO:0000259|Pfam:PF18404"
FT REGION 268..287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1583..1635
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 268..284
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1590..1622
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1635 AA; 182221 MW; AC62C6DE6C642241 CRC64;
MRVTSGWVAL AGCLLSLAGG AKANSPPVRI SLETSWAAPP LLLEILETVY EESPSSYFSL
LSLLPSLSEK DYESDESLLE SMKNLISSYS LLSGSESTFD LALALHTAVP KIQAQFSWYE
SAIRPKERQL GVEACKEDGW VEWRGKGFCG VEELKRDVEM SIEEGLHHLD LQADTLPFDH
ISSPTSTSSL SSSAVLYLKP HSQNSANLLN YLSYHESQYP NFHYIVRYLR PTSPLSENEM
QRKTPLSGWG VEMALKKMDY LVVDDRLTGS SSSSQTQNGT NIGGHSEKGL FEDVLGKDPW
TDLATPLTNV EIRDLGLKSS TLIKSSSSPL EALRVLSQDF PKYSASLARK VQVPDEIRDK
AKSLLRRGEA TEAIYINGKG WGEGLDAYGL LRAIRTERHH VLSLTSLGLT PKQAIDLIAD
PVIGEAQVED SPGEGTVDAS DRVEGGDVIV YWNNIEKDKR YKNWPTSLGG FLRQLYPGQF
HTVRKNTWNL IFVLDLAQVS SLDIIANSIS PMIQRGLPIR FGVVPMFESG KDDISAQMAK
IFHYVVKTFG RGSTRDFLAA VSDSLTGISD HSDETTVAAY DMLSLTSTKT GLPFDEVLST
ELFDPHLEKT AAYITRLMAT KEESAQGHLF VNGKHTIVNG HWPAVVQNEM ATQLAFLQEQ
VSLLFLIRGE QPEDVANFFY DLPSTSRRRN KLINPGQGEG KLKVFNLLDI FEGDITKRLM
NDFVYPGGEG VTPVTMWVIG DLDSKEGQKV VEDALRHVQN PNGASRLGFV HVPTNDPSAP
RSTYRLSTAL YQLHASSLLS KASAEELLDI IRGLDWSNDN VDRLNIPSSD DEETQAKVIG
STDSNGQKCF TVTLSEEDTK KYFDHHPIHK AAFDGVSAID TAAAAEFWKT GTAIAKRLGL
RDGKPHLLVN GRLVGPLTPQ NFILEDYDAL EAYEYRKRVK PVIDLIQTMY EDISVFDRST
LSNLLAVSSS VIASAYKPDS AEGIFVPTQA ARARLYKKLD DGTLSFTLGD PEKAILDVAV
IVDPISENAQ KWSAVLQTLS EMDNVAITVY LEPQPSLSEV KLKRFYRSSI PSKLTFDVDG
NVIAPGVTFL DLPTTPIYTL GLDTPPSWIV SPRTSPYDLD NLVLTNIQSP VHISFTLKQL
LIEGHAREAT NAPPRGLQLQ LTTDGLEVAS DTQVMANLGY FQFKATPGVY DLSIRPGRGR
EVYELESVGS EGWDSASVNI TGPSVILDSF EGNTILPRFV RRQGMEKADV LNEEEGKKDP
ESFAGAVFSK MKSIVGLSTE VLSTKPKSRH ADINIFTVAS GLLYERFASI MILSVMKHTN
SSVKFWFIEN FLSPTFIEFI PKLAEEYNFQ YEFVTYKWPH WLRAQTEKQR IIWAYKILFL
DVLFPMDLDK VIFVDADQIV RTDMKELVDV DLHGRVYGYA PMGDSRTEME GFRFWKTGYW
RDALRGRPYH ISALYVVDLK RFRQLATGDR LRGQYHALSA DPNSLANLDQ DLPNSMQDTI
PIFTLDQDWL WCQTWCSDES LASAKTIDLC QNPLTKEPKL VRARQIPEWD LYDREIASFA
AKLQGQEVGV GALAASVDDL ASDADAGTTS SAEVEEEEQD LRDEEETERV VEDNETDEEI
IDQMLEESRR LDDEL
//
