ID A0A0F4Z0Y7_TALEM Unreviewed; 1298 AA.
AC A0A0F4Z0Y7;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=UDP-glucose--glycoprotein glucose phosphotransferase {ECO:0000313|EMBL:KKA23543.1};
DE EC=2.7.8.19 {ECO:0000313|EMBL:KKA23543.1};
DE Flags: Fragment;
GN ORFNames=T310_2440 {ECO:0000313|EMBL:KKA23543.1};
OS Rasamsonia emersonii CBS 393.64.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Rasamsonia.
OX NCBI_TaxID=1408163 {ECO:0000313|EMBL:KKA23543.1, ECO:0000313|Proteomes:UP000053958};
RN [1] {ECO:0000313|EMBL:KKA23543.1, ECO:0000313|Proteomes:UP000053958}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 393.64 {ECO:0000313|EMBL:KKA23543.1,
RC ECO:0000313|Proteomes:UP000053958};
RA Heijne W.H., Fedorova N.D., Nierman W.C., Vollebregt A.W., Zhao Z., Wu L.,
RA Kumar M., Stam H., van den Berg M.A., Pel H.J.;
RL Submitted (APR-2015) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KKA23543.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LASV01000098; KKA23543.1; -; Genomic_DNA.
DR RefSeq; XP_013330155.1; XM_013474701.1.
DR STRING; 1408163.A0A0F4Z0Y7; -.
DR GeneID; 25314791; -.
DR OrthoDB; 1734at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000053958; Unassembled WGS sequence.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0047358; F:UDP-glucose-glycoprotein glucose phosphotransferase activity; IEA:UniProtKB-EC.
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 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:UP000053958};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KKA23543.1}.
FT DOMAIN 35..216
FT /note="UGGT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18400"
FT DOMAIN 271..400
FT /note="UGGT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18401"
FT DOMAIN 406..650
FT /note="UGGT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18402"
FT DOMAIN 662..859
FT /note="UDP-glucose:glycoprotein glucosyltransferase
FT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18403"
FT DOMAIN 1181..1297
FT /note="Glucosyltransferase 24 catalytic"
FT /evidence="ECO:0000259|Pfam:PF18404"
FT REGION 243..277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..273
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1298
FT /evidence="ECO:0000313|EMBL:KKA23543.1"
SQ SEQUENCE 1298 AA; 146052 MW; A3B93470102FCD37 CRC64;
MFAQDRPSMW LYKLPLTLDR ISWSFFYRAG ANSVHTSIRE TAAGENSTAY FPLLDRISEG
VFEDAVTEKQ LYDRFLKVVR EDGHLADEES LSSFKFALAI RSAAPRIEAH YQYYNTSVQY
SLGTAQDAAC QVWVHMDGKQ YCSSALERAQ QDVAGELNPR ELPFDRTFGD LSAPPAVLYA
DVASPVFGEF HQKLSALAKE GQVSYRVRYR PPQHEDPRPV FVTGYGVELA LKRTDYIVID
DRQAEAKDEK DPKRTKVTTP DTDDLEDDSP ADLKPLSSSE VDRLGLNSAS FVMDSAEPFD
TLLKLTRDFP KYSSSIADYN ATDKFLKEYH GNRAAGFPAG RKIFWINGIQ IDPRQIDAYS
LLEHLRRERK LIADFKKLGL SASEAVDLLS HRALAEVQAN NEPQRYDWRD DIEGGVVIIW
MNNLEKDKRY EDWPTSIMAL LQRTFPGQLP SVRRDIFNVI VPIDLASEAD VLLLVNYIQT
FIKRGVPVRF GLVPIVHSHD STSQAKVAHH LHETYGLATL LKYFEEALSK KKIASADKSA
FQAAVADRPV RSGRQSLTFE EVLQSKELDD VVLRTAKYLK RLDMEGPSPP SLVNGVVLTR
NENWLQEMPM RLNRDLQLLQ QGVLEEVFQE DTWLPSYFLF QAAESRNEWI IPEDASNVRI
VDLPQVADSR QDVMNNLLRV ASGEGHATNN VHLVVIGDFN TERGLELLTT ALKLHQSHGE
VEVIPLHNPD VEKPSSGISS LLYQVLTRAD RTDISELLTE IESLKSSEST AEEPAYWTEA
KPIVEDFGFV PGSRGVVLNG RAVGPLPSNV SLSEKDFEQL LSYERSKRLE PVSEALKALK
LESKIPDTLS FAKLTSLVAL STIPDVPEGL FESTSKLRQN IFKNWNDTHS AITVSNSDDP
TISIVATVDP TAELSQRWVP ILKTLSKLAG VNVKIFLSPR DHIQELPIKR FYRHVLEPEP
SFDEEGSLIR PGASFSGLPK EALFTLGMDV PSSWLVAPKE SIHDLDNIKL SSLKEGTNID
AIYALEHILI EGHSRDTTTN SPPRGVQLLL GTDKDPHFAD TIIMANLGYF QFKAQPGFWK
IELKPGRSQR IFNLDSVGGM GYIPQPGDEN NEVALLSFQG KTLFPRLSRK PGHENEDVLE
TGAKPGSAMD YVSKGLNFAS GILSNVGIGP KSGTAEKHAD INIFSVASGH LYERMLNIMM
VSVMKHTKHT VKFWFIEQFL SPSFKSFLPH LAKEYGFSYE MVTYKWPHWL RGQKEKQREI
WGYKILFLDV LFPLSLDKVI FVDADQIVRT DMYDLVSL
//
