ID A0A179FNV7_METCM Unreviewed; 1470 AA.
AC A0A179FNV7;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=UDP-glucose:glycoprotein glucosyltransferase {ECO:0000313|EMBL:OAQ66689.1};
GN ORFNames=VFPPC_08215 {ECO:0000313|EMBL:OAQ66689.1};
OS Pochonia chlamydosporia 170.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Pochonia.
OX NCBI_TaxID=1380566 {ECO:0000313|EMBL:OAQ66689.1, ECO:0000313|Proteomes:UP000078397};
RN [1] {ECO:0000313|EMBL:OAQ66689.1, ECO:0000313|Proteomes:UP000078397}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=170 {ECO:0000313|EMBL:OAQ66689.1};
RX PubMed=27416025;
RA Wang G., Liu Z., Lin R., Li E., Mao Z., Ling J., Yang Y., Yin W.B., Xie B.;
RT "Biosynthesis of antibiotic leucinostatins in bio-control fungus
RT Purpureocillium lilacinum and their inhibition on phytophthora revealed by
RT genome mining.";
RL PLoS Pathog. 12:E1005685-E1005685(2016).
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:OAQ66689.1}.
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DR EMBL; LSBJ02000004; OAQ66689.1; -; Genomic_DNA.
DR RefSeq; XP_018143776.1; XM_018286961.1.
DR STRING; 1380566.A0A179FNV7; -.
DR GeneID; 28850955; -.
DR KEGG; pchm:VFPPC_08215; -.
DR OrthoDB; 1734at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000078397; Chromosome 4.
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:UP000078397};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:OAQ66689.1}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..1470
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008101874"
FT DOMAIN 39..209
FT /note="UGGT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18400"
FT DOMAIN 261..390
FT /note="UGGT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18401"
FT DOMAIN 396..639
FT /note="UGGT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18402"
FT DOMAIN 651..847
FT /note="UDP-glucose:glycoprotein glucosyltransferase
FT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18403"
FT DOMAIN 1163..1429
FT /note="Glucosyltransferase 24 catalytic"
FT /evidence="ECO:0000259|Pfam:PF18404"
FT REGION 1438..1470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1470 AA; 164831 MW; 549C6B781576FDC4 CRC64;
MRLLPPISWL SLACLVLTPQ VLAVPAVKVG MKAAFDTAPE TAAGENESSY FPLLDRIGNG
YFATATSDSE LFRRFLEVLH HDGHITDPDA LSTFKLALSL RSAAPRIESH YQHYTTAIEP
LEGLQECDMW VLVNGKQYCT PDLDEAVANQ LLSAAVKSLP FDRALGRGTT AVLYADPTSE
GFPDYHRTLS KAARVSNLTY HLRYRRSKSH IGRPLPISGY GVELALKKTD YIVIDDRRSS
QSIEQKSLEQ EEILDGKENM SDLTALSKSE LASIGMKAAS FIQKSNEPFD TLVKFTQDFP
KFASSISSHN VSHTFTEEYK HNQAQMVRGG INFLWMNGAQ LIERQIQPFT LVNMLRRERR
LVDGIRGLGF DGNQAVRLLG HEAVSAANEN SEPLRYDWTD RLEAGQVILW LNDLENDDRY
SSYPKTLSSL LQRTFPGQIP PIGRNIFNLI IPADLSNIED LKFIAEVHSI LDRGIPIRFG
LVPLQSSHEA KIQAKIAYFL AKSYGLECVS SYVTGLTKAQ PNGANPESLL SAVTANYPLL
PEGEDMTLST ILETNEFTEK LSMAKRWSNR LKADTAVRPL FINGAAVHRD QNWMQSISLT
VGADLQTVQK GVYHGALDDH TWIPGIFIDG AATRRNIYIS GKDEKTLRML NIAKIYDESA
AQLDALPVIE SSTESTKASW AVVTVLTDTS SNAGLGFFLS ALEFRRNNPG VRLDFVNTQS
NVRLSSQINA ALKANQAKLK DIKTIQELKT LMQEATNYTA NDDYEELLSK VLAVSKTGIG
SQGLIMNGRV IGPIAPTTPF DSEDFEQLLV YEQNRRIFPV YAAVADLGLS EKLSTAMTAA
KLTSIIALST ISDLPEGIFE SAPAIRSNIY DSWNANHTVI QTGNPKTASV HIVGLLDPVS
EKAQRWAHIL KMAAELDGVY IRLFLNPREH VEELPVKRFF RYIVESTPKF DETGSVKAPT
ATFEGLPSDV LMTVGMDLPP AWLVAPKLSV HDLDNIQLSS VESDVEATYE LQHILIEGHS
RENEGSAPRG AQLVLGTENN PALTDTIVMA NLGFFQFKAN PGVYNIHLKP GRSADIYTIE
SIGANGWDAV PGDEGTELAL MDFQGTTLYP RLKRRPNMEN QDVLLDTSSQ TEGSIVSKGL
KLAEGLFGGG RNKPTISPRH AEINIFSVAS GHLYERMLNI MMVSVMRNTK HTVKFWFIEQ
FLSPSFKEFI PHLAKEYGFE YEMVTYKWPH WLRQQKEKQR EIWGYKILFL DVLFPLSLDK
VIFVDADQIV RTDMMDLVNL DLNGAPYGFT PMCDSRTEMD GFRFWKQGYW ANYLRGKPYH
ISALYVVDLR RFREMAAGDR LRQQYHALSA DPASLSNLDQ DLPNHMQFQI PIHSLPQDWL
WCETWCSDDD FAKARTIDLC NNPQTKEPKL DRAKRQVPEW MVYDEEIAAL DLRRKHREFG
QSKEQKVEKE TERTNSGDDV AESGHSRDEL
//
