ID I1RUP0_GIBZE Unreviewed; 1463 AA.
AC I1RUP0;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 24-JAN-2024, entry version 55.
DE SubName: Full=Chromosome 4, complete genome {ECO:0000313|EMBL:CEF85276.1};
GN Name=FG07940.1 {ECO:0000313|EnsemblFungi:CEF85276};
GN ORFNames=FGRAMPH1_01T26033 {ECO:0000313|EMBL:CEF85276.1};
OS Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084
OS / PH-1) (Wheat head blight fungus) (Fusarium graminearum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=229533 {ECO:0000313|EMBL:CEF85276.1, ECO:0000313|Proteomes:UP000070720};
RN [1] {ECO:0000313|EnsemblFungi:CEF85276, ECO:0000313|Proteomes:UP000070720}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1
RC {ECO:0000313|Proteomes:UP000070720}, and PH-1 / ATCC MYA-4620 / FGSC
RC 9075 / NRRL 31084 {ECO:0000313|EnsemblFungi:CEF85276};
RX PubMed=17823352; DOI=10.1126/science.1143708;
RA Cuomo C.A., Gueldener U., Xu J.-R., Trail F., Turgeon B.G., Di Pietro A.,
RA Walton J.D., Ma L.-J., Baker S.E., Rep M., Adam G., Antoniw J., Baldwin T.,
RA Calvo S.E., Chang Y.-L., DeCaprio D., Gale L.R., Gnerre S., Goswami R.S.,
RA Hammond-Kosack K., Harris L.J., Hilburn K., Kennell J.C., Kroken S.,
RA Magnuson J.K., Mannhaupt G., Mauceli E.W., Mewes H.-W., Mitterbauer R.,
RA Muehlbauer G., Muensterkoetter M., Nelson D., O'Donnell K., Ouellet T.,
RA Qi W., Quesneville H., Roncero M.I.G., Seong K.-Y., Tetko I.V., Urban M.,
RA Waalwijk C., Ward T.J., Yao J., Birren B.W., Kistler H.C.;
RT "The Fusarium graminearum genome reveals a link between localized
RT polymorphism and pathogen specialization.";
RL Science 317:1400-1402(2007).
RN [2] {ECO:0000313|EnsemblFungi:CEF85276, ECO:0000313|Proteomes:UP000070720}
RP GENOME REANNOTATION.
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1
RC {ECO:0000313|Proteomes:UP000070720}, and PH-1 / ATCC MYA-4620 / FGSC
RC 9075 / NRRL 31084 {ECO:0000313|EnsemblFungi:CEF85276};
RX PubMed=20237561; DOI=10.1038/nature08850;
RA Ma L.J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.J.,
RA Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA Houterman P.M., Kang S., Shim W.B., Woloshuk C., Xie X., Xu J.R.,
RA Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA Butchko R.A., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.,
RA Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA Kumar L., Lee Y.H., Li L., Manners J.M., Miranda-Saavedra D., Mukherjee M.,
RA Park G., Park J., Park S.Y., Proctor R.H., Regev A., Ruiz-Roldan M.C.,
RA Sain D., Sakthikumar S., Sykes S., Schwartz D.C., Turgeon B.G.,
RA Wapinski I., Yoder O., Young S., Zeng Q., Zhou S., Galagan J., Cuomo C.A.,
RA Kistler H.C., Rep M.;
RT "Comparative genomics reveals mobile pathogenicity chromosomes in
RT Fusarium.";
RL Nature 464:367-373(2010).
RN [3]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PH-1;
RA King R., Urban M., Hassani-Pak K., Hammond-Kosack K.;
RT "A revised Fusarium graminearum genomic reference sequence using whole
RT shotgun re-sequencing.";
RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:CEF85276.1, ECO:0000313|Proteomes:UP000070720}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1
RC {ECO:0000313|Proteomes:UP000070720}, and PH-1
RC {ECO:0000313|EMBL:CEF85276.1};
RX PubMed=26198851; DOI=10.1186/s12864-015-1756-1;
RA King R., Urban M., Hammond-Kosack M.C., Hassani-Pak K.,
RA Hammond-Kosack K.E.;
RT "The completed genome sequence of the pathogenic ascomycete fungus Fusarium
RT graminearum.";
RL BMC Genomics 16:544-544(2015).
RN [5] {ECO:0000313|EnsemblFungi:CEF85276}
RP IDENTIFICATION.
RC STRAIN=PH-1 / ATCC MYA-4620 / FGSC 9075 / NRRL 31084
RC {ECO:0000313|EnsemblFungi:CEF85276};
RG EnsemblFungi;
RL Submitted (JAN-2017) to UniProtKB.
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; HG970335; CEF85276.1; -; Genomic_DNA.
DR RefSeq; XP_011327782.1; XM_011329480.1.
DR STRING; 229533.I1RUP0; -.
DR EnsemblFungi; CEF85276; CEF85276; FGRRES_07940.
DR GeneID; 23554983; -.
DR KEGG; fgr:FGSG_07940; -.
DR VEuPathDB; FungiDB:FGRAMPH1_01G26033; -.
DR eggNOG; KOG1879; Eukaryota.
DR HOGENOM; CLU_002668_1_0_1; -.
DR InParanoid; I1RUP0; -.
DR OrthoDB; 1734at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000070720; 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:UP000070720};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..1463
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010124550"
FT DOMAIN 36..214
FT /note="UGGT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18400"
FT DOMAIN 265..396
FT /note="UGGT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18401"
FT DOMAIN 402..644
FT /note="UGGT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18402"
FT DOMAIN 656..851
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 1435..1463
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1463 AA; 163002 MW; 375F974621490FF0 CRC64;
MLRLSQYMAM AVLAATAASA SPSVNVGMHA AFPHGPYLLE LLETAAGENS TAYFPLLDKI
ASGHFASANS DAELYHQFLQ VLQEDRHIIA RDALSTFKLS LSLRAAAPRI EAHYQYYSTA
VDPESQIDGA GNCQSWALID NQKYCSPDLD VAVEGKVVSK QAKVLPFDRV LGIGKDAILY
ADPTHASFGP FHDVLSKAAR QGDVSYRLRY RRSPGVSNTP LPVSGYGVKL DLKRTDYIVI
DDREATQETQ KPHIVADVDL DTDEEVADLK PLSSSELASL GLKTASFILK SDNPMDALLK
STQDFPKFSA SIASHEVTPG FAQEQEKNVA AGVPSGINFL WMNGVQLIER QIEPFTLIEM
IRRERKLIDG VREIGFNGQQ AVSLLGHSEI ASSKADDEPP RFDWTDRLED GKAVMWLNDL
ETDSRYQKFP SDLTALLQRA YPGQLPQVAL NLFHVVAPID FTDLEDGRAF GQLTQFMQRG
ITIRFGIVPL ATTPASIAQA KVVYHLMETY GFESLITYLQ ESEEGPEGAA NKRSFAKAID
GREPMPAMTK MTLSEVLEAK SYAQKVKAGQ AWASRLNAAT PVRPILVNGM VIPREKNWVQ
VMGQRLTEDQ QTIQKAVYFG HVNEDTPVSD LFLKTALSKR NAHIFPDDDK TLRILDVNKL
YTDHAELFSK IAVLPADVES AKEDWAVLTV IADLNTNDGQ DLLLTALKFK RNNQGIRLDL
VHNPSLPSNA HAINGAFKLS EVKLVEMRCK DDLKAVLEAP WTAEEDGFGT ALANFLLTSN
IQPGTKGLLL NGRFVGPLPS SVSFEDDDLK LLLEFEQRSR ILPVYAAIKE LGFADRLSDP
ISAAKLTSIT ALSTISDLPQ GIFESAPSIR STLYNTWNAT HSTIEVGNPE TASVHIAGLL
NPTSEQGQRW APILKVLSEL DGIYLKLFMN PKELTGELPI KRFFRYVLDS TPSFDDSGHV
QSPKATFKGL PSEALLTAGM DVPPAWLVAA KDSIQDLDNI KLSSIKSDID VVYELENILV
EGHSRDGKRG APRGAQLALA TEKDPLITDT IVMANLGYFQ FKANPGFYSI RLKEGRSSEI
FTIESAGAHG YAAVPGDEGT EIALMDFKGT TLYPRLNRKS GMEEADVLES VDSDNDGIVA
KGLKFAESLL GGAKSPKEIS AQEHAEINIF SVASGHLYER MLNIMMVSVM RNTKHSVKFW
FIEQFLSPSF KEFIPHMAAE YGFKYEMVTY KWPHWLRQQK EKQREIWGYK ILFLDVLFPL
SLDKVIFVDA DQIVRTDMID LVNHDLEGAP YGFTPMCDSR TEMEGFRFWK QGYWANYLRG
LPYHISALYV VDLNRFRQLA AGDRLRQQYH TLSADPNSLS NLDQDLPNNM QFAIPIHSLP
QEWLWCETWC SDDSLTKART IDLCNNPQTK EPKLDRARRQ VPEWTIYDNE IAALDQRRKG
VAGKNENTRS RESEDKAHTK DEL
//
