GT2_ZYMTI
ID GT2_ZYMTI Reviewed; 471 AA.
AC F9WWD1;
DT 11-DEC-2019, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 1.
DT 25-MAY-2022, entry version 31.
DE RecName: Full=Type 2 glycosyltransferase {ECO:0000303|PubMed:29020037};
DE EC=2.4.1.- {ECO:0000305|PubMed:29020037};
GN Name=GT2 {ECO:0000303|PubMed:29020037}; ORFNames=MYCGRDRAFT_65552;
OS Zymoseptoria tritici (strain CBS 115943 / IPO323) (Speckled leaf blotch
OS fungus) (Septoria tritici).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Zymoseptoria.
OX NCBI_TaxID=336722;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 115943 / IPO323;
RX PubMed=21695235; DOI=10.1371/journal.pgen.1002070;
RA Goodwin S.B., Ben M'barek S., Dhillon B., Wittenberg A.H.J., Crane C.F.,
RA Hane J.K., Foster A.J., Van der Lee T.A.J., Grimwood J., Aerts A.,
RA Antoniw J., Bailey A., Bluhm B., Bowler J., Bristow J., van der Burgt A.,
RA Canto-Canche B., Churchill A.C.L., Conde-Ferraez L., Cools H.J.,
RA Coutinho P.M., Csukai M., Dehal P., De Wit P., Donzelli B.,
RA van de Geest H.C., van Ham R.C.H.J., Hammond-Kosack K.E., Henrissat B.,
RA Kilian A., Kobayashi A.K., Koopmann E., Kourmpetis Y., Kuzniar A.,
RA Lindquist E., Lombard V., Maliepaard C., Martins N., Mehrabi R.,
RA Nap J.P.H., Ponomarenko A., Rudd J.J., Salamov A., Schmutz J.,
RA Schouten H.J., Shapiro H., Stergiopoulos I., Torriani S.F.F., Tu H.,
RA de Vries R.P., Waalwijk C., Ware S.B., Wiebenga A., Zwiers L.-H.,
RA Oliver R.P., Grigoriev I.V., Kema G.H.J.;
RT "Finished genome of the fungal wheat pathogen Mycosphaerella graminicola
RT reveals dispensome structure, chromosome plasticity, and stealth
RT pathogenesis.";
RL PLoS Genet. 7:E1002070-E1002070(2011).
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=29020037; DOI=10.1371/journal.ppat.1006672;
RA King R., Urban M., Lauder R.P., Hawkins N., Evans M., Plummer A.,
RA Halsey K., Lovegrove A., Hammond-Kosack K., Rudd J.J.;
RT "A conserved fungal glycosyltransferase facilitates pathogenesis of plants
RT by enabling hyphal growth on solid surfaces.";
RL PLoS Pathog. 13:E1006672-E1006672(2017).
CC -!- FUNCTION: Glycosyltransferase involved in the maintenance of the
CC outermost surface of the fungal cell wall (PubMed:29020037). Likely
CC functions in the synthesis of a currently unknown, potentially minor
CC but widespread, extracellular or outer cell wall polysaccharide which
CC plays a key role in facilitating many interactions between plants and
CC fungi by enabling hyphal growth on solid matrices (PubMed:29020037).
CC {ECO:0000269|PubMed:29020037}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Severely impairs hyphal growth with filaments
CC both shorter and growing in a sinusoidal manner (PubMed:29020037).
CC Results in a dramatic loss of disease causing ability on wheat leaves
CC (PubMed:29020037). {ECO:0000269|PubMed:29020037}.
CC -!- SIMILARITY: Belongs to the GT2 glycosyltransferase family.
CC {ECO:0000305}.
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DR EMBL; CM001196; EGP92529.1; -; Genomic_DNA.
DR RefSeq; XP_003857553.1; XM_003857505.1.
DR AlphaFoldDB; F9WWD1; -.
DR EnsemblFungi; Mycgr3T65552; Mycgr3P65552; Mycgr3G65552.
DR GeneID; 13394347; -.
DR KEGG; ztr:MYCGRDRAFT_65552; -.
DR VEuPathDB; FungiDB:ZTRI_1.565; -.
DR eggNOG; ENOG502QTJK; Eukaryota.
DR HOGENOM; CLU_019940_4_1_1; -.
DR InParanoid; F9WWD1; -.
DR PHI-base; PHI:7558; -.
DR Proteomes; UP000008062; Chromosome 1.
DR GO; GO:0030446; C:hyphal cell wall; EXP:PHI-base.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016757; F:glycosyltransferase activity; TAS:PHI-base.
DR GO; GO:0030448; P:hyphal growth; IMP:PHI-base.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 3: Inferred from homology;
KW Cell membrane; Glycoprotein; Glycosyltransferase; Membrane;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix;
KW Virulence.
FT CHAIN 1..471
FT /note="Type 2 glycosyltransferase"
FT /id="PRO_0000448756"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 305..325
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 339..359
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 368..388
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 29
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 88
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 222
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 458
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 471 AA; 54871 MW; 459259FAABBDFCCA CRC64;
MLSILGWFWA FVSAFVLRYL RTIVNCISNW TYRPIPIPDN PTYGPQDVTI ILPTIAQGGE
ELEGTLRTCL RTEPYEIILV TIDANVKNLT LLAKKINSKK IRVLSVREAN KRRQMCRAIP
EVSTRITIFV DDDVIWPVKL LPWILAPFEN PQMGGVGTSQ RRVRPEKMNA WVFLNMGYLE
RRNWDCSACL HIDGGLPCLS GRTAAYRTSI LQDDAFTHGF TNETWRTMQL NADDDNFITR
WLYSHNWKIG MQYHKEAEVL TTLEAGPKYL SQCLRWVRSN WRSNIKSMFV ERHYWYTQLW
TTYSCLQTTI TAWALPWDAF LFYSLHKAST DWSDDSRKMA FTLLFLWIFG FTKNVKLWGH
YFRYPVDVIY IPVHIAFGYF HGLIKFWGLV TLSETTWGSR DGADSSELNR IRMMPLPPYG
STTPDGRKSE TFEYMQEMPL IDQLPAYDTH DRHPPLSNMT STITTTTPFH D
