GT2_MAGO7
ID GT2_MAGO7 Reviewed; 483 AA.
AC G4MWY1;
DT 26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 25-MAY-2022, entry version 34.
DE RecName: Full=Type 2 glycosyltransferase {ECO:0000303|PubMed:31484736};
DE EC=2.4.1.- {ECO:0000305|PubMed:31484736};
GN Name=GT2 {ECO:0000303|PubMed:31484736}; ORFNames=MGG_01191;
OS Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS fungus) (Pyricularia oryzae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX NCBI_TaxID=242507;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX PubMed=15846337; DOI=10.1038/nature03449;
RA Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL Nature 434:980-986(2005).
RN [2]
RP FUNCTION, DISRUPTION PHENOTYPE, DOMAIN, AND MUTAGENESIS OF ASP-156; ASP-158
RP AND GLN-301.
RX PubMed=31484736; DOI=10.1128/msphere.00309-19;
RA Deng S., Sun W., Dong L., Cui G., Deng Y.Z.;
RT "MoGT2 is essential for morphogenesis and pathogenicity of Magnaporthe
RT oryzae.";
RL MSphere 4:0-0(2019).
CC -!- FUNCTION: Glycosyltransferase that plays an important role in
CC infection-related morphogenesis and pathogenesis (PubMed:31484736).
CC Involved in stress tolerance and hyphal hydrophobicity via its
CC regulation of the expression of nydrophobin MPG1 (PubMed:31484736). May
CC regulate growth, pathogenicity, and cell wall integrity (CWI) through
CC glycosylation of heat shock protein SSB1, and other (unidentified)
CC substrates may contribute to conidiation (PubMed:31484736). Candidate
CC proteins as potential substrates of GT2 include several heat shock
CC proteins (SSB1/MGG_02503, MGG_06759 and MGG_06958), two coiled-coil
CC domain-containing proteins (MGG_04321 and MGG_09571), aminopeptidase 2
CC (MGG_16472), and a nuclease domain-containing protein (MGG_12646)
CC (PubMed:31484736). {ECO:0000269|PubMed:31484736}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- DOMAIN: The conserved DxD and QxxRW domains are necessary for the full
CC function. {ECO:0000269|PubMed:31484736}.
CC -!- DISRUPTION PHENOTYPE: Results in impairment of vegetative growth,
CC conidiation, stress response, hyphal appressorium-mediated penetration,
CC and pathogenicity (PubMed:31484736). Leads to altered glycoproteins
CC during conidiation (PubMed:31484736). Significantly reduces the
CC expression levels of hydropgobin MPG1 (PubMed:31484736).
CC {ECO:0000269|PubMed:31484736}.
CC -!- SIMILARITY: Belongs to the GT2 glycosyltransferase family.
CC {ECO:0000305}.
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DR EMBL; CM001232; EHA54273.1; -; Genomic_DNA.
DR RefSeq; XP_003714080.1; XM_003714032.1.
DR AlphaFoldDB; G4MWY1; -.
DR STRING; 318829.MGG_01191T0; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR EnsemblFungi; MGG_01191T0; MGG_01191T0; MGG_01191.
DR GeneID; 2679792; -.
DR KEGG; mgr:MGG_01191; -.
DR VEuPathDB; FungiDB:MGG_01191; -.
DR eggNOG; KOG2571; Eukaryota.
DR HOGENOM; CLU_019940_4_1_1; -.
DR InParanoid; G4MWY1; -.
DR OMA; HEKHIWY; -.
DR OrthoDB; 414342at2759; -.
DR Proteomes; UP000009058; Chromosome 2.
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; IMP:PHI-base.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Glycoprotein; Glycosyltransferase; Membrane;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix;
KW Virulence.
FT CHAIN 1..483
FT /note="Type 2 glycosyltransferase"
FT /id="PRO_0000448948"
FT TRANSMEM 21..41
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 336..356
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 369..389
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 396..416
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOTIF 156..158
FT /note="Dxd motif"
FT /evidence="ECO:0000269|PubMed:31484736"
FT MOTIF 301..305
FT /note="QxxxRW motif"
FT /evidence="ECO:0000269|PubMed:31484736"
FT CARBOHYD 313
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 421
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT MUTAGEN 156
FT /note="D->R: Leads to defective colony growth and loss of
FT conidiation and pathogenicity."
FT /evidence="ECO:0000269|PubMed:31484736"
FT MUTAGEN 158
FT /note="D->R: Leads to defective colony growth and loss of
FT conidiation and pathogenicity."
FT /evidence="ECO:0000269|PubMed:31484736"
FT MUTAGEN 301
FT /note="Q->R: Leads to reduced conidiation and
FT pathogenicity."
FT /evidence="ECO:0000269|PubMed:31484736"
SQ SEQUENCE 483 AA; 56495 MW; 3AD51ED63A35881E CRC64;
MATPLQIMPL PVWPITFLED AVVYLSALFT PWFTAFCVLW LHRYVRLIVH CYSHWTYKSK
PIPSKPSYTS DDVTVVIPTI HDNFDELRPS LESILATKPH ELIMVTTADK FEDLQRVAKT
LSSPNIRIFC TQYANKRIQV CEALPKITTR ITIMADDDVT WPSTMMPWIL APFEDPKIGG
VGTCQRVKRV REGGLGLRIW NWLGAAYIER RNFEISATHN MDGGTSCMSG RTGAYRSEIL
RDYEFLEGFM KEEWWGKILK ADDDNFVSRW LVSHKWKTWI QYEQECELET TLEDNIKFLY
QCSRWARSNW RSNWTSLVKE RHVWKQQWWC TYALHIATFT SLAFVFDFLI LAALWWGTEG
WEPVNRNRAI YAQLAFLAFS KVVKLVGLFR RHPADIMFLP VSIIFGYFHG LIKIYAGLTL
NMTSWGSRTD GDTDDAHRLA PGPVRCSSLN TPRSEHKLPH YMQERDEIVN EKQQMREEEW
EHL
