ID E3RYK2_PYRTT Unreviewed; 390 AA.
AC E3RYK2;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=1,3-beta-glucanosyltransferase {ECO:0000256|RuleBase:RU361209};
DE EC=2.4.1.- {ECO:0000256|RuleBase:RU361209};
GN ORFNames=PTT_14628 {ECO:0000313|EMBL:EFQ89199.1};
OS Pyrenophora teres f. teres (strain 0-1) (Barley net blotch fungus)
OS (Drechslera teres f. teres).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC Pyrenophora.
OX NCBI_TaxID=861557 {ECO:0000313|Proteomes:UP000001067};
RN [1] {ECO:0000313|EMBL:EFQ89199.1, ECO:0000313|Proteomes:UP000001067}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0-1 {ECO:0000313|EMBL:EFQ89199.1,
RC ECO:0000313|Proteomes:UP000001067};
RX PubMed=21067574; DOI=10.1186/gb-2010-11-11-r109;
RA Ellwood S.R., Liu Z., Syme R.A., Lai Z., Hane J.K., Keiper F., Moffat C.S.,
RA Oliver R.P., Friesen T.L.;
RT "A first genome assembly of the barley fungal pathogen Pyrenophora teres f.
RT teres.";
RL Genome Biol. 11:R109.1-R109.14(2010).
CC -!- FUNCTION: Splits internally a 1,3-beta-glucan molecule and transfers
CC the newly generated reducing end (the donor) to the non-reducing end of
CC another 1,3-beta-glucan molecule (the acceptor) forming a 1,3-beta
CC linkage, resulting in the elongation of 1,3-beta-glucan chains in the
CC cell wall. {ECO:0000256|RuleBase:RU361209}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004609,
CC ECO:0000256|RuleBase:RU361209}; Lipid-anchor, GPI-anchor
CC {ECO:0000256|ARBA:ARBA00004609, ECO:0000256|RuleBase:RU361209}.
CC Membrane {ECO:0000256|ARBA:ARBA00004589}; Lipid-anchor, GPI-anchor
CC {ECO:0000256|ARBA:ARBA00004589}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 72 family.
CC {ECO:0000256|ARBA:ARBA00007528, ECO:0000256|RuleBase:RU361209}.
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DR EMBL; GL535899; EFQ89199.1; -; Genomic_DNA.
DR RefSeq; XP_003302707.1; XM_003302659.1.
DR AlphaFoldDB; E3RYK2; -.
DR EnsemblFungi; EFQ89199; EFQ89199; PTT_14628.
DR KEGG; pte:PTT_14628; -.
DR eggNOG; ENOG502QRZZ; Eukaryota.
DR HOGENOM; CLU_021855_1_1_1; -.
DR OrthoDB; 2412687at2759; -.
DR Proteomes; UP000001067; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098552; C:side of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR004886; Glucanosyltransferase.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR31468; 1,3-BETA-GLUCANOSYLTRANSFERASE GAS1; 1.
DR PANTHER; PTHR31468:SF5; 1,3-BETA-GLUCANOSYLTRANSFERASE GAS5; 1.
DR Pfam; PF03198; Glyco_hydro_72; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE 3: Inferred from homology;
KW Glycoprotein {ECO:0000256|RuleBase:RU361209};
KW GPI-anchor {ECO:0000256|RuleBase:RU361209};
KW Lipoprotein {ECO:0000256|RuleBase:RU361209};
KW Membrane {ECO:0000256|RuleBase:RU361209};
KW Reference proteome {ECO:0000313|Proteomes:UP000001067};
KW Transferase {ECO:0000256|RuleBase:RU361209}.
SQ SEQUENCE 390 AA; 44113 MW; C3E9B7465C26BCA4 CRC64;
MNASITCPPI RVRGRFLCQR GDRTKFFVRG VAYQVRSTLD PISDDRLAEL KNDILLFKEL
GLNTLFVYCI DSTKDHTEAM KLLEEAGIYV FTTVSTPFNA INRLAPTESY NPDTMVSFFK
TVGIMASFPN TLGLLAGNEL INNDATMPVA GVLKAVVRDL KKYMKLQNEA NGQRVLPIGY
NAATSSARDQ EVLEYLTVGD DEISIDFWAC KNYDWKEISD MTRSGYNDLL HRFSGTTIPM
FFSEYGNTSH QPRLFQETTA LYSPAMSRVF SGGCVYEFWQ STNGYGLVEM LRHGSDNQVP
AYRQNPDDES KISERREIHG GMLLIFKDFV NYKTKLAEVS SVEVEVVIEA AEREGEQVQT
DTKASGPWQA KFRMLESCVD WHEMEGILSR
//
