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Database: UniProt
Entry: Q0UR94_PHANO
LinkDB: Q0UR94_PHANO
Original site: Q0UR94_PHANO 
ID   Q0UR94_PHANO            Unreviewed;       436 AA.
AC   Q0UR94;
DT   05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2006, sequence version 1.
DT   13-SEP-2023, entry version 80.
DE   RecName: Full=1,3-beta-glucanosyltransferase {ECO:0000256|RuleBase:RU361209};
DE            EC=2.4.1.- {ECO:0000256|RuleBase:RU361209};
GN   ORFNames=SNOG_05720 {ECO:0000313|EMBL:EAT86784.1};
OS   Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS   blotch fungus) (Parastagonospora nodorum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC   Parastagonospora.
OX   NCBI_TaxID=321614 {ECO:0000313|EMBL:EAT86784.1, ECO:0000313|Proteomes:UP000001055};
RN   [1] {ECO:0000313|Proteomes:UP000001055}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173
RC   {ECO:0000313|Proteomes:UP000001055};
RX   PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA   Hane J.K., Lowe R.G., Solomon P.S., Tan K.C., Schoch C.L., Spatafora J.W.,
RA   Crous P.W., Kodira C., Birren B.W., Galagan J.E., Torriani S.F.,
RA   McDonald B.A., Oliver R.P.;
RT   "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT   analysis of the wheat pathogen Stagonospora nodorum.";
RL   Plant Cell 19:3347-3368(2007).
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   -!- SIMILARITY: Belongs to the glycosyl hydrolase 72 family.
CC       {ECO:0000256|ARBA:ARBA00007528, ECO:0000256|RuleBase:RU361209}.
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DR   EMBL; CH445332; EAT86784.1; -; Genomic_DNA.
DR   RefSeq; XP_001796116.1; XM_001796064.1.
DR   AlphaFoldDB; Q0UR94; -.
DR   EnsemblFungi; SNOT_05720; SNOT_05720; SNOG_05720.
DR   GeneID; 5972993; -.
DR   KEGG; pno:SNOG_05720; -.
DR   VEuPathDB; FungiDB:JI435_057200; -.
DR   eggNOG; ENOG502SHAA; Eukaryota.
DR   HOGENOM; CLU_021855_0_0_1; -.
DR   InParanoid; Q0UR94; -.
DR   OMA; NAYEWCG; -.
DR   OrthoDB; 2783940at2759; -.
DR   Proteomes; UP000001055; Unassembled WGS sequence.
DR   GO; GO:0043188; C:cell septum edging; IEA:EnsemblFungi.
DR   GO; GO:0051286; C:cell tip; IEA:EnsemblFungi.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0000936; C:primary cell septum; IEA:EnsemblFungi.
DR   GO; GO:0098552; C:side of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0030427; C:site of polarized growth; IEA:EnsemblFungi.
DR   GO; GO:0042124; F:1,3-beta-glucanosyltransferase activity; IBA:GO_Central.
DR   GO; GO:0071970; P:fungal-type cell wall (1->3)-beta-D-glucan biosynthetic process; IBA:GO_Central.
DR   GO; GO:0031505; P:fungal-type cell wall organization; IBA:GO_Central.
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:SF8; 1,3-BETA-GLUCANOSYLTRANSFERASE GAS2; 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:UP000001055};
KW   Signal {ECO:0000256|RuleBase:RU361209};
KW   Transferase {ECO:0000256|RuleBase:RU361209}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|RuleBase:RU361209"
FT   CHAIN           22..436
FT                   /note="1,3-beta-glucanosyltransferase"
FT                   /evidence="ECO:0000256|RuleBase:RU361209"
FT                   /id="PRO_5033204573"
SQ   SEQUENCE   436 AA;  46369 MW;  EDC2886FAF0FA9AD CRC64;
     MVHFLATLAL AVTAGLSCVS AIPTISAKGS KFFTSDGNQF YVKGVAYQLV PEDPLITSSQ
     CSLDANLMKT IGANSIRVYH VDPKGNHDAC MKAFADAGIY VWLDLDTFNT QIYEAAPQWN
     SSQRDAFALV MDAFHSYDNL GGFFVGNEAI TTANGSVTAP YVKAAARDLK AYRDSKSYRK
     IPVGYSAADI ASLRPMLQNY LACGTNSSET LDFFSLNSYS WCGGSSYMQS GYDQLEKMSE
     SLHIPIFMSE TGCNTVRPRD FKDQEAIFGD MADTWSGSII YEWIEEANNY GIVKYGDKVD
     PASPRAPPDG FPRSGTPIPV QPDFSNLANV WKTLSPSGVK ESAYNPSQAP VSCPAFTAGA
     WEVNPTAALP TMGQVHNFAS GAASSTERAA GATGGPTGTS TPAPAGSQGA AADNLGRDLK
     RSATAAAGVL ALLAWL
//
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