ID Q0UFZ3_PHANO Unreviewed; 349 AA.
AC Q0UFZ3;
DT 05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 2.
DT 27-MAR-2024, entry version 68.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EAT83513.2};
GN ORFNames=SNOG_09321 {ECO:0000313|EMBL:EAT83513.2};
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:EAT83513.2, 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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC {ECO:0000256|ARBA:ARBA00009865, ECO:0000256|RuleBase:RU361187}.
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DR EMBL; CH445338; EAT83513.2; -; Genomic_DNA.
DR RefSeq; XP_001799616.1; XM_001799564.1.
DR AlphaFoldDB; Q0UFZ3; -.
DR EnsemblFungi; SNOT_09321; SNOT_09321; SNOG_09321.
DR GeneID; 5976517; -.
DR KEGG; pno:SNOG_09321; -.
DR VEuPathDB; FungiDB:JI435_093210; -.
DR eggNOG; ENOG502QTYK; Eukaryota.
DR HOGENOM; CLU_009397_4_1_1; -.
DR InParanoid; Q0UFZ3; -.
DR OrthoDB; 1849815at2759; -.
DR Proteomes; UP000001055; Unassembled WGS sequence.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR PANTHER; PTHR43772:SF2; BETA-1,4-XYLOSIDASE (EUROFUNG); 1.
DR PANTHER; PTHR43772; ENDO-1,4-BETA-XYLANASE; 1.
DR Pfam; PF04616; Glyco_hydro_43; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361187};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361187};
KW Reference proteome {ECO:0000313|Proteomes:UP000001055}.
FT SITE 141
FT /note="Important for catalytic activity, responsible for
FT pKa modulation of the active site Glu and correct
FT orientation of both the proton donor and substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-2"
SQ SEQUENCE 349 AA; 39012 MW; 194DA6D5D29FDCD6 CRC64;
MSIQAYDPPV INAFHQCDPA AHVWKHDPNT VYIYGSHDWN STSTSDDGGS QYDMKDYYVL
TQTNISAPAK VSQKILDLPD VPWAAKQLWA PDATEKDGKF YLYFPAKDHE GVFRLGVAIS
DTPDGKFQAE PSFIPGSYSI DPSVLADTDG SYYIYFGGLW GGQLQAWTNN TLVSHQRSAK
LYIANDQMQN KTAFGPNEPS SGPALGPRFA KLSADMRSFV HAPKELVIYD KDGQVMQANT
TRRFFEGPSI NKVGHEYYLQ YSTGSFHTVE VAVGSKPDGP FHWNSTLLQP VKGWTTHQSI
TKFKDDWLLY YADASLSGQD NLRNTKVRKL KYEQGTFSLA QPQPVQPAQ
//
