ID   XYN6_MAGO7              Reviewed;         380 AA.
AC   G4MPQ7;
DT   09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT   14-DEC-2011, sequence version 1.
DT   25-MAY-2022, entry version 49.
DE   RecName: Full=Endo-1,4-beta-xylanase 6;
DE            Short=Xylanase 6;
DE            EC=3.2.1.8;
DE   AltName: Full=1,4-beta-D-xylan xylanohydrolase 6;
DE   Flags: Precursor;
GN   Name=XYL6; ORFNames=MGG_02245;
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).
CC   -!- FUNCTION: Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a
CC       major structural heterogeneous polysaccharide found in plant biomass
CC       representing the second most abundant polysaccharide in the biosphere,
CC       after cellulose. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.;
CC         EC=3.2.1.8;
CC   -!- PATHWAY: Glycan degradation; xylan degradation.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F) family.
CC       {ECO:0000305}.
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DR   EMBL; CM001231; EHA56406.1; -; Genomic_DNA.
DR   RefSeq; XP_003709018.1; XM_003708970.1.
DR   AlphaFoldDB; G4MPQ7; -.
DR   SMR; G4MPQ7; -.
DR   STRING; 242507.G4MPQ7; -.
DR   CAZy; CBM1; Carbohydrate-Binding Module Family 1.
DR   CAZy; GH10; Glycoside Hydrolase Family 10.
DR   EnsemblFungi; MGG_02245T0; MGG_02245T0; MGG_02245.
DR   GeneID; 2681342; -.
DR   KEGG; mgr:MGG_02245; -.
DR   VEuPathDB; FungiDB:MGG_02245; -.
DR   eggNOG; ENOG502QSCW; Eukaryota.
DR   HOGENOM; CLU_020161_2_1_1; -.
DR   InParanoid; G4MPQ7; -.
DR   OMA; PENQMKW; -.
DR   OrthoDB; 829814at2759; -.
DR   UniPathway; UPA00114; -.
DR   PHI-base; PHI:2207; -.
DR   Proteomes; UP000009058; Chromosome 1.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0030248; F:cellulose binding; IEA:InterPro.
DR   GO; GO:0031176; F:endo-1,4-beta-xylanase activity; IEA:UniProtKB-EC.
DR   GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR035971; CBD_sf.
DR   InterPro; IPR000254; Cellulose-bd_dom_fun.
DR   InterPro; IPR044846; GH10.
DR   InterPro; IPR001000; GH10_dom.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR31490; PTHR31490; 1.
DR   Pfam; PF00734; CBM_1; 1.
DR   Pfam; PF00331; Glyco_hydro_10; 1.
DR   PRINTS; PR00134; GLHYDRLASE10.
DR   SMART; SM00236; fCBD; 1.
DR   SMART; SM00633; Glyco_10; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   SUPFAM; SSF57180; SSF57180; 1.
DR   PROSITE; PS00562; CBM1_1; 1.
DR   PROSITE; PS51164; CBM1_2; 1.
DR   PROSITE; PS51760; GH10_2; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Disulfide bond; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Reference proteome; Secreted; Signal;
KW   Xylan degradation.
FT   SIGNAL          1..21
FT   CHAIN           22..380
FT                   /note="Endo-1,4-beta-xylanase 6"
FT                   /id="PRO_0000429629"
FT   DOMAIN          22..53
FT                   /note="CBM1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00597"
FT   DOMAIN          74..379
FT                   /note="GH10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01096"
FT   REGION          53..80
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        59..73
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        205
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        316
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   DISULFID        334..340
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   380 AA;  40868 MW;  5723E7A41998CB6D CRC64;
     MRTPAIVLAL APAAAFGQAA LWGQCGGQGW TGAKTCVSGA VCQAQNEWYS QCVPGSGGGN
     PPTPQPTQPS NPPPSTGSGL NAKFKNKGKL YFGTSMDHYD LNKAQLTNIV KAQFGQITNE
     NSMKWDAIEP SRNSFSWTNA DAVVNFATAN GKLMRGHTLL WHSQLPAWVS NINDRNTLTQ
     VIQNHVTAMV TRYRGKILQW DVVNEIFAED GSLRSSVFSR VLGEDFVGIA FRAARAADPN
     AKLYINDYNL DIANYAKVTR GMVEKVNKWV SQGIPIDGIG SQAHLAQPGG WNPASGVPAA
     LRALAAANVK EIAITELDIA GASANDYVTV VNACLQISKC VGITVWGVSD AISWRPNDNP
     LLYDRNYQPK AAYTAIMNAL