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Database: UniProt
Entry: A0A409W207_9AGAR
LinkDB: A0A409W207_9AGAR
Original site: A0A409W207_9AGAR 
ID   A0A409W207_9AGAR        Unreviewed;       466 AA.
AC   A0A409W207;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   RecName: Full=Beta-xylanase {ECO:0000256|RuleBase:RU361174};
DE            EC=3.2.1.8 {ECO:0000256|RuleBase:RU361174};
GN   ORFNames=CVT26_004019 {ECO:0000313|EMBL:PPQ72541.1};
OS   Gymnopilus dilepis.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Agaricineae; Hymenogastraceae; Gymnopilus.
OX   NCBI_TaxID=231916 {ECO:0000313|EMBL:PPQ72541.1, ECO:0000313|Proteomes:UP000284706};
RN   [1] {ECO:0000313|EMBL:PPQ72541.1, ECO:0000313|Proteomes:UP000284706}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SRW20 {ECO:0000313|EMBL:PPQ72541.1,
RC   ECO:0000313|Proteomes:UP000284706};
RX   PubMed=30283667; DOI=10.1002/evl3.42;
RA   Reynolds H.T., Vijayakumar V., Gluck-Thaler E., Korotkin H.B.,
RA   Matheny P.B., Slot J.C.;
RT   "Horizontal gene cluster transfer increased hallucinogenic mushroom
RT   diversity.";
RL   Evol. Lett. 2:88-101(2018).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.;
CC         EC=3.2.1.8; Evidence={ECO:0000256|RuleBase:RU361174};
CC   -!- PATHWAY: Glycan degradation; xylan degradation.
CC       {ECO:0000256|ARBA:ARBA00004851}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F) family.
CC       {ECO:0000256|ARBA:ARBA00007495, ECO:0000256|RuleBase:RU361174}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PPQ72541.1}.
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DR   EMBL; NHYE01005452; PPQ72541.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A409W207; -.
DR   STRING; 231916.A0A409W207; -.
DR   InParanoid; A0A409W207; -.
DR   OrthoDB; 754421at2759; -.
DR   Proteomes; UP000284706; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
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:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR035971; CBD_sf.
DR   InterPro; IPR000254; Cellulose-bd_dom_fun.
DR   InterPro; IPR044846; GH10.
DR   InterPro; IPR031158; GH10_AS.
DR   InterPro; IPR001000; GH10_dom.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR31490:SF35; ENDO-1,4-BETA-XYLANASE; 1.
DR   PANTHER; PTHR31490; GLYCOSYL HYDROLASE; 1.
DR   Pfam; PF00734; CBM_1; 1.
DR   Pfam; PF00331; Glyco_hydro_10; 2.
DR   PRINTS; PR00134; GLHYDRLASE10.
DR   SMART; SM00236; fCBD; 1.
DR   SMART; SM00633; Glyco_10; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 2.
DR   SUPFAM; SSF57180; Cellulose-binding domain; 1.
DR   PROSITE; PS51164; CBM1_2; 1.
DR   PROSITE; PS00591; GH10_1; 1.
DR   PROSITE; PS51760; GH10_2; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW   ECO:0000256|RuleBase:RU361174};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361174};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361174};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW   ECO:0000256|RuleBase:RU361174};
KW   Reference proteome {ECO:0000313|Proteomes:UP000284706};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..466
FT                   /note="Beta-xylanase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5019006933"
FT   DOMAIN          21..54
FT                   /note="CBM1"
FT                   /evidence="ECO:0000259|PROSITE:PS51164"
FT   DOMAIN          133..463
FT                   /note="GH10"
FT                   /evidence="ECO:0000259|PROSITE:PS51760"
FT   ACT_SITE        385
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10061"
SQ   SEQUENCE   466 AA;  49235 MW;  FCF439D00FC6F186 CRC64;
     MALNLASTFA GLLALVPLAY AQAGAYAQCG GIGWTGPTDC VDGYTCEGYF LQCLPGTATA
     SPTPTVTVTA TITDVATTTA TATVTDTVTT TVTTTVTSTS GSGTTTSSAP GSTATVGLAV
     AAKTAGKLYF GSATDNPELT DAPYVAELSN WQDFLQLTPD ATEPTRGNFT FTGGQQIVSL
     AQQNGQLIRG HNCVWYNQLP SWVTSTNWDN ATLLEVVANH CAVIVANWAG QICGFTHTSL
     LNFSEADTFI FFSCRQLGCD QRSVYCILSA RRQKAQRVSE PFNDDGTWRQ DVFYNVTGEA
     FVATALRAAH AADPNAKLYI NDYNLEYGGA KAQAMINLVT SLQAQGVPIH GVGIQGHLLV
     GGVPGNLQSI IESFTALGVE VAITELDIRM TLPVTDALLE QQKADYQSVI TACNKVPGCI
     GVTVWDYTDK YSWVPSTFSG QGAACPFDAN LVKKPAYDGI VSGFMS
//
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