ID   A0A2L2TYQ6_9HYPO        Unreviewed;       568 AA.
AC   A0A2L2TYQ6;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=Beta-xylanase {ECO:0000256|RuleBase:RU361174};
DE            EC=3.2.1.8 {ECO:0000256|RuleBase:RU361174};
OS   Fusarium venenatum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX   NCBI_TaxID=56646 {ECO:0000313|EMBL:CEI67360.1, ECO:0000313|Proteomes:UP000245910};
RN   [1] {ECO:0000313|Proteomes:UP000245910}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A3/5 {ECO:0000313|Proteomes:UP000245910};
RA   King R.;
RL   Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; LN649229; CEI67360.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2L2TYQ6; -.
DR   STRING; 56646.A0A2L2TYQ6; -.
DR   OrthoDB; 548101at2759; -.
DR   Proteomes; UP000245910; Chromosome i.
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; 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; 1.
DR   PRINTS; PR00134; GLHYDRLASE10.
DR   SMART; SM00236; fCBD; 1.
DR   SMART; SM00633; Glyco_10; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF57180; Cellulose-binding domain; 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 {ECO:0000256|ARBA:ARBA00023277,
KW   ECO:0000256|RuleBase:RU361174};
KW   Glycosidase {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:UP000245910};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..568
FT                   /note="Beta-xylanase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5014921406"
FT   DOMAIN          16..335
FT                   /note="GH10"
FT                   /evidence="ECO:0000259|PROSITE:PS51760"
FT   DOMAIN          532..568
FT                   /note="CBM1"
FT                   /evidence="ECO:0000259|PROSITE:PS51164"
FT   REGION          370..402
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          449..473
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        385..402
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        450..473
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   568 AA;  61135 MW;  6E6391B55E20D5C7 CRC64;
     MHKSALIGLL ASSPVSAQLH SLAQAAGLKY FGSAVDNGYL SDAAYAKIAD NVEEFGQLVP
     ENGQKWETVE PSRDQFTYET ADVIPDLAKK NGQILRCHAL TWHSQLPNWV VVSAGKFSAS
     ELTEIIEAHI ANVVEHYKGD CYAWDVVNEA IDDSGEWRDS VFYQTLGTDY LAISFNAAKK
     ADPEAKLYYN DYNLEQNGKK TDRAVEIVEI LQKAGAPIDG VGFQGHLIVG ETPSRSELVT
     VLERFTSLDV EVAFTELDIR HSSVPASAAE LAKQGDEYVD VVGACLDVKG CVGVTVWGIT
     DKYSWIPDVF EGTGEALLYT DEYEKKPAWT SVSSLLAAAA TATGAPVTST VAPAVTTAAP
     TTMLTRTKPA YTDDCDDYPE TDEPVYPTTS LTNSSAPTTA MGTRTALGPV YTNIDDNDDD
     CESEEAPFPT YVIPTNGTST LPTKAPVYDG DEDCDDDAAP APAPADDDDY EEGDFEPTAA
     AISSAADSAP TRAPVVRTTS AYTYKWNTET RPSYQAPSGT APAGPVGTGN VGPVKHYYQC
     GGKNYNGPTE CEKPFKCVEH NPYYHQCI
//