ID   XYN2_CLAPU              Reviewed;         325 AA.
AC   O74717;
DT   09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   25-MAY-2022, entry version 73.
DE   RecName: Full=Endo-1,4-beta-xylanase 2;
DE            Short=Xylanase 2;
DE            EC=3.2.1.8;
DE   AltName: Full=1,4-beta-D-xylan xylanohydrolase 2;
DE   Flags: Precursor;
GN   Name=xyl2;
OS   Claviceps purpurea (Ergot fungus) (Sphacelia segetum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Claviceps.
OX   NCBI_TaxID=5111;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, AND INDUCTION.
RC   STRAIN=T5;
RX   PubMed=18944813; DOI=10.1094/phyto.1998.88.10.1020;
RA   Giesbert S., Lepping H.B., Tenberge K.B., Tudzynski P.;
RT   "The xylanolytic system of Claviceps purpurea: cytological evidence for
RT   secretion of xylanases in infected rye tissue and molecular
RT   characterization of two xylanase genes.";
RL   Phytopathology 88:1020-1030(1998).
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:0000269|PubMed:18944813}.
CC   -!- INDUCTION: Expressed throughout the entire infection process during in
CC       infection of rye tissue. {ECO:0000269|PubMed:18944813}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F) family.
CC       {ECO:0000305}.
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DR   EMBL; Y16970; CAA76571.1; -; Genomic_DNA.
DR   AlphaFoldDB; O74717; -.
DR   SMR; O74717; -.
DR   CAZy; GH10; Glycoside Hydrolase Family 10.
DR   CLAE; XYN10B_CLAPU; -.
DR   VEuPathDB; FungiDB:CPUR_08536; -.
DR   UniPathway; UPA00114; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; IPR044846; GH10.
DR   InterPro; IPR031158; GH10_AS.
DR   InterPro; IPR001000; GH10_dom.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR31490; PTHR31490; 1.
DR   Pfam; PF00331; Glyco_hydro_10; 1.
DR   PRINTS; PR00134; GLHYDRLASE10.
DR   SMART; SM00633; Glyco_10; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS00591; GH10_1; 1.
DR   PROSITE; PS51760; GH10_2; 1.
PE   2: Evidence at transcript level;
KW   Carbohydrate metabolism; Disulfide bond; Glycoprotein; Glycosidase;
KW   Hydrolase; Polysaccharide degradation; Secreted; Signal; Xylan degradation.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..325
FT                   /note="Endo-1,4-beta-xylanase 2"
FT                   /id="PRO_0000429751"
FT   DOMAIN          26..325
FT                   /note="GH10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01096"
FT   ACT_SITE        157
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        262
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10061"
FT   CARBOHYD        28
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        280..286
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   325 AA;  35603 MW;  CB30E344A8A9D52A CRC64;
     MLYTSIFAAA MAASGAMAAP TTSHGASNCT TLDSFFKSHG KLYWGTAADK NTLMKPGVAD
     FIAKEFGQVT PENSMKFDAT EPSRGQFHFD AADYLVDYAE KHDLLIRGHT FLWWSQMPAW
     VKAIKDKDTL IDVIQTHIST VAGRYKGKIY AWDVVNEIFE QDGSFRKTVY YNLLGEDYVR
     IAFEAAHKAD PKAKLYINDF NLDDPNAAKL KAMIKYVTKW RAAGWPVHGI GSQSHLFAGM
     GEKSAAAIKM LGAAADEVAI TELDITGAPQ ADYEAVTKGC IDVKNCVGIT SWGARDTDSW
     LASKSPLLFD GNFKPKAAVK AIMAI