ID   A0A139GUF1_9PEZI        Unreviewed;       372 AA.
AC   A0A139GUF1;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Beta-xylanase {ECO:0000256|RuleBase:RU361174};
DE            EC=3.2.1.8 {ECO:0000256|RuleBase:RU361174};
GN   ORFNames=AC578_9466 {ECO:0000313|EMBL:KXS93801.1};
OS   Pseudocercospora eumusae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX   NCBI_TaxID=321146 {ECO:0000313|EMBL:KXS93801.1, ECO:0000313|Proteomes:UP000070133};
RN   [1] {ECO:0000313|EMBL:KXS93801.1, ECO:0000313|Proteomes:UP000070133}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 114824 {ECO:0000313|EMBL:KXS93801.1,
RC   ECO:0000313|Proteomes:UP000070133};
RA   Chang T.-C., Salvucci A., Crous P.W., Stergiopoulos I.;
RT   "Comparative genomics of the Sigatoka disease complex on banana suggests a
RT   link between parallel evolutionary changes in Pseudocercospora fijiensis
RT   and Pseudocercospora eumusae and increased virulence on the banana host.";
RL   Submitted (JUL-2015) 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}.
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:KXS93801.1}.
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DR   EMBL; LFZN01000384; KXS93801.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A139GUF1; -.
DR   STRING; 321146.A0A139GUF1; -.
DR   OrthoDB; 548101at2759; -.
DR   Proteomes; UP000070133; Unassembled WGS sequence.
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; 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; PF00331; Glyco_hydro_10; 1.
DR   PRINTS; PR00134; GLHYDRLASE10.
DR   SMART; SM00633; Glyco_10; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 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:UP000070133};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..372
FT                   /note="Beta-xylanase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5007806176"
FT   DOMAIN          33..350
FT                   /note="GH10"
FT                   /evidence="ECO:0000259|PROSITE:PS51760"
FT   ACT_SITE        281
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10061"
SQ   SEQUENCE   372 AA;  42240 MW;  C82A705BA8CC031E CRC64;
     MYLQSTLLLG ALATSSLALP EHKIPSHGLN LVAKAVGKLW FGTAADIPGK EQQDQYYMRK
     LLNYRNFGQV TPGNSMKYMF TEPEKGVFNY SQADEFLKTV NPYGPKRKIR CHNLIWHAEI
     PDWLTKPSTP WTNETLSAVL VNHVQNLVEH FGNACHSWDV VNEGLSDSSD DPAYPYRSLY
     HPWYQYIGPE YIPMAFKAAA DTIKKHNLDV KLYYNDYGIE KAGNKSTAAE NLVKQLQSRG
     IQIDGVGLES HFTVGDTPSQ SEQEENMNCF TNLGIDVAVT ELDVRIKLPT NATNLKQQAK
     DYYNTVAACT NVKRCIGITV WDFDDTYSWI PDFFKGEGSA DIWYQREARI FGIRGKMLRI
     HRCIGRMGFI LL
//