ID   A0A2D3VPC1_9PEZI        Unreviewed;       360 AA.
AC   A0A2D3VPC1;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, 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=RCC_10652 {ECO:0000313|EMBL:CZT24924.1};
OS   Ramularia collo-cygni.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Ramularia.
OX   NCBI_TaxID=112498 {ECO:0000313|EMBL:CZT24924.1, ECO:0000313|Proteomes:UP000225277};
RN   [1] {ECO:0000313|EMBL:CZT24924.1, ECO:0000313|Proteomes:UP000225277}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=URUG2 {ECO:0000313|EMBL:CZT24924.1,
RC   ECO:0000313|Proteomes:UP000225277};
RA   Ploux O.;
RL   Submitted (MAR-2016) 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; FJUY01000023; CZT24924.1; -; Genomic_DNA.
DR   STRING; 112498.A0A2D3VPC1; -.
DR   OrthoDB; 548101at2759; -.
DR   Proteomes; UP000225277; Unassembled WGS sequence.
DR   GO; GO:0031176; F:endo-1,4-beta-xylanase activity; IEA:UniProtKB-EC.
DR   GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
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; PF00331; Glyco_hydro_10; 1.
DR   PRINTS; PR00134; GLHYDRLASE10.
DR   SMART; SM00633; Glyco_10; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 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, ECO:0000313|EMBL:CZT24924.1};
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:UP000225277};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Xylan degradation {ECO:0000313|EMBL:CZT24924.1}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..360
FT                   /note="Beta-xylanase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5013548128"
FT   DOMAIN          30..357
FT                   /note="GH10"
FT                   /evidence="ECO:0000259|PROSITE:PS51760"
SQ   SEQUENCE   360 AA;  40239 MW;  6FA2C4E99CED08C6 CRC64;
     MYIQNLLIAS LALTSHAVVA RPQPNIQERQ QEQTGLWKSL QSRNRQFLGV AVTLRNPPDT
     SETAIISNPL DFNSLTPENA QKWEEIEPSR NNFTFEAADQ HVEFAASRNY FVHCHTLVWH
     SQLPSWXEEG GFDNETLIEV MRNHIEQVAG RYKGRCKQWD VVNEALNEDG TYRSSVFYNT
     IGEAFIPLAF AMTKAVDPNA ALFYNDYNLE YGSAKYEGAL RIVELIQSYG IQIDGVGLQA
     HLTSEGTESS GGGVIPSQET LEGVLTGFTD LCVDVIYTEI DVRFTLPSTE TKVQEQKDAF
     RRIAASCIAV EKCIGMTLWG ASDKYSWIPG VFPGEGDALL WGENYERKAA YDGFLEGIQG
//