ID   A0A0K6FN87_9AGAM        Unreviewed;       720 AA.
AC   A0A0K6FN87;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Beta-xylanase {ECO:0000256|RuleBase:RU361174};
DE            EC=3.2.1.8 {ECO:0000256|RuleBase:RU361174};
GN   ORFNames=RSOLAG22IIIB_03086 {ECO:0000313|EMBL:CUA67439.1};
OS   Rhizoctonia solani.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Cantharellales; Ceratobasidiaceae; Rhizoctonia.
OX   NCBI_TaxID=456999 {ECO:0000313|EMBL:CUA67439.1, ECO:0000313|Proteomes:UP000044841};
RN   [1] {ECO:0000313|EMBL:CUA67439.1, ECO:0000313|Proteomes:UP000044841}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BBA 69670 {ECO:0000313|EMBL:CUA67439.1};
RA   Noorani M.;
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}.
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DR   EMBL; CYGV01000113; CUA67439.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0K6FN87; -.
DR   Proteomes; UP000044841; 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:0045493; P:xylan catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.80; Glycosidases; 2.
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; 2.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 2.
DR   SUPFAM; SSF57180; Cellulose-binding domain; 1.
DR   PROSITE; PS00562; CBM1_1; 1.
DR   PROSITE; PS51164; CBM1_2; 1.
DR   PROSITE; PS00591; GH10_1; 2.
DR   PROSITE; PS51760; GH10_2; 2.
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:UP000044841};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Xylan degradation {ECO:0000313|EMBL:CUA67439.1}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..720
FT                   /note="Beta-xylanase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5005502139"
FT   DOMAIN          51..325
FT                   /note="GH10"
FT                   /evidence="ECO:0000259|PROSITE:PS51760"
FT   DOMAIN          331..367
FT                   /note="CBM1"
FT                   /evidence="ECO:0000259|PROSITE:PS51164"
FT   DOMAIN          418..708
FT                   /note="GH10"
FT                   /evidence="ECO:0000259|PROSITE:PS51760"
FT   ACT_SITE        255
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10061"
FT   ACT_SITE        630
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10061"
SQ   SEQUENCE   720 AA;  78173 MW;  B93B7C095CA39638 CRC64;
     MVQSPGAILA CTLLAIVPTL VSAQTGLRGL HNLAKAKGRY FGTATDQLWT STDSAYLALT
     GNSSEFGVNT PGNQQKWDAT EGSQNVFSFT SADYQVAWGK NHSQALRGHT LVWHSQLPSW
     VSSGGFDNAT LISVMENHIS NVAGQDVVNE AFEENGTYRN SVFYNTIGPA YIPIALCAAR
     AADPSAKLYL NDYNTDWTGS KSDAYYDLAK SLLAQGVPLD GIGFQGHLTV NGFERTVQEN
     FQRFADLGLE IAITELDIRM TLPATDALLQ AQAENYAYII KSCFAIPKCV GITTWDTSDD
     LHTLLPIFDY MIFSNKKLAL SVLAAAAIQV QGVAVWGQCG GLTWTGGTTC DSGSYCQYQN
     DYYSQCVPGT STATGATSAS TTTSSAATPT ATGLRGLHAL AKAKGRYFGT ATDQLWTNTD
     STYLAITGNP NEFGVNTPGN QLKWDATEKS RNVFTYTNGD YQVSWAKNHS QVSRAHTLVW
     HSQLPSWVSS GGFDNATLIS IMQNHIANVA GHYKGKVYAW DVVNEMFNDD GTWRTSVFYT
     TIGPYYIDIA LRAARAADPT AKLYLNDYNT DWTGSKSDAM YNLAKDLLAR GVPLDGIGFQ
     AHLIVNSFSR TFQANYQRFA DLGLDVAITE LDIRYTLPQT DALVTAQAEN YKYVVNACLA
     VSHCVGITVW DTSDDYSWIP SVFPGEGNAL LFDSNKQPKP AYYSVADALA AATVQGAWSP
//