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Database: UniProt
Entry: A0A3N2Q3G8_9PEZI
LinkDB: A0A3N2Q3G8_9PEZI
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ID   A0A3N2Q3G8_9PEZI        Unreviewed;       449 AA.
AC   A0A3N2Q3G8;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   RecName: Full=Beta-xylanase {ECO:0000256|RuleBase:RU361174};
DE            EC=3.2.1.8 {ECO:0000256|RuleBase:RU361174};
GN   ORFNames=SODALDRAFT_376993 {ECO:0000313|EMBL:ROT41300.1};
OS   Sodiomyces alkalinus F11.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Sodiomyces.
OX   NCBI_TaxID=1314773 {ECO:0000313|EMBL:ROT41300.1, ECO:0000313|Proteomes:UP000272025};
RN   [1] {ECO:0000313|EMBL:ROT41300.1, ECO:0000313|Proteomes:UP000272025}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F11 {ECO:0000313|EMBL:ROT41300.1,
RC   ECO:0000313|Proteomes:UP000272025};
RX   PubMed=30368956; DOI=10.1111/mec.14912;
RA   Grum-Grzhimaylo A.A., Falkoski D.L., van den Heuvel J.,
RA   Valero-Jimenez C.A., Min B., Choi I.G., Lipzen A., Daum C.G., Aanen D.K.,
RA   Tsang A., Henrissat B., Bilanenko E.N., de Vries R.P., van Kan J.A.L.,
RA   Grigoriev I.V., Debets A.J.M.;
RT   "The obligate alkalophilic soda-lake fungus Sodiomyces alkalinus has
RT   shifted to a protein diet.";
RL   Mol. Ecol. 27:4808-4819(2018).
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; ML119052; ROT41300.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3N2Q3G8; -.
DR   STRING; 1314773.A0A3N2Q3G8; -.
DR   OrthoDB; 548101at2759; -.
DR   Proteomes; UP000272025; 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:0000272; P:polysaccharide 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; 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; 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:UP000272025};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..449
FT                   /note="Beta-xylanase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5018082833"
FT   DOMAIN          17..391
FT                   /note="GH10"
FT                   /evidence="ECO:0000259|PROSITE:PS51760"
FT   DOMAIN          414..449
FT                   /note="CBM1"
FT                   /evidence="ECO:0000259|PROSITE:PS51164"
SQ   SEQUENCE   449 AA;  49576 MW;  A93C7614B02501C1 CRC64;
     MYAKVFLAVL LGSQAVNGQL ARLARAAGLE FFGTCVGEGN TNDQQYMSIL RDLDEFDQIV
     PENGQKWDSL QPQRGRFDYS RGDIVANLAR QNGQLLRCHT LTWHSQLPAW VRDGSWNRQT
     LTEVIETHIA NVLRHYQGQC YHWDVVNEAA DDNGNWRNSV FYRVLNSDFL PISFFAARRA
     DPSTKLYVLP SPLSTLPSPL SSPLSSLPFP LSPFLSPFLS PPFFLLTPET TKLSTADNMN
     AKRYYNDYNL EYNDRKTDIT VEMVNIIQRA GAPIDGVGFQ GHLIVGSTPS RQQLATVLRR
     FTALGVEVAY TEVDIRHARM PPNQQALVTQ GNDYANVLGS CLDVQGCIGF TVWGFTDKYS
     WIPSTFPGEG DALLYNSNFG KKPAWTSVSS LLAAAATGIP PPPPPPPPPP PSGSCSGMWG
     QCGGQGWNGP TCCAQGTCQQ QNPWYSQCL
//
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