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Database: UniProt
Entry: A0A2V1CIP6_9HELO
LinkDB: A0A2V1CIP6_9HELO
Original site: A0A2V1CIP6_9HELO 
ID   A0A2V1CIP6_9HELO        Unreviewed;       386 AA.
AC   A0A2V1CIP6;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   08-NOV-2023, entry version 15.
DE   RecName: Full=Beta-xylanase {ECO:0000256|RuleBase:RU361174};
DE            EC=3.2.1.8 {ECO:0000256|RuleBase:RU361174};
GN   ORFNames=DL98DRAFT_650958 {ECO:0000313|EMBL:PVH85539.1};
OS   Cadophora sp. DSE1049.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Helotiales incertae sedis; Cadophora.
OX   NCBI_TaxID=1485229 {ECO:0000313|EMBL:PVH85539.1, ECO:0000313|Proteomes:UP000244409};
RN   [1] {ECO:0000313|EMBL:PVH85539.1, ECO:0000313|Proteomes:UP000244409}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSE1049 {ECO:0000313|EMBL:PVH85539.1,
RC   ECO:0000313|Proteomes:UP000244409};
RX   PubMed=29679020; DOI=10.1038/s41598-018-24686-4;
RA   Knapp D.G., Nemeth J.B., Barry K., Hainaut M., Henrissat B., Johnson J.,
RA   Kuo A., Lim J.H.P., Lipzen A., Nolan M., Ohm R.A., Tamas L.,
RA   Grigoriev I.V., Spatafora J.W., Nagy L.G., Kovacs G.M.;
RT   "Comparative genomics provides insights into the lifestyle and reveals
RT   functional heterogeneity of dark septate endophytic fungi.";
RL   Sci. Rep. 8:6321-6321(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   -!- 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; KZ804119; PVH85539.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2V1CIP6; -.
DR   STRING; 1485229.A0A2V1CIP6; -.
DR   Proteomes; UP000244409; 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; 1.
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:SF76; ENDO-1,4-BETA-XYLANASE C; 1.
DR   PANTHER; PTHR31490; GLYCOSYL HYDROLASE; 1.
DR   Pfam; PF00734; CBM_1; 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   SUPFAM; SSF57180; Cellulose-binding domain; 1.
DR   PROSITE; PS51760; GH10_2; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {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|RuleBase:RU361174};
KW   Reference proteome {ECO:0000313|Proteomes:UP000244409};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..386
FT                   /note="Beta-xylanase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5015961564"
FT   DOMAIN          105..385
FT                   /note="GH10"
FT                   /evidence="ECO:0000259|PROSITE:PS51760"
FT   REGION          60..87
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   386 AA;  40384 MW;  B88904C8B9BC8691 CRC64;
     MLNFKNLAAV AVLLSNIEIA QAQGGAWTQC GGVNWNGATT CVSGYVCKYS KATTLITTTS
     TSAASTSTPT TSPGTGPGDA GSSTGGANSI DVKFRARGKK YFGVATDQGR LTTGSNAAII
     QADFGQVTPE NSMKWDAIEN TQNSFTFSQA DYLVNWAVTN KKLIRGHTLC WHSQLPSWVS
     NIANAATLTK VLQDHIAAEA GRYKGKIYAW DVVNEVFNED GSMRPSVFFN VLGETFINIA
     FAAAKQADPT AKLYINDYNL DSATYAKVTT GMVNHVKKWI AAGVPIDGIG SQGHLQAGQG
     SAAAGALAAL AASGVAEVAV TELDIVGAAS SDYVAVTNAC LNLAKCVGIT VWGVRDPDSW
     RASNNPLLFD ASYAPKAAYN AILAAL
//
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