ID A0A1B8AQN0_FUSPO Unreviewed; 327 AA.
AC A0A1B8AQN0;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Beta-xylanase {ECO:0000256|RuleBase:RU361174};
DE EC=3.2.1.8 {ECO:0000256|RuleBase:RU361174};
GN ORFNames=FPOA_09175 {ECO:0000313|EMBL:OBS22852.1};
OS Fusarium poae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=36050 {ECO:0000313|EMBL:OBS22852.1, ECO:0000313|Proteomes:UP000091967};
RN [1] {ECO:0000313|EMBL:OBS22852.1, ECO:0000313|Proteomes:UP000091967}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2516 {ECO:0000313|EMBL:OBS22852.1,
RC ECO:0000313|Proteomes:UP000091967};
RA Vanheule A., Audenaert K., Warris S., Van De Geest H., Schijlen E.,
RA Hofte M., De Saeger S., Haesaert G., Waalwijk C., Van Der Lee T.;
RT "Living apart together: crosstalk between the core and supernumerary
RT genomes in a fungal plant pathogen.";
RL Submitted (JUN-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 -!- 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:OBS22852.1}.
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DR EMBL; LYXU01000003; OBS22852.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1B8AQN0; -.
DR STRING; 36050.A0A1B8AQN0; -.
DR OMA; DYITTAF; -.
DR OrthoDB; 548101at2759; -.
DR Proteomes; UP000091967; 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; 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; 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};
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:UP000091967};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..15
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 16..327
FT /note="Beta-xylanase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013062847"
FT DOMAIN 43..325
FT /note="GH10"
FT /evidence="ECO:0000259|PROSITE:PS51760"
SQ SEQUENCE 327 AA; 35727 MW; 9CDE8FF61859A77B CRC64;
MKFSALLFTA SLVAAMPASV EPRQAQDSIN KLIKNKGKTY YGTITDPNLL QSQQNNAIIK
ADFGQVTPEN SMKWDATEPQ QGKFNFGGAD QVVNFAAQNG LKVRGHALVW HSQLPQWVHN
IKDKNQMKSV IENHIKNVAG HFKGKIYAWD VLNEIFDWDG SLRKDSPFTQ VLGEEFVGIA
FRAARAADPN AKLYINDYSI DDPNAAKLKA GMVANVKKWI AQGIPIDGIG SQTHLDPGAA
NGVQAALQQM ASTGVKEVAI TELDIRSAPA ADYATVTKAC LNVPKCVGIT VWGVSDKDSW
RKEKDGLLFN AQYQPKAAYT AVVNALR
//