ID A0A1J7IP72_9PEZI Unreviewed; 422 AA.
AC A0A1J7IP72;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, 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=CONLIGDRAFT_713959 {ECO:0000313|EMBL:OIW29423.1};
OS Coniochaeta ligniaria NRRL 30616.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Coniochaetales; Coniochaetaceae; Coniochaeta.
OX NCBI_TaxID=1408157 {ECO:0000313|EMBL:OIW29423.1, ECO:0000313|Proteomes:UP000182658};
RN [1] {ECO:0000313|EMBL:OIW29423.1, ECO:0000313|Proteomes:UP000182658}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 30616 {ECO:0000313|EMBL:OIW29423.1,
RC ECO:0000313|Proteomes:UP000182658};
RG DOE Joint Genome Institute;
RA Jimenez D.J., Hector R.E., Riley R., Sun H., Grigoriev I.V.,
RA Van Elsas J.D., Nichols N.N.;
RT "Draft genome sequence of Coniochaeta ligniaria NRRL30616, a
RT lignocellulolytic fungus for bioabatement of inhibitors in plant biomass
RT hydrolysates.";
RL Submitted (OCT-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 -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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; KV875097; OIW29423.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J7IP72; -.
DR STRING; 1408157.A0A1J7IP72; -.
DR InParanoid; A0A1J7IP72; -.
DR OrthoDB; 548101at2759; -.
DR Proteomes; UP000182658; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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: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};
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:UP000182658};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..422
FT /note="Beta-xylanase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012972920"
FT DOMAIN 21..341
FT /note="GH10"
FT /evidence="ECO:0000259|PROSITE:PS51760"
FT REGION 376..399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 422 AA; 44582 MW; 9237247F45DE83AC CRC64;
MRYTYLAIGL LVRAITGVEA QSQTPGLHSL FVASGKLFFG TATDTNLFND IPYMTIANNS
NEFGIRVPEN SQKWQPTEPT ENKFVFANPD QVALTSKANR QLLRCHTLTW HSQLPEFVQT
TNWTRATLTA AIQTHISNVV GHFKGQCYSW DVVNEALNEN GTFRNDVFFQ VLGTDFIPIS
FAAAAAADPA AKLYYNDFNL ETSRAKADGA ARIVQLLQDA KVRIDGLGFQ AHLDVGRTPN
QTALAATLDR FTALGLEVAY TELDIAHAKL PATATALQQQ ARDYVSVVGS CLAVARCVGV
VVWEFTDKYS WIPSTFPGKG DACLFDANFT RKPAYSSVSS FLAAAAATGA AAGTNGSGAG
GSAKVSKTAG AFGLAATTGG TSRPSASGAG GTTEGGDPAV ESALARSGAA GRLFPIVVMS
SP
//