ID A0A1Y1V0I3_9FUNG Unreviewed; 497 AA.
AC A0A1Y1V0I3;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Beta-xylanase {ECO:0000256|RuleBase:RU361174};
DE EC=3.2.1.8 {ECO:0000256|RuleBase:RU361174};
GN ORFNames=BCR36DRAFT_585972 {ECO:0000313|EMBL:ORX44856.1},
GN BCR36DRAFT_586000 {ECO:0000313|EMBL:ORX44627.1};
OS Piromyces finnis.
OC Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC Chytridiomycota incertae sedis; Neocallimastigomycetes; Neocallimastigales;
OC Neocallimastigaceae; Piromyces.
OX NCBI_TaxID=1754191 {ECO:0000313|EMBL:ORX44627.1, ECO:0000313|Proteomes:UP000193719};
RN [1] {ECO:0000313|EMBL:ORX44627.1, ECO:0000313|Proteomes:UP000193719}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Finn {ECO:0000313|EMBL:ORX44627.1}, and finn
RC {ECO:0000313|Proteomes:UP000193719};
RG DOE Joint Genome Institute;
RA Haitjema C.H., Gilmore S.P., Henske J.K., Solomon K.V., De Groot R.,
RA Kuo A., Mondo S.J., Salamov A.A., Labutti K., Zhao Z., Chiniquy J.,
RA Barry K., Brewer H.M., Purvine S.O., Wright A.T., Boxma B., Van Alen T.,
RA Hackstein J.H., Baker S.E., Grigoriev I.V., O'Malley M.A.;
RT "Genomes of anaerobic fungi encode conserved fungal cellulosomes for
RT biomass hydrolysis.";
RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ORX44627.1, ECO:0000313|Proteomes:UP000193719}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=finn {ECO:0000313|Proteomes:UP000193719}, and Finn
RC {ECO:0000313|EMBL:ORX44627.1};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (AUG-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:ORX44627.1}.
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DR EMBL; MCFH01000044; ORX44627.1; -; Genomic_DNA.
DR EMBL; MCFH01000043; ORX44856.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y1V0I3; -.
DR EnsemblFungi; ORX44627; ORX44627; BCR36DRAFT_586000.
DR EnsemblFungi; ORX44856; ORX44856; BCR36DRAFT_585972.
DR OrthoDB; 1327901at2759; -.
DR Proteomes; UP000193719; 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; 3.90.1220.10; Cellulose docking domain, dockering; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR002883; CBM10/Dockerin_dom.
DR InterPro; IPR009034; Dockerin_dom_fun_sf.
DR InterPro; IPR044846; GH10.
DR InterPro; IPR001000; GH10_dom.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR31490:SF88; BETA-XYLANASE; 1.
DR PANTHER; PTHR31490; GLYCOSYL HYDROLASE; 1.
DR Pfam; PF02013; CBM_10; 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; SSF64571; Cellulose docking domain, dockering; 1.
DR PROSITE; PS51763; CBM10; 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:UP000193719};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..497
FT /note="Beta-xylanase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011907604"
FT DOMAIN 24..61
FT /note="CBM10"
FT /evidence="ECO:0000259|PROSITE:PS51763"
FT DOMAIN 122..457
FT /note="GH10"
FT /evidence="ECO:0000259|PROSITE:PS51760"
FT REGION 466..497
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 468..497
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 497 AA; 56808 MW; B9024ACE283ECCA4 CRC64;
MKFNSILLLS SLSAVALARP HDNACWSEKF NIPCCQTTKE VVRTTYDGIW GMENGEWCGL
GTESTRPKDD IPPSPPALLD LDSVVDPAAD CDISNVITGD SLAQEAPFRF GVGFNGAAVS
TSTTSSKVMR ELVKYQFNSF SYSNLMKPLF VLDQAGCQKN FKNGSNEIAL NFTPFVDGLD
YAQKNGLHIR GHVLVWHKQF PDWFFREEFD DAKEYVSEEV IYERLENYIK QYLGFVNYNY
PGVVDVWDVV NEAVEVLEGK FDNSTGWYTR TITYEGDRNI WYDFVGPDYV VKTFRIARKY
ALPNVKLVYN DYDTFAQQPH DKTQAIIDLM HILQKEDLVD ALGMQSYIQP IDPPFEENVA
NYDKALQRFA AEGFEIQITE FTIYATNGED WLETQVYQYR KMMETIMKNY KNGANITSVT
VFGLQDGYRF YESDSTKTRL FDHELQKKPT YEAIMEVLKA YNAEVNDESN IESDEEISVD
ADVDVAEDSA DDDSDEE
//
