UniProt: A0A1Y2DED0

Database: UniProt
Entry: A0A1Y2DED0_9FUNG

LinkDB:  A0A1Y2DED0_9FUNG 
Original site:  A0A1Y2DED0_9FUNG

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Ontology (2)   
   GO (2)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (10)   
   InterPro (5)   
   Pfam (2)   
   PROSITE (2)   
   SMART (1)   
All databases (14)   

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ID   A0A1Y2DED0_9FUNG        Unreviewed;       521 AA.
AC   A0A1Y2DED0;
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=LY90DRAFT_669095 {ECO:0000313|EMBL:ORY57599.1};
OS   Neocallimastix californiae.
OC   Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC   Chytridiomycota incertae sedis; Neocallimastigomycetes; Neocallimastigales;
OC   Neocallimastigaceae; Neocallimastix.
OX   NCBI_TaxID=1754190 {ECO:0000313|EMBL:ORY57599.1, ECO:0000313|Proteomes:UP000193920};
RN   [1] {ECO:0000313|EMBL:ORY57599.1, ECO:0000313|Proteomes:UP000193920}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G1 {ECO:0000313|EMBL:ORY57599.1,
RC   ECO:0000313|Proteomes:UP000193920};
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   "A Parts List for Fungal Cellulosomes Revealed by Comparative Genomics.";
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:ORY57599.1}.
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DR   EMBL; MCOG01000069; ORY57599.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y2DED0; -.
DR   OrthoDB; 548101at2759; -.
DR   Proteomes; UP000193920; 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   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:UP000193920};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..521
FT                   /note="Beta-xylanase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012801998"
FT   DOMAIN          32..71
FT                   /note="CBM10"
FT                   /evidence="ECO:0000259|PROSITE:PS51763"
FT   DOMAIN          132..462
FT                   /note="GH10"
FT                   /evidence="ECO:0000259|PROSITE:PS51760"
FT   REGION          474..521
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        476..492
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        503..521
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   521 AA;  59513 MW;  03D812541C9A7DC0 CRC64;
     MKIHRFITLL GVIGSLSIAV SAKNNNKSNQ GKCWSKGLFK IPCCKKTDVV VRTTYDGEWG
     QEDNGKWCSL SKKSTRPVKD VPPEPLHSSI IDSIIDPAKD CDITSLVEGD SLAKEAPFRF
     GVGLTGTNLQ VSTTVSEKMR DIIKHQFNSM TYTNLMKPLY ILDKEGSIQN IKNGIQDPKL
     NFTSIVDGLE FAYKNGIHIR GHVLIWHTQT PDWFFNEGYT DDGKKVSPEV MESRLDSYIK
     QYLSFVQFNY PGVVDVWDVV NEAIEITDGQ YDANTGWYTR TMLNNTPNPY YDMFGPDYVI
     KAFRIARKYA LPNVKLVYND FNTFQVWPHN KTQAIMDLAG ILQKEDLIDG IGLQSYLGVT
     WPSLDEYFRG VERLATTGLE LQITELTITA PDGDNWLEAQ AEQYRDFFER LMKHVEEGYN
     IGSVTVFGLQ DGYLFYASDS TKTRLLDHDL QKKPNFEAIM SILKSYKKNA YTEDINTEDT
     ETDTETETDT ETETESENKK IKKEKTKKNK KEKTKKNKNK N
//

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