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Database: UniProt
Entry: A0A135SPW2_9PEZI
LinkDB: A0A135SPW2_9PEZI
Original site: A0A135SPW2_9PEZI 
ID   A0A135SPW2_9PEZI        Unreviewed;       326 AA.
AC   A0A135SPW2;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, 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=CNYM01_08056 {ECO:0000313|EMBL:KXH37970.1};
OS   Colletotrichum nymphaeae SA-01.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum acutatum species complex.
OX   NCBI_TaxID=1460502 {ECO:0000313|EMBL:KXH37970.1, ECO:0000313|Proteomes:UP000070054};
RN   [1] {ECO:0000313|EMBL:KXH37970.1, ECO:0000313|Proteomes:UP000070054}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SA-01 {ECO:0000313|EMBL:KXH37970.1,
RC   ECO:0000313|Proteomes:UP000070054};
RA   Baroncelli R., Thon M.R.;
RT   "The genome sequence of Colletotrichum nymphaeae SA-01.";
RL   Submitted (FEB-2014) 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:KXH37970.1}.
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DR   EMBL; JEMN01001418; KXH37970.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A135SPW2; -.
DR   Proteomes; UP000070054; 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|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   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..326
FT                   /note="Beta-xylanase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5007802550"
FT   DOMAIN          27..324
FT                   /note="GH10"
FT                   /evidence="ECO:0000259|PROSITE:PS51760"
SQ   SEQUENCE   326 AA;  35554 MW;  7CB5B7299C87B400 CRC64;
     MKFSSSLVCL LAPITVLTAP LEERQASQSI DKLIKAKGKQ YFGTCSDQNR LTAGKNADII
     KANFGQVTPE NSMKWDQIEP NRGQFNWATP DYLVNFAQQN GKLVRGHTLV WHSQLAGWVN
     NVRDKAGLTT VIEDHIKAVV GRYKGKIYHW DVVNEIFNED GSLRSSVFSQ VLGEDFVGIA
     FRAARAADPN AKLYINDYNL DQASYAKTQA MARKVKEWIG KGIPIDGIGS QAHLQANQGG
     NALGALQTLA GSGVKEVAIT ELDIVGASAA DYTAVTKACL QVPQCVGITV WGVRDPDSWR
     AQNNPLLFDA NYNPKAAYNA VVTALQ
//
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