ID A0A1J9R9K7_9PEZI Unreviewed; 202 AA.
AC A0A1J9R9K7;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Beta-xylanase {ECO:0000256|RuleBase:RU361174};
DE EC=3.2.1.8 {ECO:0000256|RuleBase:RU361174};
DE Flags: Fragment;
GN ORFNames=BKCO1_9300023 {ECO:0000313|EMBL:OJD29115.1};
OS Diplodia corticola.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC Diplodia.
OX NCBI_TaxID=236234 {ECO:0000313|EMBL:OJD29115.1, ECO:0000313|Proteomes:UP000183809};
RN [1] {ECO:0000313|EMBL:OJD29115.1, ECO:0000313|Proteomes:UP000183809}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 112549 {ECO:0000313|EMBL:OJD29115.1,
RC ECO:0000313|Proteomes:UP000183809};
RA Fernandes I., De Jonge R., Van De Peer Y., Devreese B., Alves A.,
RA Esteves A.C.;
RT "Proteomics and genomics reveal pathogen-plant mechanisms compatible with a
RT hemibiotrophic lifestyle of Diplodia corticola.";
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 -!- 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:OJD29115.1}.
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DR EMBL; MNUE01000093; OJD29115.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J9R9K7; -.
DR STRING; 236234.A0A1J9R9K7; -.
DR OrthoDB; 548101at2759; -.
DR Proteomes; UP000183809; Unassembled WGS sequence.
DR GO; GO:0031176; F:endo-1,4-beta-xylanase activity; IEA:UniProtKB-EC.
DR GO; GO:0045493; P:xylan 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, ECO:0000313|EMBL:OJD29115.1};
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:UP000183809};
KW Signal {ECO:0000256|SAM:SignalP};
KW Xylan degradation {ECO:0000313|EMBL:OJD29115.1}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..202
FT /note="Beta-xylanase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012385430"
FT DOMAIN 44..202
FT /note="GH10"
FT /evidence="ECO:0000259|PROSITE:PS51760"
FT NON_TER 202
FT /evidence="ECO:0000313|EMBL:OJD29115.1"
SQ SEQUENCE 202 AA; 22073 MW; 6B1601EB4F16FBCC CRC64;
MHGSTALTLL AAFPATFAIV LPRQAASSIN DAFVAKGKKY FGTCTDQGLL SSGQSAAIIQ
ADFGQVTPEN SMKWDTIEAT QNSFNFAGAD YLVDWATAND KLVRGHTTVW HSQLPTWVSS
ITDKDTLTAV VQNHVSTEIG RYAGKVYAWD VVNEIFNEDG TLRSSVFYNV LGEDFVRIAF
EAARAADPAA KLYINDYKYV VV
//
