ID A0A094FTB2_9PEZI Unreviewed; 879 AA.
AC A0A094FTB2;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 22-FEB-2023, entry version 24.
DE RecName: Full=xylan 1,4-beta-xylosidase {ECO:0000256|ARBA:ARBA00026107};
DE EC=3.2.1.37 {ECO:0000256|ARBA:ARBA00026107};
GN ORFNames=V497_02223 {ECO:0000313|EMBL:KFY62817.1};
OS Pseudogymnoascus sp. VKM F-4516 (FW-969).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420910 {ECO:0000313|EMBL:KFY62817.1, ECO:0000313|Proteomes:UP000029268};
RN [1] {ECO:0000313|EMBL:KFY62817.1, ECO:0000313|Proteomes:UP000029268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4516 (FW-969) {ECO:0000313|Proteomes:UP000029268};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of (1->4)-beta-D-xylans, to remove successive D-
CC xylose residues from the non-reducing termini.; EC=3.2.1.37;
CC Evidence={ECO:0000256|ARBA:ARBA00024574};
CC -!- PATHWAY: Glycan degradation; xylan degradation.
CC {ECO:0000256|ARBA:ARBA00004851}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family.
CC {ECO:0000256|ARBA:ARBA00005336}.
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:KFY62817.1}.
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DR EMBL; JPJZ01000582; KFY62817.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094FTB2; -.
DR STRING; 1420910.A0A094FTB2; -.
DR HOGENOM; CLU_004542_5_3_1; -.
DR OrthoDB; 366914at2759; -.
DR UniPathway; UPA00114; -.
DR Proteomes; UP000029268; Unassembled WGS sequence.
DR GO; GO:0009044; F:xylan 1,4-beta-xylosidase activity; IEA:InterPro.
DR GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.50.1700; Glycoside hydrolase family 3 C-terminal domain; 1.
DR Gene3D; 3.20.20.300; Glycoside hydrolase, family 3, N-terminal domain; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR044993; BXL.
DR InterPro; IPR026891; Fn3-like.
DR InterPro; IPR002772; Glyco_hydro_3_C.
DR InterPro; IPR036881; Glyco_hydro_3_C_sf.
DR InterPro; IPR001764; Glyco_hydro_3_N.
DR InterPro; IPR036962; Glyco_hydro_3_N_sf.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR002889; WSC_carb-bd.
DR PANTHER; PTHR42721:SF3; BETA-D-XYLOSIDASE 5-RELATED; 1.
DR PANTHER; PTHR42721; SUGAR HYDROLASE-RELATED; 1.
DR Pfam; PF00933; Glyco_hydro_3; 1.
DR Pfam; PF01915; Glyco_hydro_3_C; 1.
DR Pfam; PF01822; WSC; 1.
DR SMART; SM01217; Fn3_like; 1.
DR SMART; SM00321; WSC; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1.
DR PROSITE; PS51212; WSC; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Reference proteome {ECO:0000313|Proteomes:UP000029268};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Xylan degradation {ECO:0000256|ARBA:ARBA00022651}.
FT DOMAIN 16..109
FT /note="WSC"
FT /evidence="ECO:0000259|PROSITE:PS51212"
SQ SEQUENCE 879 AA; 95939 MW; F24D90229AD1DF9E CRC64;
MCTPSDTGPT TAYNVSSRYL GCYQDPHVTI LSDAKLSTII MTPQYCTTWC GKNGFAYGGI
EFGTQCFCGS EPDFSQASKT DDSSCSSKCA TDPSSSCGGT YILSLYEILN PQGNTTNEGF
LPACQTQPLC SHKVCDTSMS TAERVKSLVS SMTLQEKILN VVDASAGSTR LGLPPYEWWN
EATHGVGSAP GVQFTRNSSN FGYATSFPAP ILTAASFDDA LIKEIAGVIG KEGRAFGNNG
FSGYDFWAPN INPFRDPRWG RGQETPGEDV FHVQSYIRSF VRGLQGDDPE DKQVIATCKH
YAAYDLETGR YGNNYNPTQQ DLADYYLAPF KTCARDTAVG SIMCSYNSVN GIPTCASEYL
LEEVLRKHWN FNADYNYVVS DCGAVADIWQ FHNFTDTEEA AASVALNAGT DLDCGSSYVK
LNESINAGQT TVHALDRALT RLYSAMFTVG FFDGGKYNHL GFSDVSTPRA QTLAYEAAVE
GMTLLKNDQL LPLRSLHKYK SVAVIGPFAN ATTQMQGDYS GTAPYLHSPL EAFGTHTWKV
NYAMGTDINN PSTAGFSSAL EAARKSDLVI YLGGIDNSME NEQNDRTSLA WPANQLDLIS
QLTKLSKPTI VVQFGGGQLD DSTLLKNKGI NALIWAGYPS QDGGPALFDI LTGKRSIAGR
LPVTQYPASY ADEVSIFDIN LRPDESLSFP GRTYKWYTGK PVLPFGYGLH YTKFDFKWKA
TLNHEYNIQS LVDSCKKHPH DTINDNTPFA TVKASVRNIG KENSDYIGLL FLSSQNAGPA
PRPNKSLVSY LRLNNIKTKS EQILHLPLTL GSLARADKNG NLVIFPGIYK IALDISEALT
FTFSLHGAPV VIDTLPTPKP HYEFTVPVHI QPASTEAHS
//
