ID A0A094H8Y0_9PEZI Unreviewed; 894 AA.
AC A0A094H8Y0;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 22-FEB-2023, entry version 25.
DE RecName: Full=xylan 1,4-beta-xylosidase {ECO:0000256|ARBA:ARBA00026107};
DE EC=3.2.1.37 {ECO:0000256|ARBA:ARBA00026107};
GN ORFNames=V502_07582 {ECO:0000313|EMBL:KFZ11372.1};
OS Pseudogymnoascus sp. VKM F-4520 (FW-2644).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420915 {ECO:0000313|EMBL:KFZ11372.1, ECO:0000313|Proteomes:UP000029308};
RN [1] {ECO:0000313|EMBL:KFZ11372.1, ECO:0000313|Proteomes:UP000029308}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4520 (FW-2644) {ECO:0000313|Proteomes:UP000029308};
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:KFZ11372.1}.
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DR EMBL; JPKE01002715; KFZ11372.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094H8Y0; -.
DR STRING; 1420915.A0A094H8Y0; -.
DR HOGENOM; CLU_004542_5_3_1; -.
DR OrthoDB; 366914at2759; -.
DR UniPathway; UPA00114; -.
DR Proteomes; UP000029308; 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:UP000029308};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Xylan degradation {ECO:0000256|ARBA:ARBA00022651}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..894
FT /note="xylan 1,4-beta-xylosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001898435"
FT DOMAIN 31..124
FT /note="WSC"
FT /evidence="ECO:0000259|PROSITE:PS51212"
SQ SEQUENCE 894 AA; 97080 MW; E15C1913BBD2F6BA CRC64;
MTTSKHLRAG VTPLLFITAF NLSARAAYNA TSKYLGCYDD PHVSILGDAK LSTISMTPKY
CANWCGGRGF AYGGVEFGTQ CFCGSNPNFS QATKADDSHC SSNCTTEPSS SCGATYVMSL
YEISNPEGNS TNTGFIPACQ AHPLSSHSVC DTSLSIAERV KSLVSSMTME EKVLNVVDAS
AGSARLGLAA YEWWSEGTHG VGSAPGVQFT NPPANFSYAT SFPAPILTAA SFDDALMAEI
AAVIGKEGRA FGNNGFSGYD FWAPNINPFR DPRWGRGQET PGEDVFHVQN YVRTFVRGLQ
GNDPEDKQVI ATCKHYAAYD VETGRHMNNY NPTQQDLADY YLAPFKTCAR DTDVGSIMCS
YNAVDGIPTC ASEYLLEDVL RKHWNFNADY NYVVSDCGAV ADIFNGHKFT DSEEAAAAVA
LNAGTDLDCG SSFVKLNDSI DAGQTTVEAL DRALTRLYSA MFTVGFFDGG KYSNLGFSDV
STPRARSLAY DAAVEGMTLL KNDKLLPLGS SHKFKSVAVI GPFANATDQM QGDYSGKAPY
LHSPLEAFEA QGWKVNYAAG TEINDTSTNG FAAALKAAKK SDLVVYLGGI DGSIENEEKD
RTSLTWPGNQ LDLISQLSKH SKNMIVVQFG GGQVDDSAIL KNKDIDSLIW AGYPSQDGGP
ALVDIITGKR SIAGRLPITQ YPASYANEVS MFDINLRPNK DLSYPGRTYK WYTGKPVIPF
GYGLHYTKFD FKWNATLDKV YDIRELVDSC KKHPLDPIND NTPFATLKAQ VKNVGKENSD
YVGLLFISSQ NAGPAPRPNK SLVSYQRLNN IKTRTEQTLN LPLTLGSLAR ADENGDLVIF
PGDYKIALDI SKSLTFKFTL RGPPVVIDTL PKQKPHYDFT VPVHIQSPST EAQS
//