ID A0A135T4G9_9PEZI Unreviewed; 804 AA.
AC A0A135T4G9;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 03-MAY-2023, entry version 21.
DE RecName: Full=xylan 1,4-beta-xylosidase {ECO:0000256|ARBA:ARBA00026107};
DE EC=3.2.1.37 {ECO:0000256|ARBA:ARBA00026107};
GN ORFNames=CSIM01_01759 {ECO:0000313|EMBL:KXH43005.1};
OS Colletotrichum simmondsii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum acutatum species complex.
OX NCBI_TaxID=703756 {ECO:0000313|EMBL:KXH43005.1, ECO:0000313|Proteomes:UP000070328};
RN [1] {ECO:0000313|EMBL:KXH43005.1, ECO:0000313|Proteomes:UP000070328}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS122122 {ECO:0000313|EMBL:KXH43005.1,
RC ECO:0000313|Proteomes:UP000070328};
RA Baroncelli R., Thon M.R.;
RT "The genome sequence of Colletotrichum simmondsii CBS122122.";
RL Submitted (FEB-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:KXH43005.1}.
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DR EMBL; JFBX01000289; KXH43005.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A135T4G9; -.
DR OrthoDB; 366914at2759; -.
DR UniPathway; UPA00114; -.
DR Proteomes; UP000070328; 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 PANTHER; PTHR42721:SF3; BETA-D-XYLOSIDASE 5-RELATED; 1.
DR PANTHER; PTHR42721; SUGAR HYDROLASE-RELATED; 1.
DR Pfam; PF14310; Fn3-like; 1.
DR Pfam; PF00933; Glyco_hydro_3; 1.
DR Pfam; PF01915; Glyco_hydro_3_C; 1.
DR PRINTS; PR00133; GLHYDRLASE3.
DR SMART; SM01217; Fn3_like; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 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, ECO:0000313|EMBL:KXH43005.1};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Xylan degradation {ECO:0000256|ARBA:ARBA00022651}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..804
FT /note="xylan 1,4-beta-xylosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007803228"
FT DOMAIN 711..781
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 804 AA; 87430 MW; E9D597CCEE67B25B CRC64;
MYKLIRNHLL LLPGTILAAG SGSGSSDQQK PLTSRTCLAP LPASDPRAGT SNFPDCTRDP
LCSVDVCDEF LSANQRAKAL VAELTIWEKL DNLVNEAPGV PRLGIPPYEW WSEGLHGVAS
SPGTKFAESG NFSYATSFPQ PIVIGSAFDD ELVEAIGAVV SKEARAFSND DRSGLDLYSP
NINAFKDPRW GRGQETPGED PFHLQNYVAA MLTGLEGSSD PANKNLIATC KHYAANDFEH
YNGVDRAGFN AIITTQDLSE YYLPPFKTCA VEKNVGSFMC SYNGINGTPL CANAYLLEDI
LRGHWRWNGE GQYVSTDCDC VALMVSYHHY APDLGHAAAW SMKAGTDLEC NAFPGSEALQ
LAWNQSLISE EEVDHSLTRM YTALISVGQF DSAQEQPLRS LLWRDVDTEE ARELAYRAAV
EGSVLLKNDG ILPLSAASGK KFALVGPWAK ATTQMQGNYY GPAPYLVSPY QAAQDLGLDF
TYTLGSKINA SDDSLSDALK LAKEADVVIF AGGVDNTLEA ETLDRKTLAW PKPQLELLRA
LADIGKPVIV LQFGGGQVDD TELLASDAIS AILWGGYPGQ SGGRAIFDLL FGREAPSGRL
SVTQYPAIYN EAVPSTDMNL RPVPGNSGLG RTYMWYLGET PVPYGFGLHY TTFDVKLKAL
QEPAVTITKQ LTLSEDSEDT SRVPSWQKTL ERPMLTVAVT VTNTGKVASD YVALLFLTSD
VGPEPRPLKT LAGYTRFRSI QPGQAAVKEV VITVERLVRV DELGNRVLHP GSYEVFVDLE
KRAVHKFHVG GPAVVVEKFP QQKA
//
