ID A0A166URW2_9PEZI Unreviewed; 802 AA.
AC A0A166URW2;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 22-FEB-2023, entry version 17.
DE RecName: Full=xylan 1,4-beta-xylosidase {ECO:0000256|ARBA:ARBA00026107};
DE EC=3.2.1.37 {ECO:0000256|ARBA:ARBA00026107};
GN ORFNames=CT0861_04898 {ECO:0000313|EMBL:KZL73729.1};
OS Colletotrichum tofieldiae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum spaethianum species complex.
OX NCBI_TaxID=708197 {ECO:0000313|EMBL:KZL73729.1, ECO:0000313|Proteomes:UP000076552};
RN [1] {ECO:0000313|EMBL:KZL73729.1, ECO:0000313|Proteomes:UP000076552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0861 {ECO:0000313|EMBL:KZL73729.1,
RC ECO:0000313|Proteomes:UP000076552};
RA Hacquard S., Kracher B., Hiruma K., Weinman A., Muench P., Garrido Oter R.,
RA Ver Loren van Themaat E., Dallerey J.-F., Damm U., Henrissat B.,
RA Lespinet O., Thon M., Kemen E., McHardy A.C., Schulze-Lefert P.,
RA O'Connell R.J.;
RT "Survival trade-offs in plant roots during colonization by closely related
RT pathogenic and mutualistic fungi.";
RL Submitted (JUN-2015) 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:KZL73729.1}.
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DR EMBL; LFIV01000041; KZL73729.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A166URW2; -.
DR STRING; 708197.A0A166URW2; -.
DR OrthoDB; 366914at2759; -.
DR UniPathway; UPA00114; -.
DR Proteomes; UP000076552; 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:KZL73729.1};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Reference proteome {ECO:0000313|Proteomes:UP000076552};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Xylan degradation {ECO:0000256|ARBA:ARBA00022651}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..802
FT /note="xylan 1,4-beta-xylosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007880772"
FT DOMAIN 707..777
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 802 AA; 87391 MW; 74C8FC1BFCA8E238 CRC64;
MLTFIKCSTL LFCWAVLVAG SGIDNLQKPL TSRTCLPAVK QSTDKSAIDN FPDCSRDPLC
SNYVCDETLS PKKRAAALVA ELTIWEKLDN LVNEAPGVPR LGIPPYEWWS EGLHGVASSP
GTKFAGSGNF SYATSFPQPI ILGSAFDDEL VRAVGEVVSK EARAFSNYGR SGIDLYSPNI
NAFKDPRWGR GQETPGEDPF HLQRYVAAML TGLEGDDSPK KLIATCKHYA ANDFENYNGV
DRAGFDANIT TQDLSEYYLP PFKTCAVEKS VGSFMCSYNG INGTPLCANS YLLEDILRQH
WGWNGDGQYV STDCDCIALM VSHHHYAPDL GHAAAWAMKA GTDLECNAFP GSTALQFAWN
QSLISEKEVD KSLTRLYTAL ISVGQFDSAR EQPLRSLLWD DVNTKEAQNL AYQSAIKGAV
LLKNDGILPL SVGAARKYAL IGPWVNATTQ MQGNYFGPAP YLISPYQAAK DLELGFTYTL
GSKINSTDDS FQQALESAHA ADIIVFAGGV DNTLEAETLD RKTLAWPESQ IDLLRAVAAL
GKPVIVLQFG GGQVDDTELL ANKSINAILW GGYPGQSGGK AILDLLFGRA APAGRLPVTQ
YPASYNKAVP STDMNLRPGP GNSGLGRTYM WYNGETAVPY GFGLHYTTFD VKLKTTRESA
LIKTDEVSSR LNDDDTSGTP SWQQILTKPV LSVTITVSNT GTMASDYVAL LFLRSDAGPT
PRPIKTLAGY SRFRNIQPGK QVEGEVFITV ERLVRVDELG NRVLHPGYYE LFVDLDEKST
QAFEVGGSSV VVEEFPQPKD RN
//
