ID A0A0W0FRG7_9AGAR Unreviewed; 766 AA.
AC A0A0W0FRG7;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=xylan 1,4-beta-xylosidase {ECO:0000256|ARBA:ARBA00026107};
DE EC=3.2.1.37 {ECO:0000256|ARBA:ARBA00026107};
GN ORFNames=WG66_8481 {ECO:0000313|EMBL:KTB38972.1};
OS Moniliophthora roreri.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Marasmiaceae; Moniliophthora.
OX NCBI_TaxID=221103 {ECO:0000313|EMBL:KTB38972.1, ECO:0000313|Proteomes:UP000054988};
RN [1] {ECO:0000313|EMBL:KTB38972.1, ECO:0000313|Proteomes:UP000054988}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 2952 {ECO:0000313|EMBL:KTB38972.1,
RC ECO:0000313|Proteomes:UP000054988};
RA Aime M.C., Diaz-Valderrama J.R., Kijpornyongpan T., Phillips-Mora W.;
RT "Draft genome sequence of Moniliophthora roreri, the causal agent of frosty
RT pod rot of cacao.";
RL Submitted (DEC-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:KTB38972.1}.
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DR EMBL; LATX01001716; KTB38972.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0W0FRG7; -.
DR eggNOG; ENOG502QQ55; Eukaryota.
DR UniPathway; UPA00114; -.
DR Proteomes; UP000054988; 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; PF00933; Glyco_hydro_3; 1.
DR Pfam; PF01915; Glyco_hydro_3_C; 1.
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:ARBA00022651};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:KTB38972.1};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00022651};
KW Reference proteome {ECO:0000313|Proteomes:UP000054988};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Xylan degradation {ECO:0000256|ARBA:ARBA00022651}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..766
FT /note="xylan 1,4-beta-xylosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006902052"
FT DOMAIN 674..744
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 766 AA; 83636 MW; BA911083257BC400 CRC64;
MTPVLPKLLG LVIASHLVLV CQGAFPNCED GPLATNLVCN PDVPSLDRAR ALVAEFTVPE
VIQNTGNESP GVSRLGLPAY NWWNEALHGF GGSPGSNFSE TGEFSYSTSF PAPILMAAAF
DDALIHDVST IISTEARAFH NANRSGIDFW APNINPFRDP RWGRGQETPG EDPFRIAQYV
YQYMTGMQGG VNPKPYLKIV ADCKHWAAYD IENWEGNDRT EFNAVVSTQD FAEYYSPPFQ
SCVRDAKAAS VMCSYNEVNG VPSCANSYLL QTLVRDFWEL GDDQWVVGDC AAVEAIATGH
QYTNDIVNAS ALALRAGVDI DCGITYPTNL GKALNQSLIS EDNLRKALVR QYHSLIRTGY
FDPPERQPYR QLKWSDVNTK QTQELAHRAA VEGMVLLKND GILPLKRSIR KIALVGPFAN
ATQQMQSNYA QPAPFIISPL QAFREAAFDV AFANGTAINT TDTSGFAAAI EAARKSDVII
FAGGMDLSVE DEFRDRTEIS WPGNQLDLIK ELAALKKPFI VLSMGGGQVD CSWLKGDPRV
NGIVWGGLPS QSGGPALLDI ITGKKAPAGR LPITQYPASY VDEVPMTDMS LRPKAGSSPG
RTYKWYTGKP VYEFGFGLHY TTFQFKWVDN AKGSYDIQEL VDSAKSSGVP YIDVATFDTF
KVSVTNTGKT TSDFAALLFS RTKAGPSPAP LKELVSYTKM KDIAPGQSAV ALLKVTLGSI
ARTDENGNKV LYPGKYELLF DYNGAIRKTI TLTGKETQIL AWPQAS
//
