ID A0A0G0A0B1_TRIHA Unreviewed; 872 AA.
AC A0A0G0A0B1;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 03-MAY-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=THAR02_02181 {ECO:0000313|EMBL:KKP05717.1};
OS Trichoderma harzianum (Hypocrea lixii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=5544 {ECO:0000313|EMBL:KKP05717.1, ECO:0000313|Proteomes:UP000034112};
RN [1] {ECO:0000313|Proteomes:UP000034112}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T6776 {ECO:0000313|Proteomes:UP000034112};
RX PubMed=26067977; DOI=10.1128/genomeA.00647-15;
RA Baroncelli R., Piaggeschi G., Fiorini L., Bertolini E., Zapparata A.,
RA Pe M.E., Sarrocco S., Vannacci G.;
RT "Draft whole-genome sequence of the biocontrol agent Trichoderma harzianum
RT T6776.";
RL Genome Announc. 3:E0064715-E0064715(2015).
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:KKP05717.1}.
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DR EMBL; JOKZ01000042; KKP05717.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0A0B1; -.
DR OMA; NYVVSDC; -.
DR OrthoDB; 366914at2759; -.
DR UniPathway; UPA00114; -.
DR Proteomes; UP000034112; 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; PF14310; Fn3-like; 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, ECO:0000313|EMBL:KKP05717.1};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Reference proteome {ECO:0000313|Proteomes:UP000034112};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Xylan degradation {ECO:0000256|ARBA:ARBA00022651}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..872
FT /note="xylan 1,4-beta-xylosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002530646"
FT DOMAIN 31..125
FT /note="WSC"
FT /evidence="ECO:0000259|PROSITE:PS51212"
SQ SEQUENCE 872 AA; 92668 MW; 9A376BFA2BE04C7F CRC64;
MAGLRILPWM YSMALFHLAQ SRTCLPAYQA QTTYVGCYHD PNSPRDLAGP FLTVNNLNSP
QYCANLCGAA GYQYAGVEFT IQCFCGHRIE STSVKADESQ CTSPCPADPS KICGGGNMIN
IYQVTNPSSN PPLTPSFPDC TRDPLCSNDV CDTTKSIAQR AAAIVQPMTL DEKVSNVGSS
ASGSGRLGLP AYQWQNEALH GVAGSTGVQF QSPLGANFSA ATSFPMPILL SAAFDDALVQ
SVATAISTEA RAFANYGFAG LDFWTPNINP FRDPRWGRGM ETPGEDAFRI SGYVLALVNG
LQGGIDPDYF RTISTCKHFA AYDIENGRTG NNLTPTQQDM ADYYLPMFET CVRDAKVGSI
MCAYNAVDGV PACADSYLLQ SVLRDGYNFT EDFNYVVSDC DAVENVFDPH HYAANLTQAA
AMSLNAGTDL DCGSSYNVLN ASVQAGMTTE ATLDKSLIRL YSALVKVGWF DQPAEYSSLG
WGNVNTTQTR TLAHDAATGG MTLLKNDGTL PLSPSLQNVA VIGPWANATD QLQGNYAGTA
PVLVNPLTVF QSRWRNVKYA QGTAINSQDT SGFDAALSAA SSSDVIVYLG GIDISVENEG
FDRSAITWPG NQLNLISQLA NLGKPLVIVQ FGGGQIDDSA LLSNSKVNSI LWAGYPGQEG
GNALFDVLTG ASPPAGRLPI TQYPASYINN NNIQDMNLRP SGSIPGRTYA WYTGTPVLPF
GYGLHYTNFS VSLGSTKTAG TDVATIVNNA GSNKDRATFA TIVVNVKNTG GKANLASDYV
GLLFLKSTNA GPAPHPNKQL AAYGRVKKVG VGATSQLTLT VPLGALARAD TNGDRWVYPG
AYTLTLDVNG PVTFNFTLTG SATKISTLPR RS
//