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Database: UniProt
Entry: A0A0G0A0B1_TRIHA
LinkDB: A0A0G0A0B1_TRIHA
Original site: A0A0G0A0B1_TRIHA 
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
//
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