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Database: UniProt
Entry: W3WWR6_PESFW
LinkDB: W3WWR6_PESFW
Original site: W3WWR6_PESFW 
ID   W3WWR6_PESFW            Unreviewed;       865 AA.
AC   W3WWR6;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   SubName: Full=Xyloglucanase {ECO:0000313|EMBL:ETS78323.1};
GN   ORFNames=PFICI_10385 {ECO:0000313|EMBL:ETS78323.1};
OS   Pestalotiopsis fici (strain W106-1 / CGMCC3.15140).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Xylariomycetidae; Xylariales; Sporocadaceae; Pestalotiopsis.
OX   NCBI_TaxID=1229662 {ECO:0000313|EMBL:ETS78323.1, ECO:0000313|Proteomes:UP000030651};
RN   [1] {ECO:0000313|Proteomes:UP000030651}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=W106-1 / CGMCC3.15140 {ECO:0000313|Proteomes:UP000030651};
RX   PubMed=25623211; DOI=10.1186/s12864-014-1190-9;
RA   Wang X., Zhang X., Liu L., Xiang M., Wang W., Sun X., Che Y., Guo L.,
RA   Liu G., Guo L., Wang C., Yin W.B., Stadler M., Zhang X., Liu X.;
RT   "Genomic and transcriptomic analysis of the endophytic fungus
RT   Pestalotiopsis fici reveals its lifestyle and high potential for synthesis
RT   of natural products.";
RL   BMC Genomics 16:28-28(2015).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 74 family.
CC       {ECO:0000256|ARBA:ARBA00037986}.
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DR   EMBL; KI912115; ETS78323.1; -; Genomic_DNA.
DR   RefSeq; XP_007837157.1; XM_007838966.1.
DR   AlphaFoldDB; W3WWR6; -.
DR   STRING; 1229662.W3WWR6; -.
DR   GeneID; 19275398; -.
DR   KEGG; pfy:PFICI_10385; -.
DR   eggNOG; ENOG502QR03; Eukaryota.
DR   HOGENOM; CLU_004180_1_0_1; -.
DR   InParanoid; W3WWR6; -.
DR   OMA; YSSWWPD; -.
DR   OrthoDB; 1328190at2759; -.
DR   Proteomes; UP000030651; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR   GO; GO:0030248; F:cellulose binding; IEA:InterPro.
DR   GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR   CDD; cd15482; Sialidase_non-viral; 1.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
DR   InterPro; IPR035971; CBD_sf.
DR   InterPro; IPR000254; Cellulose-bd_dom_fun.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   PANTHER; PTHR43739; XYLOGLUCANASE (EUROFUNG); 1.
DR   PANTHER; PTHR43739:SF2; XYLOGLUCANASE (EUROFUNG); 1.
DR   Pfam; PF00734; CBM_1; 1.
DR   SMART; SM00236; fCBD; 1.
DR   SUPFAM; SSF57180; Cellulose-binding domain; 1.
DR   SUPFAM; SSF110296; Oligoxyloglucan reducing end-specific cellobiohydrolase; 2.
DR   PROSITE; PS00562; CBM1_1; 1.
DR   PROSITE; PS51164; CBM1_2; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023326};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00023295};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030651};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..865
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004835160"
FT   DOMAIN          829..865
FT                   /note="CBM1"
FT                   /evidence="ECO:0000259|PROSITE:PS51164"
FT   REGION          741..825
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   865 AA;  90103 MW;  750A39D57A50F294 CRC64;
     MKHFSSLYLL LAAAALEPIR AAFTWQNVKI GGGGGFTPGI VFHPETAGVA YARTDIGGIY
     RLNADDDSWT PITDGIADNA GWHNWGIDAI ALDPQNDQKV YAAVGMYTNS WDPNNGAIIR
     SSDRGETWSF SNLTFKVGGN MPGRGVGERL AVDPANSNIL YFGARSGNGL WKSTDGGVSF
     SKVSSFTAVG TYAADPTDTT GYNNDIEGLT WVTFDSTSGT TSGATSRIFV GTADNTTASV
     YVSEDAGSTW SAVAGQPVQY FPHKGKLQPD EKALYITYAD GTGPYDGTAG AVYRYDITAG
     NWTNITPVSG SDLYFGFGGL GLDLQNPGTL VVASLNSWWP DAQIFRSTDS GATWSKLWEW
     VSYPTMAYYY GLTTSLAPWI KTGFVDLDTK KLGWMIESLE IDPHDSDHWL YGTGLTIYGG
     HDLTNWDTVH NISIQALADG IEEFAVQELA SAAGGSELLA AIYDENGFTF ASASDLDTPP
     QTNWLNPEWA SSTGVDYAGN SPANVVRVGN VAGTQQVALS TDGGASWNID YAADTATYGG
     SVAYSADADT VLWSSSSNGV LRSQYQATFS AVSSLPSGAV VVSDKKTNTY FYAGSSATFY
     VSTDTGATFA AAGTLGSATA IRDIAVNPAT AGDVWVSTDV GIFHSTDYGA TFTQPSTAVT
     NTYQIALGLG SGTTWNVYAF GTGSSGARLY ASGDSGATWT DIQGSSQGFG AIDACRVAGS
     GNTAGQVYVG TNGRGVFWAQ GSIGSGSSTT TTSRASTSTS SKSSTTSILT TSSSSVRTTS
     TSTTTARSST TSTTSTVNTS PTVTSTSTTR VGTTTSTSTS TAASSTSTAV AGQYGQCGGS
     GWTGPTACVS PYTCTYQNPY YSQCV
//
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