ID A0A164W2P7_9AGAM Unreviewed; 872 AA.
AC A0A164W2P7;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Oligoxyloglucan reducing end-specific cellobiohydrolase {ECO:0000313|EMBL:KZS94691.1};
GN ORFNames=SISNIDRAFT_484231 {ECO:0000313|EMBL:KZS94691.1};
OS Sistotremastrum niveocremeum HHB9708.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Trechisporales; Trechisporales incertae sedis; Sistotremastrum.
OX NCBI_TaxID=1314777 {ECO:0000313|EMBL:KZS94691.1, ECO:0000313|Proteomes:UP000076722};
RN [1] {ECO:0000313|EMBL:KZS94691.1, ECO:0000313|Proteomes:UP000076722}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB9708 {ECO:0000313|EMBL:KZS94691.1,
RC ECO:0000313|Proteomes:UP000076722};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 74 family.
CC {ECO:0000256|ARBA:ARBA00037986}.
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DR EMBL; KV419403; KZS94691.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A164W2P7; -.
DR STRING; 1314777.A0A164W2P7; -.
DR OrthoDB; 1328190at2759; -.
DR Proteomes; UP000076722; 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; IPR002860; BNR_rpt.
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; PF02012; BNR; 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:0000313|EMBL:KZS94691.1};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Reference proteome {ECO:0000313|Proteomes:UP000076722};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..872
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007853990"
FT DOMAIN 835..871
FT /note="CBM1"
FT /evidence="ECO:0000259|PROSITE:PS51164"
FT REGION 744..837
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 746..837
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 872 AA; 90767 MW; 8DEC0524690B2A64 CRC64;
MRSFTYLSLF AGLAVDFAQA AAQAYTWKNV KIGGGGGFVP NIVFNPSQKG LAYARTDIGS
IYKLNADDTW TPLVDFADNS HWDYWGSDAL ATDPVTPSNL YVAVGMYTNS YDPNNGSILK
STDYGSTWTA TQLPFKVGGN MPGRGMGERL AVDPNNNKIL FFGARSGHGL WKSADAGATW
TQVKSFPSVG TYIPDPTDTT GYNSDIIGLS WVTFDPSAKT TAGTSRIFVG VANLGSSNVF
VTNDGGSTWS AVAGQNSTFM PHKGVLSPAE QSLYVSYSNG AGPYDGTLGY VSKYNITAGT
WATITPPQAV TDNYYGFGGL AVDLQKPGTV MVAALNEWWP DANIFRSTDG GKTWSEIWEW
TSYPTLARYF SYDTSLAPWI GGPLGSQDVS AKLVGWMIEG LSIDPFDSNH WLYGTGETIY
GGHDLLKWDT VHNVTIKSLA DGVEETAIQG LISPPVGPSL LSAVGDVGGF VHNSLTTAPS
TGFVNPTWAT TSDIDFAGQL PTNIVRCGTG DSSTGKQVAL STNSGATWNQ DYGAADNVTG
GHIALSASAD TVLWSSSSNG VLVSRYTNAF TPVSIPSGSV IASDKVNNSI FYAASGSSFY
ISTNNGVSFT SPSKLGTSQY PVKIAVHPSI SGDVWVSSDA GLFHTTNSGA SFTAISGITE
AWAIALGAPK TTGGYPAVFA AASIGGLVAY WRSDDQGLNW VQINDAAHGF GSASANVLTG
DPRIYGRVYV GTNGRGIFYG DISGSAPPVS VSSTSTSTTS TTTSTSKSTS STTTTSSSTK
STSTTTSTTT TSSTKSTTTS STSSTKSTTT TSSSSSTKTT STSSSSTKTS STAGPTQTPY
GQCGGAGYTG PTVCAAGWTC TVGNPYYSQC TQ
//
