ID A0A166JD15_9AGAM Unreviewed; 527 AA.
AC A0A166JD15;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 28-JUN-2023, entry version 25.
DE SubName: Full=Carbohydrate-binding module family 1 protein {ECO:0000313|EMBL:KZV74432.1};
GN ORFNames=PENSPDRAFT_674245 {ECO:0000313|EMBL:KZV74432.1};
OS Peniophora sp. CONT.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Russulales; Peniophoraceae; Peniophora.
OX NCBI_TaxID=1314672 {ECO:0000313|EMBL:KZV74432.1, ECO:0000313|Proteomes:UP000077086};
RN [1] {ECO:0000313|EMBL:KZV74432.1, ECO:0000313|Proteomes:UP000077086}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CONT {ECO:0000313|EMBL:KZV74432.1,
RC ECO:0000313|Proteomes:UP000077086};
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 30 family.
CC {ECO:0000256|ARBA:ARBA00005382}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KV424480; KZV74432.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A166JD15; -.
DR STRING; 1314672.A0A166JD15; -.
DR InParanoid; A0A166JD15; -.
DR OrthoDB; 1844890at2759; -.
DR Proteomes; UP000077086; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0030248; F:cellulose binding; IEA:InterPro.
DR GO; GO:0004348; F:glucosylceramidase activity; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0006665; P:sphingolipid metabolic process; IEA:InterPro.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR InterPro; IPR039514; 6GAL-like.
DR InterPro; IPR035971; CBD_sf.
DR InterPro; IPR000254; Cellulose-bd_dom_fun.
DR InterPro; IPR033452; GH30_C.
DR InterPro; IPR001139; Glyco_hydro_30.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR11069; GLUCOSYLCERAMIDASE; 1.
DR PANTHER; PTHR11069:SF23; LYSOSOMAL ACID GLUCOSYLCERAMIDASE; 1.
DR Pfam; PF00734; CBM_1; 1.
DR Pfam; PF14587; Glyco_hydr_30_2; 1.
DR Pfam; PF17189; Glyco_hydro_30C; 1.
DR SMART; SM00236; fCBD; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF57180; Cellulose-binding domain; 1.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
DR PROSITE; PS51164; CBM1_2; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000077086};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..527
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007875786"
FT DOMAIN 491..527
FT /note="CBM1"
FT /evidence="ECO:0000259|PROSITE:PS51164"
SQ SEQUENCE 527 AA; 54336 MW; 39F1F8615EED32BA CRC64;
MHSIFAWGTL LLLERIACAT AVTVTVSVGQ TFQEMDGFGF SQAFGRANDV KNLPAAQQKQ
TLDLLFNTTT GAGMTILRNR VGSGGTGDSI EPTSPGSPSA TPKFVWDGND SGQVWFSQQA
QSYGVDTFYA DAWSAPAFMK TNNNENNGGY LCGVTGETCS SGDWKQAYAN FLVQYVKYYA
SVGITVTHLG FLNEPDYTTS YSSMNSNGQQ AADFLKVLHS TVQSAGVDVQ LTCCDATGWN
AQTTLTAGLI SAGVENIVDV MTSHSYSSSP STPLKTTRKV WETETADLDG SFAPNNWYSS
GAAGEGLTWA NNIFTAIVNA NVSAYLYWEG AEVGTTNSAL LLISGTTPQA SKRLWAFAQW
SRFVRPGAVR VGTSGTGTNL KFSAFKNVDG TVSVQVINNG ASAQSVTIAP SGFTANSAAG
FVSAQGTDFG TLCVTLAGGQ VTASIPAHAM ASFVLSDAAS SGSSGDCSSG GSGGGSTGGG
SGTGAGGSTG CTAAKYAQCV GQGFTGCTTC ASGSTCTFSN TYYSQCL
//