ID A0A0C9WM46_9AGAR Unreviewed; 544 AA.
AC A0A0C9WM46;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=glucan 1,3-beta-glucosidase {ECO:0000256|ARBA:ARBA00038929};
DE EC=3.2.1.58 {ECO:0000256|ARBA:ARBA00038929};
DE AltName: Full=Exo-1,3-beta-glucanase D {ECO:0000256|ARBA:ARBA00041260};
GN ORFNames=K443DRAFT_105002 {ECO:0000313|EMBL:KIJ97809.1};
OS Laccaria amethystina LaAM-08-1.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Hydnangiaceae; Laccaria.
OX NCBI_TaxID=1095629 {ECO:0000313|EMBL:KIJ97809.1, ECO:0000313|Proteomes:UP000054477};
RN [1] {ECO:0000313|EMBL:KIJ97809.1, ECO:0000313|Proteomes:UP000054477}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LaAM-08-1 {ECO:0000313|EMBL:KIJ97809.1,
RC ECO:0000313|Proteomes:UP000054477};
RG DOE Joint Genome Institute;
RA Kuo A., Kohler A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Sun H., Tunlid A., Henrissat B.,
RA Grigoriev I.V., Hibbett D.S., Martin F., Nordberg H.P., Cantor M.N.,
RA Hua S.X.;
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000054477}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LaAM-08-1 {ECO:0000313|Proteomes:UP000054477};
RG DOE Joint Genome Institute;
RG Mycorrhizal Genomics Consortium;
RA Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Glucosidase involved in the degradation of cellulosic
CC biomass. Active on lichenan. {ECO:0000256|ARBA:ARBA00037126}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004401};
CC Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004401}.
CC Membrane {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane
CC protein {ECO:0000256|ARBA:ARBA00004606}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC {ECO:0000256|ARBA:ARBA00005641, ECO:0000256|RuleBase:RU361153}.
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DR EMBL; KN838683; KIJ97809.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C9WM46; -.
DR STRING; 1095629.A0A0C9WM46; -.
DR HOGENOM; CLU_004624_6_1_1; -.
DR OrthoDB; 1431012at2759; -.
DR Proteomes; UP000054477; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0071704; P:organic substance metabolic process; IEA:InterPro.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR001547; Glyco_hydro_5.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR31297:SF22; GLUCAN 1,3-BETA-GLUCOSIDASE 2; 1.
DR PANTHER; PTHR31297; GLUCAN ENDO-1,6-BETA-GLUCOSIDASE B; 1.
DR Pfam; PF00150; Cellulase; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361153};
KW Hydrolase {ECO:0000256|RuleBase:RU361153, ECO:0000313|EMBL:KIJ97809.1};
KW Membrane {ECO:0000256|ARBA:ARBA00022989};
KW Reference proteome {ECO:0000313|Proteomes:UP000054477};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 90..250
FT /note="Glycoside hydrolase family 5"
FT /evidence="ECO:0000259|Pfam:PF00150"
SQ SEQUENCE 544 AA; 58811 MW; EC3D6E0216932082 CRC64;
MDNGTTFTYR NKFGGFWVSD PANPFSNNAR PNSWTPPLNT SWTWGQDRVF GVNLGGWLVM
EPFITPSYYQ KYTGAVDEFT LSTLMIADTG AGGGLQQLEA HYDTFITEQD IAEIAGAGLN
WVRVPIAFWA IETWAGEPFL ARTSWKYFLR FLGWARKYGL RVCLDLHAVP GSQNGYNHSG
MLKVVNFMSG NMGLANAQRT LDYIRVLTEF ITQPEYQDLI PIFGIVNEPT AGTAALSNFY
LEAHNLIRNI TGLGAGHGPY IAMHSAFNGA GDWVGFLQGA DRMILDEHPY FAFGGVNTSP
VNTTGATGQP GGTWPARTSF GVMIAGEFSA APNDCGLFMV GVGVVSANPQ CPEYDDWPSY
SDEMKAGLLN MVLATMDALG DWFFWTWKIG PDQSGNISSP LWSYQLGLAN GWIPTDPRTA
QGKCASLSVS INRFSGAFLP WQTGSTPSSI PDASSVKYPW PPATMTNADV SVSLLPTYTN
TGPVITMPVP TTFTSAPSKV TSGFDGWFDQ ADTAGGVVTV AGCTYPNEYT PTFAVVPTAA
CTGA
//
