ID A0A0D0C9W0_9AGAR Unreviewed; 754 AA.
AC A0A0D0C9W0;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=GYMLUDRAFT_265773 {ECO:0000313|EMBL:KIK51578.1};
OS Collybiopsis luxurians FD-317 M1.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Omphalotaceae; Collybiopsis;
OC Collybiopsis luxurians.
OX NCBI_TaxID=944289 {ECO:0000313|EMBL:KIK51578.1, ECO:0000313|Proteomes:UP000053593};
RN [1] {ECO:0000313|EMBL:KIK51578.1, ECO:0000313|Proteomes:UP000053593}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FD-317 M1 {ECO:0000313|EMBL:KIK51578.1,
RC ECO:0000313|Proteomes:UP000053593};
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 (APR-2014) 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}.
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DR EMBL; KN834860; KIK51578.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D0C9W0; -.
DR HOGENOM; CLU_004624_6_1_1; -.
DR OrthoDB; 1431012at2759; -.
DR Proteomes; UP000053593; 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};
KW Hydrolase {ECO:0000256|ARBA:ARBA00023295};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000053593};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 75..98
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 240..399
FT /note="Glycoside hydrolase family 5"
FT /evidence="ECO:0000259|Pfam:PF00150"
FT REGION 1..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 105..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..62
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..142
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 754 AA; 80375 MW; 30043834BAA1FDA7 CRC64;
MEEHISRSLA GTPLPVGGAE RFLEQPRASF PNSSAGNSIQ STPNNSLPLL VSNKAESDSS
EQLQAGSRRK RRRPIVLALF VLSILAVVVL AVILPVYFKV IKPKNNHRNP ASSSSGSSAG
NGSVGNGSEN PLSPTGATSG GDGSEIITDD GTKFTYKNPF GGYWVFDPND PFNNDARPNS
WTPPLNTSWD WTKDRIYGVN LGGLFVIEPF ITPAFFEKYP NAVDEWTLSE AMAADTSSGG
LNQLEDHYNT FITEQDIAEI AGAGLNWIRL PIPFWAIETW PGEPFLAKTS WRYIVRILNW
ARKYGLRVNL DLHTIPGSQN GYNHSGKLGQ VNFMNGVMGY ANAQRALSYI RIITEFITQE
EYLDVVLMFG IINEALIKTI GKDQMTAFYL EAHDMIRGIT GLGEGHGPFI SIHDGFSLGS
WAGFLSGSDR ISMDTHPYFA FNVDPDDSPI ATGLGSDAGG IWPASACNSW GPGINTSRSD
FGVTIAGEFS NGYNDCGLFL NGVPGGHSYP GDCNLWQDAS TWNATVIAGV KAFALASMDA
MQNWFFWTWK IGNSTANNRV ESPLWSYQLG LQGGWIPTDP REATGTCAAL GVSQPWNQKF
ESWQTGGVGA GTIAATSSAQ YVWPPTQVSG VPAAQMTFIP TYTPTGSVAT LPPPTLTATS
KSISEGNGWF DPSDTISAPT AIAGCSYPDA WDALSAAVPT SQCGGGVADS PGTTSPLTTL
PSATKASASL ATGLTSASTI SDDATVPTTV PTAI
//
