ID A0A0C3CYL3_HEBCY Unreviewed; 836 AA.
AC A0A0C3CYL3;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=M413DRAFT_102209 {ECO:0000313|EMBL:KIM49254.1};
OS Hebeloma cylindrosporum h7.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Hymenogastraceae; Hebeloma.
OX NCBI_TaxID=686832 {ECO:0000313|EMBL:KIM49254.1, ECO:0000313|Proteomes:UP000053424};
RN [1] {ECO:0000313|EMBL:KIM49254.1, ECO:0000313|Proteomes:UP000053424}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=h7 {ECO:0000313|Proteomes:UP000053424};
RG DOE Joint Genome Institute;
RA Kuo A., Gay G., Dore J., Kohler A., Nagy L.G., Floudas D., Copeland A.,
RA Barry K.W., Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A.,
RA Lipzen A., 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:UP000053424}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=h7 {ECO:0000313|Proteomes:UP000053424};
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}.
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DR EMBL; KN831768; KIM49254.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C3CYL3; -.
DR STRING; 686832.A0A0C3CYL3; -.
DR HOGENOM; CLU_004624_6_1_1; -.
DR OrthoDB; 1431012at2759; -.
DR Proteomes; UP000053424; 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:0000313|EMBL:KIM49254.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000053424};
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 162..186
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 302..327
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 360..567
FT /note="Glycoside hydrolase family 5"
FT /evidence="ECO:0000259|Pfam:PF00150"
FT REGION 1..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 813..836
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 836 AA; 90027 MW; 681A4F764950B86C CRC64;
MSNNDPTRNV AYDPLPLTGD DQHSNTLYNA PPSPDPRLSS FHTPQMTPGE LGPDDSAIPL
GAAQPRFLGA ALYDGPGSPA MRDSFASSQH TIPNSVYGSS VYALNDGQGR FEGSYRDDPR
DSYYAGEHGG VPMSPVVAGH SRVLEEKRAA YVPPKTKSRR QVMIAAIIVA IILIILAVVI
PVYFFVLKPS NNESSSVPSH SAHPSSSASV PTPSAIAVTR GDGSLITMED GTTFTYKNQF
GGTWYWDEND PFNNGARPQS WSPALNETFR YGIDKIRGVN VGGWLNTEPV SIVFCSVRST
RLFIFLVHVC LFARLFLCAV FIVIIIYSSP ALYQKYSSNP TPPVDEWTLS LAMAADTASG
GLSQMEDHYK TFITEKDFAE IAGAGLNFVR IPIGYWAIEV RNGEPFLPKV SWSYFLKAIK
WARKYGLRIN LDLHALPGSQ NGWNHSGRLG TIGFLNGPMG YANAQRSLDY IRIFAEFISQ
PQYKDVVTIF GIMNEPQGTF MGQDQLSRFY LQAYNIIRTA GGTGAGNGPY VSLHDGFFSR
TSWVNVFPNA DRVTLDTHPY LCFNGQSAAP MSSYATTPCT SWGAGVNASM GSFGLTNAGE
FSNAVTDCGL FLNGVGLGTR YEGTYSGVWP RIGSCTTWTD WQNYDRATKA AIRQFSLASM
DALQDYFFWT WKIGNSSVSG KVETPAWSYQ LGLENGWMPT DPREAAGVCG NSSPWTPPLA
AWQTGGTGAG NIPSSVTSAL AWPPPSISNG GAVSTLPAYT PTGPIPTLPG PTFAAATASI
DVGNGWANAA DTQGLSANIP GCQYLDPWVD PGTAPPPACA AAQRRDEPIA APTPAP
//
