ID A8N527_COPC7 Unreviewed; 905 AA.
AC A8N527;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 2.
DT 24-JAN-2024, entry version 60.
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=CC1G_04605 {ECO:0000313|EMBL:EAU91838.2};
OS Coprinopsis cinerea (strain Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003)
OS (Inky cap fungus) (Hormographiella aspergillata).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Psathyrellaceae; Coprinopsis.
OX NCBI_TaxID=240176 {ECO:0000313|EMBL:EAU91838.2, ECO:0000313|Proteomes:UP000001861};
RN [1] {ECO:0000313|EMBL:EAU91838.2, ECO:0000313|Proteomes:UP000001861}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003
RC {ECO:0000313|Proteomes:UP000001861};
RX PubMed=20547848; DOI=10.1073/pnas.1003391107;
RA Stajich J.E., Wilke S.K., Ahren D., Au C.H., Birren B.W., Borodovsky M.,
RA Burns C., Canback B., Casselton L.A., Cheng C.K., Deng J., Dietrich F.S.,
RA Fargo D.C., Farman M.L., Gathman A.C., Goldberg J., Guigo R., Hoegger P.J.,
RA Hooker J.B., Huggins A., James T.Y., Kamada T., Kilaru S., Kodira C.,
RA Kues U., Kupfer D., Kwan H.S., Lomsadze A., Li W., Lilly W.W., Ma L.J.,
RA Mackey A.J., Manning G., Martin F., Muraguchi H., Natvig D.O.,
RA Palmerini H., Ramesh M.A., Rehmeyer C.J., Roe B.A., Shenoy N., Stanke M.,
RA Ter-Hovhannisyan V., Tunlid A., Velagapudi R., Vision T.J., Zeng Q.,
RA Zolan M.E., Pukkila P.J.;
RT "Insights into evolution of multicellular fungi from the assembled
RT chromosomes of the mushroom Coprinopsis cinerea (Coprinus cinereus).";
RL Proc. Natl. Acad. Sci. U.S.A. 107:11889-11894(2010).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EAU91838.2}.
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DR EMBL; AACS02000003; EAU91838.2; -; Genomic_DNA.
DR RefSeq; XP_001829916.2; XM_001829864.2.
DR AlphaFoldDB; A8N527; -.
DR STRING; 240176.A8N527; -.
DR GeneID; 6006354; -.
DR KEGG; cci:CC1G_04605; -.
DR VEuPathDB; FungiDB:CC1G_04605; -.
DR eggNOG; ENOG502QRG8; Eukaryota.
DR HOGENOM; CLU_004624_6_1_1; -.
DR InParanoid; A8N527; -.
DR OMA; PLSEPWN; -.
DR OrthoDB; 1431012at2759; -.
DR Proteomes; UP000001861; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00023295};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000001861};
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 96..119
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 262..421
FT /note="Glycoside hydrolase family 5"
FT /evidence="ECO:0000259|Pfam:PF00150"
FT REGION 19..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 125..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..71
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 128..174
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 905 AA; 97596 MW; 397E7A8DE29BAA9A CRC64;
MAERPVSIVS DGALANAASV PLPQGDGNSL NDPQAALDSR TPSSAALRDS AALADSTTAL
GPGNNAVDSS KEAADSAAEG GQAGEPASTS RKRRPLLIAL LALLALAIVV LAVVLPVYFK
VIKPRQNRDG STDGSSGSGT DGNESTSAPS PTGSATPTNP TSGGDGSTVT TEDGTTFTYS
NQFGGFWYSD PDDPYNDSAQ PNSWTPPLNA SFDYTTTRIF GVNLGGLFVL EPFISPALFQ
RYPGARDEWD LSVAMAADTA NGGLDQLEEH YRTFITEQDI AEIAGAGLNW VRLPVPFWAI
DKWPGEPFLE RTSWRYIVRV LQWCRKYGLR VNLDLHTIPG SHNAYNHGGK LNAFNFLNGA
MGMANAQRAL YYIQVFTEFI NQPEWRNVVP MFSIMNEPII GTIGVDQLRS FYVEAHRIMR
EITGYGEGNG PYMVIHDSFR GPGPWAGFMT GADRVGMDVH PYFAFNGDSD PPTIDGGVGP
GAGNGWPLRA CNRFNAMMND SRRDFGVTVA GEFSNAWQDC SLFLRGVGGR ADYGGDCTPW
LDSSGWSDGV KAGLLAFASA QMDGLGDWFF WTWKIGESER GIVESPFWSY QLGLRNGWMP
TDPRTVIGTC QALGVYTPWD GTFQPYMIGG PGAGAPSDAS SYPWPPTALG DGNAVAALPT
YATTGSPVVL PAPTFTDSQG NEILPSGTQA SHPAPTPIAG CTYPDGWDSD GVPPPALCGV
FRAIETALSP FVTIASKPCS VISNMIYHVL CQKTSCSHTV RPEVSFHVAY NLKVAYTPSL
VTIGAFFVSP QVSRGSAKGT VKLRIKPYVR KPLNLYLPHH QGPRSIAFRN HFDNGDVCYN
LFNFSHPTEE TVFIVQTDKV GEKRSRHSAI SEARDLKIKG CGNSHFWTPR SYSTYLMLES
LIICA
//