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Database: UniProt
Entry: A8N527_COPC7
LinkDB: A8N527_COPC7
Original site: A8N527_COPC7 
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
//
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