ID A8NGA5_COPC7 Unreviewed; 809 AA.
AC A8NGA5;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 59.
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_05089 {ECO:0000313|EMBL:EAU88323.1};
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:EAU88323.1, ECO:0000313|Proteomes:UP000001861};
RN [1] {ECO:0000313|EMBL:EAU88323.1, 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:EAU88323.1}.
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DR EMBL; AACS02000002; EAU88323.1; -; Genomic_DNA.
DR RefSeq; XP_001833389.1; XM_001833337.1.
DR AlphaFoldDB; A8NGA5; -.
DR STRING; 240176.A8NGA5; -.
DR GeneID; 6009885; -.
DR KEGG; cci:CC1G_05089; -.
DR VEuPathDB; FungiDB:CC1G_05089; -.
DR eggNOG; ENOG502QRG8; Eukaryota.
DR InParanoid; A8NGA5; -.
DR OMA; YAITIGQ; -.
DR OrthoDB; 1431012at2759; -.
DR Proteomes; UP000001861; 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: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 153..177
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 325..487
FT /note="Glycoside hydrolase family 5"
FT /evidence="ECO:0000259|Pfam:PF00150"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 182..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..51
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 809 AA; 88369 MW; 06E2263B75D95321 CRC64;
MANNPQNPSG NVVYDPLPLT GDDVPSNALY NAPPSPDPRL TSFNTPQMGH SDLPRDDTFI
PPGAAQPRFM GQYDEASARN SFTSSQPSLR QSEYGSVYHL NDAQGSSAQF NNYRDEPNYT
DNVPMSPVGH SRGMLHEKNT AYTAPRQKSK RKVMIIGAIV AAILILAAIA IPLYFAVIKP
KTSKDNSKSD SNHDKPDSTA SPSGKPGSGA SRAVVTGGDG STITMEDGTT FVYRNPFGGY
WYYDPNDPFN NGAKAQSWTP ALNETFRYGI DKIRGVNVGG WLLTEPFMQV DSPALYEKYL
DDPAGPAIDE WDLSLRMRAD TAGGGIDQME EHYKTFITER DFAEIAGAGL NYVRVPIGYW
AVETRGDEPY LSQVSWTYFL KAVKWARKYG LRINLDLHGV PGSQNGWNHS GRFGTIGFLH
GPMGYANAQR TLDIIRVLAE FISQPQYKDV VTMFGIMNEP LGDPMGQDAL SRFYMESYNI
IRRAGGGTGE GNGVWISLHD GFFGRAPWEG FLPNADRVTL DTHPYLCFGE QSAAPMSSYA
QTPCTTWGHL VNNSMANFGL TNAGEFSNAV TDCGLFLNGV NLGTRYEGDY TPGSWPRIGD
CSEWTDYTRY SDQMKSDIRQ FALASMDALQ HYFFWTWRIG ETLRSGRVET PAWSYQLGLR
EGWMPTDPRD ADGVCGNSSP WTPPLQPWQT GGAGAGDIPP SVTEALAWPP PEIRNGGPIE
SLPRYTQTGA LPTLTGMAIT AGPSETITRT VDIGNGWNNP ADTVGFAVEI PGCTYLDPWV
TPAAAPPSPL CAAARREAAQ EPAVTLPPS
//
