ID A0A0D7AKB6_9AGAR Unreviewed; 729 AA.
AC A0A0D7AKB6;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 20.
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=FISHEDRAFT_63992 {ECO:0000313|EMBL:KIY52042.1};
OS Fistulina hepatica ATCC 64428.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Fistulinaceae; Fistulina.
OX NCBI_TaxID=1128425 {ECO:0000313|EMBL:KIY52042.1, ECO:0000313|Proteomes:UP000054144};
RN [1] {ECO:0000313|EMBL:KIY52042.1, ECO:0000313|Proteomes:UP000054144}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 64428 {ECO:0000313|EMBL:KIY52042.1,
RC ECO:0000313|Proteomes:UP000054144};
RX PubMed=25683379; DOI=10.1016/j.fgb.2015.02.002;
RA Floudas D., Held B.W., Riley R., Nagy L.G., Koehler G., Ransdell A.S.,
RA Younus H., Chow J., Chiniquy J., Lipzen A., Tritt A., Sun H., Haridas S.,
RA LaButti K., Ohm R.A., Kues U., Blanchette R.A., Grigoriev I.V., Minto R.E.,
RA Hibbett D.S.;
RT "Evolution of novel wood decay mechanisms in Agaricales revealed by the
RT genome sequences of Fistulina hepatica and Cylindrobasidium torrendii.";
RL Fungal Genet. Biol. 76:78-92(2015).
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; KN881646; KIY52042.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D7AKB6; -.
DR OrthoDB; 1431012at2759; -.
DR Proteomes; UP000054144; 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:KIY52042.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000054144};
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 55..79
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 221..376
FT /note="Glycoside hydrolase family 5"
FT /evidence="ECO:0000259|Pfam:PF00150"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 729 AA; 78778 MW; D940F4F081EF9F1A CRC64;
MVTTQTPRDS SYTDKCEGDS AANLAPSSDN AASDKAANEK PSHVRRMAPR RRQRILLFMG
IAAGVLVVLF LAIFLPIYFK IIKPSSNSSS SGNNGSSPYS PPGVAKSGYN GSTVTLANGS
TFMYINNYGG YWAYDEDDPY GSASSGKANE WTPAVNETWT WGKDRIYGVN LGGLFVLEPF
ITPSYFQEYT NSSGDHPIDE WTLSELMAAN GSLQSTLENH YDTFATEQDF AEMVGAGLNW
VRLPIPYWAI PGSVWNDEPF LEGVCWKYII RVLMWCRKYG LRVNLDLHTI PGSQNGYNHS
GKYGSINFLH DVMGIANAQR ALEYMRTITE WFAQSEYSNL VYIFGFINEP LLEVIGADAL
ESFYTHTQEV LRNITGYGEG NGMYLSIHDG FIGVPSWTNS YSGVDRLILD THPYFAFDNL
PNDAPIATGT DPETAGGQWP LEACNSWGSE MNDSRSDFGV TIAGEFSTGY NDCGLFLRGV
GSTTTYGGNC SFWEDATQWN ASVKAGLMEF ARAEMDALGD WFFWTWKVGE SISGTVESPA
WSYKLGLELG YIPTDPRTAV GKCARLNVTT DSFNGTFAAY ATGALGNSSA DYTLQSTASA
YQYTWPPSAI SDIGGSATTA PATDLPTYTA TASQVTLAAS AVFTVTETND KVATYTVGGA
GTGTQSFDGW YRTADTSSAP AAVSGCTYPD SWNATAIPLP GTTCGSAVTT TTSVYTTTSH
AATAITVTA
//
