ID A0A0D2KBD9_9EURO Unreviewed; 762 AA.
AC A0A0D2KBD9;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-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=Z520_04110 {ECO:0000313|EMBL:KIY00425.1};
OS Fonsecaea multimorphosa CBS 102226.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Fonsecaea.
OX NCBI_TaxID=1442371 {ECO:0000313|EMBL:KIY00425.1, ECO:0000313|Proteomes:UP000053411};
RN [1] {ECO:0000313|EMBL:KIY00425.1, ECO:0000313|Proteomes:UP000053411}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 102226 {ECO:0000313|EMBL:KIY00425.1,
RC ECO:0000313|Proteomes:UP000053411};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Fonsecaea multimorphosa CBS 102226.";
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; KN848067; KIY00425.1; -; Genomic_DNA.
DR RefSeq; XP_016634547.1; XM_016774620.1.
DR AlphaFoldDB; A0A0D2KBD9; -.
DR STRING; 1442371.A0A0D2KBD9; -.
DR GeneID; 27709856; -.
DR VEuPathDB; FungiDB:Z520_04110; -.
DR OrthoDB; 1431012at2759; -.
DR Proteomes; UP000053411; 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:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProt.
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 Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00023295};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000053411};
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 230..251
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 395..596
FT /note="Glycoside hydrolase family 5"
FT /evidence="ECO:0000259|Pfam:PF00150"
FT REGION 1..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 141..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 254..288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..60
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..106
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..126
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 762 AA; 85044 MW; 7D39CA644580C964 CRC64;
MPKPRRESAA RADTRPAFNR PPNARPAPVP RQTRSATTEE EDYDDYYEPR TPKRAPPREK
AKASSVPSPS PEKRPRRPSD RYRSSSNGVR DSPRREEKKK QQQQRDRAKY SSGTSTNSTS
QLLSSDALAK LNAYNARAEF EEKYEERKRN KKQQKKQYKN LKAAEATQQQ RRKKHVKNRN
VSGAILEEGR AGEKHRRAHG RGGGGGGGYG KEYQAHRRSG ADRGRRNKKF WWLLILIVVL
LAIFIPVAVV VSNNSKKSSG GSSSSSSATT SDGSSGISND CDSSSTPASA KGTYTDISTW
MDTTDFNCTY TAETVGGLSV MGLYSSWDDS TKANDNVPAL NEQWEYGTMP IRGVNIGGWL
SLEPFITPSM FNYPASAAVV DEWTLSQKLG PSAQRVIETH YATFITKQSF IDIKNAGLDH
VRIPYPYWSV TTYDGDPYVP KVAWRYLLRA IEYCRENGLR VNLDLHSVPG SQNGWAHSGH
QGDIGWILGP DGATNAQRSL DIHNQLSQFF AQDRYKNVVT IYGLVNEPKM LVIPPQSVLD
WNQKAIAIIR GNGIKQRIVF GDGFLSLDSW DDMFHGVDNN LVMDTHQYQI FNTGQLKLKH
QDKINLACSG WTGLMVAANN PQTGWGPILD GEWSQADTDC TPNLNNVGVG SRWAGTLDTG
DPSTSVLTPT CAEPPCSCEQ ANADPSQYSA AYKQFLQMYA EAQMHSFEQA WGWFYWTWKT
ENAVQWSWML GLQAGILPDK AYAPSFKCDS QVPDFSDLPE SY
//
