ID A0A2J6SFT8_9HELO Unreviewed; 445 AA.
AC A0A2J6SFT8;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=cellulase {ECO:0000256|ARBA:ARBA00012601};
DE EC=3.2.1.4 {ECO:0000256|ARBA:ARBA00012601};
GN ORFNames=K444DRAFT_657863 {ECO:0000313|EMBL:PMD49638.1};
OS Hyaloscypha bicolor E.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Hyaloscyphaceae; Hyaloscypha; Hyaloscypha bicolor.
OX NCBI_TaxID=1095630 {ECO:0000313|EMBL:PMD49638.1, ECO:0000313|Proteomes:UP000235371};
RN [1] {ECO:0000313|EMBL:PMD49638.1, ECO:0000313|Proteomes:UP000235371}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E {ECO:0000313|EMBL:PMD49638.1,
RC ECO:0000313|Proteomes:UP000235371};
RG DOE Joint Genome Institute;
RA Martino E., Morin E., Grelet G., Kuo A., Kohler A., Daghino S., Barry K.,
RA Choi C., Cichocki N., Clum A., Copeland A., Hainaut M., Haridas S.,
RA Labutti K., Lindquist E., Lipzen A., Khouja H.-R., Murat C., Ohm R.,
RA Olson A., Spatafora J., Veneault-Fourrey C., Henrissat B., Grigoriev I.,
RA Martin F., Perotto S.;
RT "A degradative enzymes factory behind the ericoid mycorrhizal symbiosis.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->4)-beta-D-glucosidic linkages in
CC cellulose, lichenin and cereal beta-D-glucans.; EC=3.2.1.4;
CC Evidence={ECO:0000256|ARBA:ARBA00000966};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC {ECO:0000256|ARBA:ARBA00005641, ECO:0000256|RuleBase:RU361153}.
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DR EMBL; KZ613920; PMD49638.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2J6SFT8; -.
DR STRING; 1095630.A0A2J6SFT8; -.
DR InParanoid; A0A2J6SFT8; -.
DR OrthoDB; 1638835at2759; -.
DR Proteomes; UP000235371; Unassembled WGS sequence.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
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; IPR018087; Glyco_hydro_5_CS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR34142:SF5; CBM1 DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR34142; ENDO-BETA-1,4-GLUCANASE A; 1.
DR Pfam; PF00150; Cellulase; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR PROSITE; PS00659; GLYCOSYL_HYDROL_F5; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361153};
KW Hydrolase {ECO:0000256|RuleBase:RU361153, ECO:0000313|EMBL:PMD49638.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000235371};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..445
FT /note="cellulase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014349862"
FT DOMAIN 57..307
FT /note="Glycoside hydrolase family 5"
FT /evidence="ECO:0000259|Pfam:PF00150"
FT REGION 388..423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 445 AA; 46805 MW; 8AF9387D0972E2CE CRC64;
MFLPSLVILG VVQAVFGKTQ LYGMNIAGFE FGCEITGTCP LDTIQPPLKS LGFGDGAGQM
DHFVKDDGMN VFRLPVSWQY LTNNVIGPLD KTNFGNYDLL MQACLKTGAY CVIDIHNFAR
WNGGIIGQGG PTDEQFADLW TQLATNYASN PFVIFELMNE PHDIDLTAWV ASCQAAVAAI
RKAEKVLHIV LLPGENFSSA GTFLTSGWGA ALATVTNPDA STTNLVLDLH KYEDVDNSGD
HPDCVMDNVA DTFEPVAAWL RKNKRQAILS ETGVGVTSES CFVDFCAQNT AINANSDVYL
GYIAWTAGSV TSDYILDLAP TLTGTKWVDQ KMTIQCVIDL WVNAPAGPAA PDWGLALGTA
LAAIPSSTGG SAKRSSSVVV STSSSGAVST PTAIVTGTGK SGSASGTQTS ASPSDTQTKT
PNSANGVKFA SGLMACSLIL AVILL
//
