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Database: UniProt
Entry: A0A3E2HET0_SCYLI
LinkDB: A0A3E2HET0_SCYLI
Original site: A0A3E2HET0_SCYLI 
ID   A0A3E2HET0_SCYLI        Unreviewed;       405 AA.
AC   A0A3E2HET0;
DT   16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT   16-JAN-2019, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=cellulase {ECO:0000256|ARBA:ARBA00012601};
DE            EC=3.2.1.4 {ECO:0000256|ARBA:ARBA00012601};
DE   Flags: Fragment;
GN   ORFNames=B7463_g4482 {ECO:0000313|EMBL:RFU31855.1};
OS   Scytalidium lignicola (Hyphomycete).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Scytalidium.
OX   NCBI_TaxID=5539 {ECO:0000313|EMBL:RFU31855.1, ECO:0000313|Proteomes:UP000258309};
RN   [1] {ECO:0000313|EMBL:RFU31855.1, ECO:0000313|Proteomes:UP000258309}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 105466 {ECO:0000313|EMBL:RFU31855.1,
RC   ECO:0000313|Proteomes:UP000258309};
RA   Buettner E., Gebauer A.M., Hofrichter M., Liers C., Kellner H.;
RT   "Draft genome sequence of Scytalidium lignicola DSM 105466, a ubiquitous
RT   saprotrophic fungus.";
RL   Submitted (MAY-2018) 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}.
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:RFU31855.1}.
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DR   EMBL; NCSJ02000066; RFU31855.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3E2HET0; -.
DR   SMR; A0A3E2HET0; -.
DR   STRING; 5539.A0A3E2HET0; -.
DR   OMA; GYMESNS; -.
DR   Proteomes; UP000258309; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR   GO; GO:0030248; F:cellulose binding; IEA:InterPro.
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; IPR035971; CBD_sf.
DR   InterPro; IPR000254; Cellulose-bd_dom_fun.
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; PF00734; CBM_1; 1.
DR   Pfam; PF00150; Cellulase; 1.
DR   SMART; SM00236; fCBD; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF57180; Cellulose-binding domain; 1.
DR   PROSITE; PS00562; CBM1_1; 1.
DR   PROSITE; PS51164; CBM1_2; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000258309};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           17..405
FT                   /note="cellulase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5017592651"
FT   DOMAIN          17..53
FT                   /note="CBM1"
FT                   /evidence="ECO:0000259|PROSITE:PS51164"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:RFU31855.1"
FT   NON_TER         405
FT                   /evidence="ECO:0000313|EMBL:RFU31855.1"
SQ   SEQUENCE   405 AA;  42415 MW;  53CE52D97816139D CRC64;
     MKLSTTSGVL LAGTAAAQSG AWGQCGGQGW TGATTCISGY TCTYSNPYYS QCLPGAGPSS
     TTTRASTPTF VTSTTSSSTN PTGSVQYAGV NIAGFDFGCG TDGTCDTTQA YPPLSSLGGP
     DGIGQMQHFV TDDNLNVFRL PVGWQYLVNN QLGGNLDQGN LANYDQLVQG CLATGAHCLI
     DIHNYARWNG QVIGQGGPTN DQFASLWSQI AEKYANNSNI IFGVMNEPHD LTVSTWATSV
     QAAVTAIRQA GATTQMILLP GTDYTSAANF ISNGSGAALL GVKNPDGTTT GLIFDVHKYL
     DSDNSGTSTE CVTNNIDSAF QPLATWLRQN GRQAFNTETG GGNTASCETY LCQQIQFVND
     NSDVYLGYIG WSAGSFDQTY ALVETPTGGS GSWQDTALVQ ACIAR
//
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