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Database: UniProt
Entry: A0A1Y2VW36_9PEZI
LinkDB: A0A1Y2VW36_9PEZI
Original site: A0A1Y2VW36_9PEZI 
ID   A0A1Y2VW36_9PEZI        Unreviewed;       385 AA.
AC   A0A1Y2VW36;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   RecName: Full=cellulase {ECO:0000256|ARBA:ARBA00012601};
DE            EC=3.2.1.4 {ECO:0000256|ARBA:ARBA00012601};
GN   ORFNames=M426DRAFT_75026 {ECO:0000313|EMBL:OTB01754.1};
OS   Hypoxylon sp. CI-4A.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Xylariomycetidae; Xylariales; Hypoxylaceae; Hypoxylon.
OX   NCBI_TaxID=1001833 {ECO:0000313|EMBL:OTB01754.1, ECO:0000313|Proteomes:UP000242955};
RN   [1] {ECO:0000313|EMBL:OTB01754.1, ECO:0000313|Proteomes:UP000242955}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CI-4A {ECO:0000313|EMBL:OTB01754.1,
RC   ECO:0000313|Proteomes:UP000242955};
RX   PubMed=28078400; DOI=10.1007/s00253-017-8091-1;
RA   Wu W., Davis R.W., Tran-Gyamfi M.B., Kuo A., LaButti K., Mihaltcheva S.,
RA   Hundley H., Chovatia M., Lindquist E., Barry K., Grigoriev I.V.,
RA   Henrissat B., Gladden J.M.;
RT   "Characterization of four endophytic fungi as potential consolidated
RT   bioprocessing hosts for conversion of lignocellulose into advanced
RT   biofuels.";
RL   Appl. Microbiol. Biotechnol. 101:2603-2618(2017).
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; KZ111578; OTB01754.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y2VW36; -.
DR   STRING; 1001833.A0A1Y2VW36; -.
DR   InParanoid; A0A1Y2VW36; -.
DR   OrthoDB; 1638835at2759; -.
DR   Proteomes; UP000242955; 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; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR34142:SF1; CELLULASE 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.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361153};
KW   Hydrolase {ECO:0000256|RuleBase:RU361153, ECO:0000313|EMBL:OTB01754.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000242955};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           17..385
FT                   /note="cellulase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5013164191"
FT   DOMAIN          42..317
FT                   /note="Glycoside hydrolase family 5"
FT                   /evidence="ECO:0000259|Pfam:PF00150"
SQ   SEQUENCE   385 AA;  41466 MW;  7B1746056E4138D8 CRC64;
     MKHSAILASL ASTASATIYY AGVAESGGEF GVWSADAIKG TGLPGTFGVE YQFIDKAGID
     VHVDQNHLNL FRIAFLLERM NPLETGLGST FNETHFDYYK EAVDYATITK GAYAILDPHS
     YMRYNDPSSQ PYSGSVIGNT TDPTAATTEQ FGEFWGELAK RFANNEKVIF ALMNEPHDMA
     TSLVLANNQA AIDAIRAANA SNLILMPGNS WTGGHAWSEG SDPSSAILHQ FIDPLNNTAI
     DIHEYLDVDF SGSHSECVSD PATNMAAVTS WLKEHNLKAF VTEFGGHNNT GCDDMLTDFL
     NYMADNDVYL GWTAWAAGPF WGTASPCCTD SASYGSLEPG SKAADGGPSL YDTVWLKVFQ
     PLVPSKLQWT GPASVSGGEL VEFPA
//
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