ID A0A165C8Y6_9APHY Unreviewed; 336 AA.
AC A0A165C8Y6;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE RecName: Full=cellulase {ECO:0000256|ARBA:ARBA00012601};
DE EC=3.2.1.4 {ECO:0000256|ARBA:ARBA00012601};
GN ORFNames=LAESUDRAFT_406376 {ECO:0000313|EMBL:KZT02406.1};
OS Laetiporus sulphureus 93-53.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Laetiporus.
OX NCBI_TaxID=1314785 {ECO:0000313|EMBL:KZT02406.1, ECO:0000313|Proteomes:UP000076871};
RN [1] {ECO:0000313|EMBL:KZT02406.1, ECO:0000313|Proteomes:UP000076871}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=93-53 {ECO:0000313|EMBL:KZT02406.1,
RC ECO:0000313|Proteomes:UP000076871};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
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; KV427652; KZT02406.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165C8Y6; -.
DR STRING; 1314785.A0A165C8Y6; -.
DR InParanoid; A0A165C8Y6; -.
DR OrthoDB; 1638835at2759; -.
DR Proteomes; UP000076871; Unassembled WGS sequence.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
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:KZT02406.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000076871};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..336
FT /note="cellulase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007855932"
FT DOMAIN 59..304
FT /note="Glycoside hydrolase family 5"
FT /evidence="ECO:0000259|Pfam:PF00150"
SQ SEQUENCE 336 AA; 36456 MW; 7E4F3E315CDA0D03 CRC64;
MKHIATILAL LSIAIAPKGA FSQLPRLGGV NTAGYDFTVY TNGSFTNSAA MPPAWQYAHF
SAEGANLYRV PFAWQEMTPV LGGPINMTFF NEEYDVTVQA ALASSPNAHA IVDLHNYARW
NGGIIAQGGP TNEQYASIWT QLAALYGNND RLLLGIMNEP HDLDIPTWAE SVQYVVNAIR
STGATNYLLL PGSNYTSAQT FPTGAGPYLL DVTDPLFGNT ERLIFDVHKY LDYDNSGTHA
ECVTNNTVVL ETLVSWMQAN GNRQAVLSET GGGDTASCEE YLGQELAYVK SAYPSLVGFS
VWAAGSFATD YILSMTPYPN GTDQPLWIDA VRPNLP
//
