ID A0A2N6NFX7_BEABA Unreviewed; 421 AA.
AC A0A2N6NFX7;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=cellulase {ECO:0000256|ARBA:ARBA00012601};
DE EC=3.2.1.4 {ECO:0000256|ARBA:ARBA00012601};
GN Name=egl2 {ECO:0000313|EMBL:PMB66189.1};
GN ORFNames=BM221_008391 {ECO:0000313|EMBL:PMB66189.1};
OS Beauveria bassiana (White muscardine disease fungus) (Tritirachium
OS shiotae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX NCBI_TaxID=176275 {ECO:0000313|EMBL:PMB66189.1, ECO:0000313|Proteomes:UP000235728};
RN [1] {ECO:0000313|EMBL:PMB66189.1, ECO:0000313|Proteomes:UP000235728}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JEF-007 {ECO:0000313|EMBL:PMB66189.1,
RC ECO:0000313|Proteomes:UP000235728};
RX PubMed=27470140; DOI=10.1007/s00253-016-7734-y;
RA Kim S., Lee S.J., Nai Y.S., Yu J.S., Lee M.R., Yang Y.T., Kim J.S.;
RT "Characterization of T-DNA insertion mutants with decreased virulence in
RT the entomopathogenic fungus Beauveria bassiana JEF-007.";
RL Appl. Microbiol. Biotechnol. 100:8889-8900(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}.
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:PMB66189.1}.
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DR EMBL; MRVG01000009; PMB66189.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N6NFX7; -.
DR OMA; YTDNKLM; -.
DR Proteomes; UP000235728; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000235728};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..421
FT /note="cellulase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014646293"
FT DOMAIN 53..307
FT /note="Glycoside hydrolase family 5"
FT /evidence="ECO:0000259|Pfam:PF00150"
FT REGION 346..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..389
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 421 AA; 44461 MW; E1F6D333A6A6CEB5 CRC64;
MRSLTSAAMV LALAAGAAAK LQYLGVALSG IDFGCDIDGS CPLDKIGLPL KNYGGADGKA
QMEHFVKNDK LNIFRLPVSW QFLTNAKGGS TLDKQGWESY DTLMQTCLDT GAYCMIDLHN
FARFDKGIIG QGGPSDATFA QLWANIASKY ADNDKVVFGI MNEPHDLDTA KWADTCQAAV
TAIRKAGAKT QIILLPGNNF SSAADFVDNK SAELLSKITN PDGSIDGLLL DLHKYLDINN
SGQHAECTTD NVEGFGTIAK WLRANNRTAM VSETGASMED SCMEKFCAQN KFISENTDVF
VGFVGWSAGS LDHTYVMSLT PTGSPGAYTD NKLMKQCILD IFDGKLSPPP SSSSATRPSK
SSTSAAQSSQ KTSDSVFIES PSSKPSQMPA NDAPAKGAAA SSSSISILAV VGAAAFVCAA
L
//
