ID   H2B656_AURPU            Unreviewed;       430 AA.
AC   H2B656;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=cellulase {ECO:0000256|ARBA:ARBA00012601};
DE            EC=3.2.1.4 {ECO:0000256|ARBA:ARBA00012601};
GN   Name=Cel5A {ECO:0000313|EMBL:AEM23896.1};
OS   Aureobasidium pullulans (Black yeast) (Pullularia pullulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX   NCBI_TaxID=5580 {ECO:0000313|EMBL:AEM23896.1};
RN   [1] {ECO:0000313|EMBL:AEM23896.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 62921 {ECO:0000313|EMBL:AEM23896.1};
RX   PubMed=21710260; DOI=10.1007/s00253-011-3419-8;
RA   Tambor J.H., Ren H., Ushinsky S., Zheng Y., Riemens A., St-Francois C.,
RA   Tsang A., Powlowski J., Storms R.;
RT   "Recombinant expression, activity screening and functional characterization
RT   identifies three novel endo-1,4-beta-glucanases that efficiently hydrolyse
RT   cellulosic substrates.";
RL   Appl. Microbiol. Biotechnol. 93:203-214(2012).
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; HQ163777; AEM23896.1; -; mRNA.
DR   AlphaFoldDB; H2B656; -.
DR   SMR; H2B656; -.
DR   CLAE; EGL5A_AURPU; -.
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; 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.
PE   2: Evidence at transcript level;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361153};
KW   Hydrolase {ECO:0000256|RuleBase:RU361153};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          17..53
FT                   /note="CBM1"
FT                   /evidence="ECO:0000259|PROSITE:PS51164"
SQ   SEQUENCE   430 AA;  44689 MW;  62C091DE856EB25D CRC64;
     MKYSTFVVAA AAGSAAASSS AYGQCGGNGW TGATDCVSGY HCAYQNDWYS QCVPGAGSGS
     TSAAAAAATT KVVTSAKAST TQAPSKAPVS TSAASTSKAV AATSGKVKYA GVNIAGFDFG
     MDTNGASSGS YVDPGTTGQN QMNHFVKDDK LNAFRLPVGW QYLVNSQLGG TLDSTFFAKY
     DQQMTYCLNS GAALCILDLH NYARWNGQIV GTSGGPTNAQ FASVWSQLAK KYSSKPKVAF
     AIMNEPHDLQ DINAWATTVQ AAVTAIRQAG ATQNMILLPG DDWTHAANFV DNGSAAALNK
     ITNLDGSKTN LVFDVHQYSD SDGSGTSSTC VSSASNIAGF TKLATWLRSN NRQAMLTEAG
     GSNDQSCLTA VCDVLNYLMT NSDVYLGWTG WSAGMFATDY VLSEVPTGSA GSYKDQAIVT
     KCIAGVFNSK
//