CELB_ASPTN
ID CELB_ASPTN Reviewed; 420 AA.
AC Q0CC84;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 25-MAY-2022, entry version 62.
DE RecName: Full=Probable endo-beta-1,4-glucanase celB;
DE Short=Endoglucanase celB;
DE EC=3.2.1.4;
DE AltName: Full=Carboxymethylcellulase celB;
DE AltName: Full=Cellulase B;
DE Flags: Precursor;
GN Name=celB; ORFNames=ATEG_08700;
OS Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=341663;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIH 2624 / FGSC A1156;
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA Nierman W.C., Milne T., Madden K.;
RT "Annotation of the Aspergillus terreus NIH2624 genome.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Has endoglucanase activity on substrates containing beta-1,4
CC glycosidic bonds, like in carboxymethylcellulose (CMC),
CC hydroxyethylcellulose (HEC) and beta-glucan. Involved in the
CC degradation of complex natural cellulosic substrates (By similarity).
CC {ECO:0000250}.
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 -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 7 (cellulase C) family.
CC {ECO:0000305}.
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DR EMBL; CH476606; EAU30832.1; -; Genomic_DNA.
DR RefSeq; XP_001217286.1; XM_001217285.1.
DR AlphaFoldDB; Q0CC84; -.
DR SMR; Q0CC84; -.
DR STRING; 341663.Q0CC84; -.
DR EnsemblFungi; EAU30832; EAU30832; ATEG_08700.
DR GeneID; 4323506; -.
DR VEuPathDB; FungiDB:ATEG_08700; -.
DR eggNOG; ENOG502SJT6; Eukaryota.
DR HOGENOM; CLU_020817_0_1_1; -.
DR OMA; VCCNEMD; -.
DR OrthoDB; 875234at2759; -.
DR Proteomes; UP000007963; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR CDD; cd07999; GH7_CBH_EG; 1.
DR Gene3D; 2.70.100.10; -; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR001722; Glyco_hydro_7.
DR InterPro; IPR037019; Glyco_hydro_7_sf.
DR PANTHER; PTHR33753; PTHR33753; 1.
DR Pfam; PF00840; Glyco_hydro_7; 1.
DR PRINTS; PR00734; GLHYDRLASE7.
DR SUPFAM; SSF49899; SSF49899; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Cellulose degradation; Glycoprotein; Glycosidase;
KW Hydrolase; Polysaccharide degradation; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..420
FT /note="Probable endo-beta-1,4-glucanase celB"
FT /id="PRO_0000395158"
FT ACT_SITE 215
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 220
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT CARBOHYD 118
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 234
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 293
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 383
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 420 AA; 45371 MW; 9EF66065C2AE30E6 CRC64;
MLRKLTPLAL ALLPLVAGQT IGETPEVHPK LPTWKCSNRH GCVKQDTSVV IDAATHWIHE
KGGETSCTGS SGPNPNLCPD KETCAANCVI EGISDYANYG VQTKGSSMTL HQYLRDGNTT
KSVSPRVYLL AEDGENYEML QLLNQEFTFD VDVSTLVCGM NGALYFSEMQ RDGGRSELNP
AGAARGTGYC DAQCFNIPWI NGEANVEGAG ACCNEMDIWE ANARATGYTP HPCNITQLYE
CSGAECEANG VCDKPGCGFN PYALGAHDFY GYDLEVDTTK PMTVVTQFYT KDNTTTGALV
EIRRLYVQNG HVIQNAVVSV DGESVDSITA DYCADPSSAF NRLGGLQRMG EALGRGMVLA
FSVWNDAGSF MSWLDGGNSG PCNATEGDPA LIEKLHPDTH VTFSNIRWGD IGSTYRGKRR