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   22-FEB-2023, entry version 64.
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   GlyCosmos; Q0CC84; 4 sites, No reported glycans.
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; 3014058at2759; -.
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; Glycoside hydrolase, family 7, domain; 1.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR001722; Glyco_hydro_7.
DR   InterPro; IPR037019; Glyco_hydro_7_sf.
DR   PANTHER; PTHR33753; 1,4-BETA-D-GLUCAN CELLOBIOHYDROLASE B; 1.
DR   PANTHER; PTHR33753:SF1; ENDO-BETA-1,4-GLUCANASE CELB; 1.
DR   Pfam; PF00840; Glyco_hydro_7; 1.
DR   PRINTS; PR00734; GLHYDRLASE7.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 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
//