ID   CELB_ASPFU              Reviewed;         407 AA.
AC   Q4WAJ6;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   25-MAY-2022, entry version 88.
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=AFUA_7G01540;
OS   Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS   A1100) (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=330879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA   Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA   Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA   Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA   Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA   Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA   Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA   O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA   Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA   Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA   Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA   Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA   Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA   Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA   Barrell B.G., Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
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; AAHF01000015; EAL84740.1; -; Genomic_DNA.
DR   RefSeq; XP_746778.1; XM_741685.1.
DR   AlphaFoldDB; Q4WAJ6; -.
DR   SMR; Q4WAJ6; -.
DR   STRING; 746128.CADAFUBP00008565; -.
DR   EnsemblFungi; EAL84740; EAL84740; AFUA_7G01540.
DR   GeneID; 3504201; -.
DR   KEGG; afm:AFUA_7G01540; -.
DR   VEuPathDB; FungiDB:Afu7g01540; -.
DR   eggNOG; ENOG502SJT6; Eukaryota.
DR   HOGENOM; CLU_020817_0_1_1; -.
DR   InParanoid; Q4WAJ6; -.
DR   OMA; VCCNEMD; -.
DR   OrthoDB; 875234at2759; -.
DR   Proteomes; UP000002530; Chromosome 7.
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..407
FT                   /note="Probable endo-beta-1,4-glucanase celB"
FT                   /id="PRO_0000395156"
FT   ACT_SITE        216
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        221
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        136
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   407 AA;  43418 MW;  040128FA260BAE75 CRC64;
     MAQTLAAASL VLVPLVTAQQ IGSIAENHPE LKTYRCGSQA GCVAQSTSVV LDINAHWIHQ
     MGAQTSCTTS SGLDPSLCPD KVTCSQNCVV EGITDYSSFG VQNSGDAITL RQYQVQNGQI
     KTLRPRVYLL AEDGINYSKL QLLNQEFTFD VDASKLPCGM NGALYLSEMD ASGGRSALNP
     AGATYGTGYC DAQCFNPGPW INGEANTLGA GACCQEMDLW EANSRSTIFS PHPCTTAGLY
     ACTGAECYSI CDGYGCTYNP YELGAKDYYG YGLTVDTAKP ITVVTQFVTA DNTATGTLAE
     IRRLYVQEGM VIGNSAVAMT EAFCSSSRTF EALGGLQRMG EALGRGMVPV FSIWDDPSLW
     MHWLDSDGAG PCGSTEGDPA FIQANYPNTA VTFSKVRWGD IDSTYSV