ID   EXGB_ASPTN              Reviewed;         404 AA.
AC   Q0C8Z0;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   25-MAY-2022, entry version 71.
DE   RecName: Full=Probable glucan endo-1,6-beta-glucosidase B;
DE            EC=3.2.1.75;
DE   AltName: Full=Beta-1,6-glucanase B;
DE   AltName: Full=Endo-1,6-beta-D-glucanase B;
DE   AltName: Full=Endo-1,6-beta-glucanase B;
DE   Flags: Precursor;
GN   Name=exgB; ORFNames=ATEG_09844;
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: Beta-glucanases participate in the metabolism of beta-glucan,
CC       the main structural component of the cell wall. Acts on lutean,
CC       pustulan and 1,6-oligo-beta-D-glucosides (By similarity).
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Random hydrolysis of (1->6)-linkages in (1->6)-beta-D-
CC         glucans.; EC=3.2.1.75;
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC       {ECO:0000305}.
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DR   EMBL; CH476608; EAU30035.1; -; Genomic_DNA.
DR   RefSeq; XP_001218466.1; XM_001218465.1.
DR   AlphaFoldDB; Q0C8Z0; -.
DR   SMR; Q0C8Z0; -.
DR   EnsemblFungi; EAU30035; EAU30035; ATEG_09844.
DR   GeneID; 4354491; -.
DR   VEuPathDB; FungiDB:ATEG_09844; -.
DR   eggNOG; ENOG502RBRB; Eukaryota.
DR   HOGENOM; CLU_004624_7_0_1; -.
DR   OMA; WMLPAEW; -.
DR   OrthoDB; 916629at2759; -.
DR   Proteomes; UP000007963; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0046557; F:glucan endo-1,6-beta-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR001547; Glyco_hydro_5.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   Pfam; PF00150; Cellulase; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Cell wall biogenesis/degradation; Glycoprotein;
KW   Glycosidase; Hydrolase; Polysaccharide degradation; Reference proteome;
KW   Secreted; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..404
FT                   /note="Probable glucan endo-1,6-beta-glucosidase B"
FT                   /id="PRO_0000394709"
FT   ACT_SITE        222
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        324
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        33
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        130
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        253
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        299
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   404 AA;  45814 MW;  57FDB335BFFF69E8 CRC64;
     MTTYQTLFLI PLAISTLVTA WLPETDKTIT SRNGTNLFAS SKGKIRGVNM GSQFVFEPWI
     AEKAWSSMGC KGQKSEFDCV VSLGQDAANK AFAQHWGSWI TQDDITEIQS YTLNTIRVPI
     GYWMKEDLVN KTSEHFPQGG FAYLEKLCGW ASDAGLYIIL DLHGAPGAQT PHNPFTGQYA
     STAGFYNDYQ FGRALEFLEW ITTKVHQSDS FRNVGMLEIV NEPLQNAQKV GSMRSTYYPD
     AFKRIRAAEQ KLNVSKSGYL HIQMMDKLWG SGDPEEYLTD KYYVAYDDHR YLKWDPKVNV
     SKENYISTSC SDELDSNTPT IVGEWSLSVP DDVASTPDWD MDTNKDFYKK WFAAQITAYE
     KQRGWVFWTW KTQLGGYRWS YKDAVAAGVV PEDIDSALNM GVCN