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Database: UniProt
Entry: A0A067M8M2_9AGAM
LinkDB: A0A067M8M2_9AGAM
Original site: A0A067M8M2_9AGAM 
ID   A0A067M8M2_9AGAM        Unreviewed;       444 AA.
AC   A0A067M8M2;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=glucan endo-1,6-beta-glucosidase {ECO:0000256|ARBA:ARBA00038935};
DE            EC=3.2.1.75 {ECO:0000256|ARBA:ARBA00038935};
DE   AltName: Full=Beta-1,6-glucanase B {ECO:0000256|ARBA:ARBA00042025};
DE   AltName: Full=Endo-1,6-beta-D-glucanase B {ECO:0000256|ARBA:ARBA00041472};
DE   AltName: Full=Endo-1,6-beta-glucanase B {ECO:0000256|ARBA:ARBA00043257};
GN   ORFNames=BOTBODRAFT_573600 {ECO:0000313|EMBL:KDQ08212.1};
OS   Botryobasidium botryosum FD-172 SS1.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Cantharellales; Botryobasidiaceae; Botryobasidium.
OX   NCBI_TaxID=930990 {ECO:0000313|EMBL:KDQ08212.1, ECO:0000313|Proteomes:UP000027195};
RN   [1] {ECO:0000313|Proteomes:UP000027195}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FD-172 SS1 {ECO:0000313|Proteomes:UP000027195};
RX   PubMed=24958869; DOI=10.1073/pnas.1400592111;
RA   Riley R., Salamov A.A., Brown D.W., Nagy L.G., Floudas D., Held B.W.,
RA   Levasseur A., Lombard V., Morin E., Otillar R., Lindquist E.A., Sun H.,
RA   LaButti K.M., Schmutz J., Jabbour D., Luo H., Baker S.E., Pisabarro A.G.,
RA   Walton J.D., Blanchette R.A., Henrissat B., Martin F., Cullen D.,
RA   Hibbett D.S., Grigoriev I.V.;
RT   "Extensive sampling of basidiomycete genomes demonstrates inadequacy of the
RT   white-rot/brown-rot paradigm for wood decay fungi.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:9923-9928(2014).
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.
CC       {ECO:0000256|ARBA:ARBA00037628}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Random hydrolysis of (1->6)-linkages in (1->6)-beta-D-
CC         glucans.; EC=3.2.1.75; Evidence={ECO:0000256|ARBA:ARBA00036633};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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; KL198094; KDQ08212.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A067M8M2; -.
DR   STRING; 930990.A0A067M8M2; -.
DR   HOGENOM; CLU_004624_7_1_1; -.
DR   InParanoid; A0A067M8M2; -.
DR   OrthoDB; 1643216at2759; -.
DR   Proteomes; UP000027195; Unassembled WGS sequence.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0071704; P:organic substance metabolic process; IEA:InterPro.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR001547; Glyco_hydro_5.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR31297; GLUCAN ENDO-1,6-BETA-GLUCOSIDASE B; 1.
DR   PANTHER; PTHR31297:SF39; GLUCAN ENDO-1,6-BETA-GLUCOSIDASE B; 1.
DR   Pfam; PF00150; Cellulase; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361153};
KW   Hydrolase {ECO:0000256|RuleBase:RU361153, ECO:0000313|EMBL:KDQ08212.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027195};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..444
FT                   /note="glucan endo-1,6-beta-glucosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001641086"
FT   DOMAIN          70..361
FT                   /note="Glycoside hydrolase family 5"
FT                   /evidence="ECO:0000259|Pfam:PF00150"
FT   REGION          398..444
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        398..416
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   444 AA;  48520 MW;  3FED5A7AB6168B2B CRC64;
     MLKVLGLSSL VFAARVLAQL PPGVDKIRGV NLGSWFVVEP YMMQDYWDNQ MGAHGACSEW
     DFVKTVGQDA ADKAFQAHWD TMITQDDVNM MKQYGINTVR IPLGFWIIES TKLAGQDYYP
     NGGLNFLTRG LGWLHSAGIA AILDLHAVPG ASTANNAFAG KCTATPGFWA NKNSNFQRAA
     NAIQELTRMA HTNPSWAGVF AIEVLNEPPM DATQTPGYAQ YLQMATAAIR DTEKSLGASN
     PLAVTYMDYN WQYGAPHPNP ADAASGKGPA LYDNHLYYSF GGLINNNAAV DYIANVCNTG
     PDRVKADAQA KNSPLVFGEW WLAERPGCSD CDAQFHKDFA DAQKIAYERD GAGWIFWAWK
     FRGTDQYRSY KDAVAAGFFS SNAATTFNPN VCTKYLSPGN RNQATMGESP ASPQGSRPDS
     LGWRAPEGAP VPSRMRRASA ARYL
//
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