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Database: UniProt
Entry: A0A165Z4F3_EXIGL
LinkDB: A0A165Z4F3_EXIGL
Original site: A0A165Z4F3_EXIGL 
ID   A0A165Z4F3_EXIGL        Unreviewed;       444 AA.
AC   A0A165Z4F3;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 16.
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=EXIGLDRAFT_476250 {ECO:0000313|EMBL:KZV79249.1};
OS   Exidia glandulosa HHB12029.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Auriculariales; Exidiaceae; Exidia.
OX   NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZV79249.1, ECO:0000313|Proteomes:UP000077266};
RN   [1] {ECO:0000313|EMBL:KZV79249.1, ECO:0000313|Proteomes:UP000077266}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HHB12029 {ECO:0000313|EMBL:KZV79249.1,
RC   ECO:0000313|Proteomes:UP000077266};
RX   PubMed=26659563; DOI=10.1093/molbev/msv337;
RA   Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA   Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA   Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA   Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT   "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT   Insights into the Origins of Lignocellulose Decay Capabilities.";
RL   Mol. Biol. Evol. 33:959-970(2016).
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; KV426650; KZV79249.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A165Z4F3; -.
DR   STRING; 1314781.A0A165Z4F3; -.
DR   InParanoid; A0A165Z4F3; -.
DR   OrthoDB; 1643216at2759; -.
DR   Proteomes; UP000077266; 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:KZV79249.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077266};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..444
FT                   /note="glucan endo-1,6-beta-glucosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5007869763"
FT   DOMAIN          109..277
FT                   /note="Glycoside hydrolase family 5"
FT                   /evidence="ECO:0000259|Pfam:PF00150"
SQ   SEQUENCE   444 AA;  47947 MW;  62087E48D23DC21C CRC64;
     MVSAMLSVLV AIAALPLAVL ASPAAIPITP MRQDMRGLNR LWNSTLAGRA IFPSGGIRGV
     NVGAWFVFEP YMAIDEWSSM GGEQCGDCTT CASDEFSLTR KLGQTQANTA FAKHWSTFIT
     QDDVNLMKQY GINSVRIPIG FWIIESTVLS NETYPRGGLN YLRAGCKMFR NAGISVLLDL
     HAAPGAQVSR NPFAGRCVAT PGFWNQANFD RMNNAAAQLT TLIHNEPDNF GSVWGLEALN
     EPPTDTNDTP GYFTFMQGFV NAVRGAENSL GIADANRISA VFMDISWQWG NPQNAANPAF
     AENGGNAYDS HLYYSFGAPC GPNGCVSGTL SSHINFACTG GGGRIQADSD QLNTPSFLGE
     WWLLPLAGTF GNFDQTSARA FGDAQKRGYS PEGGRGGFGW YFWSWKMTNS DSDGSNHMRS
     YKDAVAQGYL PSNAASYFNA NICS
//
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