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Database: UniProt
Entry: A0A179F3Z0_METCM
LinkDB: A0A179F3Z0_METCM
Original site: A0A179F3Z0_METCM 
ID   A0A179F3Z0_METCM        Unreviewed;       430 AA.
AC   A0A179F3Z0;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 20.
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=VFPPC_09937 {ECO:0000313|EMBL:OAQ59829.1};
OS   Pochonia chlamydosporia 170.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Pochonia.
OX   NCBI_TaxID=1380566 {ECO:0000313|EMBL:OAQ59829.1, ECO:0000313|Proteomes:UP000078397};
RN   [1] {ECO:0000313|EMBL:OAQ59829.1, ECO:0000313|Proteomes:UP000078397}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=170 {ECO:0000313|EMBL:OAQ59829.1};
RX   PubMed=27416025;
RA   Wang G., Liu Z., Lin R., Li E., Mao Z., Ling J., Yang Y., Yin W.B., Xie B.;
RT   "Biosynthesis of antibiotic leucinostatins in bio-control fungus
RT   Purpureocillium lilacinum and their inhibition on phytophthora revealed by
RT   genome mining.";
RL   PLoS Pathog. 12:E1005685-E1005685(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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OAQ59829.1}.
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DR   EMBL; LSBJ02000004; OAQ59829.1; -; Genomic_DNA.
DR   RefSeq; XP_018137790.1; XM_018288393.1.
DR   AlphaFoldDB; A0A179F3Z0; -.
DR   STRING; 1380566.A0A179F3Z0; -.
DR   GeneID; 28852387; -.
DR   KEGG; pchm:VFPPC_09937; -.
DR   OrthoDB; 1431012at2759; -.
DR   Proteomes; UP000078397; Chromosome 4.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProt.
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   Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361153};
KW   Hydrolase {ECO:0000256|RuleBase:RU361153, ECO:0000313|EMBL:OAQ59829.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000078397};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..430
FT                   /note="glucan endo-1,6-beta-glucosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5008101204"
FT   DOMAIN          102..355
FT                   /note="Glycoside hydrolase family 5"
FT                   /evidence="ECO:0000259|Pfam:PF00150"
SQ   SEQUENCE   430 AA;  48178 MW;  C3C3721668F3867C CRC64;
     MHLSALVLLF LTNAVSAWLP HERDLEAFNQ TARFEKLGKR FKPSLPNGVT KIRGVNFGGW
     LICEPWMMPN EWGNVMGCGD SASEFDCMRD HYAGGNREAG NQKFENHWRD WINPDTVQSV
     HDVGLNTIRI PIGYWSYTDI VDTASEPFAD GSRMLPYLDA VVQKAADLGI YVIIDLHGAP
     GGQQEDAFTG QINKPAGFFN DYNFGRAEKW LSWMTNRIHT NSAYSTVGMI EVLNEPVSKH
     DAGGRYPAPG EDPGLVQTYY PAALKAVRDA EESLNVPDGK KLHVQFMSSK WDSGDARTVA
     VVANDPMTAF DDHNYIGFAL GSNNGDQYQL MHSACTDSRV VSGQAFEFTG EWSMTSNVDW
     SDGAFFKKFF TAQQQLYEKP GMDGWVYWTW KTELNDPRWT YSYATSLKYV PTDAAGLESN
     VYQDVCNGFT
//
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