ID A0A177C9P6_9PLEO Unreviewed; 406 AA.
AC A0A177C9P6;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 17.
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=CC84DRAFT_1260703 {ECO:0000313|EMBL:OAG03572.1};
OS Paraphaeosphaeria sporulosa.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Massarineae; Didymosphaeriaceae;
OC Paraphaeosphaeria.
OX NCBI_TaxID=1460663 {ECO:0000313|EMBL:OAG03572.1, ECO:0000313|Proteomes:UP000077069};
RN [1] {ECO:0000313|EMBL:OAG03572.1, ECO:0000313|Proteomes:UP000077069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AP3s5-JAC2a {ECO:0000313|EMBL:OAG03572.1,
RC ECO:0000313|Proteomes:UP000077069};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) 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.
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KV441554; OAG03572.1; -; Genomic_DNA.
DR RefSeq; XP_018033937.1; XM_018185004.1.
DR AlphaFoldDB; A0A177C9P6; -.
DR STRING; 1460663.A0A177C9P6; -.
DR GeneID; 28768490; -.
DR InParanoid; A0A177C9P6; -.
DR OrthoDB; 1431012at2759; -.
DR Proteomes; UP000077069; Unassembled WGS sequence.
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:OAG03572.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000077069};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..406
FT /note="glucan endo-1,6-beta-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008057914"
FT DOMAIN 96..373
FT /note="Glycoside hydrolase family 5"
FT /evidence="ECO:0000259|Pfam:PF00150"
SQ SEQUENCE 406 AA; 46152 MW; CECAA0541D28AD31 CRC64;
MRGSILSLLT FGSAVSAWLP AERGFFKSEA RSLSIGQGRS ITKRFNPDKI RGVNLGSLFI
VEPWMMGQAW NDMGCGDQKS EFDCVLKLGQ DGADAAFKQH WDTWITEEDL DKMKEYGINA
IRVPVGYWMV EELVDQSEHF PRGGLEYLDR LAGWAASRNM YMNLDLHGAP YSQEIHQPFT
GQYSEEAGFY QTSQYERAYT FLQKMTERIH TTDAYRTTGM IEVLNEPQRT HDSLIPEYYA
TAYGKIRETE ANLGVSDDKK LTIQFMAESW GAGNPRQVLE GKTDVAFDDH RYLKWANIDQ
SKPSYIATSC GDTFGGNDNS PIVVGEWSLA VADNNEQTPE WEPQGNKDWY KQWWGAQVQA
YEKGLGWFFW SWKVQLGDDY RWGYRNAVEA GVIPLSPDEA AGLAKC
//
