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Database: UniProt
Entry: A0A0L0V5D3_9BASI
LinkDB: A0A0L0V5D3_9BASI
Original site: A0A0L0V5D3_9BASI 
ID   A0A0L0V5D3_9BASI        Unreviewed;       533 AA.
AC   A0A0L0V5D3;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, 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=PSTG_12216 {ECO:0000313|EMBL:KNE94421.1};
OS   Puccinia striiformis f. sp. tritici PST-78.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX   NCBI_TaxID=1165861 {ECO:0000313|EMBL:KNE94421.1, ECO:0000313|Proteomes:UP000054564};
RN   [1] {ECO:0000313|Proteomes:UP000054564}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=race PST-78 {ECO:0000313|Proteomes:UP000054564};
RG   The Broad Institute Genome Sequencing Platform;
RA   Cuomo C., Hulbert S., Chen X., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA   Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA   Berlin A.M., Chapman S.B., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Larimer J., McCowan C., Montmayeur A., Murphy C.,
RA   Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA   Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Puccinia striiformis f. sp. tritici PST-78.";
RL   Submitted (MAR-2014) 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   -!- 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:KNE94421.1}.
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DR   EMBL; AJIL01000117; KNE94421.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0L0V5D3; -.
DR   STRING; 1165861.A0A0L0V5D3; -.
DR   OrthoDB; 1431012at2759; -.
DR   Proteomes; UP000054564; 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; 2.
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; 2.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361153};
KW   Hydrolase {ECO:0000256|RuleBase:RU361153};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054564};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..533
FT                   /note="glucan endo-1,6-beta-glucosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5005549636"
FT   DOMAIN          88..235
FT                   /note="Glycoside hydrolase family 5"
FT                   /evidence="ECO:0000259|Pfam:PF00150"
FT   REGION          329..352
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          510..533
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   533 AA;  59055 MW;  2D0E6090BCB1A1E1 CRC64;
     MIFSYASVSL ASLVLLASQA VAKLPASYKY GTNLGGWLLS EPWMNPVEWA EIGGEYCPTD
     SASCAASEWG LARKLGQKPA NEAFLKHWKS WFTQDHVNQL KALKLDHVRI PLGFWIVEEL
     VEAPAELYAQ GGWMELKRGL RQLQDAGFHV TLDMHALPGV SASNQMFAGN VTSDVQFYKD
     HNYQRALTWS AVLTSMSHLD PDFSSVVAIE CINEPLSDAS LTPGLEQYYS DFVTITRVIE
     FAIGVKCEAD LRKSIQRLSQ SKNALAALRA AIPLIVTYAG KGKVDVDPKV LSVLKSSLSN
     PSPVATAPAS TQTGNTHAIP RSKIHPAITS QKDILRRRSP VSDGQNSQSK HKSCLVTVAM
     PKRWQWKGAS NSMANHTLGP AAYDDHMYFA YGGVADPNLK SYLSTMCNQQ HYQDARKIGE
     TPYGHGEFSL ANNFNATHDQ LRQWGDAQRY IFNQEQFWTF WSFRLGKVME PKLSQMMIES
     WSYLGAVEAG IWPKDPTDFY NPSICKPYLK SPGSAAEPVI KPSGQDSRAD SGY
//
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