ID   E13B2_PAPLA             Reviewed;          21 AA.
AC   P85238;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   25-MAY-2022, entry version 20.
DE   RecName: Full=Glucan endo-1,3-beta-glucosidase 2;
DE            EC=3.2.1.39;
DE   AltName: Full=(1->3)-beta-glucan endohydrolase 2;
DE            Short=(1->3)-beta-glucanase 2;
DE   Flags: Fragment;
OS   Papiliotrema laurentii (Cryptococcus laurentii).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Rhynchogastremataceae; Papiliotrema.
OX   NCBI_TaxID=5418;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE.
RC   STRAIN=RY1;
RA   Dutta D., Gachhui R.;
RL   Submitted (JUL-2007) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-
CC         beta-D-glucans.; EC=3.2.1.39;
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DR   AlphaFoldDB; P85238; -.
DR   GO; GO:0042973; F:glucan endo-1,3-beta-D-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Glycosidase; Hydrolase.
FT   CHAIN           1..>21
FT                   /note="Glucan endo-1,3-beta-glucosidase 2"
FT                   /id="PRO_0000302130"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         21
SQ   SEQUENCE   21 AA;  2087 MW;  E0F0D791CCAD9148 CRC64;
     APGDLLWSDE FDGAAGSAPN P