ID   A0A0A7CLA7_9STRA        Unreviewed;       407 AA.
AC   A0A0A7CLA7;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=glucan endo-1,3-beta-D-glucosidase {ECO:0000256|ARBA:ARBA00012780};
DE            EC=3.2.1.39 {ECO:0000256|ARBA:ARBA00012780};
DE   AltName: Full=Endo-1,3-beta-glucanase btgC {ECO:0000256|ARBA:ARBA00043078};
DE   AltName: Full=Laminarinase btgC {ECO:0000256|ARBA:ARBA00042373};
GN   ORFNames=THRCLA_01198 {ECO:0000313|EMBL:OQS06781.1};
OS   Thraustotheca clavata.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC   Thraustotheca.
OX   NCBI_TaxID=74557 {ECO:0000313|EMBL:AIG55417.1};
RN   [1] {ECO:0000313|EMBL:AIG55417.1, ECO:0000313|Proteomes:UP000243217}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 34112 {ECO:0000313|EMBL:AIG55417.1,
RC   ECO:0000313|Proteomes:UP000243217};
RX   PubMed=25527045; DOI=10.1093/gbe/evu276;
RA   Misner I., Blouin N., Leonard G., Richards T.A., Lane C.E.;
RT   "The secreted proteins of Achlya hypogyna and Thraustotheca clavata
RT   identify the ancestral oomycete secretome and reveal gene acquisitions by
RT   horizontal gene transfer.";
RL   Genome Biol. Evol. 7:120-135(2014).
CC   -!- FUNCTION: Glucanases play a role in cell expansion during growth, in
CC       cell-cell fusion during mating, and in spore release during
CC       sporulation. This enzyme may be involved in beta-glucan degradation.
CC       Active on laminarin and lichenan. {ECO:0000256|ARBA:ARBA00037649}.
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DR   EMBL; KM037956; AIG55417.1; -; Genomic_DNA.
DR   EMBL; JNBS01000308; OQS06781.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0A7CLA7; -.
DR   STRING; 74557.A0A0A7CLA7; -.
DR   OrthoDB; 811107at2759; -.
DR   Proteomes; UP000243217; Unassembled WGS sequence.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   CDD; cd00161; RICIN; 1.
DR   Gene3D; 2.80.10.50; -; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR035992; Ricin_B-like_lectins.
DR   InterPro; IPR000772; Ricin_B_lectin.
DR   PANTHER; PTHR16631; GLUCAN 1,3-BETA-GLUCOSIDASE; 1.
DR   PANTHER; PTHR16631:SF17; GLUCAN ENDO-1,3-BETA-GLUCOSIDASE BTGC; 1.
DR   Pfam; PF00652; Ricin_B_lectin; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF50370; Ricin B-like lectins; 1.
DR   PROSITE; PS50231; RICIN_B_LECTIN; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000313|EMBL:OQS06781.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000243217};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..407
FT                   /note="glucan endo-1,3-beta-D-glucosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002037964"
FT   DOMAIN          311..404
FT                   /note="Ricin B lectin"
FT                   /evidence="ECO:0000259|Pfam:PF00652"
SQ   SEQUENCE   407 AA;  45287 MW;  7A1807F03A16F18E CRC64;
     MIALRIVRRY LAASLLLLSL VHPAQSLVGI CYDNYQIEAI HNHFQMIKQR FGAVRTFQTL
     NKGVNAVDAA AKAGLKIAAG VWIRANNYKA DLDAAIDGAR RHPDTVHAIF IGNEDLLGNA
     VSIDFVVLKV QEAKDKLKQA GLKIKIGSVQ TDGDWMRAPQ LAAICDILGV NIYPFFGGSS
     VSASNPIQDL DARWNTVKQQ YGDKVLLTET GWPNDGGNYG AHVSNQANAQ AYFQAFKHWV
     QQGNGGSIPY YFMFHDNPSK HGFERYFGLA DTSAHWKYDF ASLSGDIQAQ SPKKFQIRSN
     DGQIVYQNNG AVMAHKKSNE HTKDENWLYF SDTNTVVNQG NQQCLDLASD QHIQTYMCAS
     NNTNQQWSLR DNHLVQTSFN VCLETNQGNV AVNQCTSIAS NQQFNFE
//