ID A0A067CWR7_SAPPC Unreviewed; 407 AA.
AC A0A067CWR7;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 24-JAN-2024, entry version 26.
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=SPRG_01025 {ECO:0000313|EMBL:KDO34963.1};
OS Saprolegnia parasitica (strain CBS 223.65).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Saprolegnia.
OX NCBI_TaxID=695850 {ECO:0000313|EMBL:KDO34963.1, ECO:0000313|Proteomes:UP000030745};
RN [1] {ECO:0000313|EMBL:KDO34963.1, ECO:0000313|Proteomes:UP000030745}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 223.65 {ECO:0000313|EMBL:KDO34963.1,
RC ECO:0000313|Proteomes:UP000030745};
RX PubMed=23785293;
RA Jiang R.H., de Bruijn I., Haas B.J., Belmonte R., Lobach L., Christie J.,
RA van den Ackerveken G., Bottin A., Bulone V., Diaz-Moreno S.M., Dumas B.,
RA Fan L., Gaulin E., Govers F., Grenville-Briggs L.J., Horner N.R.,
RA Levin J.Z., Mammella M., Meijer H.J., Morris P., Nusbaum C., Oome S.,
RA Phillips A.J., van Rooyen D., Rzeszutek E., Saraiva M., Secombes C.J.,
RA Seidl M.F., Snel B., Stassen J.H., Sykes S., Tripathy S., van den Berg H.,
RA Vega-Arreguin J.C., Wawra S., Young S.K., Zeng Q., Dieguez-Uribeondo J.,
RA Russ C., Tyler B.M., van West P.;
RT "Distinctive expansion of potential virulence genes in the genome of the
RT oomycete fish pathogen Saprolegnia parasitica.";
RL PLoS Genet. 9:E1003272-E1003272(2013).
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; KK583190; KDO34963.1; -; Genomic_DNA.
DR RefSeq; XP_012194617.1; XM_012339227.1.
DR AlphaFoldDB; A0A067CWR7; -.
DR STRING; 695850.A0A067CWR7; -.
DR EnsemblProtists; KDO34963; KDO34963; SPRG_01025.
DR GeneID; 24123638; -.
DR KEGG; spar:SPRG_01025; -.
DR VEuPathDB; FungiDB:SPRG_01025; -.
DR OMA; DQHFATI; -.
DR OrthoDB; 811107at2759; -.
DR Proteomes; UP000030745; Unassembled WGS sequence.
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 SMART; SM00458; RICIN; 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 Reference proteome {ECO:0000313|Proteomes:UP000030745};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..407
FT /note="glucan endo-1,3-beta-D-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001638166"
FT DOMAIN 284..407
FT /note="Ricin B lectin"
FT /evidence="ECO:0000259|SMART:SM00458"
SQ SEQUENCE 407 AA; 44116 MW; D913F4B782A447C6 CRC64;
MVRVLAASLA LLTAVVVAAG NATRGVCYDT YDIDHIDQHF ATIKERFTAV RTFQSIAKGV
NVIDAAAKAG LQIAAGVWIR ANYTADLQAA IDGARRHPDA VHAIFMGNED LFHNAMSVET
VVAKVHEAKD RLRQAGLAHI KVGSVQMDGD WLRAPALVAA CDVVGVNIYA FFGGASISWT
NPVMDLDARW KNLVRLYGPD KLTITETGWP HDGGNNGPHI SNRENAIAYY QSFVQWTQRG
NGGALPYYFM FHDNPSKGGF EANFGLAGVD GRWKFDLAAP FTGPRTFSIV SSHGQSVGAL
HGGLRAHQAA SPPSADDLWQ LRGDVLVNQG GQQPCLDVSR NGNNNNQLTV ALYPCTANNA
NQRWRQEASR LVHATYGVCL DVDPTQGNKV QVFACVNDAP NQRFSFV
//
