ID A0A9P4UID5_9PEZI Unreviewed; 491 AA.
AC A0A9P4UID5;
DT 13-SEP-2023, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2023, sequence version 1.
DT 10-JUN-2026, entry version 12.
DE RecName: Full=glucan endo-1,3-beta-D-glucosidase {ECO:0000256|ARBA:ARBA00012780};
DE EC=3.2.1.39 {ECO:0000256|ARBA:ARBA00012780};
GN ORFNames=K431DRAFT_341778 {ECO:0000313|EMBL:KAF2716742.1};
OS Polychaeton citri CBS 116435.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Capnodiales; Capnodiaceae; Polychaeton.
OX NCBI_TaxID=1314669 {ECO:0000313|EMBL:KAF2716742.1, ECO:0000313|Proteomes:UP000799441};
RN [1] {ECO:0000313|EMBL:KAF2716742.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CBS 116435 {ECO:0000313|EMBL:KAF2716742.1};
RA Haridas S., Albert R., Binder M., Bloem J., LaButti K., Salamov A.,
RA Andreopoulos B., Baker S., Barry K., Bills G., Bluhm B., Cannon C.,
RA Castanera R., Culley D., Daum C., Ezra D., Gonzalez J., Henrissat B.,
RA Kuo A., Liang C., Lipzen A., Lutzoni F., Magnuson J., Mondo S., Nolan M.,
RA Ohm R., Pangilinan J., Park H.-J., Ramirez L., Alfaro M., Sun H., Tritt A.,
RA Yoshinaga Y., Zwiers L.-H., Turgeon B., Goodwin S., Spatafora J., Crous P.,
RA Grigoriev I.;
RT "101 Dothideomycetes genomes: a test case for predicting lifestyles and
RT emergence of pathogens.";
RL Stud. Mycol. 0:0-0(2020).
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;
CC Evidence={ECO:0000256|ARBA:ARBA00000382};
CC -!- SIMILARITY: Belongs to the PGA52 family.
CC {ECO:0000256|ARBA:ARBA00006055}.
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:KAF2716742.1}.
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DR EMBL; MU003863; KAF2716742.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A9P4UID5; -.
DR OrthoDB; 118256at2759; -.
DR Proteomes; UP000799441; Unassembled WGS sequence.
DR GO; GO:0009277; C:fungal-type cell wall; IEA:TreeGrafter.
DR GO; GO:0042973; F:glucan endo-1,3-beta-D-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR InterPro; IPR018805; YJL171C/Tos1_C.
DR InterPro; IPR018807; YJL171C/Tos1_N.
DR PANTHER; PTHR31737; PROTEIN TOS1; 1.
DR PANTHER; PTHR31737:SF2; PROTEIN TOS1; 1.
DR Pfam; PF10287; YJL171C_Tos1_C; 1.
DR Pfam; PF10290; YJL171C_Tos1_N; 1.
PE 3: Inferred from homology;
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000799441};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..491
FT /note="glucan endo-1,3-beta-D-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5040273194"
FT DOMAIN 37..99
FT /note="Cell wall protein YJL171C/Tos1 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF10290"
FT DOMAIN 222..450
FT /note="Cell wall protein YJL171C/Tos1 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF10287"
FT REGION 197..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..216
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 491 AA; 52733 MW; F1B07AB5EB28BC20 CRC64;
MKYFASTAAI LGLVTIVTAQ GDGCFTEAGN WYCNEVDAIT YTDVGNYNST WKYNKLTEWS
TSCSSEPSNY QGPLSPFDEQ VSLHLRGPIN LKQFAFYAPS SSASKVKSRR AESHLRRHLH
GRNAHAHAHL KRRAEEKRQV GALVTNVVGS VTEVWTNAWN GYTSVDLSNT PATSVAAAPA
SVNTGFHNLK VADVGSDDSS SSAAASSAAS SSETSSVPVP SGNWGRSAYY NAQAGSSSGL
AFLNNKGDNE TSGIFDHVWG SSLSYATTDG CNAASAPQTL EDITFPDGEE FSIFTDQECS
GDDCGVYRTG TVAHKGFDGA NKAFFFEFSM PDSGETAADQ WDIKNAPALW MLNAQIPRTL
QYPPAQYTAC SCWYSGCGEF DIFEVITPGS DKAKSTFHGN KAAGSSDYFK RPTGDAIKVA
AVMYDDKITV RVLDSSYDFP ESLDEDTIAS LAGARTGSSF VKQLLASDTS PSEFCMEGHG
PDQSNVHYGE Y
//
