ID A0A177C3Q1_9PLEO Unreviewed; 411 AA.
AC A0A177C3Q1;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=glucan 1,3-beta-glucosidase {ECO:0000256|ARBA:ARBA00038929};
DE EC=3.2.1.58 {ECO:0000256|ARBA:ARBA00038929};
GN ORFNames=CC84DRAFT_1220467 {ECO:0000313|EMBL:OAG02105.1};
OS Paraphaeosphaeria sporulosa.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Massarineae; Didymosphaeriaceae;
OC Paraphaeosphaeria.
OX NCBI_TaxID=1460663 {ECO:0000313|EMBL:OAG02105.1, ECO:0000313|Proteomes:UP000077069};
RN [1] {ECO:0000313|EMBL:OAG02105.1, ECO:0000313|Proteomes:UP000077069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AP3s5-JAC2a {ECO:0000313|EMBL:OAG02105.1,
RC ECO:0000313|Proteomes:UP000077069};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Successive hydrolysis of beta-D-glucose units from the non-
CC reducing ends of (1->3)-beta-D-glucans, releasing alpha-glucose.;
CC EC=3.2.1.58; Evidence={ECO:0000256|ARBA:ARBA00036824};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC {ECO:0000256|ARBA:ARBA00005641, ECO:0000256|RuleBase:RU361153}.
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DR EMBL; KV441556; OAG02105.1; -; Genomic_DNA.
DR RefSeq; XP_018032470.1; XM_018183173.1.
DR AlphaFoldDB; A0A177C3Q1; -.
DR STRING; 1460663.A0A177C3Q1; -.
DR GeneID; 28766659; -.
DR InParanoid; A0A177C3Q1; -.
DR OrthoDB; 1431012at2759; -.
DR Proteomes; UP000077069; Unassembled WGS sequence.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProt.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR001547; Glyco_hydro_5.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR31297:SF1; GLUCAN 1,3-BETA-GLUCOSIDASE I_II-RELATED; 1.
DR PANTHER; PTHR31297; GLUCAN ENDO-1,6-BETA-GLUCOSIDASE B; 1.
DR Pfam; PF00150; Cellulase; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE 3: Inferred from homology;
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361153};
KW Hydrolase {ECO:0000256|RuleBase:RU361153, ECO:0000313|EMBL:OAG02105.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000077069};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..411
FT /note="glucan 1,3-beta-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008057678"
FT DOMAIN 77..306
FT /note="Glycoside hydrolase family 5"
FT /evidence="ECO:0000259|Pfam:PF00150"
SQ SEQUENCE 411 AA; 44613 MW; 0D59D82AEC5E2457 CRC64;
MHGSWSSVVA VGLLTLSSNA SPLTPYKRAP SFDYSGSKVR GVNTGGWFVL EPWITPSMFE
GNGAVDEYTL TQELGKDAAK SKLSQHWNSW ITQADFNQMA AAGLNHVRIP IGYWSVIPRD
GEPYVQGAYQ VLGQALDWAQ AAGLKVMIDL HGAAGSQNGF DNSGRYGSVQ WTQGDTVAHT
IKVLNKIRDD HASHPAVSAI ELLNEPMGPN LDMNTVKQFY MDGWGNLRDS KVAIAFHEAF
IGVTSWNDWG AGMANLLLDT HHYEVFNVDQ LGMSPDDHIK SACDFGGQMA SNNKPTISGE
WTGGITDCAK WLNGKNKGAR YDGTFENANA IGSCAGKSSG SVANLSSDDK SNIGRFIEAQ
LEGYEKGAGW IFWTWKTEGA PEWDMQDLMA NGLFPKPVND PSARKYSGIC G
//
