GenomeNet

Database: UniProt
Entry: Q9HER7_PARBR
LinkDB: Q9HER7_PARBR
Original site: Q9HER7_PARBR 
ID   Q9HER7_PARBR            Unreviewed;       416 AA.
AC   Q9HER7;
DT   01-MAR-2001, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2001, sequence version 1.
DT   27-MAR-2024, entry version 69.
DE   RecName: Full=glucan 1,3-beta-glucosidase {ECO:0000256|ARBA:ARBA00038929};
DE            EC=3.2.1.58 {ECO:0000256|ARBA:ARBA00038929};
GN   Name=gp43 {ECO:0000313|EMBL:AAG36681.1};
OS   Paracoccidioides brasiliensis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX   NCBI_TaxID=121759 {ECO:0000313|EMBL:AAG36681.1};
RN   [1] {ECO:0000313|EMBL:AAG36681.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mg5 {ECO:0000313|EMBL:AAG36681.1};
RX   PubMed=11060052;
RA   Morais F.V., Barros T.F., Fukada M.K., Cisalpino P.S., Puccia R.;
RT   "Polymorphism in the gene coding for the immunodominant antigen gp43 from
RT   the pathogenic fungus Paracoccidioides brasiliensis.";
RL   J. Clin. Microbiol. 38:3960-3966(2000).
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   -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC       {ECO:0000256|ARBA:ARBA00005641, ECO:0000256|RuleBase:RU361153}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AY005419; AAG36681.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9HER7; -.
DR   VEuPathDB; FungiDB:PADG_07615; -.
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};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..416
FT                   /note="glucan 1,3-beta-glucosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004326738"
FT   DOMAIN          86..246
FT                   /note="Glycoside hydrolase family 5"
FT                   /evidence="ECO:0000259|Pfam:PF00150"
SQ   SEQUENCE   416 AA;  45850 MW;  DA0380454731E1F4 CRC64;
     MNFSSLNLAL ASCVLAWVCL ASASSHVASH IVPRQAGSAI YGVNIGGWLL LEPWISPSVL
     EAGGSSSVDE YTLSKNLGRD AKGHLSKHWD TFITEDDFKN IAAAGLNHVR IPIGYWAVNP
     IEGEPYVQGQ LDYLDKALVW AKNSNLRVVI DLHGVPGSQN GFDNSGHRGA VNWQKGDTIR
     QTLIAIHTLA IRYANRTDVV DSIELVNKPS IPGGVQVSLL KEYYEDGYHI VRDIDSTVGV
     SISDASLPPR TWNGFLAPKT YKNVYLDTYH NQVFDDIFRT FTIDQHVKLA CSLPHDRLRG
     ADKPLIVKEW SGAMTDCAMY LNGRGIGSRF DGSFPSGKPS GACGARSKGS SSELSAQQKK
     DTLRYIEAQL DAFEVGAGWY FWTWKTEGAP GWDMQDLLNQ KLFPQPIWAR KYGGCR
//
DBGET integrated database retrieval system