ID A0A1V8UDH1_9PEZI Unreviewed; 465 AA.
AC A0A1V8UDH1;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=glucan 1,3-beta-glucosidase {ECO:0000256|ARBA:ARBA00038929};
DE EC=3.2.1.58 {ECO:0000256|ARBA:ARBA00038929};
GN ORFNames=B0A51_11283 {ECO:0000313|EMBL:OQO21393.1};
OS Rachicladosporium sp. CCFEE 5018.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Cladosporiales; Cladosporiaceae; Rachicladosporium.
OX NCBI_TaxID=1974281 {ECO:0000313|EMBL:OQO21393.1, ECO:0000313|Proteomes:UP000192386};
RN [1] {ECO:0000313|Proteomes:UP000192386}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCFEE 5018 {ECO:0000313|Proteomes:UP000192386};
RA Coleine C., Masonjones S., Stajich J.E.;
RT "Genomes of endolithic fungi from Antarctica.";
RL Submitted (MAR-2017) 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}.
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:OQO21393.1}.
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DR EMBL; NAEU01000565; OQO21393.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V8UDH1; -.
DR STRING; 1974281.A0A1V8UDH1; -.
DR Proteomes; UP000192386; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000192386};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..465
FT /note="glucan 1,3-beta-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012415701"
FT DOMAIN 66..198
FT /note="Glycoside hydrolase family 5"
FT /evidence="ECO:0000259|Pfam:PF00150"
FT REGION 409..432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 465 AA; 50213 MW; 8BA8209E33C57E11 CRC64;
MLKSGGAWLA AAAAFATGAN AVVRGVNLGG WLVLEPWMTP SIFNVSGTSY DSEWALCNGL
GKQKCLSTLQ NHWSTFYTRD DIKQIQAAGL NSIRIPLGYW AVDLLDFEPY VSGQYQYLSQ
AVQWAKEFDL TVMIDIHGAP GSQNGWEETG IVGGIEFPLN QSNTDRTLNV LKNLTEEFTK
EMYGGAVTNI ELMNEPIFEL AKLQTFYTAG AEVVSVANSS GINTTFHDAF YNPPNWKNYD
PLNMNSGSNG KYLTLDTHQF WAFPPLDTLS VPDILGRICA FGLELKQLDT GILPTIVGEW
SLSTGHTANS TTDSGQDRDK RTWFRELFEA QNAAYTPNGP GQASIGWYFW SWKTEYDIDA
WSYRKGVEQG YIPSNISDPS TYAYPITTDN TGCIDGSFNW QAPEIAQASS SATSSAGSKP
TSTGTATSGS ASAASTTASG AANVSPASGV SAALVIALAY VVCSL
//
