ID   SPR1_SACU7              Reviewed;         445 AA.
AC   Q876J2;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 61.
DE   RecName: Full=Sporulation-specific glucan 1,3-beta-glucosidase;
DE            EC=3.2.1.58;
DE   AltName: Full=Exo-1,3-beta-glucanase;
DE   Flags: Precursor;
GN   Name=SPR1;
OS   Saccharomyces uvarum (strain ATCC 76518 / CBS 7001 / CLIB 283 / NBRC 10550
OS   / MCYC 623 / NCYC 2669 / NRRL Y-11845) (Yeast) (Saccharomyces bayanus var.
OS   uvarum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=659244;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=623-6C / CBS 9787 / CLIB 533;
RX   PubMed=12594514; DOI=10.1038/nature01419;
RA   Langkjaer R.B., Cliften P.F., Johnston M., Piskur J.;
RT   "Yeast genome duplication was followed by asynchronous differentiation of
RT   duplicated genes.";
RL   Nature 421:848-852(2003).
CC   -!- FUNCTION: Probably involved in the processes of spore formation and
CC       contributes to ascospore thermoresistance by participating in the
CC       morphogenesis of ascospore walls. The enzyme may do this by modifying
CC       glucan linkages in the developing ascospore wall, thus strengthening it
CC       or lending it plasticity (By similarity). {ECO:0000250}.
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;
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC       {ECO:0000305}.
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DR   EMBL; AY144819; AAO32383.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q876J2; -.
DR   SMR; Q876J2; -.
DR   CAZy; GH5; Glycoside Hydrolase Family 5.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004338; F:glucan exo-1,3-beta-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR   InterPro; IPR001547; Glyco_hydro_5.
DR   InterPro; IPR018087; Glyco_hydro_5_CS.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   Pfam; PF00150; Cellulase; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS00659; GLYCOSYL_HYDROL_F5; 1.
PE   3: Inferred from homology;
KW   Cell wall biogenesis/degradation; Glycosidase; Hydrolase; Secreted; Signal;
KW   Sporulation.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..445
FT                   /note="Sporulation-specific glucan 1,3-beta-glucosidase"
FT                   /id="PRO_0000007897"
FT   ACT_SITE        233
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        335
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   445 AA;  51556 MW;  B22023ACDED32279 CRC64;
     MVSFKRLTTL ALSFTQLVNC NPVSPKSKDS LQFIYKEKAN VYSEANSQSI REKIRGVNLG
     GWLVLEPYIT PSIFEAFRTN PHNDNGIPVD EYRFCQSLGY EKAKERLYNH WSTFYKEEDF
     AKIASQGFNM VRIPVGYWAF TTLSHDPYVT GEQEYFLDKA VDWARKYGLK VWIDLHGAAG
     SQNGFDNSGL RDSYKFLDEE YLSATMKALT YILSKYSTDI YLDTVIGIEL LNEPLGPVFD
     MERLKNLFLK PAYDYLRNKI MSKQIIVMHD AFQPYNYWDN FLNGDKEEYG VILDHHHYQV
     FSPIELARNM NERIKIACQW GVGTLSEKHW SVAGEFSAAL TDCTKWLNGV GFGARYDGTW
     AKGNDKSYHI GSCANNENVG LWSEERKQNT RKFIEAQLDA FEMTGGWIMW CYKTENSIEW
     DVEKLIQHNL FPQPISDRKH PNQCH