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Protein

Sporulation-specific glucan 1,3-beta-glucosidase

Gene

SPR1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Probably involved in the processes of spore formation and contributes to ascospore thermoresistance by participating in the morphogenesis of ascospore walls. The enzyme may do this by modifying glucan linkages in the developing ascospore wall, thus strengthening it or lending it plasticity.

Catalytic activityi

Successive hydrolysis of beta-D-glucose units from the non-reducing ends of (1->3)-beta-D-glucans, releasing alpha-glucose.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei233 – 2331Proton donorBy similarity
Active sitei335 – 3351NucleophileBy similarity

GO - Molecular functioni

  • glucan exo-1,3-beta-glucosidase activity Source: SGD

GO - Biological processi

  • ascospore formation Source: SGD
  • carbohydrate metabolic process Source: InterPro
  • cell wall organization Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Cell wall biogenesis/degradation, Sporulation

Enzyme and pathway databases

BioCyciYEAST:YOR190W-MONOMER.

Protein family/group databases

CAZyiGH5. Glycoside Hydrolase Family 5.
mycoCLAPiEXG5C_YEAST.

Names & Taxonomyi

Protein namesi
Recommended name:
Sporulation-specific glucan 1,3-beta-glucosidase (EC:3.2.1.58)
Alternative name(s):
Exo-1,3-beta-glucanase
Gene namesi
Name:SPR1
Synonyms:SSG1
Ordered Locus Names:YOR190W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome XV

Organism-specific databases

CYGDiYOR190w.
EuPathDBiFungiDB:YOR190W.
SGDiS000005716. SPR1.

Subcellular locationi

GO - Cellular componenti

  • ascospore wall Source: SGD
  • extracellular region Source: UniProtKB-SubCell
  • fungal-type cell wall Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Sequence AnalysisAdd
BLAST
Chaini22 – 445424Sporulation-specific glucan 1,3-beta-glucosidasePRO_0000007898Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi201 – 2011N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Expressioni

Developmental stagei

Late stages of sporulation, during ascospore wall formation. Probably functions before partitioning of nuclei or is distributed to developing ascospores prior to the completion of pro-spore walls.

Interactioni

Protein-protein interaction databases

BioGridi34585. 6 interactions.
DIPiDIP-3910N.
MINTiMINT-487637.
STRINGi4932.YOR190W.

Structurei

3D structure databases

ProteinModelPortaliP32603.
SMRiP32603. Positions 42-444.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG2730.
GeneTreeiENSGT00390000009809.
HOGENOMiHOG000114462.
InParanoidiP32603.
KOiK01210.
OMAiIANTRRF.
OrthoDBiEOG7JT75H.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR001547. Glyco_hydro_5.
IPR018087. Glyco_hydro_5_CS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00150. Cellulase. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
PROSITEiPS00659. GLYCOSYL_HYDROL_F5. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P32603-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVSFRGLTTL TLLFTKLVNC NPVSTKNRDS IQFIYKEKDS IYSAINNQAI
60 70 80 90 100
NEKIHGVNLG GWLVLEPYIT PSLFETFRTN PYNDDGIPVD EYHFCEKLGY
110 120 130 140 150
EKAKERLYSH WSTFYKEEDF AKIASQGFNL VRIPIGYWAF TTLSHDPYVT
160 170 180 190 200
AEQEYFLDRA IDWARKYGLK VWIDLHGAAG SQNGFDNSGL RDSYKFLEDE
210 220 230 240 250
NLSATMKALT YILSKYSTDV YLDTVIGIEL LNEPLGPVID MERLKNLLLK
260 270 280 290 300
PAYDYLRNKI NSNQIIVIHD AFQPYHYWDG FLNDEKNEYG VIIDHHHYQV
310 320 330 340 350
FSQVELTRKM NERIKIACQW GKDAVSEKHW SVAGEFSAAL TDCTKWLNGV
360 370 380 390 400
GLGARYDGSW TKDNEKSHYI NTCANNENIA LWPEERKQNT RKFIEAQLDA
410 420 430 440
FEMTGGWIMW CYKTENSIEW DVEKLIQLNI FPQPINDRKY PNQCH
Length:445
Mass (Da):51,809
Last modified:October 1, 1993 - v1
Checksum:i0948A6E4703D41D4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S52935 Genomic DNA. Translation: AAB24895.1.
X59259 Genomic DNA. Translation: CAA41952.1.
Z75098 Genomic DNA. Translation: CAA99399.1.
AY723868 Genomic DNA. Translation: AAU09785.1.
BK006948 Genomic DNA. Translation: DAA10962.1.
PIRiA40639.
RefSeqiNP_014833.3. NM_001183609.3.

Genome annotation databases

EnsemblFungiiYOR190W; YOR190W; YOR190W.
GeneIDi854362.
KEGGisce:YOR190W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S52935 Genomic DNA. Translation: AAB24895.1.
X59259 Genomic DNA. Translation: CAA41952.1.
Z75098 Genomic DNA. Translation: CAA99399.1.
AY723868 Genomic DNA. Translation: AAU09785.1.
BK006948 Genomic DNA. Translation: DAA10962.1.
PIRiA40639.
RefSeqiNP_014833.3. NM_001183609.3.

3D structure databases

ProteinModelPortaliP32603.
SMRiP32603. Positions 42-444.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34585. 6 interactions.
DIPiDIP-3910N.
MINTiMINT-487637.
STRINGi4932.YOR190W.

Protein family/group databases

CAZyiGH5. Glycoside Hydrolase Family 5.
mycoCLAPiEXG5C_YEAST.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYOR190W; YOR190W; YOR190W.
GeneIDi854362.
KEGGisce:YOR190W.

Organism-specific databases

CYGDiYOR190w.
EuPathDBiFungiDB:YOR190W.
SGDiS000005716. SPR1.

Phylogenomic databases

eggNOGiCOG2730.
GeneTreeiENSGT00390000009809.
HOGENOMiHOG000114462.
InParanoidiP32603.
KOiK01210.
OMAiIANTRRF.
OrthoDBiEOG7JT75H.

Enzyme and pathway databases

BioCyciYEAST:YOR190W-MONOMER.

Miscellaneous databases

NextBioi976473.
PROiP32603.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR001547. Glyco_hydro_5.
IPR018087. Glyco_hydro_5_CS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00150. Cellulase. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
PROSITEiPS00659. GLYCOSYL_HYDROL_F5. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The Saccharomyces cerevisiae SPR1 gene encodes a sporulation-specific exo-1,3-beta-glucanase which contributes to ascospore thermoresistance."
    Muthukumar G., Suhng S.-H., Magee P.T., Jewell R.D., Primerano D.A.
    J. Bacteriol. 175:386-394(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "SSG1, a gene encoding a sporulation-specific 1,3-beta-glucanase in Saccharomyces cerevisiae."
    San Segundo P., Correa J., Vazquez de Aldana C.R., del Rey F.
    J. Bacteriol. 175:3823-3837(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: S288c / GRF88.
  3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."
    Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D.
    , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.
    Nature 387:98-102(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.

Entry informationi

Entry nameiSPR1_YEAST
AccessioniPrimary (citable) accession number: P32603
Secondary accession number(s): D6W2P6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: June 24, 2015
This is version 129 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XV
    Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.