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Protein

Saccharolysin

Gene

PRD1

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

Functioni

Could be involved in late stage of protein degradation.

Catalytic activityi

Cleavage of Pro-|-Phe and Ala-|-Ala bonds.

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi501 – 5011Zinc; catalyticPROSITE-ProRule annotation
Active sitei502 – 5021PROSITE-ProRule annotation
Metal bindingi505 – 5051Zinc; catalyticPROSITE-ProRule annotation
Metal bindingi508 – 5081Zinc; catalyticPROSITE-ProRule annotation

GO - Molecular functioni

  • metal ion binding Source: UniProtKB-KW
  • metalloendopeptidase activity Source: SGD

GO - Biological processi

  • peptide metabolic process Source: GO_Central
  • proteolysis Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciYEAST:YCL057W-MONOMER.

Protein family/group databases

MEROPSiM03.003.

Names & Taxonomyi

Protein namesi
Recommended name:
Saccharolysin (EC:3.4.24.37)
Alternative name(s):
Oligopeptidase YSCD
Protease D
Proteinase yscD
Gene namesi
Name:PRD1
Ordered Locus Names:YCL057W
ORF Names:YCL57W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome III

Organism-specific databases

EuPathDBiFungiDB:YCL057W.
SGDiS000000562. PRD1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: SGD
  • fungal-type vacuole Source: SGD
  • Golgi apparatus Source: SGD
  • mitochondrial intermembrane space Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 712712SaccharolysinPRO_0000078156Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei73 – 731PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP25375.

PTM databases

iPTMnetiP25375.

Interactioni

Protein-protein interaction databases

BioGridi30929. 6 interactions.
DIPiDIP-4938N.
IntActiP25375. 1 interaction.
MINTiMINT-542010.

Structurei

3D structure databases

ProteinModelPortaliP25375.
SMRiP25375. Positions 31-710.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M3 family.Curated

Phylogenomic databases

GeneTreeiENSGT00550000074738.
HOGENOMiHOG000245985.
InParanoidiP25375.
KOiK01405.
OMAiSYTVQRN.
OrthoDBiEOG7C2R8S.

Family and domain databases

Gene3Di1.10.1370.10. 2 hits.
1.20.1050.40. 1 hit.
3.40.390.10. 1 hit.
InterProiIPR024079. MetalloPept_cat_dom.
IPR024077. Neurolysin/TOP_dom2.
IPR024080. Neurolysin/TOP_N.
IPR001567. Pept_M3A_M3B.
[Graphical view]
PfamiPF01432. Peptidase_M3. 1 hit.
[Graphical view]
PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P25375-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRLLLCKNWF ASPVISPLLY TRSLYSMANT TSFPIAPQAP PNWSFTPSDI
60 70 80 90 100
SGKTNEIINN SNNFYDSMSK VESPSVSNFV EPFMKFENEL GPIINQLTFL
110 120 130 140 150
QHVSSDKEIR DASVNSSMKL DELNIDLSLR HDIFLQFARV WQDVQSKADS
160 170 180 190 200
VERETFKYVE KSYKDYIHSG LELDEGNRLK IKEIKKKISV NSINFSKNLG
210 220 230 240 250
EQKEYITFTK EQLEGVPDSI LTQFETIKSD KDSNETLYKV TFKYPDIFPV
260 270 280 290 300
MKLASSAQTR KQAFLADQNK VPENEAILLD TLKLRDELAS LLGYDTYANY
310 320 330 340 350
NLYDKMAEDS TTVMNFLNDL KDKLIPLGRK ELQVLQDMKA EDVKKLNQGA
360 370 380 390 400
DPNYYIWDHR YYDNKYLLEN FNVDLEKISE YFPLEATITG MLEIYETLFN
410 420 430 440 450
LKFIETKDSQ NKSVWHDDVK QIAVWNMDDP KSPNFVGWIY FDLHPRDGKY
460 470 480 490 500
GHAANFGLSS SFMIDDTTRS YPVTALVCNF SKSTKDKPSL LKHNEIVTFF
510 520 530 540 550
HELGHGIHDL VGQNKESRFN GPGSVPWDFV EAPSQMLEFW TWNKNELINL
560 570 580 590 600
SSHYKTGEKI PESLINSLIK TKHVNGALFT LRQLHFGLFD MKVHTCKDLQ
610 620 630 640 650
NLSICDTWNQ LRQDISLISN GGTLSKGYDS FGHIMSDSYS AGYYGYLWAE
660 670 680 690 700
VFATDMYHTK FAKDPLNAKN GIQYRDIVLA RGGLYDINDN LKEFLGREPS
710
KDAFLKELGL QN
Length:712
Mass (Da):81,934
Last modified:May 1, 1992 - v1
Checksum:i340910B7FDAFBE37
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti384 – 3841L → P in AAU09678 (PubMed:17322287).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X76504 Genomic DNA. Translation: CAA54039.1.
X59720 Genomic DNA. Translation: CAA42388.1.
AY723761 Genomic DNA. Translation: AAU09678.1.
BK006937 Genomic DNA. Translation: DAA07429.1.
PIRiS19387.
RefSeqiNP_009874.1. NM_001178701.1.

Genome annotation databases

EnsemblFungiiCAA42388; CAA42388; CAA42388.
YCL057W; YCL057W; YCL057W.
GeneIDi850301.
KEGGisce:YCL057W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X76504 Genomic DNA. Translation: CAA54039.1.
X59720 Genomic DNA. Translation: CAA42388.1.
AY723761 Genomic DNA. Translation: AAU09678.1.
BK006937 Genomic DNA. Translation: DAA07429.1.
PIRiS19387.
RefSeqiNP_009874.1. NM_001178701.1.

3D structure databases

ProteinModelPortaliP25375.
SMRiP25375. Positions 31-710.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi30929. 6 interactions.
DIPiDIP-4938N.
IntActiP25375. 1 interaction.
MINTiMINT-542010.

Protein family/group databases

MEROPSiM03.003.

PTM databases

iPTMnetiP25375.

Proteomic databases

MaxQBiP25375.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCAA42388; CAA42388; CAA42388.
YCL057W; YCL057W; YCL057W.
GeneIDi850301.
KEGGisce:YCL057W.

Organism-specific databases

EuPathDBiFungiDB:YCL057W.
SGDiS000000562. PRD1.

Phylogenomic databases

GeneTreeiENSGT00550000074738.
HOGENOMiHOG000245985.
InParanoidiP25375.
KOiK01405.
OMAiSYTVQRN.
OrthoDBiEOG7C2R8S.

Enzyme and pathway databases

BioCyciYEAST:YCL057W-MONOMER.

Miscellaneous databases

PROiP25375.

Family and domain databases

Gene3Di1.10.1370.10. 2 hits.
1.20.1050.40. 1 hit.
3.40.390.10. 1 hit.
InterProiIPR024079. MetalloPept_cat_dom.
IPR024077. Neurolysin/TOP_dom2.
IPR024080. Neurolysin/TOP_N.
IPR001567. Pept_M3A_M3B.
[Graphical view]
PfamiPF01432. Peptidase_M3. 1 hit.
[Graphical view]
PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Proteinase yscD (oligopeptidase yscD). Structure, function and relationship of the yeast enzyme with mammalian thimet oligopeptidase (metalloendopeptidase, EP 24.15)."
    Buechler M., Tisljar U., Wolf D.H.
    Eur. J. Biochem. 219:627-639(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The complete DNA sequence of yeast chromosome III."
    Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M., Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G., Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A., Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M.
    , Carcano C., Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M., Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C., Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F., Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C., Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E., Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P., Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J., Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P., Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M., Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P., Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G., Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E., Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F., Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L., Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J., Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M., Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A., Richterich P., Roberts A.B., Rodriguez F., Sanz E., Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J., Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I., Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M., Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M., Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D., Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K., Sgouros J.G.
    Nature 357:38-46(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  6. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
    Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
    J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-73, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  7. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-73, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-73, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPRTD_YEAST
AccessioniPrimary (citable) accession number: P25375
Secondary accession number(s): D6VQW0, E9P942
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: July 6, 2016
This is version 142 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 8910 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase 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 III
    Yeast (Saccharomyces cerevisiae) chromosome III: entries and gene names

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 one 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.