Reviewed, UniProtKB/Swiss-Prot P25375 (PRTD_YEAST)

Names and origin

Protein names

Recommended name:
    Saccharolysin
    EC=3.4.24.37
Alternative name(s):
    Protease D
    Proteinase yscD
    Oligopeptidase YSCD

Gene names

Name:	PRD1
Ordered Locus Names:	YCL057W
ORF Names:	YCL57W

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	712 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Could be involved in late stage of protein degradation.
Catalytic activity	Cleavage of Pro-|-Phe and Ala-|-Ala bonds.
Cofactor	Binds 1 zinc ion By similarity.
Subcellular location	Cytoplasm.
Miscellaneous	Present with 8910 molecules/cell in log phase SD medium. Ref.3
Sequence similarities	Belongs to the peptidase M3 family.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Metal-binding Zinc
Molecular function	Hydrolase Metalloprotease Protease
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	proteolysis Ref.1 Inferred from direct assay. Source: SGD
Cellular component	mitochondrial intermembrane space Ref.1 Inferred from direct assay. Source: SGD
Molecular function	metalloendopeptidase activity Ref.1 Inferred from direct assay. Source: SGD zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 712	712	Saccharolysin		PRO_0000078156
Sites
	Active site	502	1	By similarity
	Metal binding	501	1	Zinc; catalytic By similarity
	Metal binding	505	1	Zinc; catalytic By similarity
	Metal binding	508	1	Zinc; catalytic By similarity
Amino acid modifications
	Modified residue	73	1	Phosphoserine Ref.4 Ref.5
	Modified residue	75	1	Phosphoserine Ref.5

Sequences

	Sequence		Length	Mass (Da)
	P25375-1 [UniParc]. Last modified May 1, 1992. Version 1. Checksum: 340910B7FDAFBE37	FASTA	712	81,934
	10 20 30 40 50 60 MRLLLCKNWF ASPVISPLLY TRSLYSMANT TSFPIAPQAP PNWSFTPSDI SGKTNEIINN 70 80 90 100 110 120 SNNFYDSMSK VESPSVSNFV EPFMKFENEL GPIINQLTFL QHVSSDKEIR DASVNSSMKL 130 140 150 160 170 180 DELNIDLSLR HDIFLQFARV WQDVQSKADS VERETFKYVE KSYKDYIHSG LELDEGNRLK 190 200 210 220 230 240 IKEIKKKISV NSINFSKNLG EQKEYITFTK EQLEGVPDSI LTQFETIKSD KDSNETLYKV 250 260 270 280 290 300 TFKYPDIFPV MKLASSAQTR KQAFLADQNK VPENEAILLD TLKLRDELAS LLGYDTYANY 310 320 330 340 350 360 NLYDKMAEDS TTVMNFLNDL KDKLIPLGRK ELQVLQDMKA EDVKKLNQGA DPNYYIWDHR 370 380 390 400 410 420 YYDNKYLLEN FNVDLEKISE YFPLEATITG MLEIYETLFN LKFIETKDSQ NKSVWHDDVK 430 440 450 460 470 480 QIAVWNMDDP KSPNFVGWIY FDLHPRDGKY GHAANFGLSS SFMIDDTTRS YPVTALVCNF 490 500 510 520 530 540 SKSTKDKPSL LKHNEIVTFF HELGHGIHDL VGQNKESRFN GPGSVPWDFV EAPSQMLEFW 550 560 570 580 590 600 TWNKNELINL SSHYKTGEKI PESLINSLIK TKHVNGALFT LRQLHFGLFD MKVHTCKDLQ 610 620 630 640 650 660 NLSICDTWNQ LRQDISLISN GGTLSKGYDS FGHIMSDSYS AGYYGYLWAE VFATDMYHTK 670 680 690 700 710 FAKDPLNAKN GIQYRDIVLA RGGLYDINDN LKEFLGREPS KDAFLKELGL QN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 8307027] [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: 1574125] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[3]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[4]	"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: 17330950] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-73, MASS SPECTROMETRY.
[5]	"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: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-73 AND SER-75, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X76504 Genomic DNA. Translation: CAA54039.1. X59720 Genomic DNA. Translation: CAA42388.1.
PIR	S19387.
RefSeq	NP_009874.1.
3D structure databases
HSSP	HSSP built from PDB template 1I1I based on UniProtKB P42676.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:4938N.
IntAct	P25375. 2 interactions.
Protein family/group databases
MEROPS	M03.003.
Proteomic databases
PeptideAtlas	P25375.
Genome annotation databases
Ensembl	YCL057W. Saccharomyces cerevisiae. [Contig view]
GeneID	850301.
GenomeReviews	Gene locus YCL057W in contig X59720_GR.
KEGG	sce:YCL057W.
NMPDR	fig|4932.3.peg.594.
Organism-specific databases
CYGD	YCL057w.
SGD	S000000562. PRD1.
Yeast-GFP	Search...
Phylogenomic databases
HOGENOM	P25375.
OMA	P25375. EQTKCVY.
Enzyme and pathway databases
BRENDA	3.4.24.37. 250.
Gene expression databases
ArrayExpress	P25375.
GermOnline	YCL057W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR001567. Pept_M3A_M3B. IPR006025. Pept_M_Zn_BS. [Graphical view]
Pfam	PF01432. Peptidase_M3. 1 hit. [Graphical view]
PROSITE	PS00142. ZINC_PROTEASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	965679.

Entry information

Entry name

PRTD_YEAST

Accession

Primary (citable) accession number: P25375

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1992
Last sequence update:	May 1, 1992
Last modified:	June 16, 2009
This is version 82 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)