P39112 (DSS1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Exoribonuclease II, mitochondrial
Short name=RNase II
Short name=Ribonuclease II
EC=3.1.13.1

Alternative name(s):
Deletion of SUV3 suppressor 1
Mitochondrial biogenesis protein MSU1

Gene names

Name:	DSS1
Synonyms:	MSU1
Ordered Locus Names:	YMR287C
ORF Names:	YM8021.13C

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	969 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Essential for mitochondrial biogenesis. Ref.5 Ref.6 Required for intron-independent turnover and processing of mitochondrial RNA. Participates in 3' mtRNA processing where it hydrolyzes single-stranded RNA or partially double-stranded RNA with 3' single-stranded tails. Ref.5 Ref.6
Catalytic activity	Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Subunit structure	MSU1 and SUV3 are the two components of the mitochondrial degradosome (mtEXO). Ref.5
Subcellular location	Mitochondrion matrix Ref.8.
Miscellaneous	Present with 1070 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the RNR ribonuclease family.

Ontologies

Keywords
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	RNA-binding
Molecular function	Exonuclease Hydrolase Nuclease
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	mitochondrial RNA catabolic process Inferred from mutant phenotype Ref.5Ref.6. Source: SGD
Cellular_component	mitochondrial degradosome Inferred from direct assay Ref.5. Source: SGD mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	RNA binding Inferred from electronic annotation. Source: UniProtKB-KW exoribonuclease II activity Inferred from direct assay Ref.5PubMed 17658549. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 41	41	Mitochondrion Ref.5
	Chain	42 – 969	928	Exoribonuclease II, mitochondrial		PRO_0000030820
Experimental info
	Sequence conflict	222	1	H → R in AAC49144. Ref.1
	Sequence conflict	870	1	P → T in D90217. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	P39112 [UniParc]. Last modified October 1, 1996. Version 2. Checksum: E8D898F2DB4EFA2D	FASTA	969	110,822
	10 20 30 40 50 60 MVVRRKVHVL LIARSFHSYT PCFRVTTRGK RQRSKSKQQA KVELDHTREL DNDQATETVV 70 80 90 100 110 120 DRSVGPEKDI ESINKDFLQR TKGLEPDIEL KQLPQIKQEF NQRYKDRYVK PSEDWYVNSW 130 140 150 160 170 180 RSLTKPKIPL YKLINSDFQL ITKLKAPNPM EFQPVQLMES PLNVGDFVLL KMRPNELAMC 190 200 210 220 230 240 VSLPSSTMDP RYTFVTIDGT MCFATKNRVL LRIPHKLPAG IHSLIQPESH HKHLPIGTVK 250 260 270 280 290 300 NFSNQTNILP IVARQLITSR YPAQISKLAW KDLPITTKKL QLLHRSLQNY MGPWQIPFFT 310 320 330 340 350 360 LVGLVQKLDL NKALDDKNGI NYLTSLVNNY HTVNDIPINS PTFVSTYWAI MQQQESNLWG 370 380 390 400 410 420 EIHLNTALLS PISVTIIPLK SQHLYYAQVI EKLEANSYRE VNKFVKLVNE RKYRDISALY 430 440 450 460 470 480 PSVIQLLKDF AAGNFHNNGI IVALISKIFR KIERYKDCDI TRDICQDLIN EITPNSIPNP 490 500 510 520 530 540 LLLNMDLALP ASSKLVKWQQ KLYDLTNIEE LQWKKSGTDD DRYDFGDLRV FCIDSETAHE 550 560 570 580 590 600 IDDGVSVKNY GRDGLYTLYI HIADPTSMFP ESTNVDIEGI STDILNVALK RSFTTYLPDT 610 620 630 640 650 660 VVPMLPQSIC HLSDLGKQGQ RTKTISFSVD VKITSKCSGK SIEIMYDSFK IRKGIVSNFP 670 680 690 700 710 720 KATYEDVDRI LGTPNSEASP VKKDLESLSM ISKLLREQRI KNSNAVIFGE GFNKGLVMLN 730 740 750 760 770 780 ADSEGELTEV TFSDQEETLS TILVSEMMIL ANTLTGRYFA ENKIGGVFRC YKQLPLGEVA 790 800 810 820 830 840 QQQYDSMITS TKKGIFPKLK DIVKLSSLLN SSFYTGRPFR HEMIGAKQYL TVTSPLRRFP 850 860 870 880 890 900 DLINHLQIHR HLQKKPLCFN QTQIDSLIWP IQSRADILKR ASRNSSTYWT LNYLKKLTKL 910 920 930 940 950 960 EPERTFDVMV TSVPQNGFTG CVFPDLSFAR GTLKLHPSSM HYPMIGDIVK NCKISKIDCL EGMLELEKL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The novel nuclear gene DSS-1 of Saccharomyces cerevisiae is necessary for mitochondrial biogenesis." Dmochowska A., Golik P., Stepien P.P. Curr. Genet. 28:108-112(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII." Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T., Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P. , Skelton J., Walsh S.V., Whitehead S., Barrell B.G. Nature 387:90-93(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"Cloning and analysis of the nuclear gene for YmL33, a protein of the large subunit of the mitochondrial ribosome in Saccharomyces cerevisiae." Kang W.K., Matsushita Y., Grohmann L., Graack H.-R., Kitakawa M., Isono K. J. Bacteriol. 173:4013-4020(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 804-969.
[5]	"The yeast mitochondrial degradosome. Its composition, interplay between RNA helicase and RNase activities and the role in mitochondrial RNA metabolism." Dziembowski A., Piwowarski J., Hoser R., Minczuk M., Dmochowska A., Siep M., van der Spek H., Grivell L.A., Stepien P.P. J. Biol. Chem. 278:1603-1611(2003) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 42-62; 133-142; 415-428; 502-514; 702-714 AND 828-837, FUNCTION, SUBUNIT.
[6]	"The yeast nuclear gene DSS1, which codes for a putative RNase II, is necessary for the function of the mitochondrial degradosome in processing and turnover of RNA." Dziembowski A., Malewicz M., Minczuk M., Golik P., Dmochowska A., Stepien P.P. Mol. Gen. Genet. 260:108-114(1998) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[7]	"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] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[8]	"The proteome of Saccharomyces cerevisiae mitochondria." Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E., Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P., Pfanner N., Meisinger C. Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY. Strain: ATCC 76625 / YPH499.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U15461 Genomic DNA. Translation: AAC49144.1. Z49704 Genomic DNA. Translation: CAA89785.1. D90217 Genomic DNA. No translation available. BK006946 Genomic DNA. Translation: DAA10188.1.
PIR	S54594.
RefSeq	NP_014014.1. NM_001182794.1.
3D structure databases
ProteinModelPortal	P39112.
SMR	P39112. Positions 522-895.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-2936N.
IntAct	P39112. 3 interactions.
MINT	MINT-547765.
STRING	4932.YMR287C.
Proteomic databases
PaxDb	P39112.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YMR287C; YMR287C; YMR287C.
GeneID	855331.
KEGG	sce:YMR287C.
Organism-specific databases
CYGD	YMR287c.
SGD	S000004900. DSS1.
Phylogenomic databases
eggNOG	COG0557.
OMA	VFCIDSE.
OrthoDB	EOG4FBN29.
Enzyme and pathway databases
BioCyc	YEAST:G3O-32957-MONOMER.
BRENDA	3.1.13.1. 984.
Gene expression databases
Genevestigator	P39112.
GermOnline	YMR287C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR001900. RNase_II/R. IPR022966. RNase_II/R_CS. [Graphical view]
Pfam	PF00773. RNB. 1 hit. [Graphical view]
SMART	SM00955. RNB. 1 hit. [Graphical view]
PROSITE	PS01175. RIBONUCLEASE_II. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	979055.

Entry information

Entry name

DSS1_YEAST

Accession

Primary (citable) accession number: P39112
Secondary accession number(s): D6W0B4

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	October 1, 1996
Last modified:	May 29, 2013
This is version 94 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program