DSS1_YEAST
ID DSS1_YEAST Reviewed; 969 AA.
AC P39112; D6W0B4;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Exoribonuclease II, mitochondrial;
DE Short=RNase II;
DE Short=Ribonuclease II;
DE EC=3.1.13.1;
DE AltName: Full=Deletion of SUV3 suppressor 1;
DE AltName: Full=Mitochondrial biogenesis protein MSU1;
DE Flags: Precursor;
GN Name=DSS1; Synonyms=MSU1; OrderedLocusNames=YMR287C; ORFNames=YM8021.13C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8590460; DOI=10.1007/bf00315775;
RA Dmochowska A., Golik P., Stepien P.P.;
RT "The novel nuclear gene DSS-1 of Saccharomyces cerevisiae is necessary for
RT mitochondrial biogenesis.";
RL Curr. Genet. 28:108-112(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 804-969.
RX PubMed=2061283; DOI=10.1128/jb.173.13.4013-4020.1991;
RA Kang W.K., Matsushita Y., Grohmann L., Graack H.-R., Kitakawa M., Isono K.;
RT "Cloning and analysis of the nuclear gene for YmL33, a protein of the large
RT subunit of the mitochondrial ribosome in Saccharomyces cerevisiae.";
RL J. Bacteriol. 173:4013-4020(1991).
RN [5]
RP PROTEIN SEQUENCE OF 42-62; 133-142; 415-428; 502-514; 702-714 AND 828-837,
RP FUNCTION, AND SUBUNIT.
RX PubMed=12426313; DOI=10.1074/jbc.m208287200;
RA Dziembowski A., Piwowarski J., Hoser R., Minczuk M., Dmochowska A.,
RA Siep M., van der Spek H., Grivell L.A., Stepien P.P.;
RT "The yeast mitochondrial degradosome. Its composition, interplay between
RT RNA helicase and RNase activities and the role in mitochondrial RNA
RT metabolism.";
RL J. Biol. Chem. 278:1603-1611(2003).
RN [6]
RP FUNCTION.
RX PubMed=9829834; DOI=10.1007/s004380050876;
RA Dziembowski A., Malewicz M., Minczuk M., Golik P., Dmochowska A.,
RA Stepien P.P.;
RT "The yeast nuclear gene DSS1, which codes for a putative RNase II, is
RT necessary for the function of the mitochondrial degradosome in processing
RT and turnover of RNA.";
RL Mol. Gen. Genet. 260:108-114(1998).
RN [7]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [8]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 76625 / YPH499;
RX PubMed=14576278; DOI=10.1073/pnas.2135385100;
RA Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E.,
RA Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P.,
RA Pfanner N., Meisinger C.;
RT "The proteome of Saccharomyces cerevisiae mitochondria.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003).
CC -!- FUNCTION: Essential for mitochondrial biogenesis.
CC -!- FUNCTION: Required for intron-independent turnover and processing of
CC mitochondrial RNA. Participates in 3' mtRNA processing where it
CC hydrolyzes single-stranded RNA or partially double-stranded RNA with 3'
CC single-stranded tails.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Exonucleolytic cleavage in the 3'- to 5'-direction to yield
CC nucleoside 5'-phosphates.; EC=3.1.13.1;
CC -!- SUBUNIT: MSU1 and SUV3 are the two components of the mitochondrial
CC degradosome (mtEXO). {ECO:0000269|PubMed:12426313}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000269|PubMed:14576278}.
CC -!- MISCELLANEOUS: Present with 1070 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the RNR ribonuclease family. {ECO:0000305}.
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DR EMBL; U15461; AAC49144.1; -; Genomic_DNA.
DR EMBL; Z49704; CAA89785.1; -; Genomic_DNA.
DR EMBL; D90217; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BK006946; DAA10188.1; -; Genomic_DNA.
DR PIR; S54594; S54594.
DR RefSeq; NP_014014.1; NM_001182794.1.
DR AlphaFoldDB; P39112; -.
DR SMR; P39112; -.
DR BioGRID; 35467; 102.
DR ComplexPortal; CPX-3180; Mitochondrial degradosome complex.
DR DIP; DIP-2936N; -.
DR IntAct; P39112; 6.
DR MINT; P39112; -.
DR STRING; 4932.YMR287C; -.
DR iPTMnet; P39112; -.
DR MaxQB; P39112; -.
DR PaxDb; P39112; -.
DR PRIDE; P39112; -.
DR EnsemblFungi; YMR287C_mRNA; YMR287C; YMR287C.
DR GeneID; 855331; -.
DR KEGG; sce:YMR287C; -.
DR SGD; S000004900; DSS1.
DR VEuPathDB; FungiDB:YMR287C; -.
DR eggNOG; KOG2102; Eukaryota.
DR GeneTree; ENSGT00530000063106; -.
DR HOGENOM; CLU_012624_0_0_1; -.
DR InParanoid; P39112; -.
DR OMA; RTFVIQY; -.
DR BioCyc; YEAST:G3O-32957-MON; -.
DR BRENDA; 3.1.13.1; 984.
DR PRO; PR:P39112; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P39112; protein.
DR GO; GO:0000178; C:exosome (RNase complex); IBA:GO_Central.
DR GO; GO:0045025; C:mitochondrial degradosome; IDA:SGD.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0000175; F:3'-5'-exoribonuclease activity; IBA:GO_Central.
DR GO; GO:0008859; F:exoribonuclease II activity; IDA:SGD.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000957; P:mitochondrial RNA catabolic process; IDA:ComplexPortal.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR001900; RNase_II/R.
DR InterPro; IPR022966; RNase_II/R_CS.
DR Pfam; PF00773; RNB; 1.
DR SMART; SM00955; RNB; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR PROSITE; PS01175; RIBONUCLEASE_II; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Exonuclease; Hydrolase; Mitochondrion; Nuclease;
KW Reference proteome; RNA-binding; Transit peptide.
FT TRANSIT 1..41
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:12426313"
FT CHAIN 42..969
FT /note="Exoribonuclease II, mitochondrial"
FT /id="PRO_0000030820"
FT REGION 28..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..54
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 222
FT /note="H -> R (in Ref. 1; AAC49144)"
FT /evidence="ECO:0000305"
FT CONFLICT 870
FT /note="P -> T (in Ref. 4; D90217)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 969 AA; 110822 MW; E8D898F2DB4EFA2D CRC64;
MVVRRKVHVL LIARSFHSYT PCFRVTTRGK RQRSKSKQQA KVELDHTREL DNDQATETVV
DRSVGPEKDI ESINKDFLQR TKGLEPDIEL KQLPQIKQEF NQRYKDRYVK PSEDWYVNSW
RSLTKPKIPL YKLINSDFQL ITKLKAPNPM EFQPVQLMES PLNVGDFVLL KMRPNELAMC
VSLPSSTMDP RYTFVTIDGT MCFATKNRVL LRIPHKLPAG IHSLIQPESH HKHLPIGTVK
NFSNQTNILP IVARQLITSR YPAQISKLAW KDLPITTKKL QLLHRSLQNY MGPWQIPFFT
LVGLVQKLDL NKALDDKNGI NYLTSLVNNY HTVNDIPINS PTFVSTYWAI MQQQESNLWG
EIHLNTALLS PISVTIIPLK SQHLYYAQVI EKLEANSYRE VNKFVKLVNE RKYRDISALY
PSVIQLLKDF AAGNFHNNGI IVALISKIFR KIERYKDCDI TRDICQDLIN EITPNSIPNP
LLLNMDLALP ASSKLVKWQQ KLYDLTNIEE LQWKKSGTDD DRYDFGDLRV FCIDSETAHE
IDDGVSVKNY GRDGLYTLYI HIADPTSMFP ESTNVDIEGI STDILNVALK RSFTTYLPDT
VVPMLPQSIC HLSDLGKQGQ RTKTISFSVD VKITSKCSGK SIEIMYDSFK IRKGIVSNFP
KATYEDVDRI LGTPNSEASP VKKDLESLSM ISKLLREQRI KNSNAVIFGE GFNKGLVMLN
ADSEGELTEV TFSDQEETLS TILVSEMMIL ANTLTGRYFA ENKIGGVFRC YKQLPLGEVA
QQQYDSMITS TKKGIFPKLK DIVKLSSLLN SSFYTGRPFR HEMIGAKQYL TVTSPLRRFP
DLINHLQIHR HLQKKPLCFN QTQIDSLIWP IQSRADILKR ASRNSSTYWT LNYLKKLTKL
EPERTFDVMV TSVPQNGFTG CVFPDLSFAR GTLKLHPSSM HYPMIGDIVK NCKISKIDCL
EGMLELEKL
