RPM2_YEAST
ID RPM2_YEAST Reviewed; 1202 AA.
AC Q02773; D6W0J4;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Ribonuclease P protein component, mitochondrial;
DE Short=RNase P;
DE EC=3.1.26.5;
DE Flags: Precursor;
GN Name=RPM2; OrderedLocusNames=YML091C;
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, AND PROTEIN SEQUENCE OF 123-142.
RX PubMed=1409716; DOI=10.1073/pnas.89.20.9875;
RA Morales M.J., Dang Y.L., Lou Y.C., Sulo P., Martin N.C.;
RT "A 105-kDa protein is required for yeast mitochondrial RNase P activity.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:9875-9879(1992).
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 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).
CC -!- FUNCTION: Ribonuclease P generates mature tRNA molecules by cleaving
CC their 5'-ends.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage of RNA, removing 5'-extranucleotides
CC from tRNA precursor.; EC=3.1.26.5;
CC -!- SUBUNIT: Consists of an RNA moiety (RPM1) and the protein component
CC (RPM2). Both are necessary for full enzymatic activity.
CC -!- SUBCELLULAR LOCATION: Mitochondrion.
CC -!- MISCELLANEOUS: Present with 1160 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; L06209; AAA03168.1; -; Unassigned_DNA.
DR EMBL; Z46660; CAA86647.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA09808.1; -; Genomic_DNA.
DR PIR; A48773; A48773.
DR RefSeq; NP_013619.1; NM_001182450.1.
DR AlphaFoldDB; Q02773; -.
DR BioGRID; 35052; 52.
DR ComplexPortal; CPX-1294; Mitochondrial ribonuclease P complex.
DR DIP; DIP-6320N; -.
DR IntAct; Q02773; 14.
DR MINT; Q02773; -.
DR STRING; 4932.YML091C; -.
DR iPTMnet; Q02773; -.
DR MaxQB; Q02773; -.
DR PaxDb; Q02773; -.
DR PRIDE; Q02773; -.
DR EnsemblFungi; YML091C_mRNA; YML091C; YML091C.
DR GeneID; 854883; -.
DR KEGG; sce:YML091C; -.
DR SGD; S000004556; RPM2.
DR VEuPathDB; FungiDB:YML091C; -.
DR eggNOG; ENOG502S4M0; Eukaryota.
DR HOGENOM; CLU_270952_0_0_1; -.
DR InParanoid; Q02773; -.
DR OMA; LTVYQDI; -.
DR BioCyc; YEAST:YML091C-MON; -.
DR PRO; PR:Q02773; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; Q02773; protein.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:SGD.
DR GO; GO:0030678; C:mitochondrial ribonuclease P complex; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0030677; C:ribonuclease P complex; IDA:SGD.
DR GO; GO:0004526; F:ribonuclease P activity; IEA:UniProtKB-EC.
DR GO; GO:0002181; P:cytoplasmic translation; IMP:SGD.
DR GO; GO:0097745; P:mitochondrial tRNA 5'-end processing; IMP:SGD.
DR GO; GO:0007005; P:mitochondrion organization; IMP:SGD.
DR GO; GO:0006397; P:mRNA processing; IGI:SGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:SGD.
DR GO; GO:0006396; P:RNA processing; IMP:SGD.
DR GO; GO:0001682; P:tRNA 5'-leader removal; IDA:SGD.
DR InterPro; IPR013888; RNase_P_Rpm2_mt.
DR Pfam; PF08579; RPM2; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Endonuclease; Hydrolase; Mitochondrion;
KW Nuclease; Reference proteome; Transit peptide; tRNA processing.
FT TRANSIT 1..122
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:1409716"
FT CHAIN 123..1202
FT /note="Ribonuclease P protein component, mitochondrial"
FT /id="PRO_0000022247"
FT REGION 109..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1202 AA; 139348 MW; B9DA65450E8F056A CRC64;
MAFKSFIYSK GYHRSAAQKK TATSFFDSSY QYLRQNQGLV NSDPVLHASH LHPHPVVVAN
VNYNNVDDIL HPHDLDSSIN NTNNPLTHEE LLYNQNVSLR SLKQQQSTNY VNNNNNNQHR
YYSTGPTLPT NQYDPLNFSN RNFQDLSLKT SQPSVQQPQN EYSLLKDENA PVWKEDTEPC
LNKSTYLQTH IDEINRCYEQ KNYNKINSLY QSLKRNDIVP PLEIFTKVLD SLCKRPLDNN
DLDNKMYELL TCYQDMINNR LKPPDEIYNI VLLSLFKGSI LAYQFENPNG SDFYKIAIEL
FNTTTNDPKQ KSVVKFRNFS KDVLDYNLLA MNIYPGHITL SKAQQVIKSS PAFIKDSFYF
IACFSYAKLT NDKFAIKELY EDFRLSLSSG SPDQGLFDDQ FEIYSVILSS FIETGEVELA
TNLLDDLVSK IQSSNGLASN ISLLLSSFLI SMSKVDPSKA YEIWFKFHNL NWIPEFSYEF
YLVFMANSFQ DWNLTKKIYD YIFPMERNLS PLKKQKLSDY LLHPIGVDSI TTSLLDYSLQ
LKDNEVIMKI LEESIVKNFS FDIGIYPFVF NYLREIQCGE DYLMRFIESH AEFIKKSNSI
NKFQFLNMIV DNFQSQSLLN KISHAKFFKN FVEDFNLENC ELVSYNGLIS CINNFIKIPK
TIKDFPYILE IHAILVTKLF DFDTYPILQN GNNEVLLKFR DQIEHQFKML AQNFCRLNLD
PNLLAGVVSQ AMKMVNLDDT ANGQDLLNFF NHPGDWDKSY PLSLGSFIRN SPRGGIREFT
KLSKEGYCFD YDTYKELIIK RAINKQIIDK CLEVCPDSIE LKNIVNLMIS KIPGRNLTQL
IINNPKFSKV FVPNLRNDSM LKLIENCESL SNFIRICDFP EKFKSIAIQA ENKNAIELIY
ERLFDGGKYA DILRYNNIVP VLNLELLLKS CIRSGEFKKY ESLSKKFNDK ISESSKIDIQ
LEYLINKNDL KGAFTLFEKT PRELRTPHKT MDLYTFALFL DSFNRNITYY ESPENTLQFA
NILSSQTSFI NLLSTYNLIA HSDHLMNFNV GGMAAKVKKE ILNQMLNNLY DSIRLLSPSI
ENDKSMKEKL REKVKNYCRF KAYLKSPELD MDELKTLVSV ESFLNPFTPS MLFNNLIETI
YINEHASSLV LQNGLIYSLQ QKGLNKILSY LEESFITSGN DANIEKVREF RSLLRKSKPL
QA
