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Protein

Ribonuclease P protein component, mitochondrial

Gene

RPM2

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

Ribonuclease P generates mature tRNA molecules by cleaving their 5'-ends.

Catalytic activityi

Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.

GO - Molecular functioni

GO - Biological processi

  • cytoplasmic translation Source: SGD
  • mitochondrion organization Source: SGD
  • mRNA processing Source: SGD
  • positive regulation of transcription from RNA polymerase II promoter Source: SGD
  • RNA phosphodiester bond hydrolysis Source: GOC
  • RNA phosphodiester bond hydrolysis, endonucleolytic Source: GOC
  • RNA processing Source: SGD
  • tRNA 5'-leader removal Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Endonuclease, Hydrolase, Nuclease

Keywords - Biological processi

tRNA processing

Enzyme and pathway databases

BioCyciYEAST:YML091C-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribonuclease P protein component, mitochondrial (EC:3.1.26.5)
Short name:
RNase P
Gene namesi
Name:RPM2
Ordered Locus Names:YML091C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome XIII

Organism-specific databases

CYGDiYML091c.
EuPathDBiFungiDB:YML091C.
SGDiS000004556. RPM2.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial matrix Source: SGD
  • mitochondrial ribonuclease P complex Source: SGD
  • nucleus Source: SGD
  • ribonuclease P complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 122122Mitochondrion1 PublicationAdd
BLAST
Chaini123 – 12021080Ribonuclease P protein component, mitochondrialPRO_0000022247Add
BLAST

Proteomic databases

MaxQBiQ02773.
PaxDbiQ02773.
PeptideAtlasiQ02773.

Interactioni

Subunit structurei

Consists of an RNA moiety (RPM1) and the protein component (RPM2). Both are necessary for full enzymatic activity.

Protein-protein interaction databases

BioGridi35052. 39 interactions.
DIPiDIP-6320N.
IntActiQ02773. 14 interactions.
MINTiMINT-663444.
STRINGi4932.YML091C.

Structurei

3D structure databases

ProteinModelPortaliQ02773.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiNOG44485.
HOGENOMiHOG000141909.
InParanoidiQ02773.
KOiK14533.
OMAiPEFSYEF.
OrthoDBiEOG7K3TVM.

Family and domain databases

InterProiIPR013888. RNase_P_Rpm2_mt.
[Graphical view]
PfamiPF08579. RPM2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q02773-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAFKSFIYSK GYHRSAAQKK TATSFFDSSY QYLRQNQGLV NSDPVLHASH
60 70 80 90 100
LHPHPVVVAN VNYNNVDDIL HPHDLDSSIN NTNNPLTHEE LLYNQNVSLR
110 120 130 140 150
SLKQQQSTNY VNNNNNNQHR YYSTGPTLPT NQYDPLNFSN RNFQDLSLKT
160 170 180 190 200
SQPSVQQPQN EYSLLKDENA PVWKEDTEPC LNKSTYLQTH IDEINRCYEQ
210 220 230 240 250
KNYNKINSLY QSLKRNDIVP PLEIFTKVLD SLCKRPLDNN DLDNKMYELL
260 270 280 290 300
TCYQDMINNR LKPPDEIYNI VLLSLFKGSI LAYQFENPNG SDFYKIAIEL
310 320 330 340 350
FNTTTNDPKQ KSVVKFRNFS KDVLDYNLLA MNIYPGHITL SKAQQVIKSS
360 370 380 390 400
PAFIKDSFYF IACFSYAKLT NDKFAIKELY EDFRLSLSSG SPDQGLFDDQ
410 420 430 440 450
FEIYSVILSS FIETGEVELA TNLLDDLVSK IQSSNGLASN ISLLLSSFLI
460 470 480 490 500
SMSKVDPSKA YEIWFKFHNL NWIPEFSYEF YLVFMANSFQ DWNLTKKIYD
510 520 530 540 550
YIFPMERNLS PLKKQKLSDY LLHPIGVDSI TTSLLDYSLQ LKDNEVIMKI
560 570 580 590 600
LEESIVKNFS FDIGIYPFVF NYLREIQCGE DYLMRFIESH AEFIKKSNSI
610 620 630 640 650
NKFQFLNMIV DNFQSQSLLN KISHAKFFKN FVEDFNLENC ELVSYNGLIS
660 670 680 690 700
CINNFIKIPK TIKDFPYILE IHAILVTKLF DFDTYPILQN GNNEVLLKFR
710 720 730 740 750
DQIEHQFKML AQNFCRLNLD PNLLAGVVSQ AMKMVNLDDT ANGQDLLNFF
760 770 780 790 800
NHPGDWDKSY PLSLGSFIRN SPRGGIREFT KLSKEGYCFD YDTYKELIIK
810 820 830 840 850
RAINKQIIDK CLEVCPDSIE LKNIVNLMIS KIPGRNLTQL IINNPKFSKV
860 870 880 890 900
FVPNLRNDSM LKLIENCESL SNFIRICDFP EKFKSIAIQA ENKNAIELIY
910 920 930 940 950
ERLFDGGKYA DILRYNNIVP VLNLELLLKS CIRSGEFKKY ESLSKKFNDK
960 970 980 990 1000
ISESSKIDIQ LEYLINKNDL KGAFTLFEKT PRELRTPHKT MDLYTFALFL
1010 1020 1030 1040 1050
DSFNRNITYY ESPENTLQFA NILSSQTSFI NLLSTYNLIA HSDHLMNFNV
1060 1070 1080 1090 1100
GGMAAKVKKE ILNQMLNNLY DSIRLLSPSI ENDKSMKEKL REKVKNYCRF
1110 1120 1130 1140 1150
KAYLKSPELD MDELKTLVSV ESFLNPFTPS MLFNNLIETI YINEHASSLV
1160 1170 1180 1190 1200
LQNGLIYSLQ QKGLNKILSY LEESFITSGN DANIEKVREF RSLLRKSKPL

QA
Length:1,202
Mass (Da):139,348
Last modified:October 1, 1993 - v1
Checksum:iB9DA65450E8F056A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L06209 Unassigned DNA. Translation: AAA03168.1.
Z46660 Genomic DNA. Translation: CAA86647.1.
BK006946 Genomic DNA. Translation: DAA09808.1.
PIRiA48773.
RefSeqiNP_013619.1. NM_001182450.1.

Genome annotation databases

EnsemblFungiiYML091C; YML091C; YML091C.
GeneIDi854883.
KEGGisce:YML091C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L06209 Unassigned DNA. Translation: AAA03168.1.
Z46660 Genomic DNA. Translation: CAA86647.1.
BK006946 Genomic DNA. Translation: DAA09808.1.
PIRiA48773.
RefSeqiNP_013619.1. NM_001182450.1.

3D structure databases

ProteinModelPortaliQ02773.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35052. 39 interactions.
DIPiDIP-6320N.
IntActiQ02773. 14 interactions.
MINTiMINT-663444.
STRINGi4932.YML091C.

Proteomic databases

MaxQBiQ02773.
PaxDbiQ02773.
PeptideAtlasiQ02773.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYML091C; YML091C; YML091C.
GeneIDi854883.
KEGGisce:YML091C.

Organism-specific databases

CYGDiYML091c.
EuPathDBiFungiDB:YML091C.
SGDiS000004556. RPM2.

Phylogenomic databases

eggNOGiNOG44485.
HOGENOMiHOG000141909.
InParanoidiQ02773.
KOiK14533.
OMAiPEFSYEF.
OrthoDBiEOG7K3TVM.

Enzyme and pathway databases

BioCyciYEAST:YML091C-MONOMER.

Miscellaneous databases

NextBioi977834.
PROiQ02773.

Family and domain databases

InterProiIPR013888. RNase_P_Rpm2_mt.
[Graphical view]
PfamiPF08579. RPM2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A 105-kDa protein is required for yeast mitochondrial RNase P activity."
    Morales M.J., Dang Y.L., Lou Y.C., Sulo P., Martin N.C.
    Proc. Natl. Acad. Sci. U.S.A. 89:9875-9879(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE, PROTEIN SEQUENCE OF 123-142.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiRPM2_YEAST
AccessioniPrimary (citable) accession number: Q02773
Secondary accession number(s): D6W0J4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: June 24, 2015
This is version 115 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 1160 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  2. Yeast chromosome XIII
    Yeast (Saccharomyces cerevisiae) chromosome XIII: entries and gene names

External Data

Dasty 3

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 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.