Q02773 (RPM2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ribonuclease P protein component, mitochondrial
Short name=RNase P
EC=3.1.26.5

Gene names

Name:	RPM2
Ordered Locus Names:	YML091C

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	1202 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	Ribonuclease P generates mature tRNA molecules by cleaving their 5'-ends.
Catalytic activity	Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
Subunit structure	Consists of a RNA moiety (RPM1) and the protein component (RPM2). Both are necessary for full enzymatic activity.
Subcellular location	Mitochondrion.
Miscellaneous	Present with 1160 molecules/cell in log phase SD medium.

Ontologies

Keywords
Biological process	tRNA processing
Cellular component	Mitochondrion
Domain	Transit peptide
Molecular function	Endonuclease Hydrolase Nuclease
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cytoplasmic translation Inferred from mutant phenotype PubMed 11404323. Source: SGD mRNA processing Inferred from genetic interaction PubMed 17267405. Source: SGD mitochondrion organization Inferred from mutant phenotype PubMed 11404323. Source: SGD nucleic acid phosphodiester bond hydrolysis Inferred from electronic annotation. Source: GOC positive regulation of transcription from RNA polymerase II promoter Inferred from direct assay PubMed 16024791. Source: SGD tRNA 5'-leader removal Inferred from direct assay PubMed 8366116. Source: SGD
Cellular_component	mitochondrial matrix Inferred from direct assay PubMed 7544434. Source: SGD mitochondrial ribonuclease P complex Inferred from direct assay PubMed 3537697. Source: SGD nucleus Inferred from direct assay PubMed 16024791. Source: SGD
Molecular_function	ribonuclease P activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 122	122	Mitochondrion Ref.1
	Chain	123 – 1202	1080	Ribonuclease P protein component, mitochondrial		PRO_0000022247

Sequences

	Sequence		Length	Mass (Da)
	Q02773 [UniParc]. Last modified October 1, 1993. Version 1. Checksum: B9DA65450E8F056A	FASTA	1,202	139,348
	10 20 30 40 50 60 MAFKSFIYSK GYHRSAAQKK TATSFFDSSY QYLRQNQGLV NSDPVLHASH LHPHPVVVAN 70 80 90 100 110 120 VNYNNVDDIL HPHDLDSSIN NTNNPLTHEE LLYNQNVSLR SLKQQQSTNY VNNNNNNQHR 130 140 150 160 170 180 YYSTGPTLPT NQYDPLNFSN RNFQDLSLKT SQPSVQQPQN EYSLLKDENA PVWKEDTEPC 190 200 210 220 230 240 LNKSTYLQTH IDEINRCYEQ KNYNKINSLY QSLKRNDIVP PLEIFTKVLD SLCKRPLDNN 250 260 270 280 290 300 DLDNKMYELL TCYQDMINNR LKPPDEIYNI VLLSLFKGSI LAYQFENPNG SDFYKIAIEL 310 320 330 340 350 360 FNTTTNDPKQ KSVVKFRNFS KDVLDYNLLA MNIYPGHITL SKAQQVIKSS PAFIKDSFYF 370 380 390 400 410 420 IACFSYAKLT NDKFAIKELY EDFRLSLSSG SPDQGLFDDQ FEIYSVILSS FIETGEVELA 430 440 450 460 470 480 TNLLDDLVSK IQSSNGLASN ISLLLSSFLI SMSKVDPSKA YEIWFKFHNL NWIPEFSYEF 490 500 510 520 530 540 YLVFMANSFQ DWNLTKKIYD YIFPMERNLS PLKKQKLSDY LLHPIGVDSI TTSLLDYSLQ 550 560 570 580 590 600 LKDNEVIMKI LEESIVKNFS FDIGIYPFVF NYLREIQCGE DYLMRFIESH AEFIKKSNSI 610 620 630 640 650 660 NKFQFLNMIV DNFQSQSLLN KISHAKFFKN FVEDFNLENC ELVSYNGLIS CINNFIKIPK 670 680 690 700 710 720 TIKDFPYILE IHAILVTKLF DFDTYPILQN GNNEVLLKFR DQIEHQFKML AQNFCRLNLD 730 740 750 760 770 780 PNLLAGVVSQ AMKMVNLDDT ANGQDLLNFF NHPGDWDKSY PLSLGSFIRN SPRGGIREFT 790 800 810 820 830 840 KLSKEGYCFD YDTYKELIIK RAINKQIIDK CLEVCPDSIE LKNIVNLMIS KIPGRNLTQL 850 860 870 880 890 900 IINNPKFSKV FVPNLRNDSM LKLIENCESL SNFIRICDFP EKFKSIAIQA ENKNAIELIY 910 920 930 940 950 960 ERLFDGGKYA DILRYNNIVP VLNLELLLKS CIRSGEFKKY ESLSKKFNDK ISESSKIDIQ 970 980 990 1000 1010 1020 LEYLINKNDL KGAFTLFEKT PRELRTPHKT MDLYTFALFL DSFNRNITYY ESPENTLQFA 1030 1040 1050 1060 1070 1080 NILSSQTSFI NLLSTYNLIA HSDHLMNFNV GGMAAKVKKE ILNQMLNNLY DSIRLLSPSI 1090 1100 1110 1120 1130 1140 ENDKSMKEKL REKVKNYCRF KAYLKSPELD MDELKTLVSV ESFLNPFTPS MLFNNLIETI 1150 1160 1170 1180 1190 1200 YINEHASSLV LQNGLIYSLQ QKGLNKILSY LEESFITSGN DANIEKVREF RSLLRKSKPL QA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"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]	"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].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L06209 Unassigned DNA. Translation: AAA03168.1. Z46660 Genomic DNA. Translation: CAA86647.1. BK006946 Genomic DNA. Translation: DAA09808.1.
PIR	A48773.
RefSeq	NP_013619.1. NM_001182450.1.
3D structure databases
ProteinModelPortal	Q02773.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-6320N.
IntAct	Q02773. 14 interactions.
MINT	MINT-663444.
STRING	4932.YML091C.
Proteomic databases
PaxDb	Q02773.
PeptideAtlas	Q02773.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YML091C; YML091C; YML091C.
GeneID	854883.
KEGG	sce:YML091C.
Organism-specific databases
CYGD	YML091c.
SGD	S000004556. RPM2.
Phylogenomic databases
eggNOG	NOG44485.
HOGENOM	HOG000141909.
KO	K14533.
OMA	PEFSYEF.
OrthoDB	EOG490BJ8.
Gene expression databases
Genevestigator	Q02773.
GermOnline	YML091C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR013888. RNase_P_Rpm2_mt. [Graphical view]
Pfam	PF08579. RPM2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	977834.

Entry information

Entry name

RPM2_YEAST

Accession

Primary (citable) accession number: Q02773
Secondary accession number(s): D6W0J4

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	October 1, 1993
Last modified:	April 3, 2013
This is version 100 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program