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P46610 (RNPA_MYCLE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ribonuclease P protein component

Short name=RNase P protein
Short name=RNaseP protein
EC=3.1.26.5
Alternative name(s):
Protein C5
Gene names
Name:rnpA
Ordered Locus Names:ML2712
OrganismMycobacterium leprae (strain TN) [Complete proteome] [HAMAP]
Taxonomic identifier272631 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium

Protein attributes

Sequence length120 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme By similarity. HAMAP-Rule MF_00227

Catalytic activity

Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor. HAMAP-Rule MF_00227

Subunit structure

Consists of a catalytic RNA component (M1 or rnpB) and a protein subunit By similarity.

Sequence similarities

Belongs to the RnpA family.

Ontologies

Keywords
   Biological processtRNA processing
   LigandRNA-binding
   Molecular functionEndonuclease
Hydrolase
Nuclease
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processtRNA processing

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionribonuclease P activity

Inferred from electronic annotation. Source: UniProtKB-EC

tRNA binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 120120Ribonuclease P protein component HAMAP-Rule MF_00227
PRO_0000198487

Sequences

Sequence LengthMass (Da)Tools
P46610 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: B9720BA60DC5CFCE

FASTA12013,359
        10         20         30         40         50         60 
MLSACNRMRR SSEFDATVKF GLRAVQSDVI IHVWRGCNRD ETKAPHVGLI IAKTVGSAVE 

        70         80         90        100        110        120 
RHRVARRLRH VARTMLGELG GADQVVIRAL PSSRNVSSAW LAQQLRNGLR CALDLAETDW 

« Hide

References

« Hide 'large scale' references
[1]"Gene arrangement and organization in an approximately 76 kb fragment encompassing the oriC region of the chromosome of Mycobacterium leprae."
Fsihi H., de Rossi E., Salazar L., Cantoni R., Labo M., Riccardi G., Takiff H.E., Eiglmeier K., Bergh S., Cole S.T.
Microbiology 142:3147-3161(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Massive gene decay in the leprosy bacillus."
Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R., Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E., Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K., Duthoy S. expand/collapse author list , Feltwell T., Fraser A., Hamlin N., Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S., Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R., Barrell B.G.
Nature 409:1007-1011(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: TN.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L39923 Genomic DNA. Translation: AAB53139.1.
AL583926 Genomic DNA. Translation: CAC32244.1.
PIRF87248.
RefSeqNP_302732.1. NC_002677.1.

3D structure databases

ProteinModelPortalP46610.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272631.ML2712.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAC32244; CAC32244; CAC32244.
GeneID908246.
KEGGmle:ML2712.
PATRIC18060601. VBIMycLep78757_5214.

Organism-specific databases

LepromaML2712.
CMRSearch...

Phylogenomic databases

eggNOGCOG0594.
HOGENOMHOG000266301.
KOK03536.
OMAMLPTENR.
OrthoDBEOG6C01C6.
ProtClustDBPRK00588.

Family and domain databases

Gene3D3.30.230.10. 1 hit.
HAMAPMF_00227. RNase_P.
InterProIPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
IPR000100. RNase_P.
IPR020539. RNase_P_CS.
[Graphical view]
PfamPF00825. Ribonuclease_P. 1 hit.
[Graphical view]
SUPFAMSSF54211. SSF54211. 1 hit.
TIGRFAMsTIGR00188. rnpA. 1 hit.
PROSITEPS00648. RIBONUCLEASE_P. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameRNPA_MYCLE
AccessionPrimary (citable) accession number: P46610
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: April 16, 2014
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families