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Protein

Ribonuclease P protein component

Gene

rnpA

Organism
Mycobacterium abscessus (strain ATCC 19977 / DSM 44196)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

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.UniRule annotation

Catalytic activityi

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

GO - Molecular functioni

  1. ribonuclease P activity Source: UniProtKB-HAMAP
  2. tRNA binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. tRNA 5'-leader removal Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Endonuclease, Hydrolase, Nuclease

Keywords - Biological processi

tRNA processing

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

BioCyciMABS36809-WGS:GSQO-4969-MONOMER.
MABS561007:GJTG-4969-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribonuclease P protein componentUniRule annotation (EC:3.1.26.5UniRule annotation)
Short name:
RNase P proteinUniRule annotation
Short name:
RNaseP proteinUniRule annotation
Alternative name(s):
Protein C5UniRule annotation
Gene namesi
Name:rnpAUniRule annotation
Ordered Locus Names:MAB_4954c
OrganismiMycobacterium abscessus (strain ATCC 19977 / DSM 44196)
Taxonomic identifieri561007 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium abscessus
ProteomesiUP000007137: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 127127Ribonuclease P protein componentPRO_1000100373Add
BLAST

Interactioni

Subunit structurei

Consists of a catalytic RNA component (M1 or rnpB) and a protein subunit.UniRule annotation

Protein-protein interaction databases

STRINGi561007.MAB_4954c.

Structurei

3D structure databases

ProteinModelPortaliB1MN96.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the RnpA family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0594.
HOGENOMiHOG000266301.
KOiK03536.
OMAiTHHVVIR.
OrthoDBiEOG6C01C6.

Family and domain databases

Gene3Di3.30.230.10. 1 hit.
HAMAPiMF_00227. RNase_P.
InterProiIPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
IPR000100. RNase_P.
[Graphical view]
PfamiPF00825. Ribonuclease_P. 1 hit.
[Graphical view]
SUPFAMiSSF54211. SSF54211. 1 hit.
TIGRFAMsiTIGR00188. rnpA. 1 hit.

Sequencei

Sequence statusi: Complete.

B1MN96-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLPTRHRMTK SSEFRQTVKR GVRTTHADLV IHLRRGCPDS ACEQVEGPKV
60 70 80 90 100
GLIVGKSVGG AVVRHRVSRR LRHAAAELLP KLEPVDRMVI RALPSSSTAL
110 120
SASLRQQLRD GIDRSARRQE PAAERQR
Length:127
Mass (Da):14,173
Last modified:April 29, 2008 - v1
Checksum:iA8FB932DB05A572B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU458896 Genomic DNA. Translation: CAM65022.1.

Genome annotation databases

EnsemblBacteriaiCAM65022; CAM65022; MAB_4954c.
KEGGimab:MAB_4954c.
PATRICi17981746. VBIMycAbs55940_5037.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU458896 Genomic DNA. Translation: CAM65022.1.

3D structure databases

ProteinModelPortaliB1MN96.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi561007.MAB_4954c.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAM65022; CAM65022; MAB_4954c.
KEGGimab:MAB_4954c.
PATRICi17981746. VBIMycAbs55940_5037.

Phylogenomic databases

eggNOGiCOG0594.
HOGENOMiHOG000266301.
KOiK03536.
OMAiTHHVVIR.
OrthoDBiEOG6C01C6.

Enzyme and pathway databases

BioCyciMABS36809-WGS:GSQO-4969-MONOMER.
MABS561007:GJTG-4969-MONOMER.

Family and domain databases

Gene3Di3.30.230.10. 1 hit.
HAMAPiMF_00227. RNase_P.
InterProiIPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
IPR000100. RNase_P.
[Graphical view]
PfamiPF00825. Ribonuclease_P. 1 hit.
[Graphical view]
SUPFAMiSSF54211. SSF54211. 1 hit.
TIGRFAMsiTIGR00188. rnpA. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Acquisition of foreign virulence genes by the cystic fibrosis pathogen Mycobacterium abscessus."
    Genoscope
    Ripoll F., Pasek S., Schenowitz C., Dossat C., Barbe V., Rottman M., Heym B., Herrmann J.L., Daffe M., Brosch R., Risler J.L., Gaillard J.L.
    Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 19977 / DSM 44196.

Entry informationi

Entry nameiRNPA_MYCA9
AccessioniPrimary (citable) accession number: B1MN96
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: April 29, 2008
Last modified: February 4, 2015
This is version 51 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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.