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P0A0H5

- RNPA_STAAU

UniProt

P0A0H5 - RNPA_STAAU

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Protein

Ribonuclease P protein component

Gene

rnpA

Organism
Staphylococcus aureus
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

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.

Catalytic activityi

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

GO - Molecular functioni

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

GO - Biological processi

  1. tRNA processing Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Endonuclease, Hydrolase, Nuclease

Keywords - Biological processi

tRNA processing

Keywords - Ligandi

RNA-binding

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
OrganismiStaphylococcus aureus
Taxonomic identifieri1280 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 117117Ribonuclease P protein componentPRO_0000198530Add
BLAST

Interactioni

Subunit structurei

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

Structurei

Secondary structure

1
117
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 73Combined sources
Helixi13 – 219Combined sources
Beta strandi27 – 315Combined sources
Beta strandi45 – 484Combined sources
Beta strandi51 – 533Combined sources
Helixi58 – 7215Combined sources
Helixi73 – 753Combined sources
Beta strandi82 – 865Combined sources
Helixi89 – 924Combined sources
Helixi97 – 1026Combined sources
Helixi105 – 1095Combined sources
Beta strandi112 – 1143Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1D6TNMR-A1-117[»]
ProteinModelPortaliP0A0H5.
SMRiP0A0H5. Positions 1-117.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A0H5.

Family & Domainsi

Sequence similaritiesi

Belongs to the RnpA family.UniRule annotation

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.
IPR020539. RNase_P_CS.
[Graphical view]
PfamiPF00825. Ribonuclease_P. 1 hit.
[Graphical view]
ProDomiPD003629. Ribonuclease_P. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF54211. SSF54211. 1 hit.
TIGRFAMsiTIGR00188. rnpA. 1 hit.
PROSITEiPS00648. RIBONUCLEASE_P. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0A0H5-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLLEKAYRIK KNADFQRIYK KGHSVANRQF VVYTCNNKEI DHFRLGISVS
60 70 80 90 100
KKLGNAVLRN KIKRAIRENF KVHKSHILAK DIIVIARQPA KDMTTLQIQN
110
SLEHVLKIAK VFNKKIK
Length:117
Mass (Da):13,652
Last modified:February 15, 2005 - v1
Checksum:iAD5172C3654E01F0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF135268 Genomic DNA. Translation: AAF61418.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF135268 Genomic DNA. Translation: AAF61418.1 .

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1D6T NMR - A 1-117 [» ]
ProteinModelPortali P0A0H5.
SMRi P0A0H5. Positions 1-117.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P0A0H5.

Family and domain databases

Gene3Di 3.30.230.10. 1 hit.
HAMAPi MF_00227. RNase_P.
InterProi IPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
IPR000100. RNase_P.
IPR020539. RNase_P_CS.
[Graphical view ]
Pfami PF00825. Ribonuclease_P. 1 hit.
[Graphical view ]
ProDomi PD003629. Ribonuclease_P. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
SUPFAMi SSF54211. SSF54211. 1 hit.
TIGRFAMsi TIGR00188. rnpA. 1 hit.
PROSITEi PS00648. RIBONUCLEASE_P. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Cloning and characterization of Staphylococcus aureus ribonuclease P."
    Poppe S.M., Swaney S.M., Choi G.H., Hromockyj A., Shinabarger D.L.
    Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ISP3.
  2. "The structure of ribonuclease P protein from Staphylococcus aureus reveals a unique binding site for single-stranded RNA."
    Spitzfaden C., Nicholson N., Jones J.J., Guth S., Lehr R., Prescott C.D., Hegg L.A., Eggleston D.S.
    J. Mol. Biol. 295:105-115(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.

Entry informationi

Entry nameiRNPA_STAAU
AccessioniPrimary (citable) accession number: P0A0H5
Secondary accession number(s): P58031, Q9LAH9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 15, 2005
Last sequence update: February 15, 2005
Last modified: November 26, 2014
This is version 42 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

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3