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A2BMC7 (RNP1_HYPBU) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 41. 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 1

Short name=RNase P component 1
EC=3.1.26.5
Gene names
Name:rnp1
Ordered Locus Names:Hbut_1308
OrganismHyperthermus butylicus (strain DSM 5456 / JCM 9403) [Reference proteome] [HAMAP]
Taxonomic identifier415426 [NCBI]
Taxonomic lineageArchaeaCrenarchaeotaThermoproteiDesulfurococcalesPyrodictiaceaeHyperthermus

Protein attributes

Sequence length111 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Part of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends By similarity. HAMAP-Rule MF_00754

Catalytic activity

Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor. HAMAP-Rule MF_00754

Subunit structure

Consists of a catalytic RNA component and at least 4 protein subunits Potential.

Sequence similarities

Belongs to the eukaryotic/archaeal RNase P protein component 1 family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 111111Ribonuclease P protein component 1 HAMAP-Rule MF_00754
PRO_1000046610

Sequences

Sequence LengthMass (Da)Tools
A2BMC7 [UniParc].

Last modified February 20, 2007. Version 1.
Checksum: C35F35ADBBBF33F1

FASTA11112,432
        10         20         30         40         50         60 
MKRTAWNIVF HSLIGLRARV LATSDPGLRG LEGVVVEETR HSLVVETRDG RRVRVLKANS 

        70         80         90        100        110 
IFLFQLPGGS WVVVRGEEIA GSLAERVKRL GRLKGVGWLV RAGEKRRYTR G 

« Hide

References

[1]"The genome of Hyperthermus butylicus: a sulfur-reducing, peptide fermenting, neutrophilic Crenarchaeote growing up to 108 degrees C."
Bruegger K., Chen L., Stark M., Zibat A., Redder P., Ruepp A., Awayez M., She Q., Garrett R.A., Klenk H.-P.
Archaea 2:127-135(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 5456 / JCM 9403.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000493 Genomic DNA. Translation: ABM81138.1.
RefSeqYP_001013483.1. NC_008818.1.

3D structure databases

ProteinModelPortalA2BMC7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING415426.Hbut_1308.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABM81138; ABM81138; Hbut_1308.
GeneID4782900.
KEGGhbu:Hbut_1308.

Phylogenomic databases

eggNOGCOG1588.
HOGENOMHOG000231353.
KOK03538.
OMARILQYPD.

Enzyme and pathway databases

BioCycHBUT415426:GC56-1308-MONOMER.

Family and domain databases

Gene3D2.30.30.210. 1 hit.
HAMAPMF_00754. RNase_P_1.
InterProIPR002730. RNase_P/MRP_p29.
IPR023538. RNase_P_comp-1.
IPR023534. Rof/RNase_P-like.
[Graphical view]
PfamPF01868. UPF0086. 1 hit.
[Graphical view]
SUPFAMSSF101744. SSF101744. 1 hit.
ProtoNetSearch...

Entry information

Entry nameRNP1_HYPBU
AccessionPrimary (citable) accession number: A2BMC7
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: February 20, 2007
Last modified: April 16, 2014
This is version 41 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