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A2BKA5 (A2BKA5_HYPBU) Unreviewed, UniProtKB/TrEMBL

Last modified May 29, 2013. Version 31. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Ribonuclease P protein component 2 HAMAP-Rule MF_00755

Short name=RNase P component 2 HAMAP-Rule MF_00755
EC=3.1.26.5 HAMAP-Rule MF_00755
Gene names
Name:rnp2 HAMAP-Rule MF_00755
Ordered Locus Names:Hbut_0556
OrganismHyperthermus butylicus (strain DSM 5456 / JCM 9403) [Reference proteome] [HAMAP] EMBL ABM80416.1
Taxonomic identifier415426 [NCBI]
Taxonomic lineageArchaeaCrenarchaeotaThermoproteiDesulfurococcalesPyrodictiaceaeHyperthermus

Protein attributes

Sequence length189 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_00755

Catalytic activity

Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor. HAMAP-Rule MF_00755

Subunit structure

Consists of a catalytic RNA component and at least 4 protein subunits By similarity. HAMAP-Rule MF_00755

Sequence similarities

Belongs to the eukaryotic/archaeal RNase P protein component 2 family. HAMAP-Rule MF_00755

Ontologies

Keywords
   Biological processtRNA processing HAMAP-Rule MF_00755
   Molecular functionHydrolase HAMAP-Rule MF_00755
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processtRNA 5'-leader removal

Inferred from electronic annotation. Source: HAMAP

   Molecular_functionribonuclease P activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequences

Sequence LengthMass (Da)Tools
A2BKA5 [UniParc].

Last modified February 20, 2007. Version 1.
Checksum: 5FDE5ED8B096D36C

FASTA18921,158
        10         20         30         40         50         60 
MTLWEAILMG IVAVLLVLVY LLNRRVSGLT GALGEFRARL GELEESFNNV LRELGFVSRS 

        70         80         90        100        110        120 
LSTALQSIEA EDALERLRRR RRRRYIAFYV VYEGDSPPQA EEVEKAIVRA VERLAGQLTV 

       130        140        150        160        170        180 
ALARLQLVYY DHVRGAGIVR ATNDTKYVVL AAMGLVRSIG GRRVLLVPVR TTGTIKRAKK 


ALAVPRRLL 

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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: ABM80416.1.
RefSeqYP_001012761.1. NC_008818.1.

3D structure databases

ProteinModelPortalA2BKA5.
ModBaseSearch...

Protein-protein interaction databases

STRING415426.Hbut_0556.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABM80416; ABM80416; Hbut_0556.
GeneID4782770.
KEGGhbu:Hbut_0556.

Phylogenomic databases

eggNOGCOG1369.
KOK03537.
OMAGELEESF.

Enzyme and pathway databases

BioCycHBUT415426:GC56-556-MONOMER.

Family and domain databases

HAMAPMF_00755. RNase_P_2.
InterProIPR002759. RNase_P/MRP_subunit.
[Graphical view]
PfamPF01900. RNase_P_Rpp14. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameA2BKA5_HYPBU
AccessionPrimary (citable) accession number: A2BKA5
Entry history
Integrated into UniProtKB/TrEMBL: February 20, 2007
Last sequence update: February 20, 2007
Last modified: May 29, 2013
This is version 31 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)