Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q975G4 (RNP2_SULTO) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 59. 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 2

Short name=RNase P component 2
EC=3.1.26.5
Alternative name(s):
Pop5
Gene names
Name:rnp2
Ordered Locus Names:STK_04470
OrganismSulfolobus tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7) [Complete proteome] [HAMAP]
Taxonomic identifier273063 [NCBI]
Taxonomic lineageArchaeaCrenarchaeotaThermoproteiSulfolobalesSulfolobaceaeSulfolobus

Protein attributes

Sequence length123 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 4-5 protein subunits By similarity.

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00755.

Sequence similarities

Belongs to the eukaryotic/archaeal RNase P protein component 2 family.

Ontologies

Keywords
   Biological processtRNA processing
   Cellular componentCytoplasm
   Molecular functionEndonuclease
Hydrolase
Nuclease
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processtRNA 5'-leader removal

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

ribonuclease P complex

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Molecular_functionribonuclease P activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 123123Ribonuclease P protein component 2 HAMAP-Rule MF_00755
PRO_0000140030

Sequences

Sequence LengthMass (Da)Tools
Q975G4 [UniParc].

Last modified April 13, 2004. Version 2.
Checksum: 8009E7C516C3B40B

FASTA12314,431
        10         20         30         40         50         60 
MVIFSYRTRI IYIKKIKNKR DTRAKRYVIF DIISEDNFEI REIEEAVRNS VKELGGKIWL 

        70         80         90        100        110        120 
DLSNPKVIMI YNNRGIISTN RIGYKIIIAS LPLIKKIKNK EVLLVPRRTT GSLKRAKRLI 


GIE 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000023 Genomic DNA. Translation: BAK54288.1.

3D structure databases

ProteinModelPortalQ975G4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING273063.ST0447.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAK54288; BAK54288; STK_04470.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1369.
HOGENOMHOG000270360.

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 nameRNP2_SULTO
AccessionPrimary (citable) accession number: Q975G4
Secondary accession number(s): F9VMZ1
Entry history
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: April 13, 2004
Last modified: July 9, 2014
This is version 59 of the entry and version 2 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