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Q8NL51 (RNPA_CORGL) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 68. 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

Short name=RNase P protein
Short name=RNaseP protein
EC=3.1.26.5
Alternative name(s):
Protein C5
Gene names
Name:rnpA
Ordered Locus Names:Cgl3098, cg3431
OrganismCorynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025) [Reference proteome] [HAMAP]
Taxonomic identifier196627 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium

Protein attributes

Sequence length133 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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 By similarity. HAMAP-Rule MF_00227

Catalytic activity

Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor. HAMAP-Rule MF_00227

Subunit structure

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

Sequence similarities

Belongs to the RnpA family.

Ontologies

Keywords
   Biological processtRNA processing
   LigandRNA-binding
   Molecular functionEndonuclease
Hydrolase
Nuclease
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processtRNA processing

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionribonuclease P activity

Inferred from electronic annotation. Source: UniProtKB-EC

tRNA binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 133133Ribonuclease P protein component HAMAP-Rule MF_00227
PRO_0000198454

Sequences

Sequence LengthMass (Da)Tools
Q8NL51 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: 214D960133F8F4FB

FASTA13314,481
        10         20         30         40         50         60 
MLPAQHKLNS SMQFRTVMRK GRRAGSKTVV VHLWDSAESL DGTEKQGEVA SFGGPRFGLV 

        70         80         90        100        110        120 
VSKAVGNAVV RHRTSRRLRH ICASIAEKSP ELLSPTHHVV IRALAGAGNA TSAELERDIR 

       130 
YGLGKASRVR TNK 

« Hide

References

[1]"The Corynebacterium glutamicum genome: features and impacts on biotechnological processes."
Ikeda M., Nakagawa S.
Appl. Microbiol. Biotechnol. 62:99-109(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
[2]"The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its impact on the production of L-aspartate-derived amino acids and vitamins."
Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A., Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A., Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F., Moeckel B. expand/collapse author list , Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O., Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.
J. Biotechnol. 104:5-25(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000036 Genomic DNA. Translation: BAC00492.1.
BX927157 Genomic DNA. Translation: CAF19038.1.
RefSeqNP_602290.1. NC_003450.3.
YP_227348.1. NC_006958.1.

3D structure databases

ProteinModelPortalQ8NL51.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING196627.cg3431.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAC00492; BAC00492; BAC00492.
CAF19038; CAF19038; cg3431.
GeneID1021042.
KEGGcgb:cg3431.
cgl:NCgl2992.
PATRIC21498248. VBICorGlu203724_3032.

Phylogenomic databases

eggNOGCOG0594.
KOK03536.
OMAMLPAQHK.
OrthoDBEOG6C01C6.

Enzyme and pathway databases

BioCycCGLU196627:GJDM-3075-MONOMER.

Family and domain databases

Gene3D3.30.230.10. 1 hit.
HAMAPMF_00227. RNase_P.
InterProIPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
IPR000100. RNase_P.
[Graphical view]
PfamPF00825. Ribonuclease_P. 1 hit.
[Graphical view]
ProDomPD003629. Ribonuclease_P. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMSSF54211. SSF54211. 1 hit.
TIGRFAMsTIGR00188. rnpA. 1 hit.
ProtoNetSearch...

Entry information

Entry nameRNPA_CORGL
AccessionPrimary (citable) accession number: Q8NL51
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 2002
Last sequence update: October 1, 2002
Last modified: July 9, 2014
This is version 68 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