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Q81JH0 (RNPA_BACAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 75. 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:BA_5737, GBAA_5737, BAS5340
OrganismBacillus anthracis [Reference proteome] [HAMAP]
Taxonomic identifier1392 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group

Protein attributes

Sequence length119 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 – 119119Ribonuclease P protein component HAMAP-Rule MF_00227
PRO_0000198417

Sequences

Sequence LengthMass (Da)Tools
Q81JH0 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 87D7F53F280111D5

FASTA11914,027
        10         20         30         40         50         60 
MKKKHRIKKN DEFQTVFQKG KSNANRQFVV YQLDKEEQPN FRIGLSVSKK IGNAVVRNRI 

        70         80         90        100        110 
KRMIRQSITE LKDEIDSGKD FVIIARKPCA EMTYEELKKS LIHVFKRSGM KRIKSSVRK 

« Hide

References

[1]"The genome sequence of Bacillus anthracis Ames and comparison to closely related bacteria."
Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T., Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R., Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M., Kolonay J.F., Beanan M.J., Dodson R.J. expand/collapse author list , Brinkac L.M., Gwinn M.L., DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C., Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y., Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M., Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E., White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M., Hanna P.C., Kolstoe A.-B., Fraser C.M.
Nature 423:81-86(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Ames / isolate Porton.
[2]"The complete genome sequence of Bacillus anthracis Ames 'Ancestor'."
Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D., Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A.
J. Bacteriol. 191:445-446(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Ames ancestor.
[3]"Complete genome sequence of Bacillus anthracis Sterne."
Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K., Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R., Richardson P., Rubin E., Tice H.
Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Sterne.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016879 Genomic DNA. Translation: AAP29368.1.
AE017334 Genomic DNA. Translation: AAT34898.1.
AE017225 Genomic DNA. Translation: AAT57627.1.
RefSeqNP_847882.1. NC_003997.3.
YP_022423.1. NC_007530.2.
YP_031577.1. NC_005945.1.

3D structure databases

ProteinModelPortalQ81JH0.
SMRQ81JH0. Positions 1-111.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING198094.BA_5737.

Protocols and materials databases

DNASU1085509.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAP29368; AAP29368; BA_5737.
AAT34898; AAT34898; GBAA_5737.
AAT57627; AAT57627; BAS5340.
GeneID1085509.
2815593.
2847955.
KEGGban:BA_5737.
bar:GBAA_5737.
bat:BAS5340.

Phylogenomic databases

eggNOGCOG0594.
HOGENOMHOG000266301.
KOK03536.
OMAYENGISS.
OrthoDBEOG6C01C6.

Enzyme and pathway databases

BioCycANTHRA:RNPA-MONOMER.
BANT260799:GJAJ-5417-MONOMER.
BANT261594:GJ7F-5593-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.
IPR020539. RNase_P_CS.
[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.
PROSITEPS00648. RIBONUCLEASE_P. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameRNPA_BACAN
AccessionPrimary (citable) accession number: Q81JH0
Secondary accession number(s): Q6HQ11, Q6KJF6
Entry history
Integrated into UniProtKB/Swiss-Prot: March 29, 2004
Last sequence update: June 1, 2003
Last modified: May 14, 2014
This is version 75 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