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Q319V1

- RNPA_PROM9

UniProt

Q319V1 - RNPA_PROM9

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Protein
Ribonuclease P protein component
Gene
rnpA, PMT9312_1285
Organism
Prochlorococcus marinus (strain MIT 9312)
Status
Reviewed - Annotation score: 2 out of 5 - Protein inferred from homologyi

Functioni

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.UniRule annotation

Catalytic activityi

Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.UniRule annotation

GO - Molecular functioni

  1. ribonuclease P activity Source: UniProtKB-EC
  2. tRNA binding Source: InterPro
Complete GO annotation...

GO - Biological processi

  1. tRNA processing Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Endonuclease, Hydrolase, Nuclease

Keywords - Biological processi

tRNA processing

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

BioCyciPMAR74546:GHRG-1313-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribonuclease P protein component (EC:3.1.26.5)
Short name:
RNase P protein
Short name:
RNaseP protein
Alternative name(s):
Protein C5
Gene namesi
Name:rnpA
Ordered Locus Names:PMT9312_1285
OrganismiProchlorococcus marinus (strain MIT 9312)
Taxonomic identifieri74546 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus
ProteomesiUP000002715: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 128128Ribonuclease P protein componentUniRule annotation
PRO_1000194661Add
BLAST

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi74546.PMT9312_1285.

Structurei

3D structure databases

ProteinModelPortaliQ319V1.

Family & Domainsi

Sequence similaritiesi

Belongs to the RnpA family.

Phylogenomic databases

HOGENOMiHOG000266301.
KOiK03536.
OMAiMRLKGHR.
OrthoDBiEOG6N94CP.

Family and domain databases

Gene3Di3.30.230.10. 1 hit.
HAMAPiMF_00227. RNase_P.
InterProiIPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
IPR000100. RNase_P.
[Graphical view]
PfamiPF00825. Ribonuclease_P. 1 hit.
[Graphical view]
SUPFAMiSSF54211. SSF54211. 1 hit.

Sequencei

Sequence statusi: Complete.

Q319V1-1 [UniParc]FASTAAdd to Basket

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MALPKDMRLK GHRTFNYIHK NSIKYHGKLM TFKVARSNPE ILLSHNHTNA    50
SNNFRAAIAI SKKVSKKAVD RNKIRRILQE WLITNIPKIN SHKPYWLLVN 100
LKFGDFCNDK NKLLEEFQNL MFKSRLIK 128
Length:128
Mass (Da):15,132
Last modified:December 6, 2005 - v1
Checksum:iCF3808028B8CD847
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000111 Genomic DNA. Translation: ABB50344.1.
RefSeqiYP_397780.1. NC_007577.1.

Genome annotation databases

EnsemblBacteriaiABB50344; ABB50344; PMT9312_1285.
GeneIDi3766093.
KEGGipmi:PMT9312_1285.
PATRICi23006488. VBIProMar70153_1414.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000111 Genomic DNA. Translation: ABB50344.1 .
RefSeqi YP_397780.1. NC_007577.1.

3D structure databases

ProteinModelPortali Q319V1.
ModBasei Search...

Protein-protein interaction databases

STRINGi 74546.PMT9312_1285.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABB50344 ; ABB50344 ; PMT9312_1285 .
GeneIDi 3766093.
KEGGi pmi:PMT9312_1285.
PATRICi 23006488. VBIProMar70153_1414.

Phylogenomic databases

HOGENOMi HOG000266301.
KOi K03536.
OMAi MRLKGHR.
OrthoDBi EOG6N94CP.

Enzyme and pathway databases

BioCyci PMAR74546:GHRG-1313-MONOMER.

Family and domain databases

Gene3Di 3.30.230.10. 1 hit.
HAMAPi MF_00227. RNase_P.
InterProi IPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
IPR000100. RNase_P.
[Graphical view ]
Pfami PF00825. Ribonuclease_P. 1 hit.
[Graphical view ]
SUPFAMi SSF54211. SSF54211. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "Complete sequence of Prochlorococcus marinus str. MIT 9312."
    US DOE Joint Genome Institute
    Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Thiel J., Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A., Richardson P.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: MIT 9312.

Entry informationi

Entry nameiRNPA_PROM9
AccessioniPrimary (citable) accession number: Q319V1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: December 6, 2005
Last modified: May 14, 2014
This is version 49 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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