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Protein

Inactive ribonuclease PH

Gene

rph

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

Functioni

Phosphorolytic exoribonuclease that removes nucleotide residues following the -CCA terminus of tRNA and adds nucleotides to the ends of RNA molecules by using nucleoside diphosphates as substrates. Also acts to regulate the attenuation of PyrE.

Catalytic activityi

tRNA(n+1) + phosphate = tRNA(n) + a nucleoside diphosphate.

GO - Molecular functioni

  • exonuclease activity Source: EcoCyc
  • tRNA binding Source: UniProtKB-HAMAP
  • tRNA nucleotidyltransferase activity Source: EcoCyc
  • tRNA-specific ribonuclease activity Source: InterPro

GO - Biological processi

  • rRNA catabolic process Source: GO_Central
  • tRNA 3'-end processing Source: EcoCyc
  • tRNA metabolic process Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Nucleotidyltransferase, Transferase

Keywords - Biological processi

tRNA processing

Enzyme and pathway databases

BioCyciEcoCyc:EG10863-MONOMER.
MetaCyc:EG10863-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Inactive ribonuclease PH (EC:2.7.7.56)
Short name:
RNase PH
Alternative name(s):
tRNA nucleotidyltransferase
Gene namesi
Name:rph
Ordered Locus Names:b3643, JW3618
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10863. rph.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 228228Inactive ribonuclease PHPRO_0000139889Add
BLAST

Proteomic databases

EPDiP0CG19.
PaxDbiP0CG19.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

DIPiDIP-10738N.
IntActiP0CG19. 8 interactions.
MINTiMINT-1233748.
STRINGi511145.b3643.

Structurei

3D structure databases

ProteinModelPortaliP0CG19.
SMRiP0CG19. Positions 2-222.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the RNase PH family.Curated

Phylogenomic databases

eggNOGiENOG4105ED0. Bacteria.
COG0689. LUCA.
InParanoidiP0CG19.
OrthoDBiEOG6CZQQP.

Family and domain databases

Gene3Di3.30.230.70. 1 hit.
HAMAPiMF_00564. RNase_PH.
InterProiIPR001247. ExoRNase_PH_dom1.
IPR015847. ExoRNase_PH_dom2.
IPR027408. PNPase/RNase_PH_dom.
IPR020568. Ribosomal_S5_D2-typ_fold.
IPR002381. RNase_PH_bac-type.
IPR018336. RNase_PH_CS.
[Graphical view]
PfamiPF01138. RNase_PH. 1 hit.
PF03725. RNase_PH_C. 1 hit.
[Graphical view]
SUPFAMiSSF54211. SSF54211. 1 hit.
SSF55666. SSF55666. 1 hit.
TIGRFAMsiTIGR01966. RNasePH. 1 hit.
PROSITEiPS01277. RIBONUCLEASE_PH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0CG19-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRPAGRSNNQ VRPVTLTRNY TKHAEGSVLV EFGDTKVLCT ASIEEGVPRF
60 70 80 90 100
LKGQGQGWIT AEYGMLPRST HTRNAREAAK GKQGGRTMEI QRLIARALRA
110 120 130 140 150
AVDLKALGEF TITLDCDVLQ ADGGTRTASI TGACVALVDA LQKLVENGKL
160 170 180 190 200
KTNPMKGMVA AVSVGIVNGE AVCDLEYVED SAAETDMNVV MTEDGRIIEV
210 220
QGTAEGEPFT HEELLILLAL ARGESNPL
Length:228
Mass (Da):24,425
Last modified:June 15, 2010 - v1
Checksum:i028BC8F5A6859447
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V01578 Genomic DNA. No translation available.
L10328 Genomic DNA. Translation: AAA61996.1.
U00096 Genomic DNA. No translation available.
AP009048 Genomic DNA. No translation available.
X72920 Genomic DNA. No translation available.
PIRiA04470. QQECPE.

Genome annotation databases

PATRICi32122773. VBIEscCol129921_3763.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V01578 Genomic DNA. No translation available.
L10328 Genomic DNA. Translation: AAA61996.1.
U00096 Genomic DNA. No translation available.
AP009048 Genomic DNA. No translation available.
X72920 Genomic DNA. No translation available.
PIRiA04470. QQECPE.

3D structure databases

ProteinModelPortaliP0CG19.
SMRiP0CG19. Positions 2-222.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-10738N.
IntActiP0CG19. 8 interactions.
MINTiMINT-1233748.
STRINGi511145.b3643.

Proteomic databases

EPDiP0CG19.
PaxDbiP0CG19.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

PATRICi32122773. VBIEscCol129921_3763.

Organism-specific databases

EcoGeneiEG10863. rph.

Phylogenomic databases

eggNOGiENOG4105ED0. Bacteria.
COG0689. LUCA.
InParanoidiP0CG19.
OrthoDBiEOG6CZQQP.

Enzyme and pathway databases

BioCyciEcoCyc:EG10863-MONOMER.
MetaCyc:EG10863-MONOMER.

Miscellaneous databases

PROiP0CG19.

Family and domain databases

Gene3Di3.30.230.70. 1 hit.
HAMAPiMF_00564. RNase_PH.
InterProiIPR001247. ExoRNase_PH_dom1.
IPR015847. ExoRNase_PH_dom2.
IPR027408. PNPase/RNase_PH_dom.
IPR020568. Ribosomal_S5_D2-typ_fold.
IPR002381. RNase_PH_bac-type.
IPR018336. RNase_PH_CS.
[Graphical view]
PfamiPF01138. RNase_PH. 1 hit.
PF03725. RNase_PH_C. 1 hit.
[Graphical view]
SUPFAMiSSF54211. SSF54211. 1 hit.
SSF55666. SSF55666. 1 hit.
TIGRFAMsiTIGR01966. RNasePH. 1 hit.
PROSITEiPS01277. RIBONUCLEASE_PH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "DNA sequence and analysis of 136 kilobases of the Escherichia coli genome: organizational symmetry around the origin of replication."
    Burland V.D., Plunkett G. III, Daniels D.L., Blattner F.R.
    Genomics 16:551-561(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. "The Escherichia coli K-12 'wild types' W3110 and MG1655 have an rph frameshift mutation that leads to pyrimidine starvation due to low pyrE expression levels."
    Jensen K.F.
    J. Bacteriol. 175:3401-3407(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 208-228 (STRAIN W3110), EXPRESSION, LOSS OF ACTIVITY IN SOME K12 STRAINS.
    Strain: K12 / MG1655 / ATCC 47076, K12 / W1485 and K12 / W3110 / ATCC 27325 / DSM 5911.

Entry informationi

Entry nameiRNPH_ECOLI
AccessioniPrimary (citable) accession number: P0CG19
Secondary accession number(s): A8DYQ0, P03842
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: June 15, 2010
Last modified: July 6, 2016
This is version 34 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

The gene in K12 strains MG1655 and W3110 (and also other derivatives of K12 W1485) has a frameshift mutation that leads to loss of activity, although the protein is translated. Thus in those strains rph is an expressed but non-functional pseudogene. For the functional protein without the frameshift mutation see AC P0CG18.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.