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UniProtKB/Swiss-Prot entry P66679


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name RNPH_ECOL6
Primary accession number P66679
Secondary accession number Q8XD98
Integrated into Swiss-Prot on October 11, 2004
Sequence was last modified on October 11, 2004 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 23)
Name and origin of the protein
Protein name Ribonuclease PH
Synonyms RNase PH
EC 2.7.7.56
tRNA nucleotidyltransferase
Gene name
Name: rph
OrderedLocusNames: c4467
From
Escherichia coli O6 [TaxID: 217992] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=O6:H1 / CFT073 / ATCC 700928 / UPEC;
DOI=10.1073/pnas.252529799; PubMed=12471157 [NCBI, ExPASy, EBI, Israel, Japan]
Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T., Donnenberg M.S., Blattner F.R.;
"Extensive mosaic structure revealed by the complete genome sequence of uropathogenic Escherichia coli.";
Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
Comments
  • FUNCTION: 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 (By similarity).
  • CATALYTIC ACTIVITY: tRNA(n+1) + phosphate = tRNA(n) + a nucleoside diphosphate.
  • SIMILARITY: Belongs to the RNase PH family.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AE014075; AAN82903.1; ALT_INIT; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_756329.2; -.
3D structure databases
SMR P66679; 2-237.
ModBase P66679.
Ontologies
GO
GO:0000175; Molecular function: 3'-5'-exoribonuclease activity (inferred from electronic annotation from InterPro).
GO:0000049; Molecular function: tRNA binding (inferred from electronic annotation from HAMAP).
GO:0009022; Molecular function: tRNA nucleotidyltransferase activity (inferred from electronic annotation from HAMAP).
GO:0004549; Molecular function: tRNA-specific ribonuclease activity (inferred from electronic annotation from InterPro).
GO:0008033; Biological process: tRNA processing (inferred from electronic annotation from HAMAP).
QuickGo view.
Family and domain databases
HAMAP MF_00564; -; 1.
PBIL [Tree]
InterPro IPR001247; ExoRNase_PH_dom1.
IPR015847; ExoRNase_PH_dom2.
IPR002381; RNase_PH_bac-type.
Graphical view of domain structure.
Pfam PF01138; RNase_PH; 1.
PF03725; RNase_PH_C; 1.
Pfam graphical view of domain structure.
TIGRFAMs TIGR01966; RNasePH; 1.
PROSITE PS01277; RIBONUCLEASE_PH; 1.
ProtoNet P66679.
Genome annotation databases
GeneID 1038263; -.
GenomeReviews AE014075_GR; c4467.
KEGG ecc:c4467; -.
Phylogenomic databases
HOGENOM P66679; -.
Genome annotation databases
CMR P66679; c4467.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Nucleotidyltransferase; Transferase; tRNA processing.
Features
SEVIEWER logo Feature table viewer
KeyFrom To Length Description FTId
CHAIN   1   238  238     Ribonuclease PH. PRO_0000139890
Sequence information
Length: 238 AA [This is the length of the unprocessed precursor] Molecular weight: 25312 Da [This is the MW of the unprocessed precursor] CRC64: D5B174F3ECC8560E [This is a checksum on the sequence]
        10         20         30         40         50         60 
MRPAGRSNNQ VRPVTLTRNY TKHAEGSVLV EFGDTKVLCT ASIEEGVPRF LKGQGQGWIT 

        70         80         90        100        110        120 
AEYGMLPRST HTRNAREAAK GKQGGRTMEI QRLIARALRA AVDLKALGEF TITLDCDVLQ 

       130        140        150        160        170        180 
ADGGTRTASI TGACVALADA LQKLVENGKL KTNPMKGMVA AVSVGIVNGE AVCDLEYVED 

       190        200        210        220        230 
SAAETDMNVV MTEDGRIIEV QGTAEGEPFT HEELLTLLAL ARGGIESIVA TQKAALAN 

P66679 in FASTA format

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Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
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