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UniProtKB/Swiss-Prot entry Q8NMR4


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

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Entry information
Entry name RNPH_CORGL
Primary accession number Q8NMR4
Secondary accession numbers None
Integrated into Swiss-Prot on November 1, 2002
Sequence was last modified on October 1, 2002 (Sequence version 1)
Annotations were last modified on    December 16, 2008 (Entry version 30)
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: Cgl2501, cg2753
From
Corynebacterium glutamicum (Brevibacterium flavum) [TaxID: 1718] [HAMAP proteome]
Taxonomy Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; Corynebacterineae; Corynebacteriaceae; Corynebacterium.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025;
Nakagawa S.;
"Complete genomic sequence of Corynebacterium glutamicum ATCC 13032.";
Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025;
DOI=10.1016/S0168-1656(03)00154-8; PubMed=12948626 [NCBI, ExPASy, EBI, Israel, Japan]
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., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O., Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
"The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its impact on the production of L-aspartate-derived amino acids and vitamins.";
J. Biotechnol. 104:5-25(2003).
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 (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
BA000036; BAB99894.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BX927155; CAF21164.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_601703.2; -.
YP_226743.1; -.
3D structure databases
ModBase Q8NMR4.
Enzyme and pathway databases
BioCyc CGLU196627-1:CG2753-MON; -.
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.
Genome annotation databases
GeneID 1020448; -.
3342887; -.
GenomeReviews BA000036_GR; Cgl2501.
BX927147_GR; cg2753.
KEGG cgb:cg2753; -.
cgl:NCgl2415; -.
Phylogenomic databases
HOGENOM Q8NMR4; -.
Genome annotation databases
CMR Q8NMR4; Cgl2501.
Other
ProtoNet Q8NMR4.
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   245  245     Ribonuclease PH. PRO_0000139885
Sequence information
Length: 245 AA [This is the length of the unprocessed precursor] Molecular weight: 26133 Da [This is the MW of the unprocessed precursor] CRC64: 62227AC33CAEB801 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MTSSSSFSRF DGRAQDQMRA VKITRGFTSN PAGSVLVEFG NTRVMCTASV ELGVPRFKRD 

        70         80         90        100        110        120 
SGEGWLTAEY AMLPAATAER NRRESMAGKV KGRTHEISRL IGRSLRAAVD LSQLGENTIA 

       130        140        150        160        170        180 
IDCDVLQADG GTRTASITGA YVALADAIKV LQERGVVPGS PLLAPVAAVS VGLVDGNVCL 

       190        200        210        220        230        240 
DLPYEEDSRA DVDLNVVMTE HGEFVEIQGT GEETTFTRAQ LNDMLDHAEK GCRELVAAQK 


AALGI 

Q8NMR4 in FASTA format

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