ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry Q3AFA0


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

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name RNPH_CARHZ
Primary accession number Q3AFA0
Secondary accession numbers None
Integrated into Swiss-Prot on February 5, 2008
Sequence was last modified on November 22, 2005 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 22)
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: CHY_0314
From
Carboxydothermus hydrogenoformans (strain Z-2901 / DSM 6008) [TaxID: 246194] [HAMAP proteome]
Taxonomy Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales; Thermoanaerobacteraceae; Carboxydothermus.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1371/journal.pgen.0010065; PubMed=16311624 [NCBI, ExPASy, EBI, Israel, Japan]
Wu M., Ren Q., Durkin A.S., Daugherty S.C., Brinkac L.M., Dodson R.J., Madupu R., Sullivan S.A., Kolonay J.F., Nelson W.C., Tallon L.J., Jones K.M., Ulrich L.E., Gonzalez J.M., Zhulin I.B., Robb F.T., Eisen J.A.;
"Life in hot carbon monoxide: the complete genome sequence of Carboxydothermus hydrogenoformans Z-2901.";
PLoS Genet. 1:563-574(2005).
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
CP000141; ABB13662.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_359184.1; -.
3D structure databases
ModBase Q3AFA0.
Enzyme and pathway databases
BioCyc CHYD246194:CHY_0314-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.
ProtoNet Q3AFA0.
Genome annotation databases
GeneID 3726312; -.
GenomeReviews CP000141_GR; CHY_0314.
KEGG chy:CHY_0314; -.
NMPDR fig|246194.3.peg.402; -.
TIGR CHY_0314; -.
Phylogenomic databases
HOGENOM Q3AFA0; -.
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   254  254     Ribonuclease PH. PRO_1000061130
Sequence information
Length: 254 AA [This is the length of the unprocessed precursor] Molecular weight: 27772 Da [This is the MW of the unprocessed precursor] CRC64: 438344CFB5B0F5F7 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MRIDGREKDQ LRTVKITTNY IKHAEGSVLI EMGDTRVVCT ATVEDKVPPF AKGEGKGWIT 

        70         80         90        100        110        120 
AEYGMLPRST ETRNVREATK GRQSGRTLEI QRLIGRALRG VVDLKALGER TLWIDCDVIQ 

       130        140        150        160        170        180 
ADGGTRTAAI TGSFVALALA LNKLVEEGIL PVIPLKDFVA AVSVGIVDGE EILDLNFEED 

       190        200        210        220        230        240 
SKALVDMNVV MTGSNRFVEV QGTGEEATFS MEELQRLLTL AQKGIRELIE LQKQALGDIA 

       250 
RRIGMENAAD SNSQ 

Q3AFA0 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by ch flag SIB Switzerland Mirror sites: Australia  Brazil  Canada  China  Korea
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!