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UniProtKB/Swiss-Prot entry P28619


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

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Entry information
Entry name RNPH_BACSU
Primary accession number P28619
Secondary accession numbers None
Integrated into Swiss-Prot on December 1, 1992
Sequence was last modified on December 1, 1992 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 63)
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: BSU28370
From
Bacillus subtilis [TaxID: 1423] [HAMAP proteome]
Taxonomy Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1624460 [NCBI, ExPASy, EBI, Israel, Japan]
Craven M.G., Henner D.J., Alessi D., Schauer A.T., Ost K.A., Deutscher M.P., Friedman D.I.;
"Identification of the rph (RNase PH) gene of Bacillus subtilis: evidence for suppression of cold-sensitive mutations in Escherichia coli.";
J. Bacteriol. 174:4727-4735(1992).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=168;
PubMed=8969504 [NCBI, ExPASy, EBI, Israel, Japan]
Wipat A., Carter N., Brignell C.S., Guy J.B., Piper K., Sanders J., Emmerson P.T., Harwood C.R.;
"The dnaB-pheA (256 degrees-240 degrees) region of the Bacillus subtilis chromosome containing genes responsible for stress responses, the utilization of plant cell walls and primary metabolism.";
Microbiology 142:3067-3078(1996).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=168;
DOI=10.1038/36786; PubMed=9384377 [NCBI, ExPASy, EBI, Israel, Japan]
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.;
"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis.";
Nature 390:249-256(1997).
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.
  • 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
M85163; AAA22705.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z75208; CAA99554.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z99118; CAB14797.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A44914; A44914.
RefSeq NP_390715.1; -.
3D structure databases
PDB
1OYP; X-ray; 2.76 A; A/B/C/D/E/F=1-245.[ExPASy / RCSB / EBI]
1OYR; X-ray; 3.10 A; A/B/C/D/E/F=1-245.[ExPASy / RCSB / EBI]
1OYS; X-ray; 2.40 A; A=1-245.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1OYP; -.
1OYR; -.
1OYS; -.
ModBase P28619.
Enzyme and pathway databases
BioCyc BSUB224308:BSU2833-MON; -.
Organism-specific databases
SubtiList BG10357; rph. [Micado]
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.
BLOCKS P28619.
ProtoNet P28619.
Genome annotation databases
GeneID 937463; -.
GenomeReviews AL009126_GR; BSU28370.
KEGG bsu:BSU28370; -.
NMPDR fig|224308.1.peg.2840; -.
Phylogenomic databases
HOGENOM P28619; -.
Genome annotation databases
CMR P28619; BSU28370.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Complete proteome; Nucleotidyltransferase; Transferase; tRNA processing.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   245  245     Ribonuclease PH. PRO_0000139869
STRAND   14    17  4      
STRAND   28    32  5      
STRAND   35    45  11      
HELIX   49    51  3      
STRAND   58    64  7      
HELIX   86   100  15      
HELIX   104   107  4      
STRAND   111   120  10      
HELIX   125   146  22      
STRAND   149   152  4      
STRAND   159   167  9      
TURN   168   170  3      
STRAND   171   175  5      
HELIX   178   183  6      
STRAND   185   193  9      
STRAND   198   207  10      
HELIX   212   236  25      
HELIX   238   240  3      
Sequence information
Length: 245 AA [This is the length of the unprocessed precursor] Molecular weight: 26681 Da [This is the MW of the unprocessed precursor] CRC64: D180DB086A5316B8 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MRHDGRQHDE LRPITFDLDF ISHPEGSVLI TAGNTKVICN ASVEDRVPPF LRGGGKGWIT 

        70         80         90        100        110        120 
AEYSMLPRAT NQRTIRESSK GKISGRTMEI QRLIGRALRA VVDLEKLGER TIWIDCDVIQ 

       130        140        150        160        170        180 
ADGGTRTASI TGAFLAMAIA IGKLIKAGTI KTNPITDFLA AISVGIDKEQ GILLDLNYEE 

       190        200        210        220        230        240 
DSSAEVDMNV IMTGSGRFVE LQGTGEEATF SREDLNGLLG LAEKGIQELI DKQKEVLGDS 


LPELK 

P28619 in FASTA format

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