NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=USDA 110;
DOI=10.1093/dnares/9.6.189; PubMed=12597275 [NCBI, ExPASy, EBI, Israel, Japan]
Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S., Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M., Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
"Complete genomic sequence of nitrogen-fixing symbiotic bacterium Bradyrhizobium japonicum USDA110.";
DNA Res. 9:189-197(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 (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

BA000040; BAC45939.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_767314.1; -.

3D structure databases

HSSP

P50597; 1R6L. [HSSP ENTRY / PDB]

ModBase

Q89WK4.

Enzyme and pathway databases

BioCyc

BJAP224911:BLL0674-MON; -.

Ontologies

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

1049284; -.

GenomeReviews

BA000040_GR; bll0674.

KEGG

bja:bll0674; -.

NMPDR

fig|224911.1.peg.674; -.

Phylogenomic databases

HOGENOM

Q89WK4; -.

Genome annotation databases

CMR

Q89WK4; bll0674.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Complete proteome; Nucleotidyltransferase; Transferase; tRNA processing.

Features

Feature table viewer

`Key`	`From To`	`Length`		`Description`	`FTId`
`CHAIN`	`1 237`	`237`		`Ribonuclease PH.`	`PRO_0000139875`

Sequence information

Length: 237 AA [This is the length of the unprocessed precursor]

Molecular weight: 25912 Da [This is the MW of the unprocessed precursor]

CRC64: ABD1899D4DC79323 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MRPSRRAPDE LRPVTLERGV VKYAEGSCLV KFGDTHVLVT ATLEDRLPPW LKGQGRGWVT 

        70         80         90        100        110        120 
AEYGMLPRAT SERTRREASA GKQSGRTVEI QRLIGRSLRT IINLEALGER QITVDCDVLQ 

       130        140        150        160        170        180 
ADGGTRTASI TGAWVALADC VNWMKARNMV KANVLRDNVA AISCGIYNGT PVLDLDYAED 

       190        200        210        220        230 
SEAQTDANFV MTGDGRIIEV QGTAEREPFT QDELLALMAL AQKGIARLVD LQKLAVA

Q89WK4 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 submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools