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: Involved in mRNA degradation. Hydrolyzes single-stranded polyribonucleotides processively in the 3'- to 5'-direction (By similarity).
CATALYTIC ACTIVITY: RNA(n+1) + phosphate = RNA(n) + a nucleoside diphosphate.
SUBUNIT: Homotrimer. Organized into a structure (processome or RNA degradosome) containing a number of RNA-processing enzymes (By similarity).
SUBCELLULAR LOCATION: Cytoplasm (By similarity).
SIMILARITY: Belongs to the polyribonucleotide nucleotidyltransferase family.
SIMILARITY: Contains 1 KH domain.
SIMILARITY: Contains 1 S1 motif domain.

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; BAC46044.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_767419.1; -.

3D structure databases

HSSP

P05055; 1SRO. [HSSP ENTRY / PDB]

ModBase

Q89WB3.

Enzyme and pathway databases

BioCyc

BJAP224911:BLL0779-MON; -.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from HAMAP).
GO:0000175;	Molecular function: 3'-5'-exoribonuclease activity (inferred from electronic annotation from InterPro).
GO:0004654;	Molecular function: polyribonucleotide nucleotidyltransferase activity (inferred from electronic annotation from HAMAP).
GO:0003723;	Molecular function: RNA binding (inferred from electronic annotation from InterPro).
GO:0006402;	Biological process: mRNA catabolic process (inferred from electronic annotation from HAMAP).
GO:0006396;	Biological process: RNA processing (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

HAMAP

MF_01595; -; 1.
PBIL [Tree]

InterPro

IPR001247; ExoRNase_PH_dom1.
IPR015847; ExoRNase_PH_dom2.
IPR004087; KH.
IPR004088; KH_type_1.
IPR012340; NA-bd_OB-fold.
IPR012162; PNPase.
IPR015848; PNPase_PH_RNA-bd_bac/org-type.
IPR003029; S1_RNA-bd.
Graphical view of domain structure.

Gene3D

G3DSA:2.40.50.140; OB_NA_bd_sub; 1.
G3DSA:1.10.10.400; PNPase_PH_RNA-bd_bac/org-type; 1.

PANTHER

PTHR11252; PNPase; 1.

Pfam

PF00013; KH_1; 1.
PF03726; PNPase; 1.
PF01138; RNase_PH; 2.
PF03725; RNase_PH_C; 2.
PF00575; S1; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF005499; PNPase; 1.

SMART

SM00322; KH; 1.
SM00316; S1; 1.
SMART graphical view of domain structure.

PROSITE

PS50084; KH_TYPE_1; 1.
PS50126; S1; 1.
PROSITE graphical view of domain structure (profiles).

Genome annotation databases

GeneID

1048800; -.

GenomeReviews

BA000040_GR; bll0779.

KEGG

bja:bll0779; -.

NMPDR

fig|224911.1.peg.779; -.

Phylogenomic databases

HOGENOM

Q89WB3; -.

Genome annotation databases

CMR

Q89WB3; bll0779.

Other

UniRef

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

Keywords

Complete proteome; Cytoplasm; Nucleotidyltransferase; RNA-binding; Transferase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 720`	`720`	`Polyribonucleotide nucleotidyltransferase.`	`PRO_0000329542`
`DOMAIN`	`554 613`	`60`	`KH.`
`DOMAIN`	`623 691`	`69`	`S1 motif.`

Sequence information

Length: 720 AA [This is the length of the unprocessed precursor]

Molecular weight: 78299 Da [This is the MW of the unprocessed precursor]

CRC64: 12FB5FDE3A440DB2 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MFNKHSVEID WGGRPLKLET GKIARQADGA VVATYGETVV LATVVAAKAP REGVDFLPLT 

        70         80         90        100        110        120 
VDYQEKTYAA GRIPGGYFKR EGRPTEKETL VSRLIDRPIR PLFVDGWRNE TQVIATVLSH 

       130        140        150        160        170        180 
DMENDPDIVA LVASSAALTL SGAPFKGPIG AARVGFVNDE YVLNPTLDEM VDTQLDLVVA 

       190        200        210        220        230        240 
GTADAVLMVE SEAKELNEDI MLGAVMFGHR HFQPVINAII ELAEKAAKEP REVTVIDNAA 

       250        260        270        280        290        300 
LEKEMLGLVE QELRAAYAIP VKQDRYAAVG KVKEKVIAHY FPEGQEPKYD KLRIAGVFKE 

       310        320        330        340        350        360 
LEAKIVRWNI LDTGKRIDGR DSKTVRNIIA EVGVLPRAHG SALFTRGETQ AMVVTTLGTG 

       370        380        390        400        410        420 
EDEQYIDALS GTYKETFLLH YNFPPYSVGE TGRLGGTKRR EIGHGKLAWR AIHPVLPPHH 

       430        440        450        460        470        480 
EFPYTIRVVS EITESNGSSS MASVCGASLA LMDAGVPLKR PTAGIAMGLI LEDKRFAVLS 

       490        500        510        520        530        540 
DILGDEDHLG DMDFKVAGTE SGITSLQMDI KIEGITEEIM KVALGQAKDG RIHILGEMAK 

       550        560        570        580        590        600 
ALTNARAELG EYAPRIETFK IPTDKIREVI GTGGKVIREI VEKTGAKVNI EDDGTVKVAS 

       610        620        630        640        650        660 
SDGEAMKAAI KWIKSIASEP EVGQIYDGTV VKVMEFGAFV NFFGSKDGLV HISQLASARV 

       670        680        690        700        710        720 
QKTSDVVKEG DKVKVKLLGF DDRGKTRLSM KVVDQTTGED LEAKDKVAEG EKAPREAAGE

Q89WB3 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	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