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Q9RSR1 (PNP_DEIRA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Polyribonucleotide nucleotidyltransferase
EC=2.7.7.8
Alternative name(s):
Polynucleotide phosphorylase
Short name=PNPase
Gene names
Name:pnp
Ordered Locus Names:DR_2063
OrganismDeinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422) [Reference proteome] [HAMAP]
Taxonomic identifier243230 [NCBI]
Taxonomic lineageBacteria › Deinococcus-Thermus › Deinococci › Deinococcales › Deinococcaceae › Deinococcus ›

Protein attributes

Sequence length779 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Involved in mRNA degradation. Hydrolyzes single-stranded polyribonucleotides processively in the 3'- to 5'-direction By similarity. HAMAP-Rule MF_01595

Catalytic activity

RNA(n+1) + phosphate = RNA(n) + a nucleoside diphosphate. HAMAP-Rule MF_01595

Subunit structure

Homotrimer. Organized into a structure (processome or RNA degradosome) containing a number of RNA-processing enzymes By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the polyribonucleotide nucleotidyltransferase family.

Contains 1 KH domain.

Contains 1 S1 motif domain.

Sequence caution

The sequence AAF11608.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 779779Polyribonucleotide nucleotidyltransferase HAMAP-Rule MF_01595
PRO_0000329621

Regions

Domain557 – 61862KH
Domain625 – 69369S1 motif

Sequences

Sequence LengthMass (Da)Tools
Q9RSR1 [UniParc].

Last modified April 29, 2008. Version 2.
Checksum: BA5102FE4984A2BB

FASTA77984,062
        10         20         30         40         50         60 
MIGKTFTTML GGRELSIETG KLAKLVSGSV TVRYGDTLLL VTAQASDTQS KLDFLPLTVE 

        70         80         90        100        110        120 
FEERHYAVGK IPGSFQRREG RPGEKAILSA RITDRQIRPL FPKGYRHETQ VIITVLSADG 

       130        140        150        160        170        180 
QNAPDVLGPI GAAAALSISD IPWAGPTACV RVGQIDGQYV VNPTTEQLTR SRMDLVVAGT 

       190        200        210        220        230        240 
REAVMMVECG AQTVSEDDLV GAIEFAHAEM QGVIALIEQM RAEVGHEKFN FLAEEGPAND 

       250        260        270        280        290        300 
YVPELTEKAK AAGLRDALLT HGKKDRSARL KALRNGLIEG YVPDPTAEGS AELTQALKDA 

       310        320        330        340        350        360 
FGKVEKRELR RLILEENLRA DGRDSKTVRP IWIEARPLPT AHGSAVFTRG ETQVLGVTTL 

       370        380        390        400        410        420 
GTERDEILID DLTAESGDKF LLHYNFPPYS TGEVKRMGGQ SRREIGHGNL AKRAIRAVLP 

       430        440        450        460        470        480 
SFEEFPYVIR VVGDVLESNG SSSMGTVCAG TLSLMDAGVP LKAPVAGVAM GLVMEGDNYR 

       490        500        510        520        530        540 
VLTDILGLED ALGDMDFKVC GTAEGVTALQ MDIKVGGITP QIMREALAQA KEGRLHILGK 

       550        560        570        580        590        600 
MAEVLAAPRA ELSPTAPHIL SLKINPELIG KVIGPGGKQV RELEAMGAQV TIEEDGTVRI 

       610        620        630        640        650        660 
FSASGESAEA VKARIEAVTK EAKVGEEFEG TVVKIAPFGA FVNLFPGQDG MLHISQLSEQ 

       670        680        690        700        710        720 
RVENVEDVLT VGDKLKVKIA NIDDRGKIDL IRPELEGKVP LREPRAPRGG DRGPRRDSDR 

       730        740        750        760        770 
GGDRGPRREF SDRGPRPEGA RSERPEGQRT ERPATAPATQ ESSQSSDAPA APVFPRRED

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE000513 Genomic DNA. Translation: AAF11608.1. Different initiation.
PIRG75320.
RefSeqNP_295786.1. NC_001263.1.

3D structure databases

HSSPHSSP built from PDB template 1SRO based on UniProtKB P05055.
ProteinModelPortalQ9RSR1.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-58603N.
STRING243230.DR_2063.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAF11608; AAF11608; DR_2063.
GeneID1797763.
KEGGdra:DR_2063.
PATRIC21631804. VBIDeiRad64572_2288.

Phylogenomic databases

eggNOGCOG1185.
HOGENOMHOG000218326.
KOK00962.
OMAYTMRVVS.
ProtClustDBPRK11824.

Enzyme and pathway databases

BioCycDRAD243230:GH46-2431-MONOMER.

Family and domain databases

Gene3D1.10.10.400. 1 hit.
2.40.50.140. 1 hit.
HAMAPMF_01595. PNPase.
InterProIPR001247. ExoRNase_PH_dom1.
IPR015847. ExoRNase_PH_dom2.
IPR004087. KH_dom.
IPR004088. KH_dom_type_1.
IPR012340. NA-bd_OB-fold.
IPR012162. PNPase.
IPR015848. PNPase_PH_RNA-bd_bac/org-type.
IPR003029. Rbsml_prot_S1_RNA-bd_dom.
IPR020568. Ribosomal_S5_D2-typ_fold.
IPR022967. RNA-binding_domain_S1.
[Graphical view]
PANTHERPTHR11252. PTHR11252. 1 hit.
PfamPF00013. KH_1. 1 hit.
PF03726. PNPase. 1 hit.
PF01138. RNase_PH. 2 hits.
PF03725. RNase_PH_C. 2 hits.
PF00575. S1. 1 hit.
[Graphical view]
PIRSFPIRSF005499. PNPase. 1 hit.
SMARTSM00322. KH. 1 hit.
SM00316. S1. 1 hit.
[Graphical view]
SUPFAMSSF46915. 3_ExoRNase. 1 hit.
SSF55666. 3_ExoRNase. 2 hits.
SSF50249. Nucleic_acid_OB. 1 hit.
SSF54211. Ribosomal_S5_D2-typ_fold. 2 hits.
TIGRFAMsTIGR03591. polynuc_phos. 1 hit.
PROSITEPS50084. KH_TYPE_1. 1 hit.
PS50126. S1. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePNP_DEIRA
AccessionPrimary (citable) accession number: Q9RSR1
Entry history
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: April 29, 2008
Last modified: May 1, 2013
This is version 74 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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