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Q1LSL2 (PNP_BAUCH) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 40. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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:BCI_0627
OrganismBaumannia cicadellinicola subsp. Homalodisca coagulata [Complete proteome] [HAMAP]
Taxonomic identifier374463 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaCandidatus Baumannia

Protein attributes

Sequence length697 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 MF_01595

Catalytic activity

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

Sequence similarities

Belongs to the polyribonucleotide nucleotidyltransferase family.

Contains 1 KH domain.

Contains 1 S1 motif domain.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 697697Polyribonucleotide nucleotidyltransferase HAMAP MF_01595
PRO_0000329529

Regions

Domain553 – 61260KH
Domain622 – 69069S1 motif

Sequences

Sequence LengthMass (Da)Tools
Q1LSL2 [UniParc].

Last modified May 30, 2006. Version 1.
Checksum: 7420BCBEF594D25F

FASTA69776,711
        10         20         30         40         50         60 
MLNPIVHRFQ YGKHIVILET GIVARQATAA VMVNMADTIV LVTVVGVKQV KPGQKFFPLM 

        70         80         90        100        110        120 
VNYQERTYAA GRFPGGFFRR EGRPSEGEIL ISRMIDRPLR PLFPDGFLNE VQVIATVVSI 

       130        140        150        160        170        180 
NPQVSPDIVA MIGVSAALSI SGIPFNCPFG AARVGYINNQ YVLNPTIAEL VDSSLDLVVA 

       190        200        210        220        230        240 
STANAVLMVE SEAKQLSEEQ MLSAIIFGHE QQQLVIQNIN HMVTIVGKPK WSWQAQVIDT 

       250        260        270        280        290        300 
NLQLCVTELA ESRLNEAFCI SDKQERDVCI ETIKSDVLSA LQQKNETIEE ETISNIFANL 

       310        320        330        340        350        360 
EKQIARNRIL GGKLRIDGRN HKMIRSLDMR TSILPRTHGS ALFVRGETQA LVTVTLGTER 

       370        380        390        400        410        420 
NAQNIDELIG ERTDRFLLHY NFPPYCVGEI GLVGSPKRRE IGHGRLAKRG ILAVMPTANE 

       430        440        450        460        470        480 
FPYTVRVVSE ITESNGSSSM ASVCGTSLAL MDAGVPIKAA VAGVAMGLIK EDNNFVILSD 

       490        500        510        520        530        540 
ILSNEDYIGD MDFKVAGSKN GITALQMDIK TKGITNNIIQ LALNQAKDAR MHILNMMEQV 

       550        560        570        580        590        600 
ISMSRTDISP FAPRIHTIKI HPDKIKDVIG KCGSVIRALT EETKTIIDIE DDGTVTVAAT 

       610        620        630        640        650        660 
DSIKAQQAIC RIKDITAEIE VGSIYHGKVT RIVDFGAFIA ISSNKEGLVH ISQITNKRVE 

       670        680        690 
KVADYLSIDQ IVLVKVLEVD RQGRIRLSMK DTNLTNK 

« Hide

References

[1]"Metabolic complementarity and genomics of the dual bacterial symbiosis of sharpshooters."
Wu D., Daugherty S.C., Van Aken S.E., Pai G.H., Watkins K.L., Khouri H., Tallon L.J., Zaborsky J.M., Dunbar H.E., Tran P.L., Moran N.A., Eisen J.A.
PLoS Biol. 4:1079-1092(2006) [PubMed: 16729848] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000238 Genomic DNA. Translation: ABF13852.1.
RefSeqYP_589052.1. NC_007984.1.

3D structure databases

ProteinModelPortalQ1LSL2.
SMRQ1LSL2. Positions 617-691.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ1LSL2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4056300.
GenomeReviewsGene locus BCI_0627 in contig CP000238_GR.
KEGGbci:BCI_0627.
PATRIC21074761. VBIBauCic75062_0594.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1185.
HOGENOMHBG382411.
OMAYGETVVL.
PhylomeDBQ1LSL2.
ProtClustDBPRK11824.

Enzyme and pathway databases

BioCycBCIC186490:BCI_0627-MONOMER.

Family and domain databases

HAMAPMF_01595. PNPase.
[Tree]
InterProIPR001247. ExoRNase_PH_dom1.
IPR015847. ExoRNase_PH_dom2.
IPR004087. KH.
IPR004088. KH_type_1.
IPR018111. KH_type_1_subgr.
IPR012340. NA-bd_OB-fold.
IPR016027. NA-bd_OB-fold-like.
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]
Gene3DG3DSA:2.40.50.140. OB_NA_bd_sub. 1 hit.
G3DSA:1.10.10.400. PNPase_PH_RNA-bd_bac/org-type. 1 hit.
KOK00962.
PANTHERPTHR11252. PNPase. 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_BAUCH
AccessionPrimary (citable) accession number: Q1LSL2
Entry history
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: May 30, 2006
Last modified: January 25, 2012
This is version 40 of the entry and version 1 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