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Reviewed, UniProtKB/Swiss-Prot A9NGE2 (PNP_ACHLI)

Last modified June 16, 2009. Version 13. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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: ACL_0808
OrganismAcholeplasma laidlawii (strain PG-8A) [Complete proteome] [HAMAP]
Taxonomic identifier441768 [NCBI]
Taxonomic lineageBacteriaTenericutesMollicutesAcholeplasmatalesAcholeplasmataceaeAcholeplasma

Protein attributes

Sequence length715 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

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.

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 – 715715Polyribonucleotide nucleotidyltransferase HAMAP MF_01595
PRO_0000329476

Regions

Domain567 – 63468KH
Domain637 – 71276S1 motif

Sequences

Sequence LengthMass (Da)Tools
A9NGE2-1 [UniParc].

Last modified February 5, 2008. Version 1.
Checksum: 0A03C34B64B5E270

FASTA71578,666
        10         20         30         40         50         60 
MSKQVFETTL AGKPLRVEVG EIAKQANGAA MIYYGDTVVL STAVAKAKVG QTDFFPLMVI 

        70         80         90        100        110        120 
YAEKQYAAGK IPGGFFRREG RPSEVETLTS RLIDRPLRPL FDDGYRNEVQ VVNTVLSSDP 

       130        140        150        160        170        180 
EASSQMAAML GSSIALEISN IPFMGPIAGA HVGRIDGQFV LNPSSEQLNV SDIDLIVAGT 

       190        200        210        220        230        240 
KDAINMVEAG AKQVSEEVML EAILFGHEAI KELCAFQETI KKAFGVEKVE PELLSLNQAI 

       250        260        270        280        290        300 
FDEVFAYKGK ELVKAVSLVD KQERYDVIDA IKDEVVAHFE QRNFWMTVDG KEVLDADQKK 

       310        320        330        340        350        360 
ELMNQVKVSL DRIVTKEVRR LITEDKVRPD GRGLDEIRPL ASSVDLLPRT HGSALFTRGQ 

       370        380        390        400        410        420 
TQALGIVTLG SLNENQIIDG LEQETVTKRF MLHYNFPPFS VGETGRYGAP GRREIGHGAL 

       430        440        450        460        470        480 
GERALLQVLP SEDEFPYAIR VVSEITESNG SSSQATICVG SMALMAAGVP IKAPVAGIAM 

       490        500        510        520        530        540 
GLIMDGEHYS ILSDIQGMED HEGDMDFKVA GTKDGITALQ MDIKIQGITT EIMKEALEQA 

       550        560        570        580        590        600 
RKGRLHILSH MNTVISETRT ELSAFAPKVK MIRINPDKIR DVIGAGGKII TQIIEDHNNV 

       610        620        630        640        650        660 
KIDIEQDGRV FIMHTDSAWL NKTAAYIESL VREAKVGELY EAKVTRLLMD KDGKKIQGVF 

       670        680        690        700        710 
AEIFPGTEGL VHISKWEKER TESLDGKVKV GDQILVKVVK IDERGRVDLS RKDAL 

« Hide

References

[1]"Acholeplasma laidlawii complete genome."
Kovaleva G.Y., Kazanov M.D., Malko D.B., Vitreschak A.G., Sernova N.V., Gelfand M.S., Lazarev V.N., Levitskii S.A., Basovskii Y.I., Chukin M.M., Akopian T.A., Vereshchagin V.A., Kostrjukova E.S., Selezneva O.V., Vtyurin N.N., Rogov S.I., Alekseev D.G., Ladygina V.G. expand/collapse author list , Titova G.A., Karpov V.A., Govorun V.M.
Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000896 Genomic DNA. Translation: ABX81422.1.
RefSeqYP_001620798.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID5803780.
GenomeReviewsGene locus ACL_0808 in contig CP000896_GR.
KEGGacl:ACL_0808.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAA9NGE2. GHGNLAK.

Family and domain databases

HAMAPMF_01595.
[Tree]
InterProIPR001247. ExoRNase_PH_dom1.
IPR015847. ExoRNase_PH_dom2.
IPR004087. KH.
IPR018111. KH_type_1_subgr.
IPR012340. NA-bd_OB-fold.
IPR012162. PNPase.
IPR015848. PNPase_PH_RNA-bd_bac/org-type.
IPR003029. Rbsml_prot_S1_RNA-bd_dom.
[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.
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.
[Graphical view]
TIGRFAMsTIGR03591. Polynuc_phos. 1 hit.
PROSITEPS50084. KH_TYPE_1. False negative.
PS50126. S1. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePNP_ACHLI
AccessionPrimary (citable) accession number: A9NGE2
Entry history
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: February 5, 2008
Last modified: June 16, 2009
This is version 13 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents