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Q5WT40

- PNP_LEGPL

UniProt

Q5WT40 - PNP_LEGPL

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Protein
Polyribonucleotide nucleotidyltransferase
Gene
pnp, lpl2685
Organism
Legionella pneumophila (strain Lens)
Status
Reviewed - Annotation score: 3 out of 5 - Protein inferred from homologyi

Functioni

Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction By similarity.UniRule annotation

Catalytic activityi

RNA(n+1) + phosphate = RNA(n) + a nucleoside diphosphate.UniRule annotation

Cofactori

Magnesium By similarity.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi485 – 4851Magnesium By similarity
Metal bindingi491 – 4911Magnesium By similarity

GO - Molecular functioni

  1. 3'-5'-exoribonuclease activity Source: InterPro
  2. RNA binding Source: UniProtKB-HAMAP
  3. magnesium ion binding Source: UniProtKB-HAMAP
  4. polyribonucleotide nucleotidyltransferase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. RNA processing Source: InterPro
  2. mRNA catabolic process Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Nucleotidyltransferase, Transferase

Keywords - Ligandi

Magnesium, Metal-binding, RNA-binding

Enzyme and pathway databases

BioCyciLPNE297245:GJD4-2907-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Polyribonucleotide nucleotidyltransferase (EC:2.7.7.8)
Alternative name(s):
Polynucleotide phosphorylase
Short name:
PNPase
Gene namesi
Name:pnp
Ordered Locus Names:lpl2685
OrganismiLegionella pneumophila (strain Lens)
Taxonomic identifieri297245 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaLegionellalesLegionellaceaeLegionella
ProteomesiUP000002517: Chromosome

Organism-specific databases

LegioListilpl2685.

Subcellular locationi

Cytoplasm By similarity UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 729729Polyribonucleotide nucleotidyltransferaseUniRule annotation
PRO_0000329693Add
BLAST

Interactioni

Subunit structurei

Component of the RNA degradosome, which is a multiprotein complex involved in RNA processing and mRNA degradation By similarity.

Protein-protein interaction databases

STRINGi297245.lpl2685.

Structurei

3D structure databases

ProteinModelPortaliQ5WT40.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini552 – 61160KH
Add
BLAST
Domaini621 – 68969S1 motif
Add
BLAST

Sequence similaritiesi

Contains 1 KH domain.
Contains 1 S1 motif domain.

Phylogenomic databases

eggNOGiCOG1185.
HOGENOMiHOG000218326.
KOiK00962.
OMAiPRWDWVA.
OrthoDBiEOG6WT8CC.

Family and domain databases

Gene3Di1.10.10.400. 1 hit.
2.40.50.140. 1 hit.
3.30.1370.10. 1 hit.
3.30.230.70. 2 hits.
HAMAPiMF_01595. PNPase.
InterProiIPR001247. ExoRNase_PH_dom1.
IPR015847. ExoRNase_PH_dom2.
IPR004087. KH_dom.
IPR004088. KH_dom_type_1.
IPR012340. NA-bd_OB-fold.
IPR012162. PNPase.
IPR027408. PNPase/RNase_PH_dom.
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]
PANTHERiPTHR11252. PTHR11252. 1 hit.
PfamiPF00013. 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]
PIRSFiPIRSF005499. PNPase. 1 hit.
SMARTiSM00322. KH. 1 hit.
SM00316. S1. 1 hit.
[Graphical view]
SUPFAMiSSF50249. SSF50249. 1 hit.
SSF54211. SSF54211. 2 hits.
SSF54791. SSF54791. 1 hit.
SSF55666. SSF55666. 2 hits.
TIGRFAMsiTIGR03591. polynuc_phos. 1 hit.
PROSITEiPS50084. KH_TYPE_1. 1 hit.
PS50126. S1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q5WT40-1 [UniParc]FASTAAdd to Basket

« Hide

MAKITKEIVF GNHKLILETG EVARQADGAV MASMNGTQVL VTVVWKKDGG    50
ESNDFFPLTV NYQEKFYAIG KIPGGFNKRE GRPSDNETLI SRLIDRPIRP 100
LFPDNFFNEV QIIATVLSLN PEVSPDIIAM IGASAALSIS GVPFNGPIGA 150
ARVGYKDGVY LLNPSRKEQE ESKLDLVIAG TKDAILMVES EAQELSEDIM 200
RGAMLYGHEM MKNVIKSIEE LARDVGKSKP EWKAPEIDTV LKARINDVAR 250
NEVEAAYLIK DKQQRYQRLG ELREQTISAL LAENDELNAD VIANMFGELE 300
RSIVRNRILD GEPRIDGRDH RTVRPISVRT KFLERTHGSC LFTRGETQAI 350
VVATLGNERD AQILDGISGE SRDRFMLHYN FPPYSVGETG QVGSPKRREI 400
GHGRLAKRAL MAVLPDANEF PYVLRIVSEI TESNGSSSMA TVCGTSLALM 450
DAGVPLKAPV AGVAMGLIKE GDRYAVLTDI LGDEDHLGDM DFKVAGTEKG 500
ITALQMDIKI SGITNEIMER ALEQALEGRT HILGVMNNAL AEHRTELSQH 550
APRITTMKVA EDKIRTIIGK GGATIKGLIE STGVSIDIDD SGVIQLFSPD 600
KIALEEAQKQ IKALIAEIEV GQTYQGKVSK IVDFGAFINL LPGKDGLLHI 650
SQICAARTQK VEEVLQEGQE IEVFVAGIDK QGRVKLEWKD KPQAEAKEVE 700
DAPVSATFLT MEEQSEEINS GNKISEEEE 729
Length:729
Mass (Da):80,015
Last modified:November 23, 2004 - v1
Checksum:iC2A81ABF0CCF63C4
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CR628337 Genomic DNA. Translation: CAH16926.1.
RefSeqiYP_128013.1. NC_006369.1.

Genome annotation databases

EnsemblBacteriaiCAH16926; CAH16926; lpl2685.
GeneIDi3114387.
KEGGilpf:lpl2685.
PATRICi22319280. VBILegPne33733_2943.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CR628337 Genomic DNA. Translation: CAH16926.1 .
RefSeqi YP_128013.1. NC_006369.1.

3D structure databases

ProteinModelPortali Q5WT40.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 297245.lpl2685.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAH16926 ; CAH16926 ; lpl2685 .
GeneIDi 3114387.
KEGGi lpf:lpl2685.
PATRICi 22319280. VBILegPne33733_2943.

Organism-specific databases

LegioListi lpl2685.

Phylogenomic databases

eggNOGi COG1185.
HOGENOMi HOG000218326.
KOi K00962.
OMAi PRWDWVA.
OrthoDBi EOG6WT8CC.

Enzyme and pathway databases

BioCyci LPNE297245:GJD4-2907-MONOMER.

Family and domain databases

Gene3Di 1.10.10.400. 1 hit.
2.40.50.140. 1 hit.
3.30.1370.10. 1 hit.
3.30.230.70. 2 hits.
HAMAPi MF_01595. PNPase.
InterProi IPR001247. ExoRNase_PH_dom1.
IPR015847. ExoRNase_PH_dom2.
IPR004087. KH_dom.
IPR004088. KH_dom_type_1.
IPR012340. NA-bd_OB-fold.
IPR012162. PNPase.
IPR027408. PNPase/RNase_PH_dom.
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 ]
PANTHERi PTHR11252. PTHR11252. 1 hit.
Pfami PF00013. 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 ]
PIRSFi PIRSF005499. PNPase. 1 hit.
SMARTi SM00322. KH. 1 hit.
SM00316. S1. 1 hit.
[Graphical view ]
SUPFAMi SSF50249. SSF50249. 1 hit.
SSF54211. SSF54211. 2 hits.
SSF54791. SSF54791. 1 hit.
SSF55666. SSF55666. 2 hits.
TIGRFAMsi TIGR03591. polynuc_phos. 1 hit.
PROSITEi PS50084. KH_TYPE_1. 1 hit.
PS50126. S1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Evidence in the Legionella pneumophila genome for exploitation of host cell functions and high genome plasticity."
    Cazalet C., Rusniok C., Brueggemann H., Zidane N., Magnier A., Ma L., Tichit M., Jarraud S., Bouchier C., Vandenesch F., Kunst F., Etienne J., Glaser P., Buchrieser C.
    Nat. Genet. 36:1165-1173(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Lens.

Entry informationi

Entry nameiPNP_LEGPL
AccessioniPrimary (citable) accession number: Q5WT40
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: November 23, 2004
Last modified: May 14, 2014
This is version 63 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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