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Q5X1C7

- PNP_LEGPA

UniProt

Q5X1C7 - PNP_LEGPA

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Protein

Polyribonucleotide nucleotidyltransferase

Gene
pnp, lpp2816
Organism
Legionella pneumophila (strain Paris)
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. magnesium ion binding Source: UniProtKB-HAMAP
  3. polyribonucleotide nucleotidyltransferase activity Source: UniProtKB-HAMAP
  4. RNA binding Source: UniProtKB-HAMAP

GO - Biological processi

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

Keywords - Molecular functioni

Nucleotidyltransferase, Transferase

Keywords - Ligandi

Magnesium, Metal-binding, RNA-binding

Enzyme and pathway databases

BioCyciLPNE297246:GCO9-3576-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:lpp2816
OrganismiLegionella pneumophila (strain Paris)
Taxonomic identifieri297246 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaLegionellalesLegionellaceaeLegionella
ProteomesiUP000000610: Chromosome

Organism-specific databases

LegioListilpp2816.

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 annotationPRO_0000329694Add
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

STRINGi297246.lpp2816.

Structurei

3D structure databases

ProteinModelPortaliQ5X1C7.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini552 – 61160KHAdd
BLAST
Domaini621 – 68969S1 motifAdd
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.

Q5X1C7-1 [UniParc]FASTAAdd to Basket

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MAKITKEIVF GNHKLILETG EVARQADGAV MASMNGTQVL VTVVWKKDSG    50
ESNDFFPLTV NYQEKFYAIG KIPGGFNKRE GRPSDNETLI SRLIDRPIRP 100
LFPDNFFNEV QIIATVLSLN PEVSPDIIAM IGASAALSIS GVPFNGPIGA 150
ARVGYKDGVY LLNPSRKEQE ESKLDLVIAG TKDAILMVES EAQELSEDIM 200
RGAMLYGHEM MKSVIKSIEE LAREVGKSKP EWKAPEIDTV LKARINDVAR 250
NEVEAAYLIK DKQQRYQRLD ELREQTISAL LAENDELNAD VIANMFGELE 300
RSIVRNRILD GEPRIDGRDH RTVRPISIRT KFLERTHGSC LFTRGETQAI 350
VVATLGNERD AQILDGISGE TRDRFMLHYN FPPYSVGETG QVGSPKRREI 400
GHGRLAKRAL MAVLPDTNEF PYVLRIVSEI TESNGSSSMA TVCGTSLALM 450
DAGVPLKAPV AGVAMGLIKE GDRYAVLTDI LGDEDHLGDM DFKVAGTEKG 500
ITALQMDIKI SGITNEIMER ALEQALEGRT HILGVMNNAL AEHRTELSQH 550
APRITTMKVA EDKIRTIIGK GGATIKGLIE STGVSIDIDD SGVIQLFSPD 600
KMALEEAQKQ IKALIAEIEV GQTYQGKVSK IVDFGAFINL LPGKDGLLHI 650
SQICAERTQK VEEVLQEGQE IEVFVAGIDK QGRVKLEWKD KPQAEAKEVE 700
GASVSATFLT MEEQSEEINS GNKISEEEE 729
Length:729
Mass (Da):80,156
Last modified:November 23, 2004 - v1
Checksum:i6E8958CD79A44FDE
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CR628336 Genomic DNA. Translation: CAH13969.1.
RefSeqiYP_125121.1. NC_006368.1.

Genome annotation databases

EnsemblBacteriaiCAH13969; CAH13969; lpp2816.
GeneIDi3116499.
KEGGilpp:lpp2816.
PATRICi22326319. VBILegPne27771_3191.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CR628336 Genomic DNA. Translation: CAH13969.1 .
RefSeqi YP_125121.1. NC_006368.1.

3D structure databases

ProteinModelPortali Q5X1C7.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 297246.lpp2816.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAH13969 ; CAH13969 ; lpp2816 .
GeneIDi 3116499.
KEGGi lpp:lpp2816.
PATRICi 22326319. VBILegPne27771_3191.

Organism-specific databases

LegioListi lpp2816.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyci LPNE297246:GCO9-3576-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: Paris.

Entry informationi

Entry nameiPNP_LEGPA
AccessioniPrimary (citable) accession number: Q5X1C7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: November 23, 2004
Last modified: May 14, 2014
This is version 64 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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