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Protein

Polyribonucleotide nucleotidyltransferase

Gene

pnp

Organism
Psychrobacter arcticus (strain DSM 17307 / 273-4)
Status
Reviewed-Annotation score: 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.UniRule annotation

Catalytic activityi

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

Cofactori

Mg2+UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi491 – 4911MagnesiumUniRule annotation
Metal bindingi497 – 4971MagnesiumUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Nucleotidyltransferase, Transferase

Keywords - Ligandi

Magnesium, Metal-binding, RNA-binding

Enzyme and pathway databases

BioCyciPARC259536:GI3A-76-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Polyribonucleotide nucleotidyltransferaseUniRule annotation (EC:2.7.7.8UniRule annotation)
Alternative name(s):
Polynucleotide phosphorylaseUniRule annotation
Short name:
PNPaseUniRule annotation
Gene namesi
Name:pnpUniRule annotation
Ordered Locus Names:Psyc_0074
OrganismiPsychrobacter arcticus (strain DSM 17307 / 273-4)
Taxonomic identifieri259536 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaePsychrobacter
ProteomesiUP000000546 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 700700Polyribonucleotide nucleotidyltransferasePRO_0000329790Add
BLAST

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi259536.Psyc_0074.

Structurei

3D structure databases

ProteinModelPortaliQ4FVL0.
SMRiQ4FVL0. Positions 622-695.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini558 – 61760KHUniRule annotationAdd
BLAST
Domaini627 – 69569S1 motifUniRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the polyribonucleotide nucleotidyltransferase family.UniRule annotation
Contains 1 KH domain.UniRule annotation
Contains 1 S1 motif domain.UniRule annotation

Phylogenomic databases

eggNOGiCOG1185.
HOGENOMiHOG000218326.
KOiK00962.
OMAiRFMFHYN.
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. S1_dom.
[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.

Q4FVL0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTMFNTIKRE FQYGNQQVVI ETGRIARQAN SILVHMGGVT VLVAAVVKSD
60 70 80 90 100
AKEGQNFFPL TVNYQEKMYA AGKIPGAYGK REGRASESET LTSRLIDRPI
110 120 130 140 150
RPLFPEGYVN EIQITATVVS SDKTQSADIA ALIGASAALA ISDAPFNGPV
160 170 180 190 200
AAARVGFING EYVLNPTLEE LKESDLDLVV AGTKSAVLMV ESEAAELSED
210 220 230 240 250
QMLGAVLYGH QQQQIVIDNI ASMAAEIGTA KQQYTAPVRD QALETGMKEQ
260 270 280 290 300
FGAQVSDAYT ITDKQARYSK LNEIKDAAIV ALAGDAESES YSDTVSELKE
310 320 330 340 350
IYNDLKYRTV RDNILSGKPR IDGRDLETVR ALDVQVGVLP FTHGSALFTR
360 370 380 390 400
GETQALVTTT LGNTRDVNMI DSLAGTIRDH FMLHYNFPHF SVGETGREGI
410 420 430 440 450
PKRREIGHGR LARRGVQAML PDSDRFPYVI RVVSEITESN GSSSMASVCG
460 470 480 490 500
ASLALMDAGV PIKAPVAGIA MGLVKEGERF AVLSDILGDE DHLGDMDFKV
510 520 530 540 550
AGSKDGITAL QMDIKIEGIT PDIMEQALKQ AHAGRIHILD AMNKVLPESR
560 570 580 590 600
TEINAHAPNY AVIEINPDKI RDVIGKGGAT IRQLTEETGA VIDIDDAGTI
610 620 630 640 650
RIFGENKAAT KAAIAKIEAI TAEVEVGKTY EGTVARIVDF GAFVNVLPNT
660 670 680 690 700
DGLVHISQIA DERVENVSDY LKEGQIVKVL VQDVDNRGRI KLTMKGIEQS
Length:700
Mass (Da):75,652
Last modified:August 30, 2005 - v1
Checksum:i9FCAC4BEE783B9ED
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000082 Genomic DNA. Translation: AAZ17948.1.
RefSeqiWP_011279387.1. NC_007204.1.

Genome annotation databases

EnsemblBacteriaiAAZ17948; AAZ17948; Psyc_0074.
KEGGipar:Psyc_0074.
PATRICi23054287. VBIPsyArc98534_0088.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000082 Genomic DNA. Translation: AAZ17948.1.
RefSeqiWP_011279387.1. NC_007204.1.

3D structure databases

ProteinModelPortaliQ4FVL0.
SMRiQ4FVL0. Positions 622-695.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi259536.Psyc_0074.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAZ17948; AAZ17948; Psyc_0074.
KEGGipar:Psyc_0074.
PATRICi23054287. VBIPsyArc98534_0088.

Phylogenomic databases

eggNOGiCOG1185.
HOGENOMiHOG000218326.
KOiK00962.
OMAiRFMFHYN.
OrthoDBiEOG6WT8CC.

Enzyme and pathway databases

BioCyciPARC259536:GI3A-76-MONOMER.

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. S1_dom.
[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]
ProtoNetiSearch...

Publicationsi

  1. "The genome sequence of Psychrobacter arcticus 273-4, a psychroactive Siberian permafrost bacterium, reveals mechanisms for adaptation to low-temperature growth."
    Ayala-del-Rio H.L., Chain P.S., Grzymski J.J., Ponder M.A., Ivanova N., Bergholz P.W., Di Bartolo G., Hauser L., Land M., Bakermans C., Rodrigues D., Klappenbach J., Zarka D., Larimer F., Richardson P., Murray A., Thomashow M., Tiedje J.M.
    Appl. Environ. Microbiol. 76:2304-2312(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: DSM 17307 / 273-4.

Entry informationi

Entry nameiPNP_PSYA2
AccessioniPrimary (citable) accession number: Q4FVL0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: August 30, 2005
Last modified: July 22, 2015
This is version 66 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, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.