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Q53597

- PNP_STRAT

UniProt

Q53597 - PNP_STRAT

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Protein
Polyribonucleotide nucleotidyltransferase
Gene
pnp
Organism
Streptomyces antibioticus
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at protein leveli

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 bindingi514 – 5141Magnesium By similarity
Metal bindingi520 – 5201Magnesium 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

BRENDAi2.7.6.5. 5974.

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
OrganismiStreptomyces antibioticus
Taxonomic identifieri1890 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

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 – 740740Polyribonucleotide nucleotidyltransferaseUniRule annotation
PRO_0000329887Add
BLAST

Interactioni

Subunit structurei

Homotrimer.1 Publication

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 138
Helixi15 – 173
Beta strandi19 – 2911
Beta strandi33 – 419
Turni42 – 443
Beta strandi45 – 5713
Beta strandi66 – 727
Helixi74 – 774
Helixi93 – 10614
Helixi107 – 1093
Beta strandi116 – 12611
Helixi134 – 14714
Beta strandi150 – 1523
Beta strandi157 – 1648
Beta strandi167 – 1715
Helixi174 – 1774
Beta strandi180 – 19011
Beta strandi196 – 20510
Helixi209 – 2146
Helixi222 – 25029
Helixi265 – 28218
Helixi288 – 30316
Turni307 – 3104
Helixi314 – 33522
Beta strandi351 – 3555
Beta strandi358 – 36912
Beta strandi372 – 38211
Helixi383 – 3853
Beta strandi386 – 3883
Beta strandi391 – 3944
Beta strandi397 – 4059
Helixi408 – 4114
Helixi422 – 43514
Helixi436 – 4383
Turni442 – 4443
Beta strandi447 – 45711
Helixi462 – 47716
Beta strandi486 – 49914
Beta strandi501 – 5088
Helixi511 – 5166
Beta strandi518 – 5258
Beta strandi527 – 53711
Helixi544 – 56825
Helixi607 – 6115
Beta strandi626 – 6283
Helixi629 – 6324
Beta strandi657 – 6604

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1E3HX-ray2.60A1-740[»]
1E3PX-ray2.50A1-665[»]
ProteinModelPortaliQ53597.
SMRiQ53597. Positions 3-717.

Miscellaneous databases

EvolutionaryTraceiQ53597.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini580 – 63960KH
Add
BLAST
Domaini651 – 72373S1 motif
Add
BLAST

Sequence similaritiesi

Contains 1 KH domain.
Contains 1 S1 motif domain.

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.
IPR014069. pppGpp_PNP.
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]
SUPFAMiSSF46915. SSF46915. 1 hit.
SSF54211. SSF54211. 2 hits.
SSF54791. SSF54791. 1 hit.
SSF55666. SSF55666. 2 hits.
TIGRFAMsiTIGR03591. polynuc_phos. 1 hit.
TIGR02696. pppGpp_PNP. 1 hit.
PROSITEiPS50084. KH_TYPE_1. 1 hit.
PS50126. S1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q53597-1 [UniParc]FASTAAdd to Basket

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MENETHYAEA VIDNGAFGTR TIRFETGRLA KQAAGSAVAY LDDDTMVLSA    50
TTASKNPKDQ LDFFPLTVDV EERMYAAGKI PGSFFRREGR PSEDAILTCR 100
LIDRPLRPSF KKGLRNEIQV VATIMALNPD HLYDVVAINA ASASTQLAGL 150
PFSGPYGGVR VALIRGQWVA FPTHTELEDA VFDMVVAGRV LEDGDVAIMM 200
VEAEATEKTV QLVKDGAEAP TEEVVAAGLD AAKPFIKVLC KAQADLAAKA 250
AKPTGEFPVP SSTTRTTSEA LSAAVRPELS AALTIAGKQD REAELDRVKA 300
LAAEKLLPEF EGREKEISAA YRPWPSSSSA ERVIKEKKRI DGRGVTDIRT 350
LAAEVEAIPR VHGSALFERG ETQILGVTTL NMLRMEQQLD TLSPVTRKPY 400
MHNYNFPPIS VGETGRVGSP KRREIGHGAL AERAIVPVLP TREEFPYAIR 450
QVSEALGSNG STSMGSVCAS TMSLLNAGVP LKAPVAGIAM GLISQEINGE 500
THYVALTDIL GAEDAFGDMD FKVAGTKEFV TALQLDTKLD GIPASVLAAA 550
LKQARDARLH ILDVMMEAID TPDEMSPNAP RIITVKIPVD KIGEVIGPKR 600
QMINQIQEDT GAEITIEDDG TIYIGAADGP AAEAARATIN GIANPTSPEV 650
GERILGSVVK TTTFGAFVSL LPGKDGLLHI SQIRKLAGGK RVENVEDVLG 700
VGQKVQVEIA EIDSRGKLSL IPVIEGEEAA SDEKKDDAEQ 740
Length:740
Mass (Da):79,160
Last modified:November 1, 1996 - v1
Checksum:iF07224C64018BA54
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U19858 Genomic DNA. Translation: AAB17498.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U19858 Genomic DNA. Translation: AAB17498.1 .

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1E3H X-ray 2.60 A 1-740 [» ]
1E3P X-ray 2.50 A 1-665 [» ]
ProteinModelPortali Q53597.
SMRi Q53597. Positions 3-717.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

BRENDAi 2.7.6.5. 5974.

Miscellaneous databases

EvolutionaryTracei Q53597.

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.
IPR014069. pppGpp_PNP.
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 SSF46915. SSF46915. 1 hit.
SSF54211. SSF54211. 2 hits.
SSF54791. SSF54791. 1 hit.
SSF55666. SSF55666. 2 hits.
TIGRFAMsi TIGR03591. polynuc_phos. 1 hit.
TIGR02696. pppGpp_PNP. 1 hit.
PROSITEi PS50084. KH_TYPE_1. 1 hit.
PS50126. S1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Guanosine pentaphosphate synthetase from Streptomyces antibioticus is also a polynucleotide phosphorylase."
    Jones G.H., Bibb M.J.
    J. Bacteriol. 178:4281-4288(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: DSM 41481 / IMRU 3720.
  2. "A duplicated fold is the structural basis for polynucleotide phosphorylase catalytic activity, processivity, and regulation."
    Symmons M.F., Jones G.H., Luisi B.F.
    Structure 8:1215-1226(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), SUBUNIT.

Entry informationi

Entry nameiPNP_STRAT
AccessioniPrimary (citable) accession number: Q53597
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: November 1, 1996
Last modified: July 9, 2014
This is version 80 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

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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