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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.UniRule annotation

Catalytic activityi

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

Cofactori

Magnesium.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi514 – 5141MagnesiumUniRule annotation
Metal bindingi520 – 5201MagnesiumUniRule annotation

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

BRENDAi2.7.6.5. 5974.

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
OrganismiStreptomyces antibioticus
Taxonomic identifieri1890 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 740740Polyribonucleotide nucleotidyltransferasePRO_0000329887Add
BLAST

Interactioni

Subunit structurei

Homotrimer.1 Publication

Structurei

Secondary structure

1
740
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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ53597.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini580 – 63960KHUniRule annotationAdd
BLAST
Domaini651 – 72373S1 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

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. 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]
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

« Hide

        10         20         30         40         50
MENETHYAEA VIDNGAFGTR TIRFETGRLA KQAAGSAVAY LDDDTMVLSA
60 70 80 90 100
TTASKNPKDQ LDFFPLTVDV EERMYAAGKI PGSFFRREGR PSEDAILTCR
110 120 130 140 150
LIDRPLRPSF KKGLRNEIQV VATIMALNPD HLYDVVAINA ASASTQLAGL
160 170 180 190 200
PFSGPYGGVR VALIRGQWVA FPTHTELEDA VFDMVVAGRV LEDGDVAIMM
210 220 230 240 250
VEAEATEKTV QLVKDGAEAP TEEVVAAGLD AAKPFIKVLC KAQADLAAKA
260 270 280 290 300
AKPTGEFPVP SSTTRTTSEA LSAAVRPELS AALTIAGKQD REAELDRVKA
310 320 330 340 350
LAAEKLLPEF EGREKEISAA YRPWPSSSSA ERVIKEKKRI DGRGVTDIRT
360 370 380 390 400
LAAEVEAIPR VHGSALFERG ETQILGVTTL NMLRMEQQLD TLSPVTRKPY
410 420 430 440 450
MHNYNFPPIS VGETGRVGSP KRREIGHGAL AERAIVPVLP TREEFPYAIR
460 470 480 490 500
QVSEALGSNG STSMGSVCAS TMSLLNAGVP LKAPVAGIAM GLISQEINGE
510 520 530 540 550
THYVALTDIL GAEDAFGDMD FKVAGTKEFV TALQLDTKLD GIPASVLAAA
560 570 580 590 600
LKQARDARLH ILDVMMEAID TPDEMSPNAP RIITVKIPVD KIGEVIGPKR
610 620 630 640 650
QMINQIQEDT GAEITIEDDG TIYIGAADGP AAEAARATIN GIANPTSPEV
660 670 680 690 700
GERILGSVVK TTTFGAFVSL LPGKDGLLHI SQIRKLAGGK RVENVEDVLG
710 720 730 740
VGQKVQVEIA EIDSRGKLSL IPVIEGEEAA SDEKKDDAEQ
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. S1_dom.
[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: October 29, 2014
This is version 82 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