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Q53597

- PNP_STRAT

UniProt

Q53597 - PNP_STRAT

Protein

Polyribonucleotide nucleotidyltransferase

Gene

pnp

Organism
Streptomyces antibioticus
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 81 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    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

    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-SubCell

    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. 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

    « Hide

    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: October 1, 2014
    This is version 81 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