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P51006

- PAPO3_XENLA

UniProt

P51006 - PAPO3_XENLA

Protein

Poly(A) polymerase type 3

Gene
N/A
Organism
Xenopus laevis (African clawed frog)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 68 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
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    Functioni

    Polymerase that creates the 3'-poly(A) tail of mRNA's. May acquire specificity through interaction with a cleavage and polyadenylation factor (CPSF).

    Catalytic activityi

    ATP + RNA(n) = diphosphate + RNA(n+1).

    Cofactori

    Binds 2 magnesium ions. Also active with manganese By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei106 – 1061ATPBy similarity
    Metal bindingi110 – 1101Magnesium 1; catalyticBy similarity
    Metal bindingi110 – 1101Magnesium 2; catalyticBy similarity
    Metal bindingi112 – 1121Magnesium 1; catalyticBy similarity
    Metal bindingi112 – 1121Magnesium 2; catalyticBy similarity
    Metal bindingi164 – 1641Magnesium 2; catalyticBy similarity
    Binding sitei164 – 1641ATPBy similarity
    Binding sitei225 – 2251ATPBy similarity
    Binding sitei234 – 2341ATPBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi97 – 993ATPBy similarity
    Nucleotide bindingi110 – 1123ATPBy similarity
    Nucleotide bindingi243 – 2442ATPBy similarity

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. metal ion binding Source: UniProtKB-KW
    3. polynucleotide adenylyltransferase activity Source: UniProtKB-EC
    4. RNA binding Source: UniProtKB-KW

    GO - Biological processi

    1. mRNA processing Source: UniProtKB-KW
    2. RNA polyadenylation Source: InterPro

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    mRNA processing

    Keywords - Ligandi

    ATP-binding, Magnesium, Manganese, Metal-binding, Nucleotide-binding, RNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Poly(A) polymerase type 3 (EC:2.7.7.19)
    Short name:
    PAP
    Alternative name(s):
    Polynucleotide adenylyltransferase
    OrganismiXenopus laevis (African clawed frog)
    Taxonomic identifieri8355 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

    Organism-specific databases

    XenbaseiXB-GENE-944355. papola.

    Subcellular locationi

    GO - Cellular componenti

    1. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – ›400›400Poly(A) polymerase type 3PRO_0000051616Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliP51006.
    SMRiP51006. Positions 17-370.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi382 – 3909Nuclear localization signalBy similarity

    Sequence similaritiesi

    Belongs to the poly(A) polymerase family.Curated

    Phylogenomic databases

    HOVERGENiHBG053502.

    Family and domain databases

    InterProiIPR002934. Nucleotidyltransferase.
    IPR007012. PolA_pol_cen_dom.
    IPR014492. PolyA_polymerase.
    [Graphical view]
    PfamiPF01909. NTP_transf_2. 1 hit.
    PF04928. PAP_central. 1 hit.
    [Graphical view]
    PIRSFiPIRSF018425. PolyA_polymerase. 1 hit.

    Sequencei

    Sequence statusi: Fragment.

    P51006-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPFPLASQGS QQSQKTYGIT SPISLATPKD TDCTLTQKLI ETLKPYGVFE    50
    EEDELQHRIL SLGKLNNLVK EWIREISELK NLPQSVIENV GGKIFTFGSY 100
    RLGVHTKGAD IDALCVAPRH VDRSDLFSSF YEKLKQQEEV KDLRSVEEAF 150
    VPVIKLCFDG IEIDILFARL ALQTIPEDLD LRDDSLLKNL DIRCIRSLNG 200
    CRVTDEILHL VPNIDSFRLT LRAIKLWAKR HNIYSNILGF LGGVSWAMLV 250
    ARTCQLYPNA IASTLVHKFF LVFSKWEWPN PVLLKQPEEC NLNLPVWDPR 300
    VNPSDRYHLM PIITPAYPQQ NSTYNVSVST RAVMVEEFKQ GLAITDEILL 350
    LKAEWSKLFD APNFFQKYKY VFYNLLAMFA WGEIINKNKK RCYTLKKKKK 400
    Length:400
    Mass (Da):46,020
    Last modified:October 1, 1996 - v1
    Checksum:iAB4347C074E60CA3
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti61 – 611S → I in AAA64708. (PubMed:7862135)Curated
    Sequence conflicti126 – 1261L → F in AAA64708. (PubMed:7862135)Curated
    Non-terminal residuei400 – 4001

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U19975 mRNA. Translation: AAC59747.1.
    U23456 mRNA. Translation: AAA64708.1.
    PIRiI51681.
    UniGeneiXl.341.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U19975 mRNA. Translation: AAC59747.1 .
    U23456 mRNA. Translation: AAA64708.1 .
    PIRi I51681.
    UniGenei Xl.341.

    3D structure databases

    ProteinModelPortali P51006.
    SMRi P51006. Positions 17-370.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Organism-specific databases

    Xenbasei XB-GENE-944355. papola.

    Phylogenomic databases

    HOVERGENi HBG053502.

    Family and domain databases

    InterProi IPR002934. Nucleotidyltransferase.
    IPR007012. PolA_pol_cen_dom.
    IPR014492. PolyA_polymerase.
    [Graphical view ]
    Pfami PF01909. NTP_transf_2. 1 hit.
    PF04928. PAP_central. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF018425. PolyA_polymerase. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Poly(A) polymerases in the nucleus and cytoplasm of frog oocytes: dynamic changes during oocyte maturation and early development."
      Ballantyne S., Bilger A., Astrom J., Virtanen A., Wickens M.
      RNA 1:64-78(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Ovary.
    2. "Cloning and characterization of a Xenopus poly(A) polymerase."
      Gebauer F., Richter J.D.
      Mol. Cell. Biol. 15:1422-1430(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-394.
      Tissue: Ovary.

    Entry informationi

    Entry nameiPAPO3_XENLA
    AccessioniPrimary (citable) accession number: P51006
    Secondary accession number(s): Q91602
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 68 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3