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P51004

- PAPO1_XENLA

UniProt

P51004 - PAPO1_XENLA

Protein

Poly(A) polymerase alpha-A

Gene

papola-a

Organism
Xenopus laevis (African clawed frog)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 73 (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 sitei91 – 911ATPBy similarity
    Metal bindingi95 – 951Magnesium 1; catalyticBy similarity
    Metal bindingi95 – 951Magnesium 2; catalyticBy similarity
    Metal bindingi97 – 971Magnesium 1; catalyticBy similarity
    Metal bindingi97 – 971Magnesium 2; catalyticBy similarity
    Sitei135 – 1351Interaction with RNABy similarity
    Sitei140 – 1401Interaction with RNABy similarity
    Metal bindingi149 – 1491Magnesium 2; catalyticBy similarity
    Binding sitei149 – 1491ATPBy similarity
    Binding sitei210 – 2101ATPBy similarity
    Binding sitei219 – 2191ATPBy similarity
    Sitei310 – 3101Interaction with RNABy similarity
    Sitei381 – 3811Interaction with RNABy similarity
    Sitei506 – 5061Interaction with RNABy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi82 – 843ATPBy similarity
    Nucleotide bindingi95 – 973ATPBy similarity
    Nucleotide bindingi228 – 2292ATPBy 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 alpha-A (EC:2.7.7.19)
    Short name:
    PAP-alpha-A
    Alternative name(s):
    Polynucleotide adenylyltransferase alpha-A
    Gene namesi
    Name:papola-a
    OrganismiXenopus laevis (African clawed frog)
    Taxonomic identifieri8355 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

    Subcellular locationi

    GO - Cellular componenti

    1. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini‹1 – 715›715Poly(A) polymerase alpha-APRO_0000051614Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliP51004.
    SMRiP51004. Positions 4-480.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi472 – 48918Nuclear localization signal 1By similarityAdd
    BLAST
    Motifi624 – 63916Nuclear localization signal 2By similarityAdd
    BLAST

    Sequence similaritiesi

    Belongs to the poly(A) polymerase family.Curated

    Phylogenomic databases

    HOVERGENiHBG053502.

    Family and domain databases

    Gene3Di3.30.70.590. 1 hit.
    InterProiIPR002934. Nucleotidyltransferase.
    IPR011068. NuclTrfase_I_C.
    IPR007012. PolA_pol_cen_dom.
    IPR007010. PolA_pol_RNA-bd_dom.
    IPR014492. PolyA_polymerase.
    [Graphical view]
    PfamiPF01909. NTP_transf_2. 1 hit.
    PF04928. PAP_central. 1 hit.
    PF04926. PAP_RNA-bind. 1 hit.
    [Graphical view]
    PIRSFiPIRSF018425. PolyA_polymerase. 1 hit.
    SUPFAMiSSF55003. SSF55003. 1 hit.

    Sequencei

    Sequence statusi: Fragment.

    P51004-1 [UniParc]FASTAAdd to Basket

    « Hide

    PKTFGITSPI SLAAAKDTDC TLMQKLIETL KPYGVFEEEE QLQHRILGKL    50
    NNLVKEWIRE ISELKHLPQS VIENVGGKIF TFGPYRLGVH TKGADIDALC 100
    VAPRHVDRSD FFSSFYDKLK QQEEVKDLRS VEEAFVPVIK LCFDGIEIDI 150
    LFARLALQTI PEDLDLRDDS LLKNLDIRCI RSLNGCRVTD EILHLVPNID 200
    SFRLTLRAIK LWAKRHNIYS NILGFLGGVS WAMLVARTCQ LYPNAIASTL 250
    VHKFFLVFSK WEWPNPVLLK QPEECNLNLP VWDPRVNPSD RYHLMPIITP 300
    AYPQQNSTYN VSVSTRAVMI EEFKQGLAIT DEILLGKAEW SKLFDAPNFF 350
    QKYKHYILLL ASAPTEKQRL EWVGLVESKI RILVGSLEKN EFITLAHVNP 400
    RSFPAPSENM EKEEFRTMWV IGLVFKKMEN SENLSVDLTY DIQSFTDTVD 450
    RQAINSKMFE TEMKIAAMHV KRKQLHQLQP SHVSPKKKKH SFEGVKLLSL 500
    NDSSIDLSVD SDNSMSVPSP TNATRTSPLN SSGLSQGNSP AAPVSFSVTN 550
    VQATDVMVPQ NNSTENLGGS LNESIPESAT HPGFSSTPKP LVTRVVSSMR 600
    LVNQLQKPVS NTITKMPSPV AGVKRTSSPS NEDSPKKNKT EEDENDSSIS 650
    ADVDDQNKLE TEELKEVHSE EKSSSPVPGS LPFSQQSSTD LSDISVVPAT 700
    PIPVIKNSIK LRLNR 715
    Length:715
    Mass (Da):80,188
    Last modified:October 1, 1996 - v1
    Checksum:i355D74F250AD14A9
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Non-terminal residuei1 – 11

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U19973 mRNA. Translation: AAC59745.1.
    UniGeneiXl.57169.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U19973 mRNA. Translation: AAC59745.1 .
    UniGenei Xl.57169.

    3D structure databases

    ProteinModelPortali P51004.
    SMRi P51004. Positions 4-480.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    HOVERGENi HBG053502.

    Family and domain databases

    Gene3Di 3.30.70.590. 1 hit.
    InterProi IPR002934. Nucleotidyltransferase.
    IPR011068. NuclTrfase_I_C.
    IPR007012. PolA_pol_cen_dom.
    IPR007010. PolA_pol_RNA-bd_dom.
    IPR014492. PolyA_polymerase.
    [Graphical view ]
    Pfami PF01909. NTP_transf_2. 1 hit.
    PF04928. PAP_central. 1 hit.
    PF04926. PAP_RNA-bind. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF018425. PolyA_polymerase. 1 hit.
    SUPFAMi SSF55003. SSF55003. 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.

    Entry informationi

    Entry nameiPAPO1_XENLA
    AccessioniPrimary (citable) accession number: P51004
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 73 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