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P51006

- PAPO3_XENLA

UniProt

P51006 - PAPO3_XENLA

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Protein
Poly(A) polymerase type 3
Gene
N/A
Organism
Xenopus laevis (African clawed frog)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at transcript leveli

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.

Sites

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

Regions

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

GO - Molecular functioni

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

GO - Biological processi

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

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
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

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

Interactioni

Subunit structurei

Monomer By similarity.

Structurei

3D structure databases

ProteinModelPortaliP51006.
SMRiP51006. Positions 17-370.

Family & Domainsi

Motif

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

Sequence similaritiesi

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

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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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti61 – 611S → I in AAA64708. 1 Publication
Sequence conflicti126 – 1261L → F in AAA64708. 1 Publication

Non-terminal residue

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
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...

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 16, 2013
This is version 67 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

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