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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: 3 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

Mg2+By similarity, Mn2+By similarityNote: Binds 2 magnesium ions. Also active with manganese.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
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-KW
Complete GO annotation...

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

        10         20         30         40         50
MPFPLASQGS QQSQKTYGIT SPISLATPKD TDCTLTQKLI ETLKPYGVFE
60 70 80 90 100
EEDELQHRIL SLGKLNNLVK EWIREISELK NLPQSVIENV GGKIFTFGSY
110 120 130 140 150
RLGVHTKGAD IDALCVAPRH VDRSDLFSSF YEKLKQQEEV KDLRSVEEAF
160 170 180 190 200
VPVIKLCFDG IEIDILFARL ALQTIPEDLD LRDDSLLKNL DIRCIRSLNG
210 220 230 240 250
CRVTDEILHL VPNIDSFRLT LRAIKLWAKR HNIYSNILGF LGGVSWAMLV
260 270 280 290 300
ARTCQLYPNA IASTLVHKFF LVFSKWEWPN PVLLKQPEEC NLNLPVWDPR
310 320 330 340 350
VNPSDRYHLM PIITPAYPQQ NSTYNVSVST RAVMVEEFKQ GLAITDEILL
360 370 380 390 400
LKAEWSKLFD APNFFQKYKY VFYNLLAMFA WGEIINKNKK RCYTLKKKKK
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:
EMBLi
GenBanki
DDBJi
Links Updated
U19975 mRNA. Translation: AAC59747.1.
U23456 mRNA. Translation: AAA64708.1.
PIRiI51681.
UniGeneiXl.341.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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: November 26, 2014
This is version 70 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