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P51006 (PAPO3_XENLA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Poly(A) polymerase type 3
Short name=PAP
EC=2.7.7.19
Alternative name(s):
Polynucleotide adenylyltransferase
OrganismXenopus laevis (African clawed frog)
Taxonomic identifier8355 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Amphibia › Batrachia › Anura › Pipoidea › Pipidae › Xenopodinae › Xenopus › Xenopus

Protein attributes

Sequence length400 AA.
Sequence statusFragment.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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

Catalytic activity

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

Cofactor

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

Subunit structure

Monomer By similarity.

Subcellular location

Nucleus.

Sequence similarities

Belongs to the poly(A) polymerase family.

Ontologies

Keywords
   Biological processmRNA processing
   Cellular componentNucleus
   LigandATP-binding
Magnesium
Manganese
Metal-binding
Nucleotide-binding
RNA-binding
   Molecular functionTransferase
Gene Ontology (GO)
   Biological_processRNA polyadenylation

Inferred from electronic annotation. Source: InterPro

mRNA processing

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentnucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

RNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

polynucleotide adenylyltransferase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – ›400›400Poly(A) polymerase type 3
PRO_0000051616

Regions

Nucleotide binding97 – 993ATP By similarity
Nucleotide binding110 – 1123ATP By similarity
Nucleotide binding243 – 2442ATP By similarity
Motif382 – 3909Nuclear localization signal By similarity

Sites

Metal binding1101Magnesium 1; catalytic By similarity
Metal binding1101Magnesium 2; catalytic By similarity
Metal binding1121Magnesium 1; catalytic By similarity
Metal binding1121Magnesium 2; catalytic By similarity
Metal binding1641Magnesium 2; catalytic By similarity
Binding site1061ATP By similarity
Binding site1641ATP By similarity
Binding site2251ATP By similarity
Binding site2341ATP By similarity

Experimental info

Sequence conflict611S → I in AAA64708. Ref.2
Sequence conflict1261L → F in AAA64708. Ref.2
Non-terminal residue4001

Sequences

Sequence LengthMass (Da)Tools
P51006 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: AB4347C074E60CA3

FASTA40046,020
        10         20         30         40         50         60 
MPFPLASQGS QQSQKTYGIT SPISLATPKD TDCTLTQKLI ETLKPYGVFE EEDELQHRIL 

        70         80         90        100        110        120 
SLGKLNNLVK EWIREISELK NLPQSVIENV GGKIFTFGSY RLGVHTKGAD IDALCVAPRH 

       130        140        150        160        170        180 
VDRSDLFSSF YEKLKQQEEV KDLRSVEEAF VPVIKLCFDG IEIDILFARL ALQTIPEDLD 

       190        200        210        220        230        240 
LRDDSLLKNL DIRCIRSLNG CRVTDEILHL VPNIDSFRLT LRAIKLWAKR HNIYSNILGF 

       250        260        270        280        290        300 
LGGVSWAMLV ARTCQLYPNA IASTLVHKFF LVFSKWEWPN PVLLKQPEEC NLNLPVWDPR 

       310        320        330        340        350        360 
VNPSDRYHLM PIITPAYPQQ NSTYNVSVST RAVMVEEFKQ GLAITDEILL LKAEWSKLFD 

       370        380        390        400 
APNFFQKYKY VFYNLLAMFA WGEIINKNKK RCYTLKKKKK

« Hide

References

[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U19975 mRNA. Translation: AAC59747.1.
U23456 mRNA. Translation: AAA64708.1.
PIRI51681.
UniGeneXl.341.

3D structure databases

ProteinModelPortalP51006.
SMRP51006. Positions 17-370.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

XenbaseXB-GENE-944355. papola.

Phylogenomic databases

HOVERGENHBG053502.

Family and domain databases

InterProIPR002934. Nucleotidyltransferase.
IPR007012. PolA_pol_cen_dom.
IPR014492. PolyA_polymerase.
[Graphical view]
PfamPF01909. NTP_transf_2. 1 hit.
PF04928. PAP_central. 1 hit.
[Graphical view]
PIRSFPIRSF018425. PolyA_polymerase. 1 hit.
ProtoNetSearch...

Entry information

Entry namePAPO3_XENLA
AccessionPrimary (citable) accession number: P51006
Secondary accession number(s): Q91602
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: May 1, 2013
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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