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P51004 (PAPO1_XENLA) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 72. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Poly(A) polymerase alpha-A

Short name=PAP-alpha-A
EC=2.7.7.19
Alternative name(s):
Polynucleotide adenylyltransferase alpha-A
Gene names
Name:papola-a
OrganismXenopus laevis (African clawed frog)
Taxonomic identifier8355 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Protein attributes

Sequence length715 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: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain‹1 – 715›715Poly(A) polymerase alpha-A
PRO_0000051614

Regions

Nucleotide binding82 – 843ATP By similarity
Nucleotide binding95 – 973ATP By similarity
Nucleotide binding228 – 2292ATP By similarity
Motif472 – 48918Nuclear localization signal 1 By similarity
Motif624 – 63916Nuclear localization signal 2 By similarity

Sites

Metal binding951Magnesium 1; catalytic By similarity
Metal binding951Magnesium 2; catalytic By similarity
Metal binding971Magnesium 1; catalytic By similarity
Metal binding971Magnesium 2; catalytic By similarity
Metal binding1491Magnesium 2; catalytic By similarity
Binding site911ATP By similarity
Binding site1491ATP By similarity
Binding site2101ATP By similarity
Binding site2191ATP By similarity
Site1351Interaction with RNA By similarity
Site1401Interaction with RNA By similarity
Site3101Interaction with RNA By similarity
Site3811Interaction with RNA By similarity
Site5061Interaction with RNA By similarity

Experimental info

Non-terminal residue11

Sequences

Sequence LengthMass (Da)Tools
P51004 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 355D74F250AD14A9

FASTA71580,188
        10         20         30         40         50         60 
PKTFGITSPI SLAAAKDTDC TLMQKLIETL KPYGVFEEEE QLQHRILGKL NNLVKEWIRE 

        70         80         90        100        110        120 
ISELKHLPQS VIENVGGKIF TFGPYRLGVH TKGADIDALC VAPRHVDRSD FFSSFYDKLK 

       130        140        150        160        170        180 
QQEEVKDLRS VEEAFVPVIK LCFDGIEIDI LFARLALQTI PEDLDLRDDS LLKNLDIRCI 

       190        200        210        220        230        240 
RSLNGCRVTD EILHLVPNID SFRLTLRAIK LWAKRHNIYS NILGFLGGVS WAMLVARTCQ 

       250        260        270        280        290        300 
LYPNAIASTL VHKFFLVFSK WEWPNPVLLK QPEECNLNLP VWDPRVNPSD RYHLMPIITP 

       310        320        330        340        350        360 
AYPQQNSTYN VSVSTRAVMI EEFKQGLAIT DEILLGKAEW SKLFDAPNFF QKYKHYILLL 

       370        380        390        400        410        420 
ASAPTEKQRL EWVGLVESKI RILVGSLEKN EFITLAHVNP RSFPAPSENM EKEEFRTMWV 

       430        440        450        460        470        480 
IGLVFKKMEN SENLSVDLTY DIQSFTDTVD RQAINSKMFE TEMKIAAMHV KRKQLHQLQP 

       490        500        510        520        530        540 
SHVSPKKKKH SFEGVKLLSL NDSSIDLSVD SDNSMSVPSP TNATRTSPLN SSGLSQGNSP 

       550        560        570        580        590        600 
AAPVSFSVTN VQATDVMVPQ NNSTENLGGS LNESIPESAT HPGFSSTPKP LVTRVVSSMR 

       610        620        630        640        650        660 
LVNQLQKPVS NTITKMPSPV AGVKRTSSPS NEDSPKKNKT EEDENDSSIS ADVDDQNKLE 

       670        680        690        700        710 
TEELKEVHSE EKSSSPVPGS LPFSQQSSTD LSDISVVPAT PIPVIKNSIK LRLNR 

« 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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U19973 mRNA. Translation: AAC59745.1.
UniGeneXl.57169.

3D structure databases

ProteinModelPortalP51004.
SMRP51004. Positions 4-480.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG053502.

Family and domain databases

Gene3D3.30.70.590. 1 hit.
InterProIPR002934. Nucleotidyltransferase.
IPR011068. NuclTrfase_I_C.
IPR007012. PolA_pol_cen_dom.
IPR007010. PolA_pol_RNA-bd_dom.
IPR014492. PolyA_polymerase.
[Graphical view]
PfamPF01909. NTP_transf_2. 1 hit.
PF04928. PAP_central. 1 hit.
PF04926. PAP_RNA-bind. 1 hit.
[Graphical view]
PIRSFPIRSF018425. PolyA_polymerase. 1 hit.
SUPFAMSSF55003. SSF55003. 1 hit.
ProtoNetSearch...

Entry information

Entry namePAPO1_XENLA
AccessionPrimary (citable) accession number: P51004
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: October 16, 2013
This is version 72 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