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P51004

- PAPO1_XENLA

UniProt

P51004 - PAPO1_XENLA

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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

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 sitei91 – 911ATP By similarity
Metal bindingi95 – 951Magnesium 1; catalytic By similarity
Metal bindingi95 – 951Magnesium 2; catalytic By similarity
Metal bindingi97 – 971Magnesium 1; catalytic By similarity
Metal bindingi97 – 971Magnesium 2; catalytic By similarity
Sitei135 – 1351Interaction with RNA By similarity
Sitei140 – 1401Interaction with RNA By similarity
Metal bindingi149 – 1491Magnesium 2; catalytic By similarity
Binding sitei149 – 1491ATP By similarity
Binding sitei210 – 2101ATP By similarity
Binding sitei219 – 2191ATP By similarity
Sitei310 – 3101Interaction with RNA By similarity
Sitei381 – 3811Interaction with RNA By similarity
Sitei506 – 5061Interaction with RNA By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi82 – 843ATP By similarity
Nucleotide bindingi95 – 973ATP By similarity
Nucleotide bindingi228 – 2292ATP 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

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 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
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini‹1 – 715›715Poly(A) polymerase alpha-A
PRO_0000051614Add
BLAST

Interactioni

Subunit structurei

Monomer By similarity.

Structurei

3D structure databases

ProteinModelPortaliP51004.
SMRiP51004. Positions 4-480.

Family & Domainsi

Motif

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

Sequence similaritiesi

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

Non-terminal residue

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 16, 2013
This is version 72 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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