PAPO1_XENLA
ID PAPO1_XENLA Reviewed; 715 AA.
AC P51004;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Poly(A) polymerase alpha-A;
DE Short=PAP-alpha-A;
DE EC=2.7.7.19;
DE AltName: Full=Polynucleotide adenylyltransferase alpha-A;
DE Flags: Fragment;
GN Name=papola-a;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Ovary;
RX PubMed=7489490;
RA Ballantyne S., Bilger A., Astrom J., Virtanen A., Wickens M.;
RT "Poly(A) polymerases in the nucleus and cytoplasm of frog oocytes: dynamic
RT changes during oocyte maturation and early development.";
RL RNA 1:64-78(1995).
CC -!- FUNCTION: Polymerase that creates the 3'-poly(A) tail of mRNA's. May
CC acquire specificity through interaction with a cleavage and
CC polyadenylation factor (CPSF).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + RNA(n) = diphosphate + RNA(n)-3'-adenine ribonucleotide;
CC Xref=Rhea:RHEA:11332, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17347,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:140395,
CC ChEBI:CHEBI:173115; EC=2.7.7.19;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 2 magnesium ions. Also active with manganese. {ECO:0000250};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- SIMILARITY: Belongs to the poly(A) polymerase family. {ECO:0000305}.
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DR EMBL; U19973; AAC59745.1; -; mRNA.
DR AlphaFoldDB; P51004; -.
DR SMR; P51004; -.
DR Proteomes; UP000186698; Genome assembly.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004652; F:polynucleotide adenylyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0031123; P:RNA 3'-end processing; IEA:InterPro.
DR GO; GO:0043631; P:RNA polyadenylation; IEA:InterPro.
DR Gene3D; 3.30.460.10; -; 1.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR011068; NuclTrfase_I-like_C.
DR InterPro; IPR007012; PolA_pol_cen_dom.
DR InterPro; IPR007010; PolA_pol_RNA-bd_dom.
DR InterPro; IPR014492; PolyA_polymerase.
DR InterPro; IPR002934; Polymerase_NTP_transf_dom.
DR Pfam; PF01909; NTP_transf_2; 1.
DR Pfam; PF04928; PAP_central; 1.
DR Pfam; PF04926; PAP_RNA-bind; 1.
DR PIRSF; PIRSF018425; PolyA_polymerase; 1.
DR SUPFAM; SSF55003; SSF55003; 1.
DR SUPFAM; SSF81301; SSF81301; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Magnesium; Manganese; Metal-binding; mRNA processing;
KW Nucleotide-binding; Nucleus; Reference proteome; RNA-binding; Transferase.
FT CHAIN <1..715
FT /note="Poly(A) polymerase alpha-A"
FT /id="PRO_0000051614"
FT REGION 510..543
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 560..590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 607..693
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 472..489
FT /note="Nuclear localization signal 1"
FT /evidence="ECO:0000250"
FT MOTIF 624..639
FT /note="Nuclear localization signal 2"
FT /evidence="ECO:0000250"
FT COMPBIAS 607..629
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 630..672
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 673..693
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 82..84
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 91
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 95..97
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 95
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 95
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 97
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 97
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 149
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 149
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 210
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 219
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 228..229
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT SITE 135
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250"
FT SITE 140
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250"
FT SITE 310
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250"
FT SITE 381
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250"
FT SITE 506
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250"
FT NON_TER 1
SQ SEQUENCE 715 AA; 80188 MW; 355D74F250AD14A9 CRC64;
PKTFGITSPI SLAAAKDTDC TLMQKLIETL KPYGVFEEEE QLQHRILGKL NNLVKEWIRE
ISELKHLPQS VIENVGGKIF TFGPYRLGVH TKGADIDALC VAPRHVDRSD FFSSFYDKLK
QQEEVKDLRS VEEAFVPVIK LCFDGIEIDI LFARLALQTI PEDLDLRDDS LLKNLDIRCI
RSLNGCRVTD EILHLVPNID SFRLTLRAIK LWAKRHNIYS NILGFLGGVS WAMLVARTCQ
LYPNAIASTL VHKFFLVFSK WEWPNPVLLK QPEECNLNLP VWDPRVNPSD RYHLMPIITP
AYPQQNSTYN VSVSTRAVMI EEFKQGLAIT DEILLGKAEW SKLFDAPNFF QKYKHYILLL
ASAPTEKQRL EWVGLVESKI RILVGSLEKN EFITLAHVNP RSFPAPSENM EKEEFRTMWV
IGLVFKKMEN SENLSVDLTY DIQSFTDTVD RQAINSKMFE TEMKIAAMHV KRKQLHQLQP
SHVSPKKKKH SFEGVKLLSL NDSSIDLSVD SDNSMSVPSP TNATRTSPLN SSGLSQGNSP
AAPVSFSVTN VQATDVMVPQ NNSTENLGGS LNESIPESAT HPGFSSTPKP LVTRVVSSMR
LVNQLQKPVS NTITKMPSPV AGVKRTSSPS NEDSPKKNKT EEDENDSSIS ADVDDQNKLE
TEELKEVHSE EKSSSPVPGS LPFSQQSSTD LSDISVVPAT PIPVIKNSIK LRLNR
