ID PAP_DICDI Reviewed; 809 AA. AC Q54J73; DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot. DT 24-MAY-2005, sequence version 1. DT 24-JAN-2024, entry version 112. DE RecName: Full=Poly(A) polymerase; DE Short=PAP; DE EC=2.7.7.19; DE AltName: Full=Polynucleotide adenylyltransferase; GN Name=papA; ORFNames=DDB_G0288259; OS Dictyostelium discoideum (Social amoeba). OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales; OC Dictyosteliaceae; Dictyostelium. OX NCBI_TaxID=44689; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AX4; RX PubMed=15875012; DOI=10.1038/nature03481; RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G., RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.; RT "The genome of the social amoeba Dictyostelium discoideum."; RL Nature 435:43-57(2005). 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 (By similarity). {ECO:0000250}. 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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. CC -!- SIMILARITY: Belongs to the poly(A) polymerase family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AAFI02000109; EAL63311.1; -; Genomic_DNA. DR RefSeq; XP_636814.1; XM_631722.1. DR AlphaFoldDB; Q54J73; -. DR SMR; Q54J73; -. DR STRING; 44689.Q54J73; -. DR PaxDb; 44689-DDB0216279; -. DR EnsemblProtists; EAL63311; EAL63311; DDB_G0288259. DR GeneID; 8626531; -. DR KEGG; ddi:DDB_G0288259; -. DR dictyBase; DDB_G0288259; papA. DR eggNOG; KOG2245; Eukaryota. DR HOGENOM; CLU_011511_2_0_1; -. DR InParanoid; Q54J73; -. DR OMA; WEGWIES; -. DR PhylomeDB; Q54J73; -. DR PRO; PR:Q54J73; -. DR Proteomes; UP000002195; Chromosome 5. DR GO; GO:0005847; C:mRNA cleavage and polyadenylation specificity factor complex; ISS:dictyBase. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:1990817; F:poly(A) RNA polymerase activity; ISS:dictyBase. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW. DR GO; GO:0006378; P:mRNA polyadenylation; IBA:GO_Central. DR GO; GO:0030846; P:termination of RNA polymerase II transcription, poly(A)-coupled; ISS:dictyBase. DR CDD; cd05402; NT_PAP_TUTase; 1. DR Gene3D; 1.10.1410.10; -; 1. DR Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1. DR Gene3D; 3.30.70.590; Poly(A) polymerase predicted RNA binding domain; 1. DR InterPro; IPR043519; NT_sf. DR InterPro; IPR011068; NuclTrfase_I-like_C. DR InterPro; IPR007012; PolA_pol_cen_dom. DR InterPro; IPR048840; PolA_pol_NTPase. DR InterPro; IPR007010; PolA_pol_RNA-bd_dom. DR PANTHER; PTHR10682; POLY A POLYMERASE; 1. DR PANTHER; PTHR10682:SF10; POLYNUCLEOTIDE ADENYLYLTRANSFERASE; 1. DR Pfam; PF04928; PAP_central; 1. DR Pfam; PF20750; PAP_NTPase; 1. DR Pfam; PF04926; PAP_RNA-bind; 2. DR SUPFAM; SSF81301; Nucleotidyltransferase; 1. DR SUPFAM; SSF55003; PAP/Archaeal CCA-adding enzyme, C-terminal domain; 1. DR SUPFAM; SSF81631; PAP/OAS1 substrate-binding domain; 1. PE 3: Inferred from homology; KW ATP-binding; Magnesium; Manganese; Metal-binding; mRNA processing; KW Nucleotide-binding; Nucleus; Reference proteome; RNA-binding; Transferase. FT CHAIN 1..809 FT /note="Poly(A) polymerase" FT /id="PRO_0000330665" FT REGION 1..50 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 529..760 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 785..809 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 529..564 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 565..760 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 785..799 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 133..135 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250" FT BINDING 146..148 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250" FT BINDING 146 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000250" FT BINDING 146 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /ligand_note="catalytic" FT /evidence="ECO:0000250" FT BINDING 148 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000250" FT BINDING 148 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /ligand_note="catalytic" FT /evidence="ECO:0000250" FT BINDING 200 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250" FT BINDING 200 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /ligand_note="catalytic" FT /evidence="ECO:0000250" FT BINDING 262 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250" FT BINDING 271 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250" FT BINDING 280..281 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250" SQ SEQUENCE 809 AA; 88686 MW; 382E40C4D6A94D78 CRC64; MNKNGGPPVA NITTSSTTIT STTTTQAKSQ LPSSLSVNNL HTTQGSTDQP TILGVTEPIS TAPPSSIDFK LSTELENTLI SFNLFESPEE SRKREEILGK LNQIVREWAK QVSLKKGYPE QTASEVVAKI FTFGSYRLGV HGPGSDIDTL CVGPKHIMRS DFFDDLSDIL KVHPEITEFT TVKDAFVPVI TMVFSGIPID LIYAKLALTA IPEELNDLID ESFLKNIDEK SILSLNGCRV TDQILKLVPN IPNFRMALRC IKLWAIRRGI YSNILGFLGG VSWALLTARI CQLYPNSAPS TIIHRFFKVY EIWKWPAPIL LCHIQEGGIL GPKVWNPKRD KAHLMPIITP AYPSMNSTYN VSKSTLQLMK SEFVRGAEIT RKIETGECTW KNLLEKCDFF TRYSFYIEID CYSMNEEDSR KWEGWIESKL RFLISNLEST PKMKFAVPYP KGFTNNLHKA NNPDQICTSF FMGLSFNFSN TPGADKSVDL TKAVTEFTGI IKDWLRTQPN PDTMDIKVQY IKKKQLPAFV KDEGPEEPVK TTKKRSSTGE PSATRKKLKS ENSDNKLNSP KSPITTNINS TPTTSTPTTT ANTTTNTTTA TTTTTTTTVP ITSTPTSNIS SPTMNSTELT TPTSTSTTTS NDSITTPPTT TTINSVQPPS AQPTENGSST SNSPTSTSIN NTALPPNPTT NSESTIETTI TLPTTLESQT STLKDSNEIS TNGTAVATEP TITSPSVNIN ESSTSTSTTT TTTVTEQQIQ TAPTTATPIN KTIVNTMEVN ELSFISSSSE TSQSKPPPKK PTISIIRGN //