PAP_ENTHI
ID PAP_ENTHI Reviewed; 522 AA.
AC Q51D88;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Poly(A) polymerase;
DE Short=PAP;
DE EC=2.7.7.19;
DE AltName: Full=EhPAP;
DE AltName: Full=Polynucleotide adenylyltransferase;
GN ORFNames=16.t00038;
OS Entamoeba histolytica.
OC Eukaryota; Amoebozoa; Evosea; Archamoebae; Mastigamoebida; Entamoebidae;
OC Entamoeba.
OX NCBI_TaxID=5759;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DEVELOPMENTAL STAGE, AND SUBCELLULAR
RP LOCATION.
RX PubMed=15955317; DOI=10.1016/j.exppara.2005.02.017;
RA Garcia-Vivas J., Lopez-Camarillo C., Azuara-Liceaga E., Orozco E.,
RA Marchat L.A.;
RT "Entamoeba histolytica: cloning and expression of the poly(A) polymerase
RT EhPAP.";
RL Exp. Parasitol. 110:226-232(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 30459 / HM-1:IMSS;
RX PubMed=15729342; DOI=10.1038/nature03291;
RA Loftus B.J., Anderson I., Davies R., Alsmark U.C., Samuelson J., Amedeo P.,
RA Roncaglia P., Berriman M., Hirt R.P., Mann B.J., Nozaki T., Suh B., Pop M.,
RA Duchene M., Ackers J., Tannich E., Leippe M., Hofer M., Bruchhaus I.,
RA Willhoeft U., Bhattacharya A., Chillingworth T., Churcher C.M., Hance Z.,
RA Harris B., Harris D., Jagels K., Moule S., Mungall K.L., Ormond D.,
RA Squares R., Whitehead S., Quail M.A., Rabbinowitsch E., Norbertczak H.,
RA Price C., Wang Z., Guillen N., Gilchrist C., Stroup S.E., Bhattacharya S.,
RA Lohia A., Foster P.G., Sicheritz-Ponten T., Weber C., Singh U.,
RA Mukherjee C., El-Sayed N.M.A., Petri W.A., Clark C.G., Embley T.M.,
RA Barrell B.G., Fraser C.M., Hall N.;
RT "The genome of the protist parasite Entamoeba histolytica.";
RL Nature 433:865-868(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 30459 / HM-1:IMSS;
RA Lorenzi H., Amedeo P., Inman J., Schobel S., Caler E.;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000269|PubMed:15955317}.
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: Cytoplasm {ECO:0000269|PubMed:15955317}. Nucleus
CC {ECO:0000269|PubMed:15955317}.
CC -!- DEVELOPMENTAL STAGE: Mainly expressed during G1 and S phases.
CC {ECO:0000269|PubMed:15955317}.
CC -!- SIMILARITY: Belongs to the poly(A) polymerase family. {ECO:0000305}.
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DR EMBL; DS571148; EAL50821.1; -; Genomic_DNA.
DR RefSeq; XP_656205.1; XM_651113.1.
DR AlphaFoldDB; Q51D88; -.
DR SMR; Q51D88; -.
DR STRING; 5759.rna_EHI_012040-1; -.
DR GeneID; 3410521; -.
DR KEGG; ehi:EHI_012040; -.
DR VEuPathDB; AmoebaDB:EHI5A_207940; -.
DR VEuPathDB; AmoebaDB:EHI7A_168270; -.
DR VEuPathDB; AmoebaDB:EHI8A_191470; -.
DR VEuPathDB; AmoebaDB:EHI_012040; -.
DR VEuPathDB; AmoebaDB:KM1_264350; -.
DR eggNOG; KOG2245; Eukaryota.
DR InParanoid; Q51D88; -.
DR OMA; WAKVVAY; -.
DR Proteomes; UP000001926; Partially assembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0004652; F:polynucleotide adenylyltransferase activity; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006378; P:mRNA polyadenylation; IBA:GO_Central.
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; IPR002934; Polymerase_NTP_transf_dom.
DR Pfam; PF01909; NTP_transf_2; 1.
DR Pfam; PF04928; PAP_central; 1.
DR SUPFAM; SSF55003; SSF55003; 1.
DR SUPFAM; SSF81301; SSF81301; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cytoplasm; Magnesium; Manganese; Metal-binding;
KW mRNA processing; Nucleotide-binding; Nucleus; Reference proteome;
KW RNA-binding; Transferase.
FT CHAIN 1..522
FT /note="Poly(A) polymerase"
FT /id="PRO_0000051617"
FT REGION 475..522
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 475..501
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 63..65
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 76..78
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 76
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 76
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 78
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 78
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 130
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 130
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 193
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 202
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 211..212
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 522 AA; 59810 MW; B4A546672B639CBF CRC64;
MACELKEFLV KNDMYPMGDQ VEKKRKAISK MTEYIQQWGK KIYIESAGVA DDTDVKAATI
YVYGSYRLNV YGNNSDIDAC IVSNSTITRD DFYDGLYAEL LNNPDVKELK QIPSKRSPHL
SMIYLNIEFD LNFSRTAYTS LPDNLDILNE NILKNMDELD TRAINGVRNT DIIDAFVPNH
SEEAFRVMVR TIKLWTKKRG IYGYVYCFLN GISIEILVAQ VISENYQLDN VRLLEKFFQV
YSSWDWLRTP VMLGTNDDFN DKKKEGVIQI LTPASPSENA AFSITKFSLE MIKRELKRGQ
EIVHEFSSEG VNDWAKLFKP RHLFCGYYIF IEFIVTSSSL EGLTTTIGKF ESGLVNLMKG
LSEIEEIIEA NVIPNGFLDE ENEKYFYYVG MNVKRDCPVD ISTPLNSFLS IVNSGKDLIV
DASIKKRSEI PTKFAHSVKR SITKSQEIKE TSSQVPSSAI TETFDIPTKP SIEQQLKAKE
ENSIPNEEKK EQLKKEMKQE ANTIVKNSST DDDFMKRFTR KN
