ID   PAP_ENTH1               Reviewed;         522 AA.
AC   Q51D88;
DT   25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2005, sequence version 1.
DT   24-JAN-2024, entry version 96.
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 (strain ATCC 30459 / HM-1:IMSS / ABRM).
OC   Eukaryota; Amoebozoa; Evosea; Archamoebae; Mastigamoebida; Entamoebidae;
OC   Entamoeba.
OX   NCBI_TaxID=294381;
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 / ABRM;
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 / ABRM;
RX   PubMed=20559563; DOI=10.1371/journal.pntd.0000716;
RA   Lorenzi H.A., Puiu D., Miller J.R., Brinkac L.M., Amedeo P., Hall N.,
RA   Caler E.V.;
RT   "New assembly, reannotation and analysis of the Entamoeba histolytica
RT   genome reveal new genomic features and protein content information.";
RL   PLoS Negl. Trop. Dis. 4:e716-e716(2010).
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.Q51D88; -.
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; EWKWPQP; -.
DR   OrthoDB; 1351913at2759; -.
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:1990817; F:poly(A) RNA polymerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006378; P:mRNA polyadenylation; IBA:GO_Central.
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   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   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   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   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
//