ID D2VDZ6_NAEGR Unreviewed; 559 AA.
AC D2VDZ6;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 24-JAN-2024, entry version 67.
DE RecName: Full=Poly(A) polymerase {ECO:0000256|PIRNR:PIRNR018425};
DE EC=2.7.7.19 {ECO:0000256|PIRNR:PIRNR018425};
GN ORFNames=NAEGRDRAFT_33222 {ECO:0000313|EMBL:EFC44986.1};
OS Naegleria gruberi (Amoeba).
OC Eukaryota; Discoba; Heterolobosea; Tetramitia; Eutetramitia;
OC Vahlkampfiidae; Naegleria.
OX NCBI_TaxID=5762 {ECO:0000313|Proteomes:UP000006671};
RN [1] {ECO:0000313|EMBL:EFC44986.1, ECO:0000313|Proteomes:UP000006671}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NEG-M {ECO:0000313|EMBL:EFC44986.1,
RC ECO:0000313|Proteomes:UP000006671};
RX PubMed=20211133; DOI=10.1016/j.cell.2010.01.032;
RA Fritz-Laylin L.K., Prochnik S.E., Ginger M.L., Dacks J.B., Carpenter M.L.,
RA Field M.C., Kuo A., Paredez A., Chapman J., Pham J., Shu S., Neupane R.,
RA Cipriano M., Mancuso J., Tu H., Salamov A., Lindquist E., Shapiro H.,
RA Lucas S., Grigoriev I.V., Cande W.Z., Fulton C., Rokhsar D.S., Dawson S.C.;
RT "The genome of Naegleria gruberi illuminates early eukaryotic
RT versatility.";
RL Cell 140:631-642(2010).
CC -!- FUNCTION: Polymerase that creates the 3'-poly(A) tail of mRNA's.
CC {ECO:0000256|PIRNR:PIRNR018425}.
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 Evidence={ECO:0000256|PIRNR:PIRNR018425};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|PIRSR:PIRSR018425-2};
CC Note=Binds 2 magnesium ions. Also active with manganese.
CC {ECO:0000256|PIRSR:PIRSR018425-2};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|PIRNR:PIRNR018425}.
CC -!- SIMILARITY: Belongs to the poly(A) polymerase family.
CC {ECO:0000256|ARBA:ARBA00010912, ECO:0000256|PIRNR:PIRNR018425}.
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; GG738865; EFC44986.1; -; Genomic_DNA.
DR AlphaFoldDB; D2VDZ6; -.
DR STRING; 5762.D2VDZ6; -.
DR EnsemblProtists; EFC44986; EFC44986; NAEGRDRAFT_33222.
DR VEuPathDB; AmoebaDB:NAEGRDRAFT_33222; -.
DR eggNOG; KOG2245; Eukaryota.
DR InParanoid; D2VDZ6; -.
DR OMA; CVGPFFA; -.
DR OrthoDB; 1351913at2759; -.
DR Proteomes; UP000006671; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:1990817; F:poly(A) RNA polymerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0050265; F:RNA uridylyltransferase activity; IEA:UniProt.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0071076; P:RNA 3' uridylation; IEA:UniProt.
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 InterPro; IPR014492; PolyA_polymerase.
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 PIRSF; PIRSF018425; PolyA_polymerase; 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 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR018425};
KW Magnesium {ECO:0000256|PIRSR:PIRSR018425-2};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR018425-2};
KW mRNA processing {ECO:0000256|ARBA:ARBA00022664,
KW ECO:0000256|PIRNR:PIRNR018425};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR018425};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR018425};
KW Reference proteome {ECO:0000313|Proteomes:UP000006671};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR018425}.
FT DOMAIN 7..195
FT /note="Poly(A) polymerase nucleotidyltransferase"
FT /evidence="ECO:0000259|Pfam:PF20750"
FT DOMAIN 200..345
FT /note="Poly(A) polymerase central"
FT /evidence="ECO:0000259|Pfam:PF04928"
FT DOMAIN 348..405
FT /note="Poly(A) polymerase RNA-binding"
FT /evidence="ECO:0000259|Pfam:PF04926"
FT DOMAIN 410..478
FT /note="Poly(A) polymerase RNA-binding"
FT /evidence="ECO:0000259|Pfam:PF04926"
FT REGION 477..540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 484..502
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 503..520
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 521..540
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 81..83
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR018425-1"
FT BINDING 94..96
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR018425-1"
FT BINDING 94
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR018425-2"
FT BINDING 94
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR018425-2"
FT BINDING 96
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR018425-2"
FT BINDING 96
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR018425-2"
FT BINDING 148
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR018425-1"
FT BINDING 148
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR018425-2"
FT BINDING 209
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR018425-1"
FT BINDING 218
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR018425-1"
FT BINDING 227..228
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR018425-1"
SQ SEQUENCE 559 AA; 63170 MW; 46C8B9CDED19672B CRC64;
MSDSTVISAA LPTQKDLTNS EAIMEILKKE NRFPSDEENK KREEVLAKLD GIIKGWVKQV
CLKQGLSEEF VSSAGSKLVT FGSFRLGVHG PGADIDTLCI VPNMVEKHHC FTDLHDILKL
RPEIAELKPV PDAYVPLITM VFDGVEIDLL FARLSRTVIP ADLDILDESN LKDADDETQR
SLNGPRVADQ ILKLVPNQEN FRTTLRCIKL WATRRAIYGN IVGYLGGVAY AILTAKICQM
YPNAAPSTLL TKFFTVYQQW NWGKVPVLLR PIEEGTLNFK VWNPKLNPRD KQHLMPIITP
SYPCMNSTFN VSKTTLKDMK NEFERGASIT QKAENGLENW ETLFEATDFF VRYSNYLQVE
INTSNEVDHL KWIGFIQSKV RFLIPKLEAV PGLTIHIYPD YFHNNQGGAF SSYFYIGLEY
KQTKPGEGSV VNLASCIAEF EELLTWPDKN ENMEKPKIQP IKRNAIPEFV ISKKKKKELM
KKNKAQKRKA EQDDEKNKPS EETEATATAT TSTDGTTENG ESAAKKAKVD ETPAVKREHK
VELLLGDDDD DLLALYSKK
//