ID B0X0X1_CULQU Unreviewed; 375 AA. AC B0X0X1; DT 08-APR-2008, integrated into UniProtKB/TrEMBL. DT 08-APR-2008, sequence version 1. DT 24-JAN-2024, entry version 88. DE RecName: Full=polynucleotide adenylyltransferase {ECO:0000256|ARBA:ARBA00012388}; DE EC=2.7.7.19 {ECO:0000256|ARBA:ARBA00012388}; GN Name=6046023 {ECO:0000313|EnsemblMetazoa:CPIJ012940-PA}; GN ORFNames=CpipJ_CPIJ012940 {ECO:0000313|EMBL:EDS38363.1}; OS Culex quinquefasciatus (Southern house mosquito) (Culex pungens). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae; OC Culicinae; Culicini; Culex; Culex. OX NCBI_TaxID=7176; RN [1] {ECO:0000313|EMBL:EDS38363.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JHB {ECO:0000313|EMBL:EDS38363.1}; RG The Broad Institute Genome Sequencing Platform; RA Atkinson P.W., Hemingway J., Christensen B.M., Higgs S., Kodira C., RA Hannick L., Megy K., O'Leary S., Pearson M., Haas B.J., Mauceli E., RA Wortman J.R., Lee N.H., Guigo R., Stanke M., Alvarado L., Amedeo P., RA Antoine C.H., Arensburger P., Bidwell S.L., Crawford M., Camaro F., RA Devon K., Engels R., Hammond M., Howarth C., Koehrsen M., Lawson D., RA Montgomery P., Nene V., Nusbaum C., Puiu D., Romero-Severson J., RA Severson D.W., Shumway M., Sisk P., Stolte C., Zeng Q., Eisenstadt E., RA Fraser-Liggett C., Strausberg R., Galagan J., Birren B., Collins F.H.; RT "Annotation of Culex pipiens quinquefasciatus."; RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EnsemblMetazoa:CPIJ012940-PA} RP IDENTIFICATION. RC STRAIN=JHB {ECO:0000313|EnsemblMetazoa:CPIJ012940-PA}; RG EnsemblMetazoa; RL Submitted (FEB-2021) to UniProtKB. 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|ARBA:ARBA00024620}; 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 -!- SIMILARITY: Belongs to the poly(A) polymerase family. CC {ECO:0000256|ARBA:ARBA00010912}. 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; DS232247; EDS38363.1; -; Genomic_DNA. DR RefSeq; XP_001863293.1; XM_001863258.1. DR AlphaFoldDB; B0X0X1; -. DR STRING; 7176.B0X0X1; -. DR EnsemblMetazoa; CPIJ012940-RA; CPIJ012940-PA; CPIJ012940. DR KEGG; cqu:CpipJ_CPIJ012940; -. DR VEuPathDB; VectorBase:CPIJ012940; -. DR VEuPathDB; VectorBase:CQUJHB012401; -. DR eggNOG; KOG2245; Eukaryota. DR HOGENOM; CLU_738202_0_0_1; -. DR InParanoid; B0X0X1; -. DR OMA; ICEANIW; -. DR Proteomes; UP000002320; Unassembled WGS sequence. 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:1990817; F:poly(A) RNA polymerase activity; IEA:UniProtKB-EC. DR GO; GO:0003723; F:RNA binding; IEA:InterPro. DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW. DR GO; GO:0031123; P:RNA 3'-end processing; IEA:InterPro. 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; 2. DR Pfam; PF20750; PAP_NTPase; 1. DR Pfam; PF04926; PAP_RNA-bind; 1. DR PIRSF; PIRSF018425; PolyA_polymerase; 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 {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRSR:PIRSR018425- KW 1}; Magnesium {ECO:0000256|PIRSR:PIRSR018425-2}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR018425-2}; KW mRNA processing {ECO:0000256|ARBA:ARBA00022664}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, KW ECO:0000256|PIRSR:PIRSR018425-1}; Nucleus {ECO:0000256|ARBA:ARBA00023242}; KW Reference proteome {ECO:0000313|Proteomes:UP000002320}; KW Transferase {ECO:0000256|ARBA:ARBA00022679}. FT DOMAIN 36..137 FT /note="Poly(A) polymerase nucleotidyltransferase" FT /evidence="ECO:0000259|Pfam:PF20750" FT DOMAIN 142..185 FT /note="Poly(A) polymerase central" FT /evidence="ECO:0000259|Pfam:PF04928" FT DOMAIN 186..266 FT /note="Poly(A) polymerase central" FT /evidence="ECO:0000259|Pfam:PF04928" FT DOMAIN 269..336 FT /note="Poly(A) polymerase RNA-binding" FT /evidence="ECO:0000259|Pfam:PF04926" FT BINDING 38 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 38 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 90 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PIRSR:PIRSR018425-1" FT BINDING 90 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 151 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PIRSR:PIRSR018425-1" FT BINDING 160 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PIRSR:PIRSR018425-1" FT BINDING 169..170 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PIRSR:PIRSR018425-1" SQ SEQUENCE 375 AA; 43802 MW; B84940CCAF9F7F64 CRC64; MCPSRRTCRK CWQRSSAERS TLLGRTGWPL TTILTNIDAL CVAPRNIERQ DYFGSFLELL EKQPEVTECR AVEEMLVPDV KMNFDGIKID LLFARLALKE IPDNFDLRED MLLKNLDPKL MRSLNGCRAT DEILRLVPNI DNFRLALRST KLWAKKHGIY STSLGYFGGV SWAMLVARTC QLPNVVPVFL KRPDTVNLGF QVWDPRVNVQ GRFDLMPIIT PAYPQQNSTF HVSSSTRKIM LNEFNRGMQI TDEIMLGKAG WDKLFEAPSF FFKYRYFIVL LVTSNNTDDL LEWCGLVESK IRYLIQNLER ILHINLAHVH IKVLETTRDG MKTEARHVRR KQLNQYLDPN LLKRERKNQR LLRRRKCAND LLRRN //