ID A0A2S5DYQ0_9BURK Unreviewed; 512 AA. AC A0A2S5DYQ0; DT 18-JUL-2018, integrated into UniProtKB/TrEMBL. DT 18-JUL-2018, sequence version 1. DT 13-SEP-2023, entry version 20. DE RecName: Full=Poly(A) polymerase I {ECO:0000256|HAMAP-Rule:MF_00957}; DE Short=PAP I {ECO:0000256|HAMAP-Rule:MF_00957}; DE EC=2.7.7.19 {ECO:0000256|HAMAP-Rule:MF_00957}; GN Name=pcnB {ECO:0000256|HAMAP-Rule:MF_00957}; GN ORFNames=C3743_29825 {ECO:0000313|EMBL:POZ84206.1}; OS Burkholderia contaminans. OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex. OX NCBI_TaxID=488447 {ECO:0000313|EMBL:POZ84206.1, ECO:0000313|Proteomes:UP000238655}; RN [1] {ECO:0000313|EMBL:POZ84206.1, ECO:0000313|Proteomes:UP000238655} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=170816 {ECO:0000313|EMBL:POZ84206.1, RC ECO:0000313|Proteomes:UP000238655}; RA Tamma P., Fan Y., Bergman Y., Sick-Samuels A., Hsu A., Timp W., Simner P.; RT "Successful Treatment of Persistent Burkholderia cepacia Bacteremia with RT Ceftazidime-Avibactam."; RL Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Adds poly(A) tail to the 3' end of many RNAs, which usually CC targets these RNAs for decay. Plays a significant role in the global CC control of gene expression, through influencing the rate of transcript CC degradation, and in the general RNA quality control. CC {ECO:0000256|HAMAP-Rule:MF_00957}. 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; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00957}; CC -!- SIMILARITY: Belongs to the tRNA nucleotidyltransferase/poly(A) CC polymerase family. {ECO:0000256|HAMAP-Rule:MF_00957, CC ECO:0000256|RuleBase:RU003953}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:POZ84206.1}. 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; PQVP01000002; POZ84206.1; -; Genomic_DNA. DR AlphaFoldDB; A0A2S5DYQ0; -. DR EnsemblBacteria; POZ84206; POZ84206; C3743_29825. DR Proteomes; UP000238655; Chromosome 1. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0016787; F:hydrolase activity; 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-UniRule. DR GO; GO:0006378; P:mRNA polyadenylation; IEA:InterPro. DR GO; GO:0043631; P:RNA polyadenylation; IEA:UniProtKB-UniRule. DR CDD; cd05398; NT_ClassII-CCAase; 1. DR Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1. DR Gene3D; 1.10.3090.10; cca-adding enzyme, domain 2; 1. DR HAMAP; MF_00957; PolyA_pol; 1. DR InterPro; IPR043519; NT_sf. DR InterPro; IPR002646; PolA_pol_head_dom. DR InterPro; IPR010206; PolA_pol_I. DR InterPro; IPR025866; PolyA_pol_arg_C_dom. DR InterPro; IPR032828; PolyA_RNA-bd. DR NCBIfam; TIGR01942; pcnB; 1. DR PANTHER; PTHR43051; POLYNUCLEOTIDE ADENYLYLTRANSFERASE FAMILY PROTEIN; 1. DR PANTHER; PTHR43051:SF1; POLYNUCLEOTIDE ADENYLYLTRANSFERASE FAMILY PROTEIN; 1. DR Pfam; PF01743; PolyA_pol; 1. DR Pfam; PF12626; PolyA_pol_arg_C; 1. DR Pfam; PF12627; PolyA_pol_RNAbd; 1. DR SUPFAM; SSF81301; Nucleotidyltransferase; 1. DR SUPFAM; SSF81891; Poly A polymerase C-terminal region-like; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00957}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842}; KW mRNA processing {ECO:0000256|ARBA:ARBA00022664, ECO:0000256|HAMAP- KW Rule:MF_00957}; Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00957}; KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, KW ECO:0000313|EMBL:POZ84206.1}; KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_00957, KW ECO:0000256|RuleBase:RU003953}; KW Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP- KW Rule:MF_00957}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_00957}. FT DOMAIN 86..232 FT /note="Poly A polymerase head" FT /evidence="ECO:0000259|Pfam:PF01743" FT DOMAIN 259..319 FT /note="tRNA nucleotidyltransferase/poly(A) polymerase RNA FT and SrmB- binding" FT /evidence="ECO:0000259|Pfam:PF12627" FT DOMAIN 373..487 FT /note="Polymerase A arginine-rich C-terminal" FT /evidence="ECO:0000259|Pfam:PF12626" FT REGION 8..58 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 470..512 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 104 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00957" FT ACT_SITE 106 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00957" FT ACT_SITE 201 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00957" SQ SEQUENCE 512 AA; 57191 MW; 56A7A2CDC5E3C339 CRC64; MIKKFIRKLL GQDETEQTSP ATAPADEAAP ATPRTPKGAR GGGAKKPRSN HEPTVVPASV HGINPALISK NAVRVTDTLQ QAGFRAFIVG GAVRDLLLGI APKDFDVATD ATPTEVQRLF RRARLIGRRF QIVHVQFGQE LIEVSTFRAL VDAPPEAAAA EPPKRLKRDE LDRRTHAVDA SGRVLRDNVW GEQHEDAARR DFTINAMYYD PSTQTVLDYH DGMADVRARL LRMIGDPATR FREDPVRMLR VVRFAAKLGF EIEPHTREPI NALADLINNV PAARLFDEML KLLLSGHALA CLQRLRKEGL HHGLLPLLDV VLEQPQGEKF ITLALNNTDA RVRAGKTVSP GFLFATLLWH DMRQRFEQYT AEGEIPVPAL HRAMDDVLDM QTEKLAIHKR YSADMREIWG LQLRLEKRSG RSAMRLLEHQ RFRAGYDFLL LRCESGELDA EVGQWWTDFI EGDAAAREAL LTQGGTKEKS PRKRRRRGGV RNRKPGEGAA EPAPDASGGS DD //