ID A0A2S5DYQ0_9BURK Unreviewed; 512 AA. AC A0A2S5DYQ0; DT 18-JUL-2018, integrated into UniProtKB/TrEMBL. DT 18-JUL-2018, sequence version 1. DT 08-MAY-2019, entry version 6. 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; Proteobacteria; 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., RA Simner P.; RT "Successful Treatment of Persistent Burkholderia cepacia Bacteremia RT with 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 CC usually targets these RNAs for decay. Plays a significant role in CC the global control of gene expression, through influencing the CC rate of transcript degradation, and in the general RNA quality CC control. {ECO:0000256|HAMAP-Rule:MF_00957}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + RNA(n) = diphosphate + RNA(n)-3'-adenine CC ribonucleotide; Xref=Rhea:RHEA:11332, Rhea:RHEA-COMP:11128, CC Rhea:RHEA-COMP:14647, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, CC ChEBI:CHEBI:83400, ChEBI:CHEBI:140626; EC=2.7.7.19; CC Evidence={ECO:0000256|HAMAP-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, ECO:0000256|SAAS:SAAS00577624}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {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 Proteomes; UP000238655; Chromosome 1. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0004652; F:polynucleotide adenylyltransferase activity; IEA:UniProtKB-UniRule. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule. DR GO; GO:0006378; P:mRNA polyadenylation; IEA:InterPro. DR CDD; cd05398; NT_ClassII-CCAase; 1. DR HAMAP; MF_00957; PolyA_pol; 1. 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 Pfam; PF01743; PolyA_pol; 1. DR Pfam; PF12626; PolyA_pol_arg_C; 1. DR Pfam; PF12627; PolyA_pol_RNAbd; 1. DR TIGRFAMs; TIGR01942; pcnB; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00957, KW ECO:0000256|SAAS:SAAS00415369}; KW Complete proteome {ECO:0000313|Proteomes:UP000238655}; KW mRNA processing {ECO:0000256|HAMAP-Rule:MF_00957}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00957, KW ECO:0000256|SAAS:SAAS00415411}; KW Nucleotidyltransferase {ECO:0000313|EMBL:POZ84206.1}; KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_00957, KW ECO:0000256|RuleBase:RU003953, ECO:0000256|SAAS:SAAS00468387}; KW Transcription {ECO:0000256|HAMAP-Rule:MF_00957}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00957, KW ECO:0000256|RuleBase:RU003953, ECO:0000256|SAAS:SAAS00468438, KW ECO:0000313|EMBL:POZ84206.1}. FT DOMAIN 86 232 PolyA_pol. {ECO:0000259|Pfam:PF01743}. FT DOMAIN 259 319 PolyA_pol_RNAbd. {ECO:0000259|Pfam: FT PF12627}. FT DOMAIN 373 487 PolyA_pol_arg_C. {ECO:0000259|Pfam: FT PF12626}. FT ACT_SITE 104 104 {ECO:0000256|HAMAP-Rule:MF_00957}. FT ACT_SITE 106 106 {ECO:0000256|HAMAP-Rule:MF_00957}. FT ACT_SITE 201 201 {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 //