ID A0A1P8FDU5_9PROT Unreviewed; 455 AA.
AC A0A1P8FDU5;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=BWI17_00295 {ECO:0000313|EMBL:APV48250.1};
OS Betaproteobacteria bacterium GR16-43.
OC Bacteria; Pseudomonadota; Betaproteobacteria.
OX NCBI_TaxID=1904640 {ECO:0000313|EMBL:APV48250.1, ECO:0000313|Proteomes:UP000185830};
RN [1] {ECO:0000313|EMBL:APV48250.1, ECO:0000313|Proteomes:UP000185830}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GR16-43 {ECO:0000313|EMBL:APV48250.1,
RC ECO:0000313|Proteomes:UP000185830};
RA Choi A.;
RT "Complete genome sequence of betaproteobacterium GR16-43, isolated from a
RT freshwater pond in South Korea.";
RL Submitted (DEC-2016) 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}.
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DR EMBL; CP019169; APV48250.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1P8FDU5; -.
DR STRING; 1904640.BWI17_00295; -.
DR KEGG; beba:BWI17_00295; -.
DR OrthoDB; 9805698at2; -.
DR Proteomes; UP000185830; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0043633; P:polyadenylation-dependent RNA catabolic process; IEA:InterPro.
DR GO; GO:0031123; P:RNA 3'-end processing; IEA:UniProt.
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 mRNA processing {ECO:0000256|ARBA:ARBA00022664, ECO:0000256|HAMAP-
KW Rule:MF_00957};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00957};
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 55..179
FT /note="Poly A polymerase head"
FT /evidence="ECO:0000259|Pfam:PF01743"
FT DOMAIN 207..269
FT /note="tRNA nucleotidyltransferase/poly(A) polymerase RNA
FT and SrmB- binding"
FT /evidence="ECO:0000259|Pfam:PF12627"
FT DOMAIN 321..438
FT /note="Polymerase A arginine-rich C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12626"
FT REGION 414..455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 414..428
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 73
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00957"
FT ACT_SITE 75
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00957"
FT ACT_SITE 149
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00957"
SQ SEQUENCE 455 AA; 51394 MW; 91BDDB9619FBB654 CRC64;
MIKRYIDKLF GRKAASGKDA KPVIYGPDKH GIRRDAISKC ARRTCEDLQR AGHAAFVVGG
AVRDHLLGHT PKDYDVATSA TPEEVRSIFR RSRIIGRRFQ IVHVLCGQDV VEVSTFRALL
DGEAGTDEHG RVLSDNVFGT QAEDATRRDF TVNALFFDPV KEEVWDYHHG VKDINAKRLV
MIGDAAQRYR EDPVRMLRAA RLAAKLGLTI DAKTEAPIHA HKHLIQNVPQ SRLFEEILKL
LLSGNAVACT KLLRKLELHH GLLPLLDDAL EDKGTGPFAL AALKATDDRL REDKSVSPAF
LLAALLWGRV ERELRKHEDA GQPSIPALHT AMHEALDAQR ESLAIPRRFD ATMKELWLLQ
PRFLQRGGQR PYRLLEHPRF RAAYDFFELR AQSGNAPMDI AQWWDRFQHA NADEREEMMV
EDEAGPKKKR RRRRGKRKEE GGPPEGGAPP QDDAS
//
