ID A0A369AKU1_9BURK Unreviewed; 564 AA.
AC A0A369AKU1;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
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=DFR45_104158 {ECO:0000313|EMBL:RCX09791.1};
OS Extensimonas vulgaris.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Extensimonas.
OX NCBI_TaxID=1031594 {ECO:0000313|EMBL:RCX09791.1, ECO:0000313|Proteomes:UP000252174};
RN [1] {ECO:0000313|EMBL:RCX09791.1, ECO:0000313|Proteomes:UP000252174}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 100911 {ECO:0000313|EMBL:RCX09791.1,
RC ECO:0000313|Proteomes:UP000252174};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (JUL-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:RCX09791.1}.
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DR EMBL; QPJU01000004; RCX09791.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A369AKU1; -.
DR OrthoDB; 9805698at2; -.
DR Proteomes; UP000252174; Unassembled WGS sequence.
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}; Reference proteome {ECO:0000313|Proteomes:UP000252174};
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 62..211
FT /note="Poly A polymerase head"
FT /evidence="ECO:0000259|Pfam:PF01743"
FT DOMAIN 241..301
FT /note="tRNA nucleotidyltransferase/poly(A) polymerase RNA
FT and SrmB- binding"
FT /evidence="ECO:0000259|Pfam:PF12627"
FT DOMAIN 354..471
FT /note="Polymerase A arginine-rich C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12626"
FT REGION 455..564
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 80
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00957"
FT ACT_SITE 82
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00957"
FT ACT_SITE 180
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00957"
SQ SEQUENCE 564 AA; 61976 MW; 39DFF5F64DF83FA9 CRC64;
MIKNFIDKLL GKAPAGSAKT KKKPSFGRRA EVPASVHGID PNLVDRRAAE VVHTLKQAGF
EAYIVGGAVR DLLLGLRPKD FDVATNATPE QVKQLFRRAF IIGRRFRIVH VVFGRGREHE
VIEVSTFRAY LDSAAAEQVS GNEKSSRQAL AGVQHAVDAS GRVLRDNVWG SQEEDAARRD
FTINAMYYDP ETQIVVDYHK GIQDAQKKLL RMIGDPATRY REDPVRIVRA VRFAAKLSAL
GFTLAPQTAA PLAASLPLLA DVPPSRMFDE MLKLLQTGHA IASVEQLRKL GLARGIYPLL
DMVVERADTP FVRAALLDTD RRVAEGKSVV ASFLLACVLW DDVRAAWQQR LHTQHPLPAL
HEAIDEVFER RIGDVSGRGK LAADMREIWV MQPRFEKRTG NTPFGLVEQP RFRAGFDFLR
LRADVGEVEE ALAEWWQDFQ NADDERRADL IAQAREEQKG QEKSRKRPTK PRRAALPPSE
DGTPPTAEPA PSTAADAVAD EAADADQPPK KRRRRRRKPA AQGTGAEAGG DASNHADAGT
DAGANAAGRN AESGAAPNAV PDSH
//
