ID A0A285NWA8_9PSED Unreviewed; 457 AA.
AC A0A285NWA8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-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=SAMN05660463_02532 {ECO:0000313|EMBL:SNZ13764.1};
OS Pseudomonas sp. URIL14HWK12:I9.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1261633 {ECO:0000313|EMBL:SNZ13764.1, ECO:0000313|Proteomes:UP000232228};
RN [1] {ECO:0000313|EMBL:SNZ13764.1, ECO:0000313|Proteomes:UP000232228}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=URIL14HWK12:I9 {ECO:0000313|EMBL:SNZ13764.1,
RC ECO:0000313|Proteomes:UP000232228};
RA Ehlers B., Leendertz F.H.;
RL Submitted (SEP-2017) 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; OBEM01000005; SNZ13764.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A285NWA8; -.
DR OrthoDB; 9805698at2; -.
DR Proteomes; UP000232228; 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:UP000232228};
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 56..188
FT /note="Poly A polymerase head"
FT /evidence="ECO:0000259|Pfam:PF01743"
FT DOMAIN 215..275
FT /note="tRNA nucleotidyltransferase/poly(A) polymerase RNA
FT and SrmB- binding"
FT /evidence="ECO:0000259|Pfam:PF12627"
FT DOMAIN 330..452
FT /note="Polymerase A arginine-rich C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12626"
FT REGION 425..457
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 425..444
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 74
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00957"
FT ACT_SITE 76
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00957"
FT ACT_SITE 157
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00957"
SQ SEQUENCE 457 AA; 51943 MW; 6E12949653462D2C CRC64;
MLKKLFQSIR PSGRPSHALR TTPQVLGSQQ HSLQRQQFSR HAVGIVERLQ QAGYQAYLVG
GCVRDLLLGI TPKDFDVATS ATPEQVRAEF RNARIIGRRF KLVHVHFGRE IIEVATFRAN
HPEDEAEDSR HSSRNESGRI LRDNVYGTLE EDAQRRDFTI NALYYDPVAE RILDYAGGVH
DVRNKLIRLI GDPTQRYQED AVRMLRAVRF AAKLDFGIER RTVEPIRGLA ASLRDIPAAR
LFEETLKLFL SGHGATVYEM LVDLHLFDAL FPASAYALEH EPEYTHTLIR NALVNTDLRV
AQGKPVTPAF LFAALLWPAL PMRAAYLQGQ GLPPIPAMQE AAHGLISEQC QRIAIPKRFT
LPIKEIWDMQ ERLPRRTGKR ADVLLENPRF RAGYDFLLLR ESAGEQTNGL GQWWTEYQEL
PDRDRRAMIS ELAGGDEDSG AAPRKRRRNS KRKSDAE
//
