ID A0A0J0YPL7_9NEIS Unreviewed; 453 AA.
AC A0A0J0YPL7;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
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=PL75_10230 {ECO:0000313|EMBL:KLT72069.1};
OS Neisseria arctica.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=1470200 {ECO:0000313|EMBL:KLT72069.1, ECO:0000313|Proteomes:UP000036027};
RN [1] {ECO:0000313|EMBL:KLT72069.1, ECO:0000313|Proteomes:UP000036027}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KH1503 {ECO:0000313|EMBL:KLT72069.1,
RC ECO:0000313|Proteomes:UP000036027};
RA Hansen C.M., Hueffer K., Choi S.C.;
RT "Genome of a novel goose pathogen.";
RL Submitted (NOV-2014) 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:KLT72069.1}.
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DR EMBL; JTDO01000022; KLT72069.1; -; Genomic_DNA.
DR RefSeq; WP_047761853.1; NZ_JTDO01000022.1.
DR AlphaFoldDB; A0A0J0YPL7; -.
DR STRING; 1470200.PL75_10230; -.
DR PATRIC; fig|1470200.3.peg.1337; -.
DR OrthoDB; 9805698at2; -.
DR Proteomes; UP000036027; 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:UP000036027};
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 52..174
FT /note="Poly A polymerase head"
FT /evidence="ECO:0000259|Pfam:PF01743"
FT DOMAIN 202..263
FT /note="tRNA nucleotidyltransferase/poly(A) polymerase RNA
FT and SrmB- binding"
FT /evidence="ECO:0000259|Pfam:PF12627"
FT DOMAIN 317..445
FT /note="Polymerase A arginine-rich C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12626"
FT REGION 415..453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 70
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00957"
FT ACT_SITE 72
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00957"
FT ACT_SITE 144
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00957"
SQ SEQUENCE 453 AA; 51422 MW; 0BA48B203B52252D CRC64;
MLKKWLHKVL PGGRGRVQKQ VLEFAEHGIR ADMISFAAEK VVKRLHQEGF QAYVVGGAVR
DLLLGIDPKD FDVATDATPE QVRKVFRRSR IIGRRFQIVH VMVGPETIEV TTFRGGSKVQ
QNEHGRIMKD NTYGSIEEDA MRRDFTCNAL YYDPIRQQLL DFHCGVEAVR ARKLVMIGNP
AARYQEDPVR VLRAVRLSGK LGFEVDAPTA EPIPHEAGRL KQEPVARLFD EIMKLLFSGH
ALQCLQQLKI LGVDANIHPL LNALCQSAQE NGQNIVTLAL HNTDARLRAD KSVSVGFVLA
AVLWPQLNGR WRQYLMQGQK PAGAMNSAIA DFRDEMEKGW GVPQRFAATM REIWVLQPQF
EYCKGARPHR LLAQQRFRAA YDFLILRAQM GEVDEALAQW WTAFQHADEV LRNEMAQSSM
RSESASWDDG GEVAVKKKRR RKPRKRKPKA EAA
//
