PCNB_ECO57
ID PCNB_ECO57 Reviewed; 465 AA.
AC P0ABF3; P13685; P78050; Q8X910;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 2.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Poly(A) polymerase I {ECO:0000255|HAMAP-Rule:MF_00957};
DE Short=PAP I {ECO:0000255|HAMAP-Rule:MF_00957};
DE EC=2.7.7.19 {ECO:0000255|HAMAP-Rule:MF_00957};
GN Name=pcnB {ECO:0000255|HAMAP-Rule:MF_00957};
GN OrderedLocusNames=Z0154, ECs0147;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
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:0000255|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:0000255|HAMAP-
CC Rule:MF_00957};
CC -!- SIMILARITY: Belongs to the tRNA nucleotidyltransferase/poly(A)
CC polymerase family. {ECO:0000255|HAMAP-Rule:MF_00957}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG54447.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB33570.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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; AE005174; AAG54447.1; ALT_INIT; Genomic_DNA.
DR EMBL; BA000007; BAB33570.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_308174.3; NC_002695.1.
DR RefSeq; WP_010723084.1; NZ_BFBO01000008.1.
DR AlphaFoldDB; P0ABF3; -.
DR SMR; P0ABF3; -.
DR STRING; 155864.EDL933_0147; -.
DR PRIDE; P0ABF3; -.
DR EnsemblBacteria; AAG54447; AAG54447; Z0154.
DR EnsemblBacteria; BAB33570; BAB33570; ECs_0147.
DR GeneID; 58461933; -.
DR GeneID; 913763; -.
DR KEGG; ece:Z0154; -.
DR KEGG; ecs:ECs_0147; -.
DR PATRIC; fig|386585.9.peg.246; -.
DR eggNOG; COG0617; Bacteria.
DR HOGENOM; CLU_015961_0_0_6; -.
DR OMA; FMAKLDM; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
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 Gene3D; 3.30.460.10; -; 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 Pfam; PF01743; PolyA_pol; 1.
DR Pfam; PF12626; PolyA_pol_arg_C; 1.
DR Pfam; PF12627; PolyA_pol_RNAbd; 1.
DR SUPFAM; SSF81301; SSF81301; 1.
DR TIGRFAMs; TIGR01942; pcnB; 1.
PE 3: Inferred from homology;
KW ATP-binding; mRNA processing; Nucleotide-binding; Reference proteome;
KW RNA-binding; Transcription; Transferase.
FT CHAIN 1..465
FT /note="Poly(A) polymerase I"
FT /id="PRO_0000139091"
FT REGION 429..465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 80
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00957"
FT ACT_SITE 82
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00957"
FT ACT_SITE 162
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00957"
SQ SEQUENCE 465 AA; 53871 MW; 0FAE30F2F95FB76E CRC64;
MFTRVANFCR KVLSREESEA EQAVARPQVT VIPREQHAIS RKDISENALK VMYRLNKAGY
EAWLVGGGVR DLLLGKKPKD FDVTTNATPE QVRKLFRNCR LVGRRFRLAH VMFGPEIIEV
ATFRGHHEGN VSDRTTSQRG QNGMLLRDNI FGSIEEDAQR RDFTINSLYY SVADFTVRDY
VGGMKDLKDG VIRLIGNPET RYREDPVRML RAVRFAAKLG MRISPETAEP IPRLATLLND
IPPARLFEES LKLLQAGYGY ETYKLLCEYH LFQPLFPTIT RYFTENGDSP MERIIEQVLK
NTDTRIHNDM RVNPAFLFAA MFWYPLLETA QKIAQESGLT YHDAFALAMN DVLDEACRSL
AIPKRLTTLT RDIWQLQLRM SRRQGKRAWK LLEHPKFRAA YDLLALRAEV ERNAELQRLV
KWWGEFQVSA PPDQKGMLNE LDEEPSPRRR TRRPRKRAPR REGTA
