(data stored in ACNUC7421 zone)

SWISSPROT: 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   07-JUN-2017, entry version 71.
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.,
RA   Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A.,
RA   Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L.,
RA   Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K.,
RA   Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C.,
RA   Welch R.A., 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.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and 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
CC       usually targets these RNAs for decay. Plays a significant role in
CC       the global control of gene expression, through influencing the
CC       rate of transcript degradation, and in the general RNA quality
CC       control. {ECO:0000255|HAMAP-Rule:MF_00957}.
CC   -!- CATALYTIC ACTIVITY: ATP + RNA(n) = diphosphate + RNA(n+1).
CC       {ECO:0000255|HAMAP-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=Translation N-terminally extended.; Evidence={ECO:0000305};
CC       Sequence=BAB33570.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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   ProteinModelPortal; P0ABF3; -.
DR   SMR; P0ABF3; -.
DR   STRING; 155864.Z0154; -.
DR   PRIDE; P0ABF3; -.
DR   EnsemblBacteria; AAG54447; AAG54447; Z0154.
DR   EnsemblBacteria; BAB33570; BAB33570; BAB33570.
DR   GeneID; 913763; -.
DR   KEGG; ece:Z0154; -.
DR   KEGG; ecs:ECs0147; -.
DR   PATRIC; fig|386585.9.peg.246; -.
DR   eggNOG; ENOG4105DJ0; Bacteria.
DR   eggNOG; COG0617; LUCA.
DR   HOGENOM; HOG000256527; -.
DR   KO; K00970; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004652; F:polynucleotide adenylyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006378; P:mRNA polyadenylation; IEA:InterPro.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR   CDD; cd05398; NT_ClassII-CCAase; 1.
DR   HAMAP; MF_00957; PolyA_pol; 1.
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   TIGRFAMs; TIGR01942; pcnB; 1.
PE   3: Inferred from homology;
DR   PRODOM; P0ABF3.
DR   SWISS-2DPAGE; P0ABF3.
KW   ATP-binding; Complete proteome; mRNA processing; Nucleotide-binding;
KW   RNA-binding; Transcription; Transferase.
FT   CHAIN         1    465       Poly(A) polymerase I.
FT                                /FTId=PRO_0000139091.
FT   ACT_SITE     80     80       {ECO:0000255|HAMAP-Rule:MF_00957}.
FT   ACT_SITE     82     82       {ECO:0000255|HAMAP-Rule:MF_00957}.
FT   ACT_SITE    162    162       {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
//

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