ID   PCNB_SALTI              Reviewed;         465 AA.
AC   Q8Z9C3;
DT   27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2006, sequence version 2.
DT   27-MAR-2024, entry version 122.
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=STY0209, t0192;
OS   Salmonella typhi.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=90370;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CT18;
RX   PubMed=11677608; DOI=10.1038/35101607;
RA   Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA   Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA   Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA   Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA   Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA   Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA   Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA   Barrell B.G.;
RT   "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT   serovar Typhi CT18.";
RL   Nature 413:848-852(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700931 / Ty2;
RX   PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA   Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA   Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT   "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT   CT18.";
RL   J. Bacteriol. 185:2330-2337(2003).
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=AAO67924.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=CAD01345.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AL513382; CAD01345.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AE014613; AAO67924.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_454800.1; NC_003198.1.
DR   AlphaFoldDB; Q8Z9C3; -.
DR   SMR; Q8Z9C3; -.
DR   STRING; 220341.gene:17584247; -.
DR   KEGG; stt:t0192; -.
DR   KEGG; sty:STY0209; -.
DR   PATRIC; fig|220341.7.peg.212; -.
DR   eggNOG; COG0617; Bacteria.
DR   HOGENOM; CLU_015961_0_0_6; -.
DR   OMA; FMAKLDM; -.
DR   Proteomes; UP000000541; Chromosome.
DR   Proteomes; UP000002670; Chromosome.
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; mRNA processing; Nucleotide-binding; RNA-binding;
KW   Transcription; Transferase.
FT   CHAIN           1..465
FT                   /note="Poly(A) polymerase I"
FT                   /id="PRO_0000139094"
FT   REGION          430..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;  53902 MW;  A94E6DFAFBC83720 CRC64;
     MFTRVANFCR KVLSREESEA EQAVARPHMT IIPREQHAIS RKDISENALK VLYRLNKAGY
     EAYLVGGGVR DLLLGKKPKD FDVTTNATPD QVRKLFRNCR LVGRRFRLAH VMFGPEIIEV
     ATFRGHNEGS ESDRTTSQRG QNGMLLRDNI FGSIEEDAQR RDFTINSLYY SVADFTVRDY
     VGGMQDLQEG VIRLIGNPET RYREDPVRML RAVRFAAKLN MRISPETAEP IPRLATLLND
     IPPARLFEES LKLLQAGNGF ETYQQLREYH LFQPLFPTIT RYFTENGDSA MERIIAQVLK
     NTDNRIRNEM RVNPAFLFAA MFWYPLLEMA QKIAQESGLA YYDAFALAMN DVLDEACRSL
     AIPKRLTTLT RDIWQLQLRM SRRQGKRAWK LMEHPKFRAA FDLLELRAQV ENNTELQRLA
     QWWAEFQASA PPEQKGMLNE LDDDPAPRRR RSRPRKRAPR REGTV
//