PCNB_SALTI
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 25-MAY-2022, entry version 113.
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; Proteobacteria; 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; 220341.16501473; -.
DR EnsemblBacteria; AAO67924; AAO67924; t0192.
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: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; 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
