PNP_ACIC1
ID PNP_ACIC1 Reviewed; 782 AA.
AC A0LV20;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Polyribonucleotide nucleotidyltransferase {ECO:0000255|HAMAP-Rule:MF_01595};
DE EC=2.7.7.8 {ECO:0000255|HAMAP-Rule:MF_01595};
DE AltName: Full=Polynucleotide phosphorylase {ECO:0000255|HAMAP-Rule:MF_01595};
DE Short=PNPase {ECO:0000255|HAMAP-Rule:MF_01595};
GN Name=pnp {ECO:0000255|HAMAP-Rule:MF_01595}; OrderedLocusNames=Acel_1508;
OS Acidothermus cellulolyticus (strain ATCC 43068 / DSM 8971 / 11B).
OC Bacteria; Actinobacteria; Acidothermales; Acidothermaceae; Acidothermus.
OX NCBI_TaxID=351607;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43068 / DSM 8971 / 11B;
RX PubMed=19270083; DOI=10.1101/gr.084848.108;
RA Barabote R.D., Xie G., Leu D.H., Normand P., Necsulea A., Daubin V.,
RA Medigue C., Adney W.S., Xu X.C., Lapidus A., Parales R.E., Detter C.,
RA Pujic P., Bruce D., Lavire C., Challacombe J.F., Brettin T.S., Berry A.M.;
RT "Complete genome of the cellulolytic thermophile Acidothermus
RT cellulolyticus 11B provides insights into its ecophysiological and
RT evolutionary adaptations.";
RL Genome Res. 19:1033-1043(2009).
CC -!- FUNCTION: Involved in mRNA degradation. Catalyzes the phosphorolysis of
CC single-stranded polyribonucleotides processively in the 3'- to 5'-
CC direction. {ECO:0000255|HAMAP-Rule:MF_01595}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=phosphate + RNA(n+1) = a ribonucleoside 5'-diphosphate +
CC RNA(n); Xref=Rhea:RHEA:22096, Rhea:RHEA-COMP:14527, Rhea:RHEA-
CC COMP:17342, ChEBI:CHEBI:43474, ChEBI:CHEBI:57930, ChEBI:CHEBI:140395;
CC EC=2.7.7.8; Evidence={ECO:0000255|HAMAP-Rule:MF_01595};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01595};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01595}.
CC -!- SIMILARITY: Belongs to the polyribonucleotide nucleotidyltransferase
CC family. {ECO:0000255|HAMAP-Rule:MF_01595}.
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DR EMBL; CP000481; ABK53280.1; -; Genomic_DNA.
DR RefSeq; WP_011720343.1; NC_008578.1.
DR AlphaFoldDB; A0LV20; -.
DR SMR; A0LV20; -.
DR STRING; 351607.Acel_1508; -.
DR PRIDE; A0LV20; -.
DR EnsemblBacteria; ABK53280; ABK53280; Acel_1508.
DR KEGG; ace:Acel_1508; -.
DR eggNOG; COG1185; Bacteria.
DR HOGENOM; CLU_004217_2_2_11; -.
DR OMA; LHILDVM; -.
DR OrthoDB; 122725at2; -.
DR Proteomes; UP000008221; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004654; F:polyribonucleotide nucleotidyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006402; P:mRNA catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.30.1370.10; -; 1.
DR Gene3D; 3.30.230.70; -; 2.
DR HAMAP; MF_01595; PNPase; 1.
DR InterPro; IPR001247; ExoRNase_PH_dom1.
DR InterPro; IPR036345; ExoRNase_PH_dom2_sf.
DR InterPro; IPR014069; GPSI/PNP.
DR InterPro; IPR004087; KH_dom.
DR InterPro; IPR004088; KH_dom_type_1.
DR InterPro; IPR036612; KH_dom_type_1_sf.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR012162; PNPase.
DR InterPro; IPR027408; PNPase/RNase_PH_dom_sf.
DR InterPro; IPR015848; PNPase_PH_RNA-bd_bac/org-type.
DR InterPro; IPR036456; PNPase_PH_RNA-bd_sf.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR022967; S1_dom.
DR InterPro; IPR003029; S1_domain.
DR PANTHER; PTHR11252; PTHR11252; 1.
DR Pfam; PF00013; KH_1; 1.
DR Pfam; PF03726; PNPase; 1.
DR Pfam; PF01138; RNase_PH; 2.
DR Pfam; PF00575; S1; 1.
DR PIRSF; PIRSF005499; PNPase; 1.
DR SMART; SM00322; KH; 1.
DR SMART; SM00316; S1; 1.
DR SUPFAM; SSF46915; SSF46915; 1.
DR SUPFAM; SSF54211; SSF54211; 2.
DR SUPFAM; SSF54791; SSF54791; 1.
DR SUPFAM; SSF55666; SSF55666; 2.
DR TIGRFAMs; TIGR03591; polynuc_phos; 1.
DR TIGRFAMs; TIGR02696; pppGpp_PNP; 1.
DR PROSITE; PS50084; KH_TYPE_1; 1.
DR PROSITE; PS50126; S1; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Magnesium; Metal-binding; Nucleotidyltransferase;
KW Reference proteome; RNA-binding; Transferase.
FT CHAIN 1..782
FT /note="Polyribonucleotide nucleotidyltransferase"
FT /id="PRO_0000329479"
FT DOMAIN 580..639
FT /note="KH"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
FT DOMAIN 651..723
FT /note="S1 motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
FT REGION 734..782
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 759..775
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 514
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
FT BINDING 520
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
SQ SEQUENCE 782 AA; 83621 MW; BA7AD1196DED3CC2 CRC64;
MADHDVHTAE AVIDNGSFGV RTVRFETGRL ARQAGGSAVA YLGDTMVLSA TTASKEPREQ
FDFFPLTVDV EERLYAAGRI PGSFFRREGR PSEEAILTCR LIDRPLRPSF VKGLRNEVQV
VVTVLAVDPE HLYDVVAINA ASMSTLLAGL PFSGPIGGVR MAHIDGTWVA FPTYSELERA
TFDMVVAGRV LPDGDVAIMM VEAEATEETI PLIREGAPAP TEEVVAGGLE AAKPFIRTLC
AAQSELAARA AKPVTEFPLF RDYEDDVYDA VAATVRDDVA RALTIAGKQE REAALDEVAN
TALGRLGERF AGREKEILAA LRALTKKLVR ERIIREKVRI DGRGLTDIRP LTAEVGIVPR
VHGSALFERG ETQILGVTTL NMLRMEQQLD TVSPRTKKRY MHHYNFPPYS TGEVGRVGSP
KRREIGHGAL AERALIPVLP SREEFPYAIR QVSEAIGSNG STSMGSVCAS TLSLLNAGVP
LRAPVAGIAM GLISDTVDGE THYVTLTDIL GAEDAYGDMD FKVAGTRDFV TALQLDTKLD
GIPASVLAAA LPQAREARLT ILDVMAKAIS EPAPMSPYAP RIITIKIPVD QIGAVIGPKG
KIINQIQDDT GAEITIEDDG TIYIGATEGT AAEAARAAIS AIANPQLPEV GERYLGTVVK
ATPFGVFVSL LPGKDGLLHI SELRKMAGGR RVENVEDVLK VGDKIQVEIR DIDARGKLSL
VPVDVPGAVL AEDAGAGESA ASGGAPRSAG GPQPREHQGP GRPRGRGGDH GGEGRQRTRR
RH
