PNP_DICTD
ID PNP_DICTD Reviewed; 693 AA.
AC B8E2S5;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 73.
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=Dtur_1146;
OS Dictyoglomus turgidum (strain DSM 6724 / Z-1310).
OC Bacteria; Dictyoglomi; Dictyoglomales; Dictyoglomaceae; Dictyoglomus.
OX NCBI_TaxID=515635;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6724 / Z-1310;
RX PubMed=28066333; DOI=10.3389/fmicb.2016.01979;
RA Brumm P.J., Gowda K., Robb F.T., Mead D.A.;
RT "The complete genome sequence of hyperthermophile Dictyoglomus turgidum DSM
RT 6724 reveals a specialized carbohydrate fermentor.";
RL Front. Microbiol. 7:1979-1979(2016).
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; CP001251; ACK42425.1; -; Genomic_DNA.
DR RefSeq; WP_012583507.1; NC_011661.1.
DR RefSeq; YP_002353039.1; NC_011661.1.
DR AlphaFoldDB; B8E2S5; -.
DR SMR; B8E2S5; -.
DR STRING; 515635.Dtur_1146; -.
DR EnsemblBacteria; ACK42425; ACK42425; Dtur_1146.
DR KEGG; dtu:Dtur_1146; -.
DR PATRIC; fig|515635.4.peg.1183; -.
DR eggNOG; COG1185; Bacteria.
DR HOGENOM; CLU_004217_2_2_0; -.
DR InParanoid; B8E2S5; -.
DR OMA; LHILDVM; -.
DR OrthoDB; 122725at2; -.
DR Proteomes; UP000007719; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0000175; F:3'-5'-exoribonuclease activity; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004654; F:polyribonucleotide nucleotidyltransferase activity; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006402; P:mRNA catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006401; P:RNA catabolic process; IBA:GO_Central.
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; IPR015847; ExoRNase_PH_dom2.
DR InterPro; IPR036345; ExoRNase_PH_dom2_sf.
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; PF03725; RNase_PH_C; 1.
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; SSF50249; SSF50249; 1.
DR SUPFAM; SSF54211; SSF54211; 2.
DR SUPFAM; SSF54791; SSF54791; 1.
DR SUPFAM; SSF55666; SSF55666; 2.
DR TIGRFAMs; TIGR03591; polynuc_phos; 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..693
FT /note="Polyribonucleotide nucleotidyltransferase"
FT /id="PRO_1000185736"
FT DOMAIN 552..611
FT /note="KH"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
FT DOMAIN 621..691
FT /note="S1 motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
FT BINDING 485
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
FT BINDING 491
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
SQ SEQUENCE 693 AA; 76821 MW; A0F962C980F2976D CRC64;
MRQTYSFKKD FAGKTLKIDI GKVAWQATGA ALVQYGETTV LVTVVASEEK KEDVDFFPLT
VEYVERLYAA GKIPGGFFKR EGKPTEPEIL FARLIDRPLR PLFSKDFRNE VQVIVTVLSY
DHENSTDIPS IIGASCAIML AGLPFKGPIG AVRVGWDGKE WYINPSVALS NSLLLDLVVA
GTKDAVLMIE GDGKEVPEEI FLEGIIRAHE QIGEVINFQE EILSMVNPVP FNYEPFVVNE
NLKKDVLEYV TVDQIRDAIF TPSKSERQKA LEDLKKRVIE HFKPIYGEIT AQIDEIINQE
AKAILTKVIL EEKRRVDGRR LNELRPVSCE VGVLSRVHGS ALFQRGETQV LSVVTLGAGE
EQIIESVIES EPKRYIHHYN FPPFSVGEAK PLRGPKRREI GHGALAERAL LPLIPKEEEF
PYTIRVVSEV LSSNGSTSMA SVCGSSLSLM DAGVPIKTHV AGVAMGLIKE GEKFEVLTDI
QGLEDALGGM DFKIAGTKNG ITAVQLDIKV DGLSYEIIEK TLKQAKEARY QILDIMEKTI
SQPRPEISPY APRIMVLEIN PNKIGDLIGP SGKNIKKIIE ETHTTINIKP EGLVYISAPD
QESAEKAAQM VQEYTRDIKE GDIFLGKVIR VTDYGAFVEI LPGKIGLLHI SKYKTTGTGK
NQTREEINLG DEILIKVDSI DPSGRISLSR KDL
