ID PNP_DESRM Reviewed; 740 AA.
AC A4J5W6;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 1.
DT 27-NOV-2024, entry version 96.
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=Dred_1950;
OS Desulforamulus reducens (strain ATCC BAA-1160 / DSM 100696 / MI-1)
OS (Desulfotomaculum reducens).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae;
OC Desulforamulus.
OX NCBI_TaxID=349161;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1160 / DSM 100696 / MI-1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Sims D., Brettin T., Bruce D., Han C., Tapia R., Schmutz J., Larimer F.,
RA Land M., Hauser L., Kyrpides N., Kim E., Tebo B.M., Richardson P.;
RT "Complete sequence of Desulfotomaculum reducens MI-1.";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
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=RNA(n+1) + phosphate = RNA(n) + a ribonucleoside 5'-
CC diphosphate; 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; CP000612; ABO50469.1; -; Genomic_DNA.
DR RefSeq; WP_011878279.1; NC_009253.1.
DR AlphaFoldDB; A4J5W6; -.
DR SMR; A4J5W6; -.
DR STRING; 349161.Dred_1950; -.
DR KEGG; drm:Dred_1950; -.
DR eggNOG; COG1185; Bacteria.
DR HOGENOM; CLU_004217_2_2_9; -.
DR OrthoDB; 9804305at2; -.
DR Proteomes; UP000001556; Chromosome.
DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR GO; GO:0000175; F:3'-5'-RNA exonuclease activity; IEA:TreeGrafter.
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 CDD; cd02393; KH-I_PNPase; 1.
DR CDD; cd11363; RNase_PH_PNPase_1; 1.
DR CDD; cd11364; RNase_PH_PNPase_2; 1.
DR CDD; cd04472; S1_PNPase; 1.
DR FunFam; 3.30.1370.10:FF:000001; Polyribonucleotide nucleotidyltransferase; 1.
DR FunFam; 3.30.230.70:FF:000001; Polyribonucleotide nucleotidyltransferase; 1.
DR FunFam; 3.30.230.70:FF:000002; Polyribonucleotide nucleotidyltransferase; 1.
DR Gene3D; 3.30.230.70; GHMP Kinase, N-terminal domain; 2.
DR Gene3D; 3.30.1370.10; K Homology domain, type 1; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
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_Su5_D2-typ_SF.
DR InterPro; IPR003029; S1_domain.
DR NCBIfam; TIGR03591; polynuc_phos; 1.
DR PANTHER; PTHR11252; POLYRIBONUCLEOTIDE NUCLEOTIDYLTRANSFERASE; 1.
DR PANTHER; PTHR11252:SF0; POLYRIBONUCLEOTIDE NUCLEOTIDYLTRANSFERASE 1, MITOCHONDRIAL; 1.
DR Pfam; PF00013; KH_1; 1.
DR Pfam; PF03726; PNPase; 1.
DR Pfam; PF01138; RNase_PH; 2.
DR Pfam; PF03725; RNase_PH_C; 2.
DR Pfam; PF00575; S1; 1.
DR PIRSF; PIRSF005499; PNPase; 1.
DR SMART; SM00322; KH; 1.
DR SMART; SM00316; S1; 1.
DR SUPFAM; SSF54791; Eukaryotic type KH-domain (KH-domain type I); 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR SUPFAM; SSF46915; Polynucleotide phosphorylase/guanosine pentaphosphate synthase (PNPase/GPSI), domain 3; 1.
DR SUPFAM; SSF55666; Ribonuclease PH domain 2-like; 2.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 2.
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..740
FT /note="Polyribonucleotide nucleotidyltransferase"
FT /id="PRO_0000329624"
FT DOMAIN 563..622
FT /note="KH"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
FT DOMAIN 632..706
FT /note="S1 motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
FT REGION 707..740
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 721..740
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 496
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
FT BINDING 502
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
SQ SEQUENCE 740 AA; 81425 MW; DB1993E12F953C1C CRC64;
MSENQVLIRE ISLGGRTLTL ETGRMAKQAS GAVLVTYGET VVLVTATVAK NTRDIDFFPL
TVDYEERLYA VGKIPGGFIK REGRPSEKAI LSGRLIDRPI RPLFPKHMRN EVQVVATVMS
VDQDNAPEIA AMIGASAALH ISKIPLKKPI GGVIVGRVDG QFVINPMVRQ AENSDMHLVV
AGTDDAVMMV EAGAKEVPES EMLEGIMYGH EKVKEIVKFI EDFRTEALGM GLAFEKMEIP
EPQFDSNMSE AILTIAEEAI REAVLHCSRE KLTKKQREVY MDEVMSGLQE KFLEQFPENP
KEVTMLIEKA EKKVVRRIIT HDKLRIDGRA IDEIRPISVE VGVLPRTHGT GLFTRGQTQI
LSVATLGSIS EEQILDGLGV EESKRYMHHY NFPPFSTGET KPMRSPGRRE IGHGALAERA
LEPMIPPEEV FPYTIRVVSE AIESNGSTSM GSVCGSTLSL MDAGVPLKAP VAGVAMGLIM
EEDQFTVLTD IQGLEDHLGD MDFKVAGSAN GVTALQMDIK IPGITREVFE QALEQAHRGR
MFILGKMLEV LSTPRAEISV HAPAIIRTSI HPDKIRDIIG PGGKIIKKLV EETGADIDIE
DDGRVFIAAV DREKGKRALE IIQSITAEVQ VGKLYNGKVT RVTDFGCFVE VIPGVMGLPG
KEGLVHISQL AFQRVEKTED IVKEGEVIAV KAIGYDQQGR LKLSKKEAMR DMGLAPAEST
SEQPEKRERR PFSRPKATKE
//
