ID PNP_CAMJR Reviewed; 719 AA. AC Q5HTK8; DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot. DT 15-FEB-2005, sequence version 1. DT 27-MAR-2024, entry version 103. 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=CJE1390; OS Campylobacter jejuni (strain RM1221). OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=195099; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RM1221; RX PubMed=15660156; DOI=10.1371/journal.pbio.0030015; RA Fouts D.E., Mongodin E.F., Mandrell R.E., Miller W.G., Rasko D.A., RA Ravel J., Brinkac L.M., DeBoy R.T., Parker C.T., Daugherty S.C., RA Dodson R.J., Durkin A.S., Madupu R., Sullivan S.A., Shetty J.U., RA Ayodeji M.A., Shvartsbeyn A., Schatz M.C., Badger J.H., Fraser C.M., RA Nelson K.E.; RT "Major structural differences and novel potential virulence mechanisms from RT the genomes of multiple Campylobacter species."; RL PLoS Biol. 3:72-85(2005). 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; Evidence={ECO:0000255|HAMAP- CC 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000025; AAW35710.1; -; Genomic_DNA. DR RefSeq; WP_002908583.1; NC_003912.7. DR AlphaFoldDB; Q5HTK8; -. DR SMR; Q5HTK8; -. DR KEGG; cjr:CJE1390; -. DR HOGENOM; CLU_004217_2_2_7; -. 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 CDD; cd02393; KH-I_PNPase; 1. DR CDD; cd11364; RNase_PH_PNPase_2; 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; IPR020568; Ribosomal_Su5_D2-typ_SF. DR InterPro; IPR003029; S1_domain. 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; 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; RNA-binding; KW Transferase. FT CHAIN 1..719 FT /note="Polyribonucleotide nucleotidyltransferase" FT /id="PRO_0000329572" FT DOMAIN 573..633 FT /note="KH" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595" FT DOMAIN 658..719 FT /note="S1 motif" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595" FT BINDING 507 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595" FT BINDING 513 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595" SQ SEQUENCE 719 AA; 79018 MW; E9EA95891AAE6FEB CRC64; MQYSIEINKN TEIFNIDKVA KQAAGAVLMR QGKSVVLATV AREEKQVEED FLPLTVQYIE KAYAAGKIPG GYVKRETKPS DAETLTARII DRSLRPLFPK GYAYPTQIVV MVLSADPKVD LQVMSLNAAS VALYLSDIPM KAPVCGVRIG KIDGNFILNP NNEELQNSTL DLYVAGVKDE LLMIEMRALP DQKENEIFIE APYADVLTQT TSQNMNELSE DEILEALNLA QKAILNGSNA YEEAFSKHKK NSQIELKNEI EYPEILAFIE NNFQKQIKEA INQMAKSERA SELNKIAKEI SNLEIAKEWS EESVLNTLAK VKRKLIRGQI LNEGKRADGR SLNEVRPISI ETNILPNAHG SCLFTRGQTQ ALVVATLGGE NDAQMIDLLT EKNPISERFM VNYNFPGFSV GEASPIKAPG RRELGHGNLA KRALYPSVDE NYPYVIRLVS EILESNGSSS MATVCGGSLA LKAAGVPSLK LVAGVAMGLI FEDNKYAVLT DIMGLEDHDG DMDFKVAGSK DGVTALQMDI KLGGIDQETL KQALYQAKEG RIHILNIMEE AAKEIIVNEE VLPKLELFSV DPSKIVDIIG QAGKTIKEIV EKFGVSIDLD REKGEVKIAG SQNEQIKAAK DYIINITSSQ KGTKKGSKDK DISGFELGQE FQGIVKKIAP FGAFVELKNG VDGLLHSSKS KHLNLSENQS LKVKISEIKN GKISVDLCE //