PNP_PELTS
ID PNP_PELTS Reviewed; 734 AA.
AC A5D2S6;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 85.
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=PTH_1275;
OS Pelotomaculum thermopropionicum (strain DSM 13744 / JCM 10971 / SI).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Desulfotomaculaceae;
OC Pelotomaculum.
OX NCBI_TaxID=370438;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13744 / JCM 10971 / SI;
RX PubMed=18218977; DOI=10.1101/gr.7136508;
RA Kosaka T., Kato S., Shimoyama T., Ishii S., Abe T., Watanabe K.;
RT "The genome of Pelotomaculum thermopropionicum reveals niche-associated
RT evolution in anaerobic microbiota.";
RL Genome Res. 18:442-448(2008).
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}.
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; AP009389; BAF59456.1; -; Genomic_DNA.
DR AlphaFoldDB; A5D2S6; -.
DR SMR; A5D2S6; -.
DR STRING; 370438.PTH_1275; -.
DR EnsemblBacteria; BAF59456; BAF59456; PTH_1275.
DR KEGG; pth:PTH_1275; -.
DR eggNOG; COG1185; Bacteria.
DR HOGENOM; CLU_004217_2_2_9; -.
DR OMA; LHILDVM; -.
DR Proteomes; UP000006556; 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; 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_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; 2.
DR Pfam; PF00575; S1; 1.
DR PIRSF; PIRSF005499; PNPase; 1.
DR SMART; SM00322; KH; 1.
DR SMART; SM00316; S1; 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..734
FT /note="Polyribonucleotide nucleotidyltransferase"
FT /id="PRO_0000329755"
FT DOMAIN 564..623
FT /note="KH"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
FT DOMAIN 633..707
FT /note="S1 motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
FT REGION 700..734
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 718..734
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 497
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
FT BINDING 503
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
SQ SEQUENCE 734 AA; 80315 MW; 2BFC34A2A6CA8297 CRC64;
MADRSILTRE IIVGGRPMIL ETGRLANQAS GAVFVRYGDT AVLVTATVAP TVRAGIDFFP
LTVDYEERFY AVGKIPGGFI KRESRPSEKA ILSGRLIDRP IRPLFPKEMR NEVQVIATIL
SVDQDNAPEI AAMVGASAAL HISEIPLKFP IGGVIVGRVD GRFVINPVLA QAEKSDMHLV
VAGTKDAVMM VEAGAKEVPE EVILEAISFG HETVKEIVAF IERYREEALE MGLAKEKMVI
EVAEPDPVLV EAVTGPATEK LDGVLRRCVN ERLSKQERDS LLNNIKDELM QKFLADYPEQ
ESLIKDLLDS IEKKLVRRMI TEEGLRIDGR ALNEVRPISV EVGVLPRPHG SGLFTRGQTQ
ILSVVTLGTV SEEQILDGLG VEESKRFMHH YNFPPYSTGE TRPLRSPGRR EIGHGALAER
ALAAVIPGEE EFPYTIRIVS EALESNGSTS MGSVCGSTLA LMDAGVPISA PVAGVAMGLI
KEGDNFTVLT DIQGFEDHLG DMDFKVAGTA KGITALQMDI KIPGITREVF EKALAQAYEG
RMHILNKMLE VLPAPRPELS PHAPRIIHIT IDPDKIRDVI GPGGKVIKKI VEETGAEIDI
EDDGRVFIAA VDQEKGRKAQ EIIETLTKEV QTGEIYTGRV TRITDFGCFV EIIPGVLGMQ
GKEGLVHISQ LAHHRVNRVE DVVKEGDVIL VKVTGYDSQG RLKLSKKEAT PPPESTAMKE
GRAHRPSRRR ESAR
