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ID PNP_RHOPS Reviewed; 722 AA.
AC Q13EM2;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 08-MAY-2019, entry version 79.
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};
GN OrderedLocusNames=RPD_0227;
OS Rhodopseudomonas palustris (strain BisB5).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC Bradyrhizobiaceae; Rhodopseudomonas.
OX NCBI_TaxID=316057;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BisB5;
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.,
RA Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Pelletier D.A., Kyrpides N.,
RA Lykidis A., Oda Y., Harwood C.S., Richardson P.;
RT "Complete sequence of Rhodopseudomonas palustris BisB5.";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in mRNA degradation. Catalyzes the
CC phosphorolysis of single-stranded polyribonucleotides processively
CC in the 3'- to 5'-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:11128, Rhea:RHEA-
CC COMP:11129, ChEBI:CHEBI:43474, ChEBI:CHEBI:57930,
CC ChEBI:CHEBI:83400; EC=2.7.7.8; Evidence={ECO:0000255|HAMAP-
CC 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
CC nucleotidyltransferase family. {ECO:0000255|HAMAP-Rule:MF_01595}.
DR EMBL; CP000283; ABE37467.1; -; Genomic_DNA.
DR RefSeq; WP_011500657.1; NC_007958.1.
DR SMR; Q13EM2; -.
DR STRING; 316057.RPD_0227; -.
DR EnsemblBacteria; ABE37467; ABE37467; RPD_0227.
DR KEGG; rpd:RPD_0227; -.
DR eggNOG; ENOG4105C62; Bacteria.
DR eggNOG; COG1185; LUCA.
DR HOGENOM; HOG000218327; -.
DR KO; K00962; -.
DR OMA; RYMHNYN; -.
DR OrthoDB; 122725at2; -.
DR BioCyc; RPAL316057:RPD_RS01150-MONOMER; -.
DR Proteomes; UP000001818; 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; 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;
DR PRODOM; Q13EM2.
DR SWISS-2DPAGE; Q13EM2.
KW Complete proteome; Cytoplasm; Magnesium; Metal-binding;
KW Nucleotidyltransferase; RNA-binding; Transferase.
FT CHAIN 1 722 Polyribonucleotide
FT nucleotidyltransferase.
FT /FTId=PRO_0000329812.
FT DOMAIN 554 613 KH. {ECO:0000255|HAMAP-Rule:MF_01595}.
FT DOMAIN 623 691 S1 motif. {ECO:0000255|HAMAP-
FT Rule:MF_01595}.
FT METAL 487 487 Magnesium. {ECO:0000255|HAMAP-
FT Rule:MF_01595}.
FT METAL 493 493 Magnesium. {ECO:0000255|HAMAP-
FT Rule:MF_01595}.
SQ SEQUENCE 722 AA; 78316 MW; 0C84CEAFB2BF2B00 CRC64;
MFNKHSVEID WGGRPLRLET GKVARQADGA VVATYGETVV LATVVAAKTP REGVDFLPLT
VDYQEKTYAA GRIPGGYFKR EGRPTEKETL VSRLIDRPIR PLFADGWRNE TQVIVTVLSH
DMENDPDILA LVASSAALTL SGAPFKGPIG AARVGFINDE YVLNPVLDEM PETQLDLVVA
GTSDAVLMVE SEAKELSEEI MLGAVMFGHR HFQPVIDAII ALAEKAAKEP RELTVIDDSA
IEKEMLGLVE QELRAAYAIA VKQERYAAVG KVKEKAIAHF FPEGQEPKYD KLRIAGVFKE
LEAKIVRWNI LDTGKRIDGR DSKTVRSIIA EAGVLPRAHG SALFTRGETQ ALVVTTLGTG
EDEQYVDSLA GTYKETFLLH YNFPPYSVGE TGRLGGTKRR EIGHGKLAWR AIRPVLPPHH
EFPYTIRVVS EITESNGSSS MASVCGASLA LMDAGVPLKR PTAGIAMGLI LEGERFAVLS
DILGDEDHLG DMDFKVAGTE QGVTSLQMDI KIAGITEEIM KVALGQAKDG RIHILGEMSK
ALDRARAELG EHAPRIETFK IPTDKIREVI GTGGKVIREI VEKTGAKVNI EDDGTVKVAS
SDGESIKAAI KWIKSIASDP EVGEIYEGTV VKVMEFGAFV NFFGAKDGLV HISQLAAGRV
QKTSDVVKEG DKVKVKLLGF DDRGKTRLSM KVVDQDTGED LEAKQKAEAK AEDEAPAQAA
GE
//
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