PNP_PSEMY
ID PNP_PSEMY Reviewed; 702 AA.
AC A4XYD6;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 2.
DT 03-AUG-2022, entry version 84.
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=Pmen_3604;
OS Pseudomonas mendocina (strain ymp).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=399739;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ymp;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Kiss H., Brettin T., Detter J.C., Bruce D., Han C.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Hersman L., Dubois J., Maurice P., Richardson P.;
RT "Complete sequence of Pseudomonas mendocina ymp.";
RL Submitted (APR-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=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 -!- SUBUNIT: Component of the RNA degradosome, which is a multiprotein
CC complex involved in RNA processing and mRNA degradation.
CC {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 -!- SEQUENCE CAUTION:
CC Sequence=ABP86352.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000680; ABP86352.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_003240580.1; NC_009439.1.
DR AlphaFoldDB; A4XYD6; -.
DR SMR; A4XYD6; -.
DR STRING; 399739.Pmen_3604; -.
DR PRIDE; A4XYD6; -.
DR EnsemblBacteria; ABP86352; ABP86352; Pmen_3604.
DR KEGG; pmy:Pmen_3604; -.
DR PATRIC; fig|399739.8.peg.3653; -.
DR eggNOG; COG1185; Bacteria.
DR HOGENOM; CLU_004217_2_2_6; -.
DR OrthoDB; 122725at2; -.
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; RNA-binding;
KW Transferase.
FT CHAIN 1..702
FT /note="Polyribonucleotide nucleotidyltransferase"
FT /id="PRO_0000329783"
FT DOMAIN 555..614
FT /note="KH"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
FT DOMAIN 624..692
FT /note="S1 motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
FT BINDING 488
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
FT BINDING 494
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
SQ SEQUENCE 702 AA; 75496 MW; 50649D1BE23BCD37 CRC64;
MNPVIKQFKF GQSTVTLETG RIARQASGAV LVTVDNDVTV LVTVVGAKTA DPSKGFFPLS
VHYQEKTYAA GKIPGGFFKR EGRPSEKETL TSRLIDRPIR PLFPEGFMNE VQVVCTVVST
SKKTDPDIAS MIGTSAALAV SGIPFNGPIG AARVAFHPDT GYLLNPNYEQ LKASSLDMVV
AGTETAVLMV ESEADELTED QMLGAVLFAH QEFQAVIQAV KEFAAEAGKP TWNWQAPAAN
TPLLDAIRSQ FGEAISQAYT ITIKQDRYNR LDELREQVIA ALAGEGEGKF AADEVKAAFG
EIEYRTVRQN IVDGKPRIDG RDTRTVRPLK IEVGVLDKTH GSALFTRGET QALVVATLGT
ARDAQLLDTL EGEKKDPFML HYNFPPFSVG ECGRMGGAGR REIGHGRLAR RGVAAMLPKD
DEFPYTIRVV SEITESNGSS SMASVCGASL ALMDAGVPMK APVAGIAMGL VLEGEKFAVL
TDILGDEDHL GDMDFKVAGT AKGVTALQMD IKIQGITEEI MEQALEQALE ARLNILGQMN
QVISQSRTEL SANAPTMLAM KIDQDKIRDV IGKGGATIRA ICEETKASID IEDDGSIKIF
GETKDAAEAA KQRVLAITAE AEIGKIYVGK VERIVDFGAF VNILPGKDGL VHISMLSDQR
VEKVTDVLKE GQEVKVLVLD VDNRGRIKLS IKDVAAAEAS GV
