PNP_NOSS1
ID PNP_NOSS1 Reviewed; 718 AA.
AC Q8YP11;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 105.
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=all4396;
OS Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=103690;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT "Complete genomic sequence of the filamentous nitrogen-fixing
RT cyanobacterium Anabaena sp. strain PCC 7120.";
RL DNA Res. 8:205-213(2001).
RN [2]
RP PROTEIN SEQUENCE OF 50-64; 141-150 AND 255-267, INDUCTION, AND MASS
RP SPECTROMETRY.
RA Singh H., Rajaram H., Apte S.K.;
RL Submitted (DEC-2008) to UniProtKB.
RN [3]
RP SUBUNIT.
RC STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX PubMed=24563514; DOI=10.1261/rna.043513.113;
RA Zhang J.Y., Deng X.M., Li F.P., Wang L., Huang Q.Y., Zhang C.C., Chen W.L.;
RT "RNase E forms a complex with polynucleotide phosphorylase in cyanobacteria
RT via a cyanobacterial-specific nonapeptide in the noncatalytic region.";
RL RNA 20:568-579(2014).
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: May form homodimers or higher order multimers. Interacts with
CC RNase E (rne). {ECO:0000269|PubMed:24563514}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01595}.
CC -!- INDUCTION: Repressed by radiation. {ECO:0000269|Ref.2}.
CC -!- MASS SPECTROMETRY: Mass=78000; Mass_error=1; Method=MALDI;
CC Evidence={ECO:0000269|Ref.2};
CC -!- SIMILARITY: Belongs to the polyribonucleotide nucleotidyltransferase
CC family. {ECO:0000255|HAMAP-Rule:MF_01595}.
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DR EMBL; BA000019; BAB76095.1; -; Genomic_DNA.
DR PIR; AD2355; AD2355.
DR RefSeq; WP_010998533.1; NZ_RSCN01000051.1.
DR AlphaFoldDB; Q8YP11; -.
DR SMR; Q8YP11; -.
DR STRING; 103690.17133532; -.
DR EnsemblBacteria; BAB76095; BAB76095; BAB76095.
DR KEGG; ana:all4396; -.
DR eggNOG; COG1185; Bacteria.
DR OMA; LHILDVM; -.
DR OrthoDB; 122725at2; -.
DR BRENDA; 2.7.7.8; 4371.
DR Proteomes; UP000002483; 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; 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; 2.
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 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Magnesium; Metal-binding;
KW Nucleotidyltransferase; Reference proteome; RNA-binding; Transferase.
FT CHAIN 1..718
FT /note="Polyribonucleotide nucleotidyltransferase"
FT /id="PRO_0000329496"
FT DOMAIN 563..622
FT /note="KH"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
FT DOMAIN 632..700
FT /note="S1 motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
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 718 AA; 77790 MW; 45D4A2A03EE2D3BD CRC64;
MAEFEKSISF DGRDIRLKVG LLAPQAGGSV LIESGDTAVL VTATRSPGRE GIDFLPLTVD
YEERLYAAGR IPGGIMRREG RPPEKTILTS RLIDRPLRPL FPSWLRDDLQ VVALTMSMDE
QVPPDVLAVT GASIATLIAK IPFNGPMAAV RVGLVGDDFI INPTYAEIEA GDLDLVVAGS
PHGVIMVEAG ANQLPERDII EAIDFGYEAV RDLIKAQLDL VAELGLEIVQ EAPPEVDQTL
ENYIRDRASD EIKKILAQFE LTKPERDAAL DVVKDNIATA IAELPEEDPI RLAATANSKA
LGNTFKDITK YFMRRQIVED NVRVDGRKLD QVRPVSSQVG VLPKRVHGSG LFNRGLTQVL
SACTLGTPGD AQNLNDDLQT DQSKRYLHHY NFPPFSVGET KPLRAPGRRE IGHGALAERA
ILPVLPPKEQ FPYVIRVVSE VLSSNGSTSM GSVCGSTLAL MDAGVPILKP VSGAAMGLIK
EGDEVRVLTD IQGIEDFLGD MDFKVAGTDA GITALQMDMK ISGLSLEVIA QAIHQAKDAR
LHILDKMLQT IDQPRTETSP YAPRLLTIKI DPDMIGLVIG PGGKTIKGIT EETGAKIDIE
DDGTVTISAV DENKAKRARN IVQGMTRKLN EGDVYAGRVT RIIPIGAFVE FLPGKEGMIH
ISQLADYRVG KVEDEVAVGD EVIVKVREID NKGRINLTRL GIHPDQAAAA REAAAVNR
