PNP_PAEAT
ID PNP_PAEAT Reviewed; 750 AA.
AC A1R525;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 109.
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=AAur_1570;
OS Paenarthrobacter aurescens (strain TC1).
OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Paenarthrobacter.
OX NCBI_TaxID=290340;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TC1;
RX PubMed=17194220; DOI=10.1371/journal.pgen.0020214;
RA Mongodin E.F., Shapir N., Daugherty S.C., DeBoy R.T., Emerson J.B.,
RA Shvartzbeyn A., Radune D., Vamathevan J., Riggs F., Grinberg V.,
RA Khouri H.M., Wackett L.P., Nelson K.E., Sadowsky M.J.;
RT "Secrets of soil survival revealed by the genome sequence of Arthrobacter
RT aurescens TC1.";
RL PLoS Genet. 2:2094-2106(2006).
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}.
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DR EMBL; CP000474; ABM06299.1; -; Genomic_DNA.
DR RefSeq; WP_011774282.1; NC_008711.1.
DR AlphaFoldDB; A1R525; -.
DR SMR; A1R525; -.
DR STRING; 290340.AAur_1570; -.
DR PRIDE; A1R525; -.
DR EnsemblBacteria; ABM06299; ABM06299; AAur_1570.
DR KEGG; aau:AAur_1570; -.
DR eggNOG; COG1185; Bacteria.
DR HOGENOM; CLU_004217_2_2_11; -.
DR OMA; LHILDVM; -.
DR OrthoDB; 122725at2; -.
DR Proteomes; UP000000637; 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; IPR036345; ExoRNase_PH_dom2_sf.
DR InterPro; IPR014069; GPSI/PNP.
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; 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 TIGRFAMs; TIGR02696; pppGpp_PNP; 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..750
FT /note="Polyribonucleotide nucleotidyltransferase"
FT /id="PRO_0000329504"
FT DOMAIN 585..644
FT /note="KH"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
FT DOMAIN 656..728
FT /note="S1 motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
FT REGION 725..750
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 736..750
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 519
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
FT BINDING 525
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
SQ SEQUENCE 750 AA; 80381 MW; 8A05AD6ED26E8FEB CRC64;
MEGPEIQFSE AIIDNGRFGK RVIRFETGRL AKQAAGASMV YIDEDTALLS ATTAGKQPRE
GFDFFPLTVD VEERMYAAGR IPGSFFRREG RPSTEAILAC RLMDRPLRPA FVKGLRNEVQ
IVVTVLAINP DELYDVVAIN ASSMSTQLSG LPFSGPIGGV RVALIADEQG SQWVAFPKHS
QLENAVFNMV VAGRIAGDDV AIMMVEAEAT DNSWNLIKEQ GATAPTEEVV SEGLEAAKPF
IKALCEAQAD LAARAAKPTV EFPVFLDYQD DVYAAVEAAA ADKLAAVFQI ADKQDRDNAS
DELKDEVLGA LAGQFEGREK ELSAAFRSVT KHVVRQRILK DQVRIDGRGL TDIRQLTAEV
EVLPRVHGSA IFERGETQIM GVTTLNMLKM EQQIDSLSPV TRKRYMHNYN FPPYSTGETG
RVGSPKRREI GHGALAERAL VPVLPTREEF PYAIRQVSEA LGSNGSTSMG SVCASTLSML
NAGVPLKAAV AGIAMGLVSD QVDGQTRYAA LTDILGAEDA FGDMDFKVAG TSEFVTAIQL
DTKLDGIPAS VLAAALKQAR EARLHILEVI NAAIDTPDEL SEFAPRVIAV KIPVDKIGEV
IGPKGKMINQ IQEDTGADIS IEDDGTVYIG ATNGPSADAA RSAINAIANP QVPEIGERYL
GTVVKTTTFG AFVSLTPGKD GLLHISELRK LANGKRVDNV DDVVSVGQKV QVEITKIDDR
GKLSLSPVVA EEEGAASEDA PAEAAEESAE
