PNP_AQUAE
ID PNP_AQUAE Reviewed; 775 AA.
AC O66593;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 117.
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=aq_221;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
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; AE000657; AAC06562.1; -; Genomic_DNA.
DR PIR; E70320; E70320.
DR RefSeq; NP_213153.1; NC_000918.1.
DR RefSeq; WP_010880091.1; NC_000918.1.
DR AlphaFoldDB; O66593; -.
DR SMR; O66593; -.
DR STRING; 224324.aq_221; -.
DR EnsemblBacteria; AAC06562; AAC06562; aq_221.
DR KEGG; aae:aq_221; -.
DR PATRIC; fig|224324.8.peg.184; -.
DR eggNOG; COG1185; Bacteria.
DR HOGENOM; CLU_004217_2_2_0; -.
DR InParanoid; O66593; -.
DR OMA; LHILDVM; -.
DR OrthoDB; 122725at2; -.
DR Proteomes; UP000000798; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0000175; F:3'-5'-exoribonuclease activity; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004654; F:polyribonucleotide nucleotidyltransferase activity; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006402; P:mRNA catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006401; P:RNA catabolic process; IBA:GO_Central.
DR GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR Gene3D; 2.40.50.140; -; 2.
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; 2.
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; 2.
DR PIRSF; PIRSF005499; PNPase; 1.
DR SMART; SM00322; KH; 1.
DR SMART; SM00316; S1; 2.
DR SUPFAM; SSF46915; SSF46915; 1.
DR SUPFAM; SSF50249; SSF50249; 2.
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; 2.
PE 3: Inferred from homology;
KW Cytoplasm; Magnesium; Metal-binding; Nucleotidyltransferase;
KW Reference proteome; Repeat; RNA-binding; Transferase.
FT CHAIN 1..775
FT /note="Polyribonucleotide nucleotidyltransferase"
FT /id="PRO_0000329502"
FT DOMAIN 554..613
FT /note="KH"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
FT DOMAIN 623..693
FT /note="S1 motif 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
FT DOMAIN 707..775
FT /note="S1 motif 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
FT BINDING 487
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
FT BINDING 493
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
SQ SEQUENCE 775 AA; 86489 MW; 391F3B28E2AF3E67 CRC64;
MSVEEKARIG NSEEPIIIET GKYAKLTDGS VVVRQGGTAV LVTAVMSDEP ITDVDFTPLA
VDYRERASAY GRIPGGFTKR EGKPTDREIL VSRVIDRPIR PLFPEGFFHD VIITALTLSA
DDKYDPDVLA ITGASAALHI SRIPFEGPIA GVRVCRVNGE FVANPTYEQR KEADLDIVMA
GTKDAIVMVE GGGKEIPEEV LADALFFGLD AIKEVIEAQE RLREKVGKPK FEYQKVELPE
DILKALEEEC TPKILEAFNI KDKKERYSTL DKIVEEFIEA HQIPEELHFA VKYFYKKLES
RLMREKVLKE GVRIDGRKPN EIRPIWIEVH PFERPHGNAI FTRGQTQAYV TVTLGTPDEA
LIIETIAEGE VFKRFMLHYS MPPFSVGEAK PWGPPRRREI GHGALAERAI EPLLPPEEEY
PFIIRVVSDI LESNGSTSMA TVCGASLALF DAGVPMKDNK HVAGIAMGLI LEKDRYVILS
DILGDEDHLG DMDFKVAGTK DGITSVQMDI KVKGITKEIM LDALKQAREG RLYILEKMYE
AIPEPRKEPH PYTPKVEVVD VPEEKAPLII GPGGSTVKKI YDETGVKVWV GEQGKVYLFV
FPGGDVEKAK QMIQDIVREV EVGAVYKGTI TRVEPYGVFV ELWPGKIGLL HVSKMAEPVR
SATEKYKVGE EIIVKVLDLD ELGRPRFTTI GIEDVGTEKK EVKPKVGDVY EGKVVRVEPY
GAFIEYAPGK VGLLHVSKMK ERVKDARQKY KVGDVVKVKV VEIDEQGRPK FTDDV
