PNP_WOLPM
ID PNP_WOLPM Reviewed; 757 AA.
AC Q73GN4;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 112.
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=WD_0906;
OS Wolbachia pipientis wMel.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Wolbachieae; Wolbachia; unclassified Wolbachia.
OX NCBI_TaxID=163164;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15024419; DOI=10.1371/journal.pbio.0020069;
RA Wu M., Sun L.V., Vamathevan J.J., Riegler M., DeBoy R.T., Brownlie J.C.,
RA McGraw E.A., Martin W., Esser C., Ahmadinejad N., Wiegand C., Madupu R.,
RA Beanan M.J., Brinkac L.M., Daugherty S.C., Durkin A.S., Kolonay J.F.,
RA Nelson W.C., Mohamoud Y., Lee P., Berry K.J., Young M.B., Utterback T.R.,
RA Weidman J.F., Nierman W.C., Paulsen I.T., Nelson K.E., Tettelin H.,
RA O'Neill S.L., Eisen J.A.;
RT "Phylogenomics of the reproductive parasite Wolbachia pipientis wMel: a
RT streamlined genome overrun by mobile genetic elements.";
RL PLoS Biol. 2:327-341(2004).
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; AE017196; AAS14582.1; -; Genomic_DNA.
DR RefSeq; WP_010962918.1; NC_002978.6.
DR AlphaFoldDB; Q73GN4; -.
DR SMR; Q73GN4; -.
DR STRING; 163164.WD_0906; -.
DR EnsemblBacteria; AAS14582; AAS14582; WD_0906.
DR GeneID; 29555234; -.
DR KEGG; wol:WD_0906; -.
DR eggNOG; COG1185; Bacteria.
DR OMA; LHILDVM; -.
DR OrthoDB; 122725at2; -.
DR Proteomes; UP000008215; 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; 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..757
FT /note="Polyribonucleotide nucleotidyltransferase"
FT /id="PRO_0000329935"
FT DOMAIN 549..608
FT /note="KH"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
FT DOMAIN 618..686
FT /note="S1 motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
FT REGION 698..757
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 698..712
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 742..757
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 482
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
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"
SQ SEQUENCE 757 AA; 84015 MW; 5855FA395748B918 CRC64;
MFKIIKKSIE WGGRALSLET GKIARQAHGS VVVNYGDTSV LVTVVRKKKE ESVDFLPLNV
QFIAKSYAMG KIPGGFFKRE GKPSDRETLI SRVIDRSIRP LFPEGFHDEI SVVCNLLTYD
TVNPPEVPAL IGAVAALAIS GVPFHFTIAG VMVGCDENNN YILNPSVQEM KASSLDLFLS
GDENSILMVE SEVKELSEEN VFNAIKFGHE HLKPVIKLIK EFADTIGNKP ESFAPIDASD
ITQELEKYGK DFEKAYSQTV KQERVQALEA IRENILNTLK ETGKDEKLIT YAVKNFERSL
VREIIRKKSV RIDGRKHDEI RQIEVEVDIL SKTHGSALFT RGNTQALVVT ALGTTQDEQI
VDDIEGDRRE HFMLHYNFPS FAVGETSAAR APGRREIGHG KLAWKAIHPV LPDKSEFPYT
IRVVSEILES DGSSSMATVC GTSLALMDTG VPIKAPVAGI AMGLIKDKDE YVILSDILGD
EDYLGDMDFK VAGTSEGVTA LQMDMKISGI SFEIVEKSLE QAKAGRLHIL EKMNAVISEH
SDDVKDHAPR MLSFYIDKDK ISAAIGSKGK NIRSVCERSN AKIEIGDDGK VSVFATSGTE
AEIAKSMMID SITELEQGSI VDVKVVRIEK SIVELEFLNG RKGKMHISEV ANEHIDSIES
VLKQDDTFKA LVIDFEKGGC PKLSRRRVDQ ETGEFFEGEL YNEERKDGPN DRDNYYNNSF
SRKPGGSHHK RPPRPHSGFS NRNRPKFGNN DSSSGFY
