PNP_WOLPP
ID PNP_WOLPP Reviewed; 758 AA.
AC B3CM21;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 1.
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=WP0831;
OS Wolbachia pipientis subsp. Culex pipiens (strain wPip).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Wolbachieae; Wolbachia; unclassified Wolbachia.
OX NCBI_TaxID=570417;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=wPip;
RX PubMed=18550617; DOI=10.1093/molbev/msn133;
RA Klasson L., Walker T., Sebaihia M., Sanders M.J., Quail M.A., Lord A.,
RA Sanders S., Earl J., O'Neill S.L., Thomson N., Sinkins S.P., Parkhill J.;
RT "Genome evolution of Wolbachia strain wPip from the Culex pipiens group.";
RL Mol. Biol. Evol. 25:1877-1887(2008).
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; AM999887; CAQ54939.1; -; Genomic_DNA.
DR RefSeq; WP_012481924.1; NC_010981.1.
DR AlphaFoldDB; B3CM21; -.
DR SMR; B3CM21; -.
DR STRING; 570417.WP0831; -.
DR PRIDE; B3CM21; -.
DR EnsemblBacteria; CAQ54939; CAQ54939; WP0831.
DR KEGG; wpi:WP0831; -.
DR eggNOG; COG1185; Bacteria.
DR HOGENOM; CLU_004217_2_2_5; -.
DR OMA; LHILDVM; -.
DR Proteomes; UP000008814; 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..758
FT /note="Polyribonucleotide nucleotidyltransferase"
FT /id="PRO_1000192505"
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 707..758
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 733..758
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 758 AA; 84663 MW; 256402174A833358 CRC64;
MFEIIKKSID WEGRTLSLET GKIARQADGS VVVNYGDTSI LVTVVRKKKE ESVDFLPLNV
QFIAKSYAMG KIPGGFFKRE GKPSDRETLI SRVIDRSIRP LFPEGFHDEI SVVCNLLTYD
TVNSPEVPAL IGTVAALAIS GVPFHFTIAG VMVGCDENNN YILNPSVQEM KASNLDLFLS
GDENSILMVE SEVKELSEEN VLNAIKFGHE HLQPVIKLIK EFADTVGNKP ESFAPVDISD
ITQELEKYRK DFEEAYSKTV KQERVQALEV VRNNILNTLK EAGKDEKLIT YAVKSFERSL
VREMIRRKSV RIDSRKYDEI RQIEIEADIL PKTHGSALFT RGSTQALVVT ALGTTQDEQI
VDDIEGDRRE HFMLHYNFPP FAVGEASAIR APGRREIGHG KLAWKAIHPV LPDKSEFPYT
IRVVSEIMES DGSSSMATVC GTSIALMDTG VPIKAPVAGI AMGLIKDKNE HIILSDILGD
EDYLGDMDFK VAGTSEGITA LQMDMKIPGI SFEIVEKSLE QAKVGRLHIL EKMNAVISEH
RKDIKDHVPR VLSFYIDKDK ISAAIGTKGK NIRSVCERSN AKIEIGDDGK VSVFAISSTE
AEAAKNMMID SITELEQGSI IDAKVVKIEK SIVELELLNG RKGKMHISEV ANQHVESIED
ILKQGDTFKA LIIDFEKGGC PKLSRRRVDQ ETGEFFEGKL YNEERRDGLN NRDNYYNNSF
NKKPEDNYHS NRPTRPRSGF SNRSRPKFGN NDSSSGFY
