PNP_PORGI
ID PNP_PORGI Reviewed; 743 AA.
AC Q7MW79;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 104.
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=PG_0766;
OS Porphyromonas gingivalis (strain ATCC BAA-308 / W83).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=242619;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-308 / W83;
RX PubMed=12949112; DOI=10.1128/jb.185.18.5591-5601.2003;
RA Nelson K.E., Fleischmann R.D., DeBoy R.T., Paulsen I.T., Fouts D.E.,
RA Eisen J.A., Daugherty S.C., Dodson R.J., Durkin A.S., Gwinn M.L.,
RA Haft D.H., Kolonay J.F., Nelson W.C., Mason T.M., Tallon L., Gray J.,
RA Granger D., Tettelin H., Dong H., Galvin J.L., Duncan M.J., Dewhirst F.E.,
RA Fraser C.M.;
RT "Complete genome sequence of the oral pathogenic bacterium Porphyromonas
RT gingivalis strain W83.";
RL J. Bacteriol. 185:5591-5601(2003).
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; AE015924; AAQ65927.1; -; Genomic_DNA.
DR RefSeq; WP_004585303.1; NC_002950.2.
DR AlphaFoldDB; Q7MW79; -.
DR SMR; Q7MW79; -.
DR STRING; 242619.PG_0766; -.
DR DNASU; 2552025; -.
DR EnsemblBacteria; AAQ65927; AAQ65927; PG_0766.
DR KEGG; pgi:PG_0766; -.
DR eggNOG; COG1185; Bacteria.
DR HOGENOM; CLU_004217_2_2_10; -.
DR OMA; LHILDVM; -.
DR OrthoDB; 122725at2; -.
DR Proteomes; UP000000588; 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;
KW Reference proteome; RNA-binding; Transferase.
FT CHAIN 1..743
FT /note="Polyribonucleotide nucleotidyltransferase"
FT /id="PRO_0000329762"
FT DOMAIN 556..618
FT /note="KH"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
FT DOMAIN 628..698
FT /note="S1 motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
FT REGION 704..743
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 489
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
FT BINDING 495
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
SQ SEQUENCE 743 AA; 82258 MW; A7E47E1F8FDEB855 CRC64;
MLNVVSKTID LGDGRSIKIE TGKLAKQADG AVTVTMGNTV LLATVCAAKD ANPGCDFMPL
QVEYKEKYSA IGRFPGGFTR REGKASDYEI LTCRLVDRAL RPLFPDNYHA EVFVNVILFS
ADGEDMPDAL AGLAASAALA VSDIPFNGPI SEVRVARVDG RYIVNPTFEQ LERADIDLMV
GATMDNIMMV EGEMDEVQES EMLEGIRVAH EAIKVQCKAQ LELSEAVGKL QKREYSHEVN
DEDLRKKVHD ECYARAYEVA TSGTGKHERG EAFEKIVEEF KAQYTEEELA EKAEMIARYY
HDVEKEAMRR AILDEGKRLD GRKTTEIRPI WIETDCLPGP HGSAIFTRGE TQSLTTVTLG
TKSDEKLVDD VLNYTKERFL LHYNFPPFST GEARPQRGVG RREIGHGNLA HRALKRMIPT
DYPYVVRVIS DILESNGSSS MATVCAGTLA LRDAGVQIRK PVSGIAMGLI SENQGKNYAI
LSDILGDEDH LGDMDFKVTG TKDGITATQM DIKVDGLSYE ILENALEQAK QGRLHILGKI
MEAQPETRDD LKPHAPRIEK MHIGKEFIGA VIGPGGKIIQ GIQEKSGATV NIEEVDGMGV
IEISGTNKPC IDAAIGMIKG IVAMPEVGET YPGKITSVMP YGCFVEFLPG KEGLLHISEV
DWKRFETIED TNLKEGESIN VKLLDIDPKT GKFKLSRKVL LEKPEGYVEP QPRERRERRE
GGREGGRNFE RRGGDRDHRE PRG
