GenomeNet

Database: UniProt
Entry: PNP_PHOPR
LinkDB: PNP_PHOPR
Original site: PNP_PHOPR 
ID   PNP_PHOPR               Reviewed;         707 AA.
AC   Q6LUI8;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-MAY-2019, entry version 91.
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};
GN   OrderedLocusNames=PBPRA0616;
OS   Photobacterium profundum (strain SS9).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales;
OC   Vibrionaceae; Photobacterium.
OX   NCBI_TaxID=298386;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1253 / SS9;
RX   PubMed=15746425; DOI=10.1126/science.1103341;
RA   Vezzi A., Campanaro S., D'Angelo M., Simonato F., Vitulo N.,
RA   Lauro F.M., Cestaro A., Malacrida G., Simionati B., Cannata N.,
RA   Romualdi C., Bartlett D.H., Valle G.;
RT   "Life at depth: Photobacterium profundum genome sequence and
RT   expression analysis.";
RL   Science 307:1459-1461(2005).
CC   -!- FUNCTION: Involved in mRNA degradation. Catalyzes the
CC       phosphorolysis of single-stranded polyribonucleotides processively
CC       in the 3'- to 5'-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:11128, Rhea:RHEA-
CC         COMP:11129, ChEBI:CHEBI:43474, ChEBI:CHEBI:57930,
CC         ChEBI:CHEBI:83400; EC=2.7.7.8; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01595};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01595};
CC   -!- SUBUNIT: Component of the RNA degradosome, which is a multiprotein
CC       complex involved in RNA processing and mRNA degradation.
CC       {ECO:0000255|HAMAP-Rule:MF_01595}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01595}.
CC   -!- SIMILARITY: Belongs to the polyribonucleotide
CC       nucleotidyltransferase family. {ECO:0000255|HAMAP-Rule:MF_01595}.
DR   EMBL; CR378664; CAG19037.1; -; Genomic_DNA.
DR   RefSeq; WP_011217386.1; NC_006370.1.
DR   SMR; Q6LUI8; -.
DR   STRING; 298386.PBPRA0616; -.
DR   EnsemblBacteria; CAG19037; CAG19037; PBPRA0616.
DR   KEGG; ppr:PBPRA0616; -.
DR   eggNOG; ENOG4105C62; Bacteria.
DR   eggNOG; COG1185; LUCA.
DR   HOGENOM; HOG000218326; -.
DR   KO; K00962; -.
DR   OMA; RYMHNYN; -.
DR   OrthoDB; 122725at2; -.
DR   Proteomes; UP000000593; Chromosome 1.
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; 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; 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; 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   PROSITE; PS50084; KH_TYPE_1; 1.
DR   PROSITE; PS50126; S1; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; Magnesium; Metal-binding;
KW   Nucleotidyltransferase; Reference proteome; RNA-binding; Transferase.
FT   CHAIN         1    707       Polyribonucleotide
FT                                nucleotidyltransferase.
FT                                /FTId=PRO_0000329757.
FT   DOMAIN      552    611       KH. {ECO:0000255|HAMAP-Rule:MF_01595}.
FT   DOMAIN      621    689       S1 motif. {ECO:0000255|HAMAP-
FT                                Rule:MF_01595}.
FT   METAL       485    485       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_01595}.
FT   METAL       491    491       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_01595}.
SQ   SEQUENCE   707 AA;  76579 MW;  D605D1C0FC8D5ECB CRC64;
     MNPIVKTFQY GNHTVTLETG VMARQATAAV MASMDDTSVF VSVVGKKAAV EGQDFFPLTV
     NYQERTYAAG KIPGGFFKRE GRPSEGETLT ARLIDRPIRP LFPSAFKNEV QVIATVVSVN
     PEVNPDMITM IATSAALAIS GLPFNGPIGA ARVGFINDQF VLNPSNTELE ESRLDLVVSG
     TKDAVLMVES EADRLSEETM LQAVVYGHDQ QQVVINAINE FAAEVATPAW DWTAPVVNAE
     LKARVADKAA TRLSDAYQIT EKMARYDEVG SIKNDVVASL LAEDETLDER ELRGMLSSLE
     KHVVRGRIIA GHPRIDGREK DMVRALDVRT GVLPRTHGSS LFTRGETQAL VTATLGTQRD
     AQIIDSIMGE KKDHFLLHYN FPPYCVGETG FVGSPKRREI GHGKLAKRGI AAVMPSVEEF
     PYTVRVVSEI TESNGSSSMA SVCGTSLALM DAGVPIKASV AGIAMGLVKE GDDFVVLSDI
     LGDEDHLGDM DFKVAGTDDG ITALQMDIKI EGITKEIMQI ALNQAKGARK HILSVMDDAI
     GTHRDDISQF APRIHTMKIN SDKIKDVIGK GGAVIRALTE ETGTTIEIED DGTIKIAATE
     GAAAKEAIRR IEEITADVEV GRIYTGKVMR IVDFGAFVSV IGAKEGLVHI SQIAQERVEK
     VSDHLQMGQE VQVKVLEIDR QGRIRLSMKE AVADQNPATV QDEQPQG
//
DBGET integrated database retrieval system