(data stored in ACNUC7421 zone)

SWISSPROT: PNP_EDWI9

ID   PNP_EDWI9               Reviewed;         707 AA.
AC   C5BFC1;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   07-JUN-2017, entry version 54.
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=NT01EI_0472;
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146;
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT   "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
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: RNA(n+1) + phosphate = RNA(n) + a nucleoside
CC       diphosphate. {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   -!- 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; CP001600; ACR67707.1; -; Genomic_DNA.
DR   RefSeq; WP_015869908.1; NC_012779.2.
DR   ProteinModelPortal; C5BFC1; -.
DR   SMR; C5BFC1; -.
DR   STRING; 634503.NT01EI_0472; -.
DR   PRIDE; C5BFC1; -.
DR   EnsemblBacteria; ACR67707; ACR67707; NT01EI_0472.
DR   GeneID; 7961294; -.
DR   KEGG; eic:NT01EI_0472; -.
DR   PATRIC; fig|634503.3.peg.428; -.
DR   eggNOG; ENOG4105C62; Bacteria.
DR   eggNOG; COG1185; LUCA.
DR   HOGENOM; HOG000218327; -.
DR   KO; K00962; -.
DR   OMA; RYMHNYN; -.
DR   OrthoDB; POG091H00M0; -.
DR   Proteomes; UP000001485; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000175; F:3'-5'-exoribonuclease activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004654; F:polyribonucleotide nucleotidyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006402; P:mRNA catabolic process; IEA:InterPro.
DR   GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR   Gene3D; 1.10.10.400; -; 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; IPR004087; KH_dom.
DR   InterPro; IPR004088; KH_dom_type_1.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR012162; PNPase.
DR   InterPro; IPR027408; PNPase/RNase_PH_dom.
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; 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;
DR   PRODOM; C5BFC1.
DR   SWISS-2DPAGE; C5BFC1.
KW   Complete proteome; Cytoplasm; Magnesium; Metal-binding;
KW   Nucleotidyltransferase; Reference proteome; RNA-binding; Transferase.
FT   CHAIN         1    707       Polyribonucleotide
FT                                nucleotidyltransferase.
FT                                /FTId=PRO_1000215658.
FT   DOMAIN      553    612       KH. {ECO:0000255|HAMAP-Rule:MF_01595}.
FT   DOMAIN      622    690       S1 motif. {ECO:0000255|HAMAP-
FT                                Rule:MF_01595}.
FT   METAL       486    486       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_01595}.
FT   METAL       492    492       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_01595}.
SQ   SEQUENCE   707 AA;  76491 MW;  405B2BEEEFC93597 CRC64;
     MLTPTVRKFQ YGQHTVTLET GMMARQATAA VMVTMDDTAV FVTVVGAKKA REGQDFFPLT
     VNYQERAYAA GRFPGGFFRR EGRPGEGETL TARLIDRPIR PLFPEGFLNE VQVVATVVSV
     NPQVSPDIVA MIGASAALSL SGIPFNGPIG AARVGYINDQ YVLNPTQDEL KQSRLDLVVA
     GTDNAVLMVE SEADLLSEDQ MLGAVVFGHE QQQIVIENIK ALAAEVGKPR WEWHAPEVNV
     ALQRRVAEMA EARLGEAYHI TEKQARYAKV DEIKESVIAD LLAEDDALDA GEISDILGAL
     EKAVVRGRVL RGEPRIDGRE KDMIRALDVR TGVLPRTHGS ALFTRGETQA LVTATLGTER
     DAQNIDELMG ERTDRFLLHY NFPPYSVGET GMMGSPKRRE IGHGRLAKRG VLAVMPSQDA
     FPYTVRVVSE ITESNGSSSM ASVCGASLAL MDAGVPIKAA VAGIAMGLVK EQDNFVVLSD
     ILGDEDHLGD MDFKVAGSRD GVTALQMDIK IEGITREIMQ VALNQAKGAR LHILGVMEQA
     INAPRGDISE FAPRIHTIKI NPEKIKDVIG KGGSVIRALT EETGTTIEIE DDGTVKIAAT
     DGDKAKHAIR RIEEITAEIE VGRIYQGKVT RIVDFGAFVA IGGGKEGLVH ISQIADKRVE
     KVTDYLQMGQ EVAVKVLEVD RQGRVRLSIK EANASAAAGQ DAPTDAE
//

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