ID   PNP_ALHEH               Reviewed;         698 AA.
AC   Q0A7A1;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 2.
DT   16-JUN-2009, entry version 19.
DE   RecName: Full=Polyribonucleotide nucleotidyltransferase;
DE            EC=2.7.7.8;
DE   AltName: Full=Polynucleotide phosphorylase;
DE            Short=PNPase;
GN   Name=pnp; OrderedLocusNames=Mlg_1944;
OS   Alkalilimnicola ehrlichei (strain MLHE-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Alkalilimnicola.
OX   NCBI_TaxID=187272;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Sims D., Brettin T., Bruce D., Han C., Tapia R., Gilna P.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Oremland R.S., Hoeft S.E., Switzer-Blum J., Kulp T.,
RA   King G., Tabita R., Witte B., Santini J.M., Basu P., Hollibaugh J.T.,
RA   Xie G., Stolz J.F., Richardson P.;
RT   "Complete sequence of Alkalilimnicola ehrilichei MLHE-1.";
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in mRNA degradation. Hydrolyzes single-stranded
CC       polyribonucleotides processively in the 3'- to 5'-direction (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: RNA(n+1) + phosphate = RNA(n) + a nucleoside
CC       diphosphate.
CC   -!- SUBUNIT: Homotrimer. Organized into a structure (processome or RNA
CC       degradosome) containing a number of RNA-processing enzymes (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the polyribonucleotide
CC       nucleotidyltransferase family.
CC   -!- SIMILARITY: Contains 1 KH domain.
CC   -!- SIMILARITY: Contains 1 S1 motif domain.
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DR   EMBL; CP000453; ABI57286.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; YP_742776.1; -.
DR   GeneID; 4268112; -.
DR   GenomeReviews; CP000453_GR; Mlg_1944.
DR   KEGG; aeh:Mlg_1944; -.
DR   NMPDR; fig|187272.6.peg.1852; -.
DR   HOGENOM; Q0A7A1; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000175; F:3'-5'-exoribonuclease activity; IEA:InterPro.
DR   GO; GO:0004654; F:polyribonucleotide nucleotidyltransferase a...; IEA:HAMAP.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006402; P:mRNA catabolic process; IEA:HAMAP.
DR   GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR   HAMAP; MF_01595; -; 1.
DR   InterPro; IPR001247; ExoRNase_PH_dom1.
DR   InterPro; IPR015847; ExoRNase_PH_dom2.
DR   InterPro; IPR004087; KH.
DR   InterPro; IPR004088; KH_type_1.
DR   InterPro; IPR018111; KH_type_1_subgr.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR012162; PNPase.
DR   InterPro; IPR015848; PNPase_PH_RNA-bd_bac/org-type.
DR   InterPro; IPR003029; Rbsml_prot_S1_RNA-bd_dom.
DR   Gene3D; G3DSA:2.40.50.140; OB_NA_bd_sub; 1.
DR   Gene3D; G3DSA:1.10.10.400; PNPase_PH_RNA-bd_bac/org-type; 1.
DR   PANTHER; PTHR11252; PNPase; 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   SMART; SM00322; KH; 1.
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; Nucleotidyltransferase; RNA-binding;
KW   Transferase.
FT   CHAIN         1    698       Polyribonucleotide
FT                                nucleotidyltransferase.
FT                                /FTId=PRO_0000329490.
FT   DOMAIN      555    614       KH.
FT   DOMAIN      624    692       S1 motif.
SQ   SEQUENCE   698 AA;  75642 MW;  E0A4CEEC4D99642F CRC64;
     MKSVKKSFQY GNHTVTLETG GVARQADGAV LVNMSDTVVL VTAVGRKEAD PGKGFFPLTV
     NYQERTYAAG KIPGGFFKRE GRPSEKETLT CRLIDRPIRP LFPEGFYNEV QVVATVLSMN
     PEVDADIPAL IGASAALSIS GIPFDGPIGA ARVGYKDGEY LLNPTFEETA ASDLDLVVAG
     TENAVLMVES EANQLPEEAM LGAVLYGHEQ MQVAIQAINE LTAEAGKPRW DWHPPQGDAA
     LETAIKDLVG DDLAAAYQIP EKQERQNRIG ELRQRAVEAL GENREEEGGW PEKDVGDAFK
     GLEKDIVRGR ILAGERRIDG RDTRTVRPID IEVGSLPRTH GSAIFTRGET QAVVVTTLGT
     GRDAQIIDAI EGERKEQFML HYNFPPYCVG ETGFMGTPKR REIGHGKLAK RGIEAVMPAA
     DDCPYVIRVV SEITESNGSS SMATVCGTSL SLMDAGVPVK APVAGIAMGL IKEDEQFAVL
     SDILGDEDHL GDMDFKVAGT ESGVTALQMD IKIQGITREI MEQALEQARE GRLHILGEMN
     NAISGPRSEM SEYAPRLLTI RIDPDKIRDV IGKGGATIRA LTEETGTTID ISDDGKVTIA
     SADKAAADEA RRRIELLTAD VEVGTVYEGK VSKLMDFGAF VNILPGRDGL VHISQISNER
     VERVGDYLKE GDTVRVKVLE VDRQGRIRLS MKAVQDGE
//