ID   PNP_ACHLI               Reviewed;         715 AA.
AC   A9NGE2;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   16-JUN-2009, entry version 13.
DE   RecName: Full=Polyribonucleotide nucleotidyltransferase;
DE            EC=2.7.7.8;
DE   AltName: Full=Polynucleotide phosphorylase;
DE            Short=PNPase;
GN   Name=pnp; OrderedLocusNames=ACL_0808;
OS   Acholeplasma laidlawii (strain PG-8A).
OC   Bacteria; Tenericutes; Mollicutes; Acholeplasmatales;
OC   Acholeplasmataceae; Acholeplasma.
OX   NCBI_TaxID=441768;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Kovaleva G.Y., Kazanov M.D., Malko D.B., Vitreschak A.G.,
RA   Sernova N.V., Gelfand M.S., Lazarev V.N., Levitskii S.A.,
RA   Basovskii Y.I., Chukin M.M., Akopian T.A., Vereshchagin V.A.,
RA   Kostrjukova E.S., Selezneva O.V., Vtyurin N.N., Rogov S.I.,
RA   Alekseev D.G., Ladygina V.G., Titova G.A., Karpov V.A., Govorun V.M.;
RT   "Acholeplasma laidlawii complete genome.";
RL   Submitted (NOV-2007) 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; CP000896; ABX81422.1; -; Genomic_DNA.
DR   RefSeq; YP_001620798.1; -.
DR   GeneID; 5803780; -.
DR   GenomeReviews; CP000896_GR; ACL_0808.
DR   KEGG; acl:ACL_0808; -.
DR   OMA; A9NGE2; GHGNLAK.
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; 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   PIRSF; PIRSF005499; PNPase; 1.
DR   SMART; SM00322; KH; 1.
DR   TIGRFAMs; TIGR03591; Polynuc_phos; 1.
DR   PROSITE; PS50084; KH_TYPE_1; FALSE_NEG.
DR   PROSITE; PS50126; S1; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; Nucleotidyltransferase; RNA-binding;
KW   Transferase.
FT   CHAIN         1    715       Polyribonucleotide
FT                                nucleotidyltransferase.
FT                                /FTId=PRO_0000329476.
FT   DOMAIN      567    634       KH.
FT   DOMAIN      637    712       S1 motif.
SQ   SEQUENCE   715 AA;  78666 MW;  0A03C34B64B5E270 CRC64;
     MSKQVFETTL AGKPLRVEVG EIAKQANGAA MIYYGDTVVL STAVAKAKVG QTDFFPLMVI
     YAEKQYAAGK IPGGFFRREG RPSEVETLTS RLIDRPLRPL FDDGYRNEVQ VVNTVLSSDP
     EASSQMAAML GSSIALEISN IPFMGPIAGA HVGRIDGQFV LNPSSEQLNV SDIDLIVAGT
     KDAINMVEAG AKQVSEEVML EAILFGHEAI KELCAFQETI KKAFGVEKVE PELLSLNQAI
     FDEVFAYKGK ELVKAVSLVD KQERYDVIDA IKDEVVAHFE QRNFWMTVDG KEVLDADQKK
     ELMNQVKVSL DRIVTKEVRR LITEDKVRPD GRGLDEIRPL ASSVDLLPRT HGSALFTRGQ
     TQALGIVTLG SLNENQIIDG LEQETVTKRF MLHYNFPPFS VGETGRYGAP GRREIGHGAL
     GERALLQVLP SEDEFPYAIR VVSEITESNG SSSQATICVG SMALMAAGVP IKAPVAGIAM
     GLIMDGEHYS ILSDIQGMED HEGDMDFKVA GTKDGITALQ MDIKIQGITT EIMKEALEQA
     RKGRLHILSH MNTVISETRT ELSAFAPKVK MIRINPDKIR DVIGAGGKII TQIIEDHNNV
     KIDIEQDGRV FIMHTDSAWL NKTAAYIESL VREAKVGELY EAKVTRLLMD KDGKKIQGVF
     AEIFPGTEGL VHISKWEKER TESLDGKVKV GDQILVKVVK IDERGRVDLS RKDAL
//