ID   PNP_ALCBS               Reviewed;         697 AA.
AC   Q0VSR7;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   16-JUN-2009, entry version 23.
DE   RecName: Full=Polyribonucleotide nucleotidyltransferase;
DE            EC=2.7.7.8;
DE   AltName: Full=Polynucleotide phosphorylase;
DE            Short=PNPase;
GN   Name=pnp; OrderedLocusNames=ABO_0333;
OS   Alcanivorax borkumensis (strain SK2 / ATCC 700651 / DSM 11573).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Alcanivoracaceae; Alcanivorax.
OX   NCBI_TaxID=393595;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16878126; DOI=10.1038/nbt1232;
RA   Schneiker S., Martins dos Santos V.A.P., Bartels D., Bekel T.,
RA   Brecht M., Buhrmester J., Chernikova T.N., Denaro R., Ferrer M.,
RA   Gertler C., Goesmann A., Golyshina O.V., Kaminski F., Khachane A.N.,
RA   Lang S., Linke B., McHardy A.C., Meyer F., Nechitaylo T., Puehler A.,
RA   Regenhardt D., Rupp O., Sabirova J.S., Selbitschka W., Yakimov M.M.,
RA   Timmis K.N., Vorhoelter F.-J., Weidner S., Kaiser O., Golyshin P.N.;
RT   "Genome sequence of the ubiquitous hydrocarbon-degrading marine
RT   bacterium Alcanivorax borkumensis.";
RL   Nat. Biotechnol. 24:997-1004(2006).
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; AM286690; CAL15781.1; -; Genomic_DNA.
DR   RefSeq; YP_692053.1; -.
DR   GeneID; 4212265; -.
DR   GenomeReviews; AM286690_GR; ABO_0333.
DR   KEGG; abo:ABO_0333; -.
DR   NMPDR; fig|393595.12.peg.333; -.
DR   HOGENOM; Q0VSR7; -.
DR   OMA; Q0VSR7; GHGNLAK.
DR   BioCyc; ABOR393595:ABO_0333-MON; -.
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   PIRSF; PIRSF005499; PNPase; 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    697       Polyribonucleotide
FT                                nucleotidyltransferase.
FT                                /FTId=PRO_0000329489.
FT   DOMAIN      555    614       KH.
FT   DOMAIN      624    692       S1 motif.
SQ   SEQUENCE   697 AA;  75304 MW;  29A4A86B27D2FD6F CRC64;
     MFNKITKQIQ FGRDTVTLET GQIARQATAA VMVRIGDTQV LVTVVGRKEA NPGQNFFPLT
     VNYQEKTYAT GRIPGGFLKR EGRPSEKETL TCRLIDRPIR PLFPKGFMNE VQVVATVMSS
     DKNRDPDIAA LIGTSAALSI SGIPFSGPIG AARVGYKDGM YILNPSYSEL AESALDLVVA
     GTEPAVLMVE SEAQELSEDQ MLGAVLFGHM EMQPLIQGIK EFAAEVGTET WDWKPAEQNE
     TLKAAIKDKF AAALGEAYTI TEKMARYAKV GELRDACVAE FATGEDGAPE ADEVKDLFGK
     IEKSVVREAV VSGKPRIDGR ALDAVRAIDC QVGTLAKTHG SALFTRGETQ AIVTATLGGM
     RDAQFIDALE GSHQDHFMLQ YNFPPYCVGE TGFIGSPKRR EIGHGRLARR GVEAVVPSVQ
     DFPYTIRVVS EITESNGSSS MASVCGTSMA LMDAGVPLTA PVAGIAMGLV KEEDGRYAVL
     SDILGDEDHL GDMDFKVAGT ARGVTALQMD IKIEGITEEI MEKALNQANA GRLHILGEMN
     KAIAESRSEV SDNAPTLLTL KINPDKIRDV IGKGGATIRA LTEETGCTID IEDDGSVKIY
     GETREKADEA VRRVEEITAE AEVGAIYEGK VTRVVDFGAF VAIMPGTEGL LHISQIAEER
     VEKVTDYVNE GEIIKVKVLD VDQRGRIKLS MKEAKED
//