ID   PNP_ANAPZ               Reviewed;         838 AA.
AC   Q2GJV5;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   16-JUN-2009, entry version 24.
DE   RecName: Full=Polyribonucleotide nucleotidyltransferase;
DE            EC=2.7.7.8;
DE   AltName: Full=Polynucleotide phosphorylase;
DE            Short=PNPase;
GN   Name=pnp; OrderedLocusNames=APH_0767;
OS   Anaplasma phagocytophilum (strain HZ).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Anaplasma; phagocytophilum group.
OX   NCBI_TaxID=212042;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16482227; DOI=10.1371/journal.pgen.0020021;
RA   Dunning Hotopp J.C., Lin M., Madupu R., Crabtree J., Angiuoli S.V.,
RA   Eisen J.A., Seshadri R., Ren Q., Wu M., Utterback T.R., Smith S.,
RA   Lewis M., Khouri H., Zhang C., Niu H., Lin Q., Ohashi N., Zhi N.,
RA   Nelson W.C., Brinkac L.M., Dodson R.J., Rosovitz M.J., Sundaram J.P.,
RA   Daugherty S.C., Davidsen T., Durkin A.S., Gwinn M.L., Haft D.H.,
RA   Selengut J.D., Sullivan S.A., Zafar N., Zhou L., Benahmed F.,
RA   Forberger H., Halpin R., Mulligan S., Robinson J., White O.,
RA   Rikihisa Y., Tettelin H.;
RT   "Comparative genomics of emerging human ehrlichiosis agents.";
RL   PLoS Genet. 2:208-222(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; CP000235; ABD44311.1; -; Genomic_DNA.
DR   RefSeq; YP_505346.1; -.
DR   GeneID; 3930955; -.
DR   GenomeReviews; CP000235_GR; APH_0767.
DR   KEGG; aph:APH_0767; -.
DR   NMPDR; fig|212042.5.peg.742; -.
DR   TIGR; APH_0767; -.
DR   HOGENOM; Q2GJV5; -.
DR   OMA; Q2GJV5; GHGNLAK.
DR   BioCyc; APHA212042:APH_0767-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   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    838       Polyribonucleotide
FT                                nucleotidyltransferase.
FT                                /FTId=PRO_0000329501.
FT   DOMAIN      561    620       KH.
FT   DOMAIN      630    697       S1 motif.
SQ   SEQUENCE   838 AA;  89762 MW;  27ABDC2FF220C83B CRC64;
     MFDITRKCVE WGDRSLTIES GKIARQAGGA VVVDYGGTSV LATVVSQKSK EAVDFLPLTV
     QFLAKSYAVG KIPGGFFKRE GKPSDRETLI SRIIDRSIRP LFPSGFSDEV AVVCNLLSYD
     ASSPPETVAL IGASAALAIS GIPFHCPVAG ARIGYIRGEG RYILNPSADE LSVSALDMFY
     ARTDTSILMV ESEAHELTEA EMLGALQFGH EHCEEIIKVI GEFAEEARKC APAEFVPCDL
     STIIDSIGSD YKERFLVAYS EKEKKARVAK LDAVRASLTE DLRVKFLSES EGGSKYIAQD
     IVYAMKTFER SLVRERVLES KSRIDGRAYD QIRNIEIEVD LISKAHGSAL FTRGDTQALV
     ITALGTPQDE QIVDGFDGDK RERFLLHYNF PPYAVGEASA LRPPGRREIG HGKLAWRAIH
     PVLPSKADFP YTIRVVSEIT ESDGSSSMAT VCGASLALMD TGVPLKSSVA GIAMGLIKEG
     DRYAILSDIL GDEDYLGDMD FKVAGTREGI TALQMDMKVK GIDFAVLGTA LDQAKEGRFF
     IIEKMDRVIK ESRGAVREHV PRMESMLIDK GKIKNVIGAG GKNVREICEK TGAKIEISQD
     GTVMIYAVGR EAIESAKDMI TGIVSEPEVG KIYSGEVCEL AKYGAFVTFL GARKGLVHIS
     EIRNEHINAV ADVLAVGDKV KVLVIDMDKD HIQLSMRRID QETGDQVDCE LYAPQRRNGV
     AAGNTVGDSS VNGGGAGSVY VPRGDYGGAS AGRNGRGGGK RDGAAKSSSS AGNGGGRSSS
     STRRRHSAGS SGYSSDSSSG NTKSSSSESS GGTGGRGRNG ANGDVQNGPA APKKPRFF
//