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PNP_PHYAS
ID   PNP_PHYAS               Reviewed;         710 AA.
AC   B1VAN5;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   03-AUG-2022, entry version 75.
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}; OrderedLocusNames=PA0674;
OS   Phytoplasma australiense.
OC   Bacteria; Tenericutes; Mollicutes; Acholeplasmatales; Acholeplasmataceae;
OC   Candidatus Phytoplasma; 16SrXII (Stolbur group).
OX   NCBI_TaxID=59748;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=18359806; DOI=10.1128/jb.01301-07;
RA   Tran-Nguyen L.T., Kube M., Schneider B., Reinhardt R., Gibb K.S.;
RT   "Comparative genome analysis of 'Candidatus Phytoplasma australiense'
RT   (subgroup tuf-Australia I; rp-A) and 'Ca. Phytoplasma asteris' strains OY-M
RT   and AY-WB.";
RL   J. Bacteriol. 190:3979-3991(2008).
CC   -!- FUNCTION: Involved in mRNA degradation. Catalyzes the phosphorolysis of
CC       single-stranded polyribonucleotides processively in the 3'- to 5'-
CC       direction. {ECO:0000255|HAMAP-Rule:MF_01595}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=phosphate + RNA(n+1) = a ribonucleoside 5'-diphosphate +
CC         RNA(n); Xref=Rhea:RHEA:22096, Rhea:RHEA-COMP:14527, Rhea:RHEA-
CC         COMP:17342, ChEBI:CHEBI:43474, ChEBI:CHEBI:57930, ChEBI:CHEBI:140395;
CC         EC=2.7.7.8; Evidence={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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01595}.
CC   -!- SIMILARITY: Belongs to the polyribonucleotide nucleotidyltransferase
CC       family. {ECO:0000255|HAMAP-Rule:MF_01595}.
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DR   EMBL; AM422018; CAM12008.1; -; Genomic_DNA.
DR   RefSeq; WP_012359136.1; NC_010544.1.
DR   AlphaFoldDB; B1VAN5; -.
DR   SMR; B1VAN5; -.
DR   STRING; 59748.PA0674; -.
DR   EnsemblBacteria; CAM12008; CAM12008; PA0674.
DR   KEGG; pal:PA0674; -.
DR   eggNOG; COG1185; Bacteria.
DR   OMA; LHILDVM; -.
DR   Proteomes; UP000008323; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004654; F:polyribonucleotide nucleotidyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006402; P:mRNA catabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR   Gene3D; 2.40.50.140; -; 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; IPR036345; ExoRNase_PH_dom2_sf.
DR   InterPro; IPR004087; KH_dom.
DR   InterPro; IPR004088; KH_dom_type_1.
DR   InterPro; IPR036612; KH_dom_type_1_sf.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR012162; PNPase.
DR   InterPro; IPR027408; PNPase/RNase_PH_dom_sf.
DR   InterPro; IPR036456; PNPase_PH_RNA-bd_sf.
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; PF01138; RNase_PH; 2.
DR   Pfam; PF03725; RNase_PH_C; 2.
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;
KW   Cytoplasm; Magnesium; Metal-binding; Nucleotidyltransferase;
KW   Reference proteome; RNA-binding; Transferase.
FT   CHAIN           1..710
FT                   /note="Polyribonucleotide nucleotidyltransferase"
FT                   /id="PRO_1000192481"
FT   DOMAIN          568..628
FT                   /note="KH"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
FT   DOMAIN          638..710
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
FT   BINDING         501
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
FT   BINDING         507
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
SQ   SEQUENCE   710 AA;  80156 MW;  12161A596AB8036E CRC64;
     MLKQVFETTD LKNSFQVEIG TYARNVDPSV LIRFQDTVVL TTTVFSNKKN NFDFLPLTVI
     YQEKFYAAGK IPGSFLRREG RSTDHEILSS RLIDRSLRPL FPKEFRQEIQ VINTVLSSNP
     DFKSEIASIL GSSLSLLISE IPFFEPVAGV YVAYIQNQFV INPNAQQLTN SPLHLLVAGT
     KKNVVMIEAH ASEVSEEMFL EAIVFAHEYI KKLCLFQEDV QKKVGQTKKL IDLDAELQSL
     EKEFNEQYHE QTRTLVANVF EQDQKNDLQV FKKKILAKAQ QKAFVKTIDQ ITFFDVEEQK
     NYLLLIENLF QKLFNQEMRN YIIKNKKRPD KRTLEEVRNL DSQIDLLPRP HGSALFTRGQ
     TQSLAVVTLG TLSESKIIDD LSGESNKRFM LHYNFPPFAV GSIGRYAAPS RREIGHGNLA
     EKAILPLLPE ENDFPYAIRV VSEILESNGS SSQATVCATS MSLMAAGVPL KRAVSGIAMG
     LFMDSKTNEY VILSDIQGLE DHIGDMDLKI AGSDKGITAL QMDLKIEGIS QAILKQAFFQ
     AKKGRLHILE HMNKTIASPR KEMSQYAPKV QMFQIKPEKI RDVIGSAGKI INQIIENHDG
     VKIDIEQDGR IFVMHSNLET VKQAILFIKN LIQDAEVNSI YHAHISRFLN DKAGNILGAF
     AQVSPSIEGL IRFSKAKKEN DVVKIGDKVL VKCVKINERG RIDFVLISKK
 
 
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