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PNP_DESOH
ID   PNP_DESOH               Reviewed;         721 AA.
AC   A8ZZ59;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   03-AUG-2022, entry version 78.
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=Dole_3029;
OS   Desulfococcus oleovorans (strain DSM 6200 / JCM 39069 / Hxd3).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfobacterales;
OC   Desulfosudaceae; Desulfosudis.
OX   NCBI_TaxID=96561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6200 / JCM 39069 / Hxd3;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Detter J.C., Han C.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Wawrik B.,
RA   Richardson P.;
RT   "Complete sequence of Desulfococcus oleovorans Hxd3.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000859; ABW68832.1; -; Genomic_DNA.
DR   RefSeq; WP_012176443.1; NC_009943.1.
DR   AlphaFoldDB; A8ZZ59; -.
DR   SMR; A8ZZ59; -.
DR   STRING; 96561.Dole_3029; -.
DR   PRIDE; A8ZZ59; -.
DR   EnsemblBacteria; ABW68832; ABW68832; Dole_3029.
DR   KEGG; dol:Dole_3029; -.
DR   eggNOG; COG1185; Bacteria.
DR   HOGENOM; CLU_004217_2_2_7; -.
DR   OMA; LHILDVM; -.
DR   OrthoDB; 122725at2; -.
DR   Proteomes; UP000008561; 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; IPR015848; PNPase_PH_RNA-bd_bac/org-type.
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; 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   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..721
FT                   /note="Polyribonucleotide nucleotidyltransferase"
FT                   /id="PRO_1000147915"
FT   DOMAIN          552..611
FT                   /note="KH"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
FT   DOMAIN          621..689
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
FT   REGION          687..721
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         485
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
FT   BINDING         491
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
SQ   SEQUENCE   721 AA;  78781 MW;  4287C377C4AA9D4F CRC64;
     MTEHVFEATV NGKPFTIKTG RLAKQAAGAA LVQYGETIVL VTVAAATEPK EDADFLPLSV
     EYQEKIYSAG RIPGNYFRRE IGRPSEKETL TCRLTDRPIR PLFPAGYTFE TQVITTVLSM
     DRENDPDVLS IVGASAALTI SDLPFDGPLA AVRVGRLNGT LVANPTNTEL DDCDINIVVA
     GSRSGVVMVE GGSNVVSEAE MLEAIFFGHN ALLPLIDIQD QMRNACGKPK RVIVPPEKDT
     ELETRIAELV GDAVAQAVTE PEKDARKSAL SKVRENLFQG LGEAFADRKR EIKGLFSDLV
     KKVCRDIVLN QGRRIDGRAF DEVRPISCEV GVLPRTHGSA LFTRGETQVL GVMTLGSGHD
     EQRVETLFGD ETRPFMLHYN FPPFCVGEVK RVMGPSRRDI GHGNLAHRGI SYVLPDKETF
     DYTIRLVSEV LESNGSSSMG TVCSCILALM DGGVPIKAPV SGIAMGLVAD GDKVAVLSDI
     LGDEDHFGDM DFKVTGTEKG ITALQMDIKI KSLSREILEK ALHQAKDGRI HILGKMLEAL
     SHYRDDISPY APKIYIVKIH PDKIREIIGP GGKVIRELQA MSNTRIEVDD SGTVKIAAST
     EEEARIAIKA VEDIGRVPEP GEIYEGEVVR ITDFGAFIQI KNGTDGLCHI SELEHHHVKS
     VTDVVKMGDK VRVKVLEVSP EGKIRLSRKA LLPAPEKGEE DEKSAPRSRR PGGNSDRRNN
     R
 
 
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