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PNP_DESAH
ID   PNP_DESAH               Reviewed;         695 AA.
AC   C0QHM6;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 73.
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=HRM2_04700;
OS   Desulforapulum autotrophicum (strain ATCC 43914 / DSM 3382 / VKM B-1955 /
OS   HRM2) (Desulfobacterium autotrophicum).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfobacterales;
OC   Desulfobacteraceae; Desulforapulum.
OX   NCBI_TaxID=177437;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43914 / DSM 3382 / VKM B-1955 / HRM2;
RX   PubMed=19187283; DOI=10.1111/j.1462-2920.2008.01825.x;
RA   Strittmatter A.W., Liesegang H., Rabus R., Decker I., Amann J., Andres S.,
RA   Henne A., Fricke W.F., Martinez-Arias R., Bartels D., Goesmann A.,
RA   Krause L., Puehler A., Klenk H.P., Richter M., Schuler M., Gloeckner F.O.,
RA   Meyerdierks A., Gottschalk G., Amann R.;
RT   "Genome sequence of Desulfobacterium autotrophicum HRM2, a marine sulfate
RT   reducer oxidizing organic carbon completely to carbon dioxide.";
RL   Environ. Microbiol. 11:1038-1055(2009).
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; CP001087; ACN13584.1; -; Genomic_DNA.
DR   RefSeq; WP_012662833.1; NC_012108.1.
DR   AlphaFoldDB; C0QHM6; -.
DR   SMR; C0QHM6; -.
DR   STRING; 177437.HRM2_04700; -.
DR   EnsemblBacteria; ACN13584; ACN13584; HRM2_04700.
DR   KEGG; dat:HRM2_04700; -.
DR   eggNOG; COG1185; Bacteria.
DR   HOGENOM; CLU_004217_2_2_7; -.
DR   OMA; LHILDVM; -.
DR   OrthoDB; 122725at2; -.
DR   Proteomes; UP000000442; 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; 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; 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..695
FT                   /note="Polyribonucleotide nucleotidyltransferase"
FT                   /id="PRO_0000381883"
FT   DOMAIN          551..610
FT                   /note="KH"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
FT   DOMAIN          620..688
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
FT   BINDING         484
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
FT   BINDING         490
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
SQ   SEQUENCE   695 AA;  75737 MW;  492B170347DA21A2 CRC64;
     MEQVFKTELN GKEFSLRAGK IAKQASGSVI VQYGETIVLV TAVAAKEARD SVSFLPLTVE
     YQEKIYAAGR IPGNYFRREI GRPSEKETLT ARLIDRPIRP LFEKGWASEI QVIATVISTD
     KENDPDVLAL VGASAALQMS DIPFAGPIAG LRVGRIDGKF IANPTVQEME NSDIELVVAG
     SKTGVVMVEG GADVVSEADM LEAIFFGHQA MQPLIQLQED LKKALGKEKR AYTPPLVDEE
     LMAKVVELAQ DKIHTAVQTQ GKFERVKALD DVRTEVIETL GEAFADRINE IKSMFGDLVK
     KVSRKIVLTE NQRIDGRAFD EVREITCEVG VLPRPHGSAL FTRGETQVLG VLTLGSGPDE
     QRIETLNGNE TRNFMLHYNF PPFSVGECRR AGGPSRRDVG HGNLAHRALA RVLPDQADFE
     YTIRLVGEVM ESNGSSSMGT VCAGTLALMD GGVPIAAPVS GIAMGLVSDA DNTVVLTDIL
     GDEDHFGDMD FKVAGTEQGI TALQMDIKIR ELPKAVLVKA LDQARIGRLH ILKRMLATLE
     IHRDKMSPYA PKIITVKINP DKIREIIGPG GKMIRSIQAD TNTNIEVDDS GLIKIAAENQ
     EDGEAAAKIV SDIGMDPEIG GIYEGEVVKT TDFGAFVRIK TGTDGLVHIS ELANHRVKKV
     TDVVKEGEVI RVKVLEITRD GKIRLSCKAL EEEEK
 
 
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