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Database: UniProt
Entry: Q8RA43
LinkDB: Q8RA43
Original site: Q8RA43 
ID   PNP_CALS4               Reviewed;         707 AA.
AC   Q8RA43;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   27-MAR-2024, entry version 111.
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=TTE1387;
OS   Caldanaerobacter subterraneus subsp. tengcongensis (strain DSM 15242 / JCM
OS   11007 / NBRC 100824 / MB4) (Thermoanaerobacter tengcongensis).
OC   Bacteria; Bacillota; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Caldanaerobacter.
OX   NCBI_TaxID=273068;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15242 / JCM 11007 / NBRC 100824 / MB4;
RX   PubMed=11997336; DOI=10.1101/gr.219302;
RA   Bao Q., Tian Y., Li W., Xu Z., Xuan Z., Hu S., Dong W., Yang J., Chen Y.,
RA   Xue Y., Xu Y., Lai X., Huang L., Dong X., Ma Y., Ling L., Tan H., Chen R.,
RA   Wang J., Yu J., Yang H.;
RT   "A complete sequence of the T. tengcongensis genome.";
RL   Genome Res. 12:689-700(2002).
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; AE008691; AAM24609.1; -; Genomic_DNA.
DR   RefSeq; WP_011025675.1; NZ_JANUCV010000001.1.
DR   AlphaFoldDB; Q8RA43; -.
DR   SMR; Q8RA43; -.
DR   STRING; 273068.TTE1387; -.
DR   KEGG; tte:TTE1387; -.
DR   eggNOG; COG1185; Bacteria.
DR   HOGENOM; CLU_004217_2_2_9; -.
DR   OrthoDB; 9804305at2; -.
DR   Proteomes; UP000000555; 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   CDD; cd02393; KH-I_PNPase; 1.
DR   CDD; cd11363; RNase_PH_PNPase_1; 1.
DR   CDD; cd11364; RNase_PH_PNPase_2; 1.
DR   CDD; cd04472; S1_PNPase; 1.
DR   Gene3D; 3.30.230.70; GHMP Kinase, N-terminal domain; 2.
DR   Gene3D; 3.30.1370.10; K Homology domain, type 1; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
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_Su5_D2-typ_SF.
DR   InterPro; IPR003029; S1_domain.
DR   NCBIfam; TIGR03591; polynuc_phos; 1.
DR   PANTHER; PTHR11252; POLYRIBONUCLEOTIDE NUCLEOTIDYLTRANSFERASE; 1.
DR   PANTHER; PTHR11252:SF0; POLYRIBONUCLEOTIDE NUCLEOTIDYLTRANSFERASE 1, MITOCHONDRIAL; 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; SSF54791; Eukaryotic type KH-domain (KH-domain type I); 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR   SUPFAM; SSF46915; Polynucleotide phosphorylase/guanosine pentaphosphate synthase (PNPase/GPSI), domain 3; 1.
DR   SUPFAM; SSF55666; Ribonuclease PH domain 2-like; 2.
DR   SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 2.
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..707
FT                   /note="Polyribonucleotide nucleotidyltransferase"
FT                   /id="PRO_0000329909"
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   REGION          688..707
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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   707 AA;  78520 MW;  779E64C04BBA3331 CRC64;
     MEERTFEMEL AGRKLVVQTG KVAQQANGAA WVKYGDTVVL VTACASKEPR EGIDFFPLTV
     EYEERLYSIG KIPGGFIKRE GKPSEKAILS ARLIDRPIRP LFPEGYRNDV QVIATVLSVD
     PDAQPEIVAM IGSSVALSIS DIPFNGPTGS VAVGLVDGKF VINPTYEQRE KSLMHLVVSG
     TKDAIVMVEA GAKEVPEETI LDAIVYAHQY IKQIVEFIEG IVKEVGVPKA EVVLHEIDKE
     LEEKVRAYAT EKIYNALRTP EKKERNDNLD KVEQEVLEHF KDEYPDNLAD IDEVLYKIMK
     EQMRKMIKEE KIRVDGRGLD DIRPIWCEVG VLPRTHGSAI FTRGQTQVLT VATLGAIGDI
     QILEGIGDEE FKRYMHHYNF PPYSVGEVRP LRGPGRREIG HGALAERALE PVIPSEEEFP
     YTIRLVSEVL SSNGSTSQAS VCGSTLALMD AGVPIKAPVA GIAMGLIKEE DEVLILTDIQ
     GIEDFLGDMD FKVAGTEKGV TAIQMDIKIP GIDRDILQMA LEKARKARLY VLQKMLEVIK
     EPRKELSKYA PRVVRMVVNP EKIRDIIGPA GKTITKIISE TGVKIDIEED GRLYITAPNL
     EAGERAKQMI EAITKDIEVG GIYLGKVLRI APFGAFVEIA PGKEGLVHIS NLSKKRVRRV
     EDVVKVGDNI LVKVTEIDKL GRIVLSRKDA MPDEEESDNR KSDNRKK
//
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