PNP_THETH
ID PNP_THETH Reviewed; 713 AA.
AC Q9ZAE1;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 85.
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};
OS Thermus thermophilus.
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=274;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=VK1;
RA Serganov A.A., Garber M.B., Portier C.;
RT "Polynucleotide phosphorylase from Thermus thermophilus: cloning,
RT sequencing and expression of the gene and biochemical properties of the
RT enzyme.";
RL Submitted (JAN-1997) 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; Z84207; CAB06341.1; -; Genomic_DNA.
DR RefSeq; WP_011173207.1; NZ_CP053287.1.
DR AlphaFoldDB; Q9ZAE1; -.
DR SMR; Q9ZAE1; -.
DR BRENDA; 2.7.7.8; 2305.
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; RNA-binding;
KW Transferase.
FT CHAIN 1..713
FT /note="Polyribonucleotide nucleotidyltransferase"
FT /id="PRO_0000329915"
FT DOMAIN 565..631
FT /note="KH"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
FT DOMAIN 633..701
FT /note="S1 motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
FT BINDING 498
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
FT BINDING 504
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
SQ SEQUENCE 713 AA; 78193 MW; 2979859D9AC5EA82 CRC64;
MEGTPNVPQA HRYELTLAGR PLVLETGKYA KQASGSVLVR YADTVVLATA QASETPVEAD
FLPLTVEFEE RHYAVGKIPG SFMRREGRPG EKAILSARMT DRPIRPLFPK GFRHEVQIIV
TVLSADQKNP PDILGPIAAS AALMLSDIPW EGPIAAVRVG LIGGSFVLNP TLQELEESQL
DLVVAGSKEA ILMVEAEAGE VDEETLVQAL EFAHKEMQPI LELQEAMARE LAKPKMAWTP
PESLPEEEKE ALYRLALERG LSQVLQTASK GERSRALAEF AERLIAEALP KGEDGTPDEG
KKPLYESAFD EVVRRELRRL VLEEGKRADG RGPKDLRPIW IEVDVLPRAH GSAVFTRGET
QVLGTVTLGT GRDEQILDDL GIDETEKFLV HYNFPPFSTG EVRRLRGVSR REVGHGNLAK
RALKAVMPKE EDFPYTIRVV GDVLESNGSS SMATVCAGCL ALMDAGVPIR APVAGVAMGL
VWEENRAVIL TDILGLEDAL GDMDFKVAGT RKGVTALQMD NKVGGLPREV LKEALLQARE
ARLKILDLME TVLPAPRPEL KPFAPRILSL KVPVEKIGLV IGPGGKNVRA LEELGVEVDI
EEDGTVRIYS SDLNAALEAK KRIEDLTREA KVGEIYEGTV TRITPFGAFI SLFPGTEGLL
HISQIAPGRV ERVEDHLKVG DVIKVKVHRI DERGKIDLIR PELEGKIPPR RRK