PNP_THEP1
ID PNP_THEP1 Reviewed; 708 AA.
AC A5IMM8;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 88.
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=Tpet_1438;
OS Thermotoga petrophila (strain ATCC BAA-488 / DSM 13995 / JCM 10881 /
OS RKU-1).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=390874;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-488 / DSM 13995 / JCM 10881 / RKU-1;
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., Sims D., Brettin T., Bruce D., Detter J.C., Han C.,
RA Tapia R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Nelson K., Gogarten J.P., Noll K., Richardson P.;
RT "Complete sequence of Thermotoga petrophila RKU-1.";
RL Submitted (MAY-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; CP000702; ABQ47451.1; -; Genomic_DNA.
DR RefSeq; WP_011943899.1; NC_009486.1.
DR AlphaFoldDB; A5IMM8; -.
DR SMR; A5IMM8; -.
DR STRING; 390874.Tpet_1438; -.
DR EnsemblBacteria; ABQ47451; ABQ47451; Tpet_1438.
DR KEGG; tpt:Tpet_1438; -.
DR eggNOG; COG1185; Bacteria.
DR HOGENOM; CLU_004217_2_2_0; -.
DR OMA; LHILDVM; -.
DR Proteomes; UP000006558; 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; RNA-binding;
KW Transferase.
FT CHAIN 1..708
FT /note="Polyribonucleotide nucleotidyltransferase"
FT /id="PRO_0000329914"
FT DOMAIN 555..615
FT /note="KH"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
FT DOMAIN 625..692
FT /note="S1 motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
FT BINDING 488
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
FT BINDING 494
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
SQ SEQUENCE 708 AA; 78591 MW; EC60D4CE5F025BC7 CRC64;
MKEWRRNILG RELVVQYGKV AKQSSGSALV RFGDTVVLAT ANISDKAVEG IDFVPLTVEF
QERFYAAGKI PGGFIKREGK PSESAILSAR LIDRPIRPLF PKKLRNEVQV IVTVLSVDPN
VPPDVVGIFA ASLALNVSKI PFEGIVAGIR VGYRDGQFIA LPSEEDIEKG LMDITVAGTK
DAVTMVEGEA KEVAEEDMVK ALRFAHSVIK ELVDFQEEIL SEFNVEKIPV VEPTPPEGLV
EAFKDLLNKE ELERRILVKV KKEREVALKE YEEQLLNQIA EKLSVTDLEG IKPFVSELYE
DAVKKTMRRL IVEKGIRADG RKPTEIRPIS CEVGLFPRTH GSALFTRGET QSLGIVTLGA
PMDVQIIDTL LEEGVKRFML HYNFPPFCTG EVKPLRGPSR REIGHGHLAE RALKNMLPPE
EEFPYTIRVV SEILESNGSS SMATVCSGSL ALMDAGVPIK KHVAGIAMGL ILEEDAEIIL
TDIIGMEDHY GDMDFKVAGT RDGITAFQMD CKVSGVSDEL LMKALMQARE ARMYILDRMY
ETISAPRPHL SKYAPIIKVT KVDPEKVADV IGPGGRVIKK IIKDFDVKVE IDDETGLVKV
VGSSEENVDK AIELIREIAK EIEVGEVLEG KVTRIEPYGL FIEVRPGKIG LLHQSKVGED
MRQFLKKVKV GDTIKVQVIN IDDLGRLQFK RVTEGENTQH GKTHSKRN
