PNP_THERP
ID PNP_THERP Reviewed; 790 AA.
AC B9KYR9;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 76.
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=trd_0623;
OS Thermomicrobium roseum (strain ATCC 27502 / DSM 5159 / P-2).
OC Bacteria; Chloroflexi; Thermomicrobiales; Thermomicrobiaceae;
OC Thermomicrobium.
OX NCBI_TaxID=309801;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27502 / DSM 5159 / P-2;
RX PubMed=19148287; DOI=10.1371/journal.pone.0004207;
RA Wu D., Raymond J., Wu M., Chatterji S., Ren Q., Graham J.E., Bryant D.A.,
RA Robb F., Colman A., Tallon L.J., Badger J.H., Madupu R., Ward N.L.,
RA Eisen J.A.;
RT "Complete genome sequence of the aerobic CO-oxidizing thermophile
RT Thermomicrobium roseum.";
RL PLoS ONE 4:E4207-E4207(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; CP001275; ACM05386.1; -; Genomic_DNA.
DR RefSeq; WP_012642019.1; NC_011959.1.
DR AlphaFoldDB; B9KYR9; -.
DR SMR; B9KYR9; -.
DR STRING; 309801.trd_0623; -.
DR PRIDE; B9KYR9; -.
DR EnsemblBacteria; ACM05386; ACM05386; trd_0623.
DR KEGG; tro:trd_0623; -.
DR eggNOG; COG1185; Bacteria.
DR HOGENOM; CLU_004217_2_2_0; -.
DR OMA; LHILDVM; -.
DR OrthoDB; 122725at2; -.
DR Proteomes; UP000000447; 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; RNA-binding;
KW Transferase.
FT CHAIN 1..790
FT /note="Polyribonucleotide nucleotidyltransferase"
FT /id="PRO_0000381924"
FT DOMAIN 565..624
FT /note="KH"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
FT DOMAIN 634..702
FT /note="S1 motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
FT REGION 710..790
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 739..753
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 790 AA; 86688 MW; 6295D2A0E06D767B CRC64;
MPPIIHERSI EIAGRLLTIE TGRVAEQADG AVLVRYGETV VLTTVVGAKQ PVEGIDFFPL
TVEYEEKMYA AGKIPGGFFR REGKPSEAAI LAARLTDRPI RPLFPKGYRN EVQVISTVLS
ADQENEPDVL SIIGASAALT LSDIPWYGPV GAVRIGELDG ELVINPTSHQ LLESRMDIVV
AGTADAILMV EGQANEISED RFIEAVVRAH QEIKRIVAVQ LELQAVAGKP KREFVPPQEN
VELKQQIADY LGDRLREAVF NPDKTLRVQA TAALREEVIA HFVPNEPLAI GTPQSGLPTA
KEVGDLFDSL VKELVRRTIL EQGERPDGRK PDEIREIWIQ VGLLPRPHGS ALFTRGQTQV
LTVCTLGTKE EEQFLDSLGI EETKRYMHHY NFPPFSTGEI RRLRGPSRRD IGHGALAERA
LLAVLPSEDE FPYTMRLVSE VLSSNGSTSM ASVCGSSLAL MDAGVPIRKP VAGVAMGLVT
DQTTGRYTIL TDIQGIEDAL GDMDFKVAGT RDGITAIQMD IKVMGITPEI MRDALEQARR
GRLFILDKMS EVIDAPRPEM SPYAPRILRI KIKPEQIGEV IGPGGRVIRA IQEQTGTKIS
IEEDGTVFIS AANEDAARRA VREIERLTRV PEVGEIFYGR VVTIIPSGAF VEILPGKDGF
LHISEIAPER VRSVEDVLKV GQEINVMVIG VRPDGKINLS RKALLEKEAA ERAATAQAPA
DGRSHQPRAP QRPSGTAQPE RRPGPPTPRR PEQRGPSRPP RPQAQRSTPP PGQYRIGDRL
KELLGEDEPN
