PNP_METRJ
ID PNP_METRJ Reviewed; 739 AA.
AC B1LZQ1;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 77.
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};
GN OrderedLocusNames=Mrad2831_0939;
OS Methylobacterium radiotolerans (strain ATCC 27329 / DSM 1819 / JCM 2831 /
OS NBRC 15690 / NCIMB 10815 / 0-1).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Methylobacteriaceae; Methylobacterium.
OX NCBI_TaxID=426355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27329 / DSM 1819 / JCM 2831 / NBRC 15690 / NCIMB 10815 / 0-1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T., Detter J.C., Han C.,
RA Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Marx C.J., Richardson P.;
RT "Complete sequence of chromosome of Methylobacterium radiotolerans JCM
RT 2831.";
RL Submitted (MAR-2008) 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; CP001001; ACB22949.1; -; Genomic_DNA.
DR RefSeq; WP_012317942.1; NC_010505.1.
DR AlphaFoldDB; B1LZQ1; -.
DR SMR; B1LZQ1; -.
DR STRING; 426355.Mrad2831_0939; -.
DR EnsemblBacteria; ACB22949; ACB22949; Mrad2831_0939.
DR KEGG; mrd:Mrad2831_0939; -.
DR eggNOG; COG1185; Bacteria.
DR HOGENOM; CLU_004217_2_2_5; -.
DR OMA; LHILDVM; -.
DR OrthoDB; 122725at2; -.
DR Proteomes; UP000006589; 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..739
FT /note="Polyribonucleotide nucleotidyltransferase"
FT /id="PRO_1000147931"
FT DOMAIN 554..613
FT /note="KH"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
FT DOMAIN 623..691
FT /note="S1 motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
FT REGION 694..739
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 697..739
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 487
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
FT BINDING 493
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
SQ SEQUENCE 739 AA; 80455 MW; 0E6293D77C0FD3DE CRC64;
MFDVQREELM WGDRKLVLET GKVARQADGA VIATYGETSV LATVVAAKEP KPGIDFMPLT
VNYQERAYAA GRIPGGYFKR EGRPSEKETL VSRLIDRPIR PLFIEGWRND TQVVVTVLTH
DLENDPDIVA MVAASAALTL SGVPFMGPIG GARVGYINGG YRLNPLVTET KEESSLDLVV
AGTQDAVLMV ESEAKELSED VMLGAVMFGH KHFQPVIEAI IRLAEKAAKE PRDFKAPENA
DVEKAVLEVC EAELRAAYTK TVKQERYAAV DAVKAKVMAA LCPEGAEKFP AEKVKAAFKE
AQSKVVRWNI LDSGARIDGR DVKTVRSILS EVGVLPRAHG SALFTRGETQ ALVVATLGTG
EDEQFIDALE GTYKERFLLH YNFPPYSVGE TGRMGSPGRR EIGHGKLAWR AIRPVLPPAH
EFPYTIRVVS EITESNGSSS MASVCGGSLS LMDAGVPLRR PVAGIAMGLI LEGERFAVLS
DILGDEDHLG DMDFKVAGTD EGVTSLQMDI KIAGITEEIM KIALAQAKDG RAHILAEMAK
ALTAARPELG EYAPRIETMQ IPTDKIRDVI GTGGKVIREI VEKTGAKINI EDTGVVKIAS
ADGKAIKAAY NWIRSIVAEP EVGVIYDGTI VKCMEFGAFV NFFGAKDGLV HISELAAQRV
AKVQDVVKEG DKVKVKFLGQ DDRGKIRLSM KVVDQQTGED ITDKIKAQRD AERAERGDEP
REPREGGRHR GERRREAGE
