PNP_ERYLH
ID PNP_ERYLH Reviewed; 769 AA.
AC Q2NBZ2;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 91.
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=ELI_03535;
OS Erythrobacter litoralis (strain HTCC2594).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Erythrobacter.
OX NCBI_TaxID=314225;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTCC2594;
RX PubMed=19168610; DOI=10.1128/jb.00026-09;
RA Oh H.M., Giovannoni S.J., Ferriera S., Johnson J., Cho J.C.;
RT "Complete genome sequence of Erythrobacter litoralis HTCC2594.";
RL J. Bacteriol. 191:2419-2420(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; CP000157; ABC62799.1; -; Genomic_DNA.
DR RefSeq; WP_011413675.1; NC_007722.1.
DR AlphaFoldDB; Q2NBZ2; -.
DR SMR; Q2NBZ2; -.
DR STRING; 314225.ELI_03535; -.
DR PRIDE; Q2NBZ2; -.
DR EnsemblBacteria; ABC62799; ABC62799; ELI_03535.
DR KEGG; eli:ELI_03535; -.
DR eggNOG; COG1185; Bacteria.
DR HOGENOM; CLU_004217_2_2_5; -.
DR OMA; LHILDVM; -.
DR OrthoDB; 122725at2; -.
DR Proteomes; UP000008808; 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;
KW Reference proteome; RNA-binding; Transferase.
FT CHAIN 1..769
FT /note="Polyribonucleotide nucleotidyltransferase"
FT /id="PRO_0000329638"
FT DOMAIN 558..617
FT /note="KH"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
FT DOMAIN 627..695
FT /note="S1 motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
FT REGION 698..769
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 698..733
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 491
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
FT BINDING 497
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
SQ SEQUENCE 769 AA; 82950 MW; 81697AD58792862A CRC64;
MFDKKTVSIE WGGKTLTLET GQIARQADGA VLATYGETVV LCAVTAARSV KEGQDFFPLT
VHYQEKFSAA GRIPGGFFKR EGRATEKETL TSRLIDRPVR PLFPEGFYNE INVIAQVLSY
DGETEPDIVA MIAASAALTI SGLPFMGPIG AARVGFTNDG EYVLNPSVVD ALGEDGNLDL
VVAATQDAVM MVESEAKELT EEQMLGAVMF AHEESRKVIG AIIDLAEQAA KDPWELDPVE
DKSAALEKLR GVIGDDLAKA YKITNKAQRQ DAVNAARTKA REHYSDLEES DPAEYMGRLK
LVKKLESDIV RKAILKDGQR IDGRKTDEVR PIEAMVGLLP RTHGSALFTR GETQAICTTT
LGTKDSEQMI DGLEGLSYSN FMLHYNFPPY SVGEVGRFGF TSRRETGHGK LAFRALRPVL
PDNEEFPYTI RVLSDITESN GSSSMATVCG GSLSMMDAGV PLKRPVSGIA MGLILEGDDF
TVLSDILGDE DHLGDMDFKV AGSEEGITSL QMDIKVAGIT QEIMTKALEQ AKAGRAHILG
KMTEALGSSR GEVSKHAPRI ETMQIDKSKI RDVIGTGGKV IREIVAETGA KVDIDDEGVI
KISSSNADEI EAARKWIEGI VEEAEVGKIY NGKVVNIVDF GAFVNFMGGK DGLVHVSEMK
NERVEKPTDV VSEGQEVKVK VLEIDQRGKV RLSMRVVDQE TGEELEDTRP PREPRGDRGP
RSGGGDRRGG RGGPRRGGGG GGGGGRDRGG RDGGNDGGGE AHVPDFLKD
