PNP_GLOC7
ID PNP_GLOC7 Reviewed; 718 AA.
AC B7KIQ3;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 73.
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=PCC7424_1005;
OS Gloeothece citriformis (strain PCC 7424) (Cyanothece sp. (strain PCC
OS 7424)).
OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales;
OC Aphanothecaceae; Gloeothece; Gloeothece citriformis.
OX NCBI_TaxID=65393;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7424;
RX PubMed=21972240; DOI=10.1128/mbio.00214-11;
RA Bandyopadhyay A., Elvitigala T., Welsh E., Stockel J., Liberton M., Min H.,
RA Sherman L.A., Pakrasi H.B.;
RT "Novel metabolic attributes of the genus Cyanothece, comprising a group of
RT unicellular nitrogen-fixing Cyanobacteria.";
RL MBio 2:E214-E214(2011).
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; CP001291; ACK69459.1; -; Genomic_DNA.
DR RefSeq; WP_012598406.1; NC_011729.1.
DR AlphaFoldDB; B7KIQ3; -.
DR SMR; B7KIQ3; -.
DR STRING; 65393.PCC7424_1005; -.
DR EnsemblBacteria; ACK69459; ACK69459; PCC7424_1005.
DR KEGG; cyc:PCC7424_1005; -.
DR eggNOG; COG1185; Bacteria.
DR HOGENOM; CLU_004217_2_2_3; -.
DR OMA; LHILDVM; -.
DR OrthoDB; 122725at2; -.
DR Proteomes; UP000002384; 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..718
FT /note="Polyribonucleotide nucleotidyltransferase"
FT /id="PRO_1000147912"
FT DOMAIN 564..623
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 497
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
FT BINDING 503
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
SQ SEQUENCE 718 AA; 77907 MW; 142EB0797189C04C CRC64;
MEEFDRSISF DGRDIRLKLG LLAPQAGGSV LIQSGDTAVL VTATKAASRE GVDFLPLTVD
YEERLYAAGR IPGGFLRREG RPPEKAILIS RLIDRPLRPL FPHWLRDDIQ VIATTLSMDE
EVPPDVLAVT GASLAVILAE IPFFGPMAAV RVGLVGDDFI INPTYKEINT GDLDLVVAGS
PDGVVMVEAG ANQLPEQDII EAIDFGYEAV RDLIAAQQDV METLGVKLAT LDPPPVNESV
LEFIKTQTAD EIKKVLSQYD LDKNGRDTAL DEIKAAKVEE VIASLPEEDP IKVATTEEAK
LVDTLFKDVT KKLMRSQIIN EGVRVDGRQL DQVRPISCRV GLLPPRVHGS GLFCRGLTQV
LSIATLGTPG DAQELADDLH PEDEKRYLHH YNFPPYSVGE TRPMRSPGRR EIGHGALAER
AILPVLPTQQ EFPYVVRVVS EVLSSNGSTS MGSVCGSTLA LMDAGVPIIK PVSGAAMGLI
KDGDEVRILT DIQGIEDFLG DMDFKVAGTD NGITALQMDM KITGLSMDIV AKAIEQARPA
RLHILDKMLS VIDSPRPELS PYAPRLLTMR IDPDMIGLVI GPGGKTVKSI TEQTKTKIDI
DDDGTVTISA SEAEQAERAK QLIHNMTRKL NEGEVYVGRV TRIIQIGAFV EIMPGKEGMI
HISQLAEGRV GKVEDELAVG DEVVVKVREI DNKGRLNLTR LGIHPDEAAA ARKAAALL
