ID PNP_CAMC5 Reviewed; 735 AA.
AC A7GX79;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 27-NOV-2024, entry version 96.
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=Ccur92_05170;
GN ORFNames=CCV52592_0953;
OS Campylobacter curvus (strain 525.92).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=360105;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=525.92;
RA Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G.,
RA Mandrell R.E., Lastovica A.J., Nelson K.E.;
RT "Genome sequence of Campylobacter curvus 525.92 isolated from human
RT feces.";
RL Submitted (JUL-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=RNA(n+1) + phosphate = RNA(n) + a ribonucleoside 5'-
CC diphosphate; 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; CP000767; EAU00019.1; -; Genomic_DNA.
DR RefSeq; WP_011992002.1; NC_009715.2.
DR AlphaFoldDB; A7GX79; -.
DR SMR; A7GX79; -.
DR STRING; 360105.CCV52592_0953; -.
DR KEGG; ccv:CCV52592_0953; -.
DR HOGENOM; CLU_004217_2_2_7; -.
DR OrthoDB; 9804305at2; -.
DR Proteomes; UP000006380; Chromosome.
DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR GO; GO:0000175; F:3'-5'-RNA exonuclease activity; IEA:TreeGrafter.
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 CDD; cd02393; KH-I_PNPase; 1.
DR CDD; cd11364; RNase_PH_PNPase_2; 1.
DR FunFam; 3.30.1370.10:FF:000001; Polyribonucleotide nucleotidyltransferase; 1.
DR FunFam; 3.30.230.70:FF:000026; Polyribonucleotide nucleotidyltransferase; 1.
DR FunFam; 3.30.230.70:FF:000029; Polyribonucleotide nucleotidyltransferase; 1.
DR Gene3D; 3.30.230.70; GHMP Kinase, N-terminal domain; 2.
DR Gene3D; 3.30.1370.10; K Homology domain, type 1; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
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_Su5_D2-typ_SF.
DR InterPro; IPR003029; S1_domain.
DR PANTHER; PTHR11252; POLYRIBONUCLEOTIDE NUCLEOTIDYLTRANSFERASE; 1.
DR PANTHER; PTHR11252:SF0; POLYRIBONUCLEOTIDE NUCLEOTIDYLTRANSFERASE 1, MITOCHONDRIAL; 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; SSF54791; Eukaryotic type KH-domain (KH-domain type I); 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR SUPFAM; SSF55666; Ribonuclease PH domain 2-like; 2.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 2.
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..735
FT /note="Polyribonucleotide nucleotidyltransferase"
FT /id="PRO_0000329568"
FT DOMAIN 581..641
FT /note="KH"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
FT DOMAIN 675..734
FT /note="S1 motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
FT REGION 649..671
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 651..671
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 515
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
FT BINDING 521
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
SQ SEQUENCE 735 AA; 80567 MW; 9B6E933740BAC0AD CRC64;
MQYSIEVNNQ VEIFDLNKVA KQAAGAVMLR VKNTVVLATV ARDDVQVEED FLPLTVQYIE
KAYAAGRIPG GYVKRETKPG DFETLTARII DRSLRPLFPK GYAYPTQIVV MVLSADPEVD
LQVVGLNAAS VALYLSDIPV NRPVCGVRVG YIDDKFVINP SNSELKSSAL DLYVAGTKDE
LLMIEMRSIA QQSSQIIPII AIDPMMDPSL NDSITQKQDM NEFSEDRIVE AIDFAGKAIL
RASNAYEEAF KEHKKEDAIL ELKPEIENEN IAIYIDKFYK NDVKNAINQM AKSERASELG
KIAKQIASDE VAQKEGWEEG VISNVLGKYK KKIVREQIIN EGVRADGRAL DEVRPISIET
NVLPNAHGSC LFTRGQTQAL VVATLGTDGD AQMYDILTEK TALIEKFMFN YNFPGFSVGE
ASPLKAPGRR ELGHGNLAKR ALAPSIDINS PYTIRLVSEI LESNGSSSMA SVCGGALALR
AAGVDTQKLV AGVAMGLIFE GDKHAVLTDI MGLEDHDGDM DFKVAGSSDG ITALQMDIKL
GGISLEVLKE ALYQAKRGRE HILNLMHQAD SKIEVNEDVL PKLELFSVDP SKIVDIIGQA
GKTIKEIIER FEVSIDLDRE KGEVKIAGGA KKNVDAAKDY IISITSKENS RGFGKKPHGH
DRRDKDRQKP TFNIGDEFDG VVKSVVDFGA FIELKDGVDG LLHISKIKTP LNVGDRLKVC
VSEQKGNKIS LSLVE
//
