ID PNP_ANAMF Reviewed; 805 AA.
AC B9KIE3;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 27-NOV-2024, entry version 82.
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=AMF_391;
OS Anaplasma marginale (strain Florida).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Anaplasma.
OX NCBI_TaxID=320483;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Florida;
RX PubMed=19134224; DOI=10.1186/1471-2164-10-16;
RA Dark M.J., Herndon D.R., Kappmeyer L.S., Gonzales M.P., Nordeen E.,
RA Palmer G.H., Knowles D.P. Jr., Brayton K.A.;
RT "Conservation in the face of diversity: multistrain analysis of an
RT intracellular bacterium.";
RL BMC Genomics 10:16-16(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=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; CP001079; ACM49255.1; -; Genomic_DNA.
DR RefSeq; WP_012658930.1; NC_012026.1.
DR AlphaFoldDB; B9KIE3; -.
DR SMR; B9KIE3; -.
DR STRING; 320483.AMF_391; -.
DR GeneID; 7397935; -.
DR KEGG; amf:AMF_391; -.
DR PATRIC; fig|320483.3.peg.455; -.
DR eggNOG; COG1185; Bacteria.
DR HOGENOM; CLU_004217_2_2_5; -.
DR Proteomes; UP000007307; 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 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:000001; Polyribonucleotide nucleotidyltransferase; 1.
DR FunFam; 3.30.230.70:FF:000002; 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; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR InterPro; IPR003029; S1_domain.
DR NCBIfam; TIGR03591; polynuc_phos; 1.
DR PANTHER; PTHR11252; POLYRIBONUCLEOTIDE NUCLEOTIDYLTRANSFERASE; 1.
DR PANTHER; PTHR11252:SF0; POLYRIBONUCLEOTIDE NUCLEOTIDYLTRANSFERASE 1, MITOCHONDRIAL; 1.
DR Pfam; PF00013; KH_1; 1.
DR Pfam; PF01138; RNase_PH; 2.
DR Pfam; PF03725; RNase_PH_C; 1.
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..805
FT /note="Polyribonucleotide nucleotidyltransferase"
FT /id="PRO_0000381865"
FT DOMAIN 558..617
FT /note="KH"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
FT DOMAIN 627..694
FT /note="S1 motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
FT REGION 702..805
FT /note="Disordered"
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 805 AA; 87147 MW; 58EB5A9260C4E15A CRC64;
MFDITRKCVE WGDRLLVIES GKIARQADGA VVVDYGGTSV LSTVVSQKSK EPVDFLPLTV
QFLAKSYAIG RIPGGFFKRE GKPSDRETLI SRLVDRSIRP LFPTGFCDEI VIVCNLLSYD
QVSPPETVAL IGAAAALAIS GIPFPTPIAG AKIGYIREEE RYILNPSAEE LARSELDMFY
SGTKSSVVMV ESEASELSEE EMLGAVTFGH ENCAQVLDLI EEFAEAAGPK DVVEFVPHDI
GKVVSDISSG YSEKFSVAYS DHNKKPECSS LMPPGKACTQ ICAGKHVEES GEYTEQEVLL
AIKTFERSLV RARVLDTLKR VDGRGFDQIR NIEIEVDLIP RSHGSALFTR GDTQALVITA
LGTPQDEQVV DGFDGDRRER FLLHYNFPSY AVGEAAALRP PGRREIGHGK LAWRAIHPVL
PTKADFPYTI RVVSEITESD GSSSMATVCG ASLALMDTGV PLKSSVAGIA MGLIKEGDRY
AVLSDIIGDE DYLGDMDFKV AGTKDGITAL QMDMKIRGIG FDIIEKSLQQ AKDGRLFIIG
KMDKVIKESR EGVRDHVPRM ESMIIDKNKI KNVIGTGGKN VREICEKTGV KIEISQDGTV
MIYAVSRDAV EEAKNMIMCI VSEPEVGKVF SGVISEIAKY GAFVSFLGGR RGLVHISEIK
NEHIGSVSDV LAVDDKVKVL VIGIDKDHVQ LSMRRVDQDS GDLLEHESYS SNKKNGPQFG
DASGGASGFR DYASGPARER RRSGGSGGRP VRRRSAGSSG SGSGGCYSVP QHVGTPDPVH
GNDRRRGSGP QHASGGGGNK KPRFF
//
