ID A0A1P8F7S3_9CHLR Unreviewed; 733 AA.
AC A0A1P8F7S3;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 28-JAN-2026, entry version 36.
DE RecName: Full=Polyribonucleotide nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_01595};
DE EC=2.7.7.8 {ECO:0000256|HAMAP-Rule:MF_01595};
DE AltName: Full=Polynucleotide phosphorylase {ECO:0000256|HAMAP-Rule:MF_01595};
DE Short=PNPase {ECO:0000256|HAMAP-Rule:MF_01595};
GN Name=pnp {ECO:0000256|HAMAP-Rule:MF_01595,
GN ECO:0000313|EMBL:APV44517.1};
GN ORFNames=Dform_01185 {ECO:0000313|EMBL:APV44517.1};
OS Dehalogenimonas formicexedens.
OC Bacteria; Bacillati; Chloroflexota; Dehalococcoidia; Dehalococcoidales;
OC Dehalococcoidaceae; Dehalogenimonas.
OX NCBI_TaxID=1839801 {ECO:0000313|EMBL:APV44517.1, ECO:0000313|Proteomes:UP000185934};
RN [1] {ECO:0000313|Proteomes:UP000185934}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NSZ-14 {ECO:0000313|Proteomes:UP000185934};
RA Key T.A., Bowman K.S., Lee I., Chun J., Albuquerque L., da Costa M.S.,
RA Rainey F.A., Moe W.M.;
RT "Dehalogenimonas formicexedens sp. nov., a chlorinated alkane respiring
RT bacterium isolated from contaminated groundwater.";
RL Submitted (NOV-2016) 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:0000256|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:0000256|HAMAP-Rule:MF_01595};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01595};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_01595}.
CC -!- SIMILARITY: Belongs to the polyribonucleotide nucleotidyltransferase
CC family. {ECO:0000256|ARBA:ARBA00007404, ECO:0000256|HAMAP-
CC Rule:MF_01595}.
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DR EMBL; CP018258; APV44517.1; -; Genomic_DNA.
DR RefSeq; WP_076004190.1; NZ_CP018258.1.
DR AlphaFoldDB; A0A1P8F7S3; -.
DR STRING; 1839801.Dform_01185; -.
DR KEGG; dfo:Dform_01185; -.
DR OrthoDB; 9804305at2; -.
DR Proteomes; UP000185934; 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; cd11363; RNase_PH_PNPase_1; 1.
DR CDD; cd11364; RNase_PH_PNPase_2; 1.
DR CDD; cd04472; S1_PNPase; 1.
DR FunFam; 2.40.50.140:FF:000023; Polyribonucleotide nucleotidyltransferase; 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; IPR015848; PNPase_PH_RNA-bd_bac/org-type.
DR InterPro; IPR036456; PNPase_PH_RNA-bd_sf.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR InterPro; IPR003029; S1_domain.
DR NCBIfam; TIGR03591; polynuc_phos; 1.
DR NCBIfam; NF008805; PRK11824.1; 1.
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; 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; SSF46915; Polynucleotide phosphorylase/guanosine pentaphosphate synthase (PNPase/GPSI), domain 3; 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 {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01595};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01595};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01595};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW Rule:MF_01595}; Reference proteome {ECO:0000313|Proteomes:UP000185934};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_01595};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01595}.
FT DOMAIN 622..690
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 689..733
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 486
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01595"
FT BINDING 492
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01595"
SQ SEQUENCE 733 AA; 79511 MW; F38E0F22C8A19A5C CRC64;
MASIHTFERT IGGRKLVIEH GKLAWQANGA VTLRYGDTEI LATAVVAKEA KPGTDFLPLT
IDVEERMYAA GKIPGGFIRR EGRATEAATL ASRLADRPIR PLLPKYWRRE IQVILTVLAA
DQENDPDVLG VIGASCALGI SEMPFEGPIS AVHVGYINGE FVLNPTFSQL PESKLDVVVA
STKHAVTMLE AGARETPEAL MLEAIRFGHA ANQEIIALQE EVIAAVGKTK WHVDPPVVDE
ALVQKISIAI DDRLPGAFYQ ADKAQRTENL EKLSQELIAD LGEEFETAAI MAAYDKKIRK
LVRSTALDKN ERVSGRGITE IRELSADVSI LPRVHGSALF SRGMTQILNV ITLGSLQMEQ
KLDNISPEET KRYIHHYNFP PYSTGETKRL GGQGRREIGH GALAERALLP VIPSESEFPY
AMRLVSEAVS SNGSTSMAST CASSLSLMDA GVPIKKAVAG ISIGLITDDE NRDRFVTLTD
IEGLEDNYGD MDFKVAGTRD GITAIQLDIK LKGISFAIIE KTLSQAREAR MVILDVMDKS
ISQPRAELSP FAPRMYKLKI DPGKIGTVIG PGGRVIRSII DETKTTIDIE DDGTVIIGAT
DAAAANKAIA IVEGLTKDVE PGSVYTGKVT RIMSFGAFVE ILPGKEGMVH ISELANRRVD
KVEDVVKLGD VIQVKVTEID SQGRINLSRR ALLPPPTAEE QEAMKRQGPP PGGFPRSAPG
APMDRGGRPP FRR
//
