ID A0A0K9GE23_9BACI Unreviewed; 704 AA.
AC A0A0K9GE23;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 29.
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 ORFNames=AC622_12655 {ECO:0000313|EMBL:KMY44965.1};
OS Bacillus sp. FJAT-27916.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1679169 {ECO:0000313|EMBL:KMY44965.1, ECO:0000313|Proteomes:UP000036953};
RN [1] {ECO:0000313|Proteomes:UP000036953}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FJAT-27916 {ECO:0000313|Proteomes:UP000036953};
RA Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Che J., Ge C., Shi H.,
RA Pan Z., Liu X.;
RT "Genome sequencing project for genomic taxonomy and phylogenomics of
RT Bacillus-like bacteria.";
RL Submitted (JUL-2015) 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=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: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|HAMAP-Rule:MF_01595}.
CC -!- SIMILARITY: Belongs to the polyribonucleotide nucleotidyltransferase
CC family. {ECO:0000256|ARBA:ARBA00007404, ECO:0000256|HAMAP-
CC Rule:MF_01595}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KMY44965.1}.
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DR EMBL; LFZV01000001; KMY44965.1; -; Genomic_DNA.
DR RefSeq; WP_049671387.1; NZ_LFZV01000001.1.
DR AlphaFoldDB; A0A0K9GE23; -.
DR STRING; 1679169.AC622_12655; -.
DR PATRIC; fig|1679169.3.peg.2719; -.
DR OrthoDB; 9804305at2; -.
DR Proteomes; UP000036953; Unassembled WGS sequence.
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 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 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 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; 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 {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01595};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01595};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01595};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW Rule:MF_01595}; Reference proteome {ECO:0000313|Proteomes:UP000036953};
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 623..691
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT BINDING 487
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01595"
FT BINDING 493
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01595"
SQ SEQUENCE 704 AA; 77476 MW; 471E2DC27022812E CRC64;
MEQTKRTFSL DWAGRPLTVE IGQLAKQANG AALIRYGDSA VLSTAVASKE PKNIDFFPLT
VSYEEKLYAV GKIPGGFIKR EGRPSEKAVL TSRLIDRPIR PLFADGFRND VQVVSMVLSV
DQDCPTEMAA MFGSSLALCV SDIPFEGPIA GVIVGRVDGK FVINPTIEQL DKSDIHLTVA
GTMDAINMVE AGADEVPEET MLEAIMFGHE EIKKLIKFQQ EIVEAVGKEK REIVLYELDA
ALVDEVKGMC LEEMNGAVQV QEKHAREDAI SAVKDKVLAV FEEREADEDT LKQVKEILSK
LVKDEVRRLI TEEKVRPDGR NPEEIRPLSS EVGLLPRTHG SGLFTRGQTQ ALSIATLGAL
GDVQILDGLG LEESKRFMHH YNFPHFSVGE TGPIRGPGRR EIGHGALGER ALEPVIPNEN
DFPYTIRLVS EVLESNGSTS QASICASTLA LMDAGVPIKA PVAGIAMGLV KQGEHYTVLS
DIQGMEDHLG DMDFKVAGTK KGVTALQMDI KIAGLTREIL EEALMQAQKG RNHILEHLMG
TLDQPRNQLS QYAPKILTMT IKPDKIRDVI GPSGKQINKI IEETGVKIDI EQDGTVYIAS
TDQEMNEKAK SIIEDIVREV EVGQMYLGTV KRIEKFGCFV EIFKGKDGLV HISELAEERV
GKVEDVVKIG DEILVKVTEI DRQGRVNLSR KAVLKEQKEK AEQQ
//
