ID T5HV38_BACLI Unreviewed; 705 AA.
AC T5HV38;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 24-JAN-2024, entry version 44.
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=N399_10625 {ECO:0000313|EMBL:EQM28217.1};
OS Bacillus licheniformis CG-B52.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1368424 {ECO:0000313|EMBL:EQM28217.1, ECO:0000313|Proteomes:UP000017025};
RN [1] {ECO:0000313|Proteomes:UP000017025}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CG-B52 {ECO:0000313|Proteomes:UP000017025};
RA Galvez-Bobadilla E.J., Zarate-Bonilla L.J., Carrillo-Castro K., Guiza L.,
RA Pieper D.H., Salazar M., Junca H.;
RT "Draft genome of a Bacillus sp. strain CG-B52 virulent to shrimps.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EQM28217.1, ECO:0000313|Proteomes:UP000017025}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CG-B52 {ECO:0000313|EMBL:EQM28217.1,
RC ECO:0000313|Proteomes:UP000017025};
RX PubMed=27174263;
RA Galvez E.J., Carrillo-Castro K., Zarate L., Guiza L., Pieper D.H.,
RA Garcia-Bonilla E., Salazar M., Junca H.;
RT "Draft Genome Sequence of Bacillus licheniformis CG-B52, a Highly Virulent
RT Bacterium of Pacific White Shrimp (Litopenaeus vannamei), Isolated from a
RT Colombian Caribbean Aquaculture Outbreak.";
RL Genome Announc. 4:0-0(2016).
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:EQM28217.1}.
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DR EMBL; AVEZ01000029; EQM28217.1; -; Genomic_DNA.
DR RefSeq; WP_003181881.1; NZ_AVEZ01000029.1.
DR AlphaFoldDB; T5HV38; -.
DR SMR; T5HV38; -.
DR GeneID; 66216095; -.
DR PATRIC; fig|1368424.3.peg.1599; -.
DR Proteomes; UP000017025; 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};
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 705 AA; 77533 MW; 3DCB36019B3A4D83 CRC64;
MGQEKHVFSI DWAGRKLTVE TGQLAKQANG AVMVRYGDTA VLSTATASKE PKTVDFFPLT
VNYEERLYAV GKIPGGFIKR EGRPSEKAIL ASRLIDRPIR PLFADGFRNE VQVVSIVMSV
DQDCSSEMAA MFGSSLALCV SDIPFEGPIA GVTVGRVDNK FIINPTLEQL EKSDIHLVVA
GTKDAINMVE AGADEVPEEI MLEAIMFGHE EIKRLIAFQE EIVAAVGKEK SEITLYEIDS
DLKEKVRGMA ESNLLKAIQV HEKHAREDAI SEVKNEVLAK FEEEEHDEET LKQVKDILSQ
LVKNEVRRLI TEEKVRPDGR AVDEIRPLSS EVGLLPRTHG SGLFTRGQTQ ALSICTLGAL
GDVQILDGLG VEESKRFMHH YNFPQFSVGE TGPMRGPGRR EIGHGALGER ALEPIVPSEK
DFPYTIRLVS EVLESNGSTS QASICASTLA MMDAGVPIKA PVAGIAMGLV KSGDNYTVLT
DIQGMEDHLG DMDFKVAGTS KGVTALQMDI KIEGLSREIL EEALQQAKKG RMEILESMLS
TLAESRKELS PYAPKILTMS INPDKIRDVI GPSGKQINKI IEDTGVKIDI EQDGTIFISS
TDESMNQKAK KIIEDLVREV EVGQLYLGKV KRIEKFGAFV ELFSGKDGLV HISELALERV
GKVEDVVKIG DELLVKVTEI DKQGRVNLSR KAVLREQKEK EEQKS
//
