PNP_HELAH
ID PNP_HELAH Reviewed; 688 AA.
AC Q17VM4;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 97.
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=Hac_1591;
OS Helicobacter acinonychis (strain Sheeba).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=382638;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sheeba;
RX PubMed=16789826; DOI=10.1371/journal.pgen.0020120;
RA Eppinger M., Baar C., Linz B., Raddatz G., Lanz C., Keller H., Morelli G.,
RA Gressmann H., Achtman M., Schuster S.C.;
RT "Who ate whom? Adaptive Helicobacter genomic changes that accompanied a
RT host jump from early humans to large felines.";
RL PLoS Genet. 2:1097-1110(2006).
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=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: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; AM260522; CAK00302.1; -; Genomic_DNA.
DR RefSeq; WP_011578385.1; NC_008229.1.
DR AlphaFoldDB; Q17VM4; -.
DR SMR; Q17VM4; -.
DR STRING; 382638.Hac_1591; -.
DR EnsemblBacteria; CAK00302; CAK00302; Hac_1591.
DR KEGG; hac:Hac_1591; -.
DR eggNOG; COG1185; Bacteria.
DR HOGENOM; CLU_004217_2_2_7; -.
DR OMA; LHILDVM; -.
DR OrthoDB; 122725at2; -.
DR BioCyc; HACI382638:HAC_RS06740-MON; -.
DR Proteomes; UP000000775; Chromosome.
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 Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.30.1370.10; -; 1.
DR Gene3D; 3.30.230.70; -; 2.
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; IPR036456; PNPase_PH_RNA-bd_sf.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR022967; S1_dom.
DR InterPro; IPR003029; S1_domain.
DR PANTHER; PTHR11252; PTHR11252; 1.
DR Pfam; PF00013; KH_1; 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; SSF46915; SSF46915; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR SUPFAM; SSF54211; SSF54211; 2.
DR SUPFAM; SSF54791; SSF54791; 1.
DR SUPFAM; SSF55666; SSF55666; 2.
DR TIGRFAMs; TIGR03591; polynuc_phos; 1.
DR PROSITE; PS50084; KH_TYPE_1; 1.
DR PROSITE; PS50126; S1; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Magnesium; Metal-binding; Nucleotidyltransferase; RNA-binding;
KW Transferase.
FT CHAIN 1..688
FT /note="Polyribonucleotide nucleotidyltransferase"
FT /id="PRO_0000329676"
FT DOMAIN 550..609
FT /note="KH"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
FT DOMAIN 626..688
FT /note="S1 motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
FT BINDING 484
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
FT BINDING 490
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
SQ SEQUENCE 688 AA; 77044 MW; 837788E61EE63F4E CRC64;
MDFITINSIN KTEEFALKQV AKQATSSLLY RLGKTIILAS VCVERELVSE DFLPLVVQFL
EKSYAAGKIP GGFVKREGRA QDFEILTSRL IDRTLRPLFP KDYRYPTQIT LMVLSHDIEN
DLQVSALNAA SAALFLAHAA PFKSVSACRI ARIDNEFIIN PSTSLLNQSS LDLFVSGTKE
SLNMIEMRSL GQKLNALEEP LMLEALELAQ KSLKETCTLY EETFTPHQNA LLFKESQGIV
FNERLLDLLK NQYFNEIIKG IESSALSERE NVFNEIARKI SEAHSEFNLE EIELSLEKVK
KTEIRRMIIR DKIRPDKRAL EEVRPISIES NLLPMAHSSI LFTRGQTQSL VVGVLGTDND
AQTHESLEHK APIKERFMFH YNFPPFCVGE ASSIGATSRR ELGHGNLAKR ALETSIKNKD
QVIRLVSEIL ESNGSSSMAS VCAGSLALYA SGVEIHDLVA GVAMGMVSEG QDYAILSDIS
GLEDAEGDMD FKIAGNLEGI TAMQMDTKMS GIQLEILYQT LLQAKRVREH ILKIMHEAKE
KIVINFSHLP TTEIFNVAPD KIIEIIGQGG RVIREIVEKF EVKIDLNKPS GEVKIMGNKE
RVLKTKEFIL NYLHSLDQEL EQYAIDEVLE AQVKRIVDFG AFLSLPKGGE GLLRKQHMER
CQVALKEGDS IRCRVISFNK GKIALDLA
