PNP_DEHMB
ID PNP_DEHMB Reviewed; 720 AA.
AC A5FQT2;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 85.
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};
GN OrderedLocusNames=DehaBAV1_0861;
OS Dehalococcoides mccartyi (strain ATCC BAA-2100 / JCM 16839 / KCTC 5957 /
OS BAV1).
OC Bacteria; Chloroflexi; Dehalococcoidia; Dehalococcoidales;
OC Dehalococcoidaceae; Dehalococcoides.
OX NCBI_TaxID=216389;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-2100 / JCM 16839 / KCTC 5957 / BAV1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Lowry S., Clum A.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA Ritalahti K.M., Loeffler F., Richardson P.;
RT "Complete sequence of Dehalococcoides sp. BAV1.";
RL Submitted (MAY-2007) 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: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; CP000688; ABQ17443.1; -; Genomic_DNA.
DR RefSeq; WP_011929148.1; NC_009455.1.
DR AlphaFoldDB; A5FQT2; -.
DR SMR; A5FQT2; -.
DR KEGG; deb:DehaBAV1_0861; -.
DR PATRIC; fig|216389.18.peg.911; -.
DR HOGENOM; CLU_004217_2_2_0; -.
DR OMA; LHILDVM; -.
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; IPR015848; PNPase_PH_RNA-bd_bac/org-type.
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; 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; 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..720
FT /note="Polyribonucleotide nucleotidyltransferase"
FT /id="PRO_0000329618"
FT DOMAIN 551..610
FT /note="KH"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
FT DOMAIN 620..688
FT /note="S1 motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
FT REGION 697..720
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 720 AA; 78297 MW; DCB40A3BE568B277 CRC64;
MITANSFERT IGGRKLVIES GKLARLADAA ITIRYADTEL LVTLCSAKKP REGVDFLPLT
IDYEERMYAA GKIPGGFIRR EGRPSEQAIL AGRLTDRPLR PLLPKEWRND LQIIITVIAS
DKENDADIWG VVGASTVLAM SEIPYEGPVG ASRIGYINGE FVLNPTFAQL ESSQLDLVVV
STRKAVVMIE AGSKEIPEDI MINAIEFAHK ANQELIDLQD EIRAKLGKEK LPVPVLEIPE
EVKTAVAAFV KGRVNEALSH QDKTARENAV EGLQAELVAA LSETFAEGDI LAAYDKEIKK
AIRSTILEKD IRVNGRGIKQ LRQLDAETGL LPRVHGSALF TRGDTQVMAI TTLGSLQESQ
QLDGLSAEDT KRFMLHYNFA PFSTGEVKRS GSPGRREIGH GALAERALVP ILPTPEEFPY
TIRLVADVVG SSGSTSMGSV CSSSLSLMDA GVPVKKAVAG ISIGLITGEN GTYCTITDIE
GIEDNYGDMD FKVAGTRDGI TAIQVDMKVK GISFDIIRDA IYQAKEARYN ILDVMDKALA
QPKTELSPYA PRMYKINIDP SKIGSVIGSG GKTIRSIIEQ TNTTVDIEND GTVVIGAIDE
ASAKKAIKII EDLTKDIEAG SIYTGKVTRI MTFGAFVEIL PGKEGMVHIS ELADHRVEKV
EDIVKVGDDI TVKVIEIDNQ GRVNLSHRVI LNPNAVPISR NRDSQPRRPG PFRPSDRSNS
