PNP_ARTS2
ID PNP_ARTS2 Reviewed; 746 AA.
AC A0JUV8;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 03-AUG-2022, entry version 91.
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=Arth_1434;
OS Arthrobacter sp. (strain FB24).
OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Arthrobacter.
OX NCBI_TaxID=290399;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FB24;
RX PubMed=24501649; DOI=10.4056/sigs.4438185;
RA Nakatsu C.H., Barabote R., Thompson S., Bruce D., Detter C., Brettin T.,
RA Han C., Beasley F., Chen W., Konopka A., Xie G.;
RT "Complete genome sequence of Arthrobacter sp. strain FB24.";
RL Stand. Genomic Sci. 9:106-116(2013).
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; CP000454; ABK02828.1; -; Genomic_DNA.
DR RefSeq; WP_011691295.1; NC_008541.1.
DR AlphaFoldDB; A0JUV8; -.
DR SMR; A0JUV8; -.
DR STRING; 290399.Arth_1434; -.
DR PRIDE; A0JUV8; -.
DR EnsemblBacteria; ABK02828; ABK02828; Arth_1434.
DR KEGG; art:Arth_1434; -.
DR eggNOG; COG1185; Bacteria.
DR HOGENOM; CLU_004217_2_2_11; -.
DR OMA; LHILDVM; -.
DR OrthoDB; 122725at2; -.
DR Proteomes; UP000000754; 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; IPR036345; ExoRNase_PH_dom2_sf.
DR InterPro; IPR014069; GPSI/PNP.
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; 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; SSF54211; SSF54211; 2.
DR SUPFAM; SSF54791; SSF54791; 1.
DR SUPFAM; SSF55666; SSF55666; 2.
DR TIGRFAMs; TIGR03591; polynuc_phos; 1.
DR TIGRFAMs; TIGR02696; pppGpp_PNP; 1.
DR PROSITE; PS50084; KH_TYPE_1; 1.
DR PROSITE; PS50126; S1; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Magnesium; Metal-binding; Nucleotidyltransferase;
KW Reference proteome; RNA-binding; Transferase.
FT CHAIN 1..746
FT /note="Polyribonucleotide nucleotidyltransferase"
FT /id="PRO_0000329505"
FT DOMAIN 585..644
FT /note="KH"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
FT DOMAIN 656..728
FT /note="S1 motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
FT BINDING 519
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
FT BINDING 525
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
SQ SEQUENCE 746 AA; 80006 MW; 8EFCEE2F544353A7 CRC64;
MEGPEIQFSE AVIDNGRFGK RVIRFETGRL AKQAAGAAMV YIDEDTALLS ATTAGKHPRE
GFDFFPLTVD VEERMYAAGR IPGSFFRREG RPSTEAILAC RLMDRPLRPA FIKGLRNEVQ
IVVTVLAINP DELYDVVAIN ASSMSTQLSG LPFSGPIGGV RVALVADEHG SQWVAFPKHS
QLENSVFNMV VAGRVAGDDV AIMMVEAEAT DNSWNLIKEQ GATAPTEEVV SEGLEAAKPF
IKALCDAQAD LAARAAKPTV EFPVFLDYED DAYAAVEAAA AEKLAAVFQI ADKQERDAAS
DQLKDDVTSS LAGQFEGREK ELSAAFRSVT KHVVRQRILK DQIRIDGRGL TDIRQLTAEV
EVLPRVHGSA IFERGETQIM GVTTLNMLKM EQQIDSLSPV TRKRYMHNYN FPPYSTGETG
RVGSPKRREI GHGALAERAL VPVLPSREEF PYAIRQVSEA LSSNGSTSMG SVCASTLSML
NAGVPLKAAV AGIAMGLVSD QVDGQTRYAA LTDILGAEDA FGDMDFKVAG TSEFVTAIQL
DTKLDGIPAS VLAAALKQAR EARLHILEVI NSAIDTPDEL SEFAPRVIAV KIPVDKIGEV
IGPKGKMINQ IQEDTGADIS IEDDGTVYIG ATNGPSADAA RSAINAIANP QVPEIGERYL
GTVVKTTTFG AFISLTPGKD GLLHISELRK IAGGKRVDNV EDVVSVGQKI QVEITKIDDR
GKLSLSPVIA EEEGAENAEV AEAAAE
