PNP_PSECP
ID PNP_PSECP Reviewed; 752 AA.
AC B8HG67;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 87.
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=Achl_1439;
OS Pseudarthrobacter chlorophenolicus (strain ATCC 700700 / DSM 12829 / CIP
OS 107037 / JCM 12360 / KCTC 9906 / NCIMB 13794 / A6) (Arthrobacter
OS chlorophenolicus).
OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Pseudarthrobacter.
OX NCBI_TaxID=452863;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700700 / DSM 12829 / CIP 107037 / JCM 12360 / KCTC 9906 / NCIMB
RC 13794 / A6;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Goltsman E., Clum A., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Jansson J., Richardson P.;
RT "Complete sequence of chromosome of Arthrobacter chlorophenolicus A6.";
RL Submitted (JAN-2009) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001341; ACL39429.1; -; Genomic_DNA.
DR RefSeq; WP_015936652.1; NC_011886.1.
DR AlphaFoldDB; B8HG67; -.
DR SMR; B8HG67; -.
DR STRING; 452863.Achl_1439; -.
DR EnsemblBacteria; ACL39429; ACL39429; Achl_1439.
DR KEGG; ach:Achl_1439; -.
DR eggNOG; COG1185; Bacteria.
DR HOGENOM; CLU_004217_2_2_11; -.
DR OMA; LHILDVM; -.
DR OrthoDB; 122725at2; -.
DR Proteomes; UP000002505; 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; 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 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; RNA-binding;
KW Transferase.
FT CHAIN 1..752
FT /note="Polyribonucleotide nucleotidyltransferase"
FT /id="PRO_1000185718"
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 REGION 727..752
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 733..752
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 752 AA; 80574 MW; 588C18EAA6EE4AD5 CRC64;
MEGPEIQFSE AVIDNGRFGK RVIRFETGRL AKQAAGAAMV YIDEDTALLS ATTAGKHPRE
GFDFFPLTVD VEERMYAAGR IPGSFFRREG RPSTEAILAC RLMDRPLRPA FVKGLRNEVQ
IVVTVLAINP DELYDVVAIN ASSMSTQLSG LPFSGPIGGV RVALVADENG SQWVAFPKHS
QLENSVFNMV VAGRVAGDDV AIMMVEAEAT DNSWNLIKEQ GATAPTEEVV SEGLEAAKPF
IKALCDAQAD LAARAAKPTV EFPVFLDYQD DVYAAVEAAA ADKLAAVFQI ADKQERDTAS
DALKDEVTSS LAGQFEGREK ELSAAFRSVT KHVVRQRILK DQIRIDGRGL TDIRQLTAEV
EVLPRVHGSA IFERGETQIM GVTTLNMLKM EQQIDSLSPV TRKRYMHNYN FPPYSTGETG
RVGSPKRREI GHGALAERAL VPVLPSREEF PYAIRQVSEA LGSNGSTSMG SVCASTLSML
NAGVPLKAAV AGIAMGLVSD QVDGQTRYAA LTDILGAEDA FGDMDFKVAG TSEFVTAIQL
DTKLDGIPAS VLAAALKQAR EARLHILEVI NSAIDTPDEL SEFAPRVIAV KIPVDKIGEV
IGPKGKMINQ IQEDTGADIS IEDDGTVYIG ATNGPSADAA RSAINAIANP QVPEIGERYL
GTVVKTTTFG AFVSLTPGKD GLLHISELRK LANGKRVDNV DDVVSVGQKV QVEITKIDDR
GKLSLSPVVA EEEGAEGAER AHATEPAEGA EI
