ID PNP_LEPCP Reviewed; 767 AA.
AC B1Y823;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 01-MAY-2013, entry version 37.
DE RecName: Full=Polyribonucleotide nucleotidyltransferase;
DE EC=2.7.7.8;
DE AltName: Full=Polynucleotide phosphorylase;
DE Short=PNPase;
GN Name=pnp; OrderedLocusNames=Lcho_1497;
OS Leptothrix cholodnii (strain ATCC 51168 / LMG 8142 / SP-6) (Leptothrix
OS discophora (strain SP-6)).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Leptothrix.
OX NCBI_TaxID=395495;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51168 / LMG 8142 / SP-6;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E.,
RA Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T.,
RA Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Lykidis A., Emerson D., Richardson P.;
RT "Complete sequence of Leptothrix cholodnii SP-6.";
RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in mRNA degradation. Hydrolyzes single-stranded
CC polyribonucleotides processively in the 3'- to 5'-direction (By
CC similarity).
CC -!- CATALYTIC ACTIVITY: RNA(n+1) + phosphate = RNA(n) + a nucleoside
CC diphosphate.
CC -!- SUBUNIT: Homotrimer. Organized into a structure (processome or RNA
CC degradosome) containing a number of RNA-processing enzymes (By
CC similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- SIMILARITY: Belongs to the polyribonucleotide
CC nucleotidyltransferase family.
CC -!- SIMILARITY: Contains 1 KH domain.
CC -!- SIMILARITY: Contains 1 S1 motif domain.
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DR EMBL; CP001013; ACB33765.1; -; Genomic_DNA.
DR RefSeq; YP_001790530.1; NC_010524.1.
DR ProteinModelPortal; B1Y823; -.
DR SMR; B1Y823; 619-692.
DR STRING; 395495.Lcho_1497; -.
DR EnsemblBacteria; ACB33765; ACB33765; Lcho_1497.
DR GeneID; 6162411; -.
DR KEGG; lch:Lcho_1497; -.
DR PATRIC; 22393293; VBILepCho83238_1499.
DR eggNOG; COG1185; -.
DR HOGENOM; HOG000218326; -.
DR KO; K00962; -.
DR OMA; YTMRVVS; -.
DR ProtClustDB; PRK11824; -.
DR BioCyc; LCHO395495:GHYL-1515-MONOMER; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000175; F:3'-5'-exoribonuclease activity; IEA:InterPro.
DR GO; GO:0004654; F:polyribonucleotide nucleotidyltransferase activity; IEA:HAMAP.
DR GO; GO:0003723; F:RNA binding; IEA:HAMAP.
DR GO; GO:0006402; P:mRNA catabolic process; IEA:HAMAP.
DR GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR Gene3D; 1.10.10.400; -; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR HAMAP; MF_01595; PNPase; 1; -.
DR InterPro; IPR001247; ExoRNase_PH_dom1.
DR InterPro; IPR015847; ExoRNase_PH_dom2.
DR InterPro; IPR004087; KH_dom.
DR InterPro; IPR004088; KH_dom_type_1.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR012162; PNPase.
DR InterPro; IPR015848; PNPase_PH_RNA-bd_bac/org-type.
DR InterPro; IPR003029; Rbsml_prot_S1_RNA-bd_dom.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR022967; RNA-binding_domain_S1.
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; 2.
DR Pfam; PF00575; S1; 1.
DR PIRSF; PIRSF005499; PNPase; 1.
DR SMART; SM00322; KH; 1.
DR SMART; SM00316; S1; 1.
DR SUPFAM; SSF46915; 3_ExoRNase; 1.
DR SUPFAM; SSF55666; 3_ExoRNase; 2.
DR SUPFAM; SSF50249; Nucleic_acid_OB; 1.
DR SUPFAM; SSF54211; Ribosomal_S5_D2-typ_fold; 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 Complete proteome; Cytoplasm; Nucleotidyltransferase; RNA-binding;
KW Transferase.
FT CHAIN 1 767 Polyribonucleotide
FT nucleotidyltransferase.
FT /FTId=PRO_1000147928.
FT DOMAIN 555 614 KH.
FT DOMAIN 624 692 S1 motif.
SQ SEQUENCE 767 AA; 82747 MW; C612CD85B1CEF76E CRC64;
MSLFNKVTKT FQWGQHTVTL ETGEISRQAG GAVIVNIDDT VVLATVVGAK NAKPGQDFFP
LTVDYIEKTY AAGKIPGSFF KREAKPSELE VLTSRLIDRP LRPLFPEGFY NEVHVVVHVL
SLNPEASADI AALIGSSAAL AISGIPFNGP VGAARVGYVN GEYVLNPGPT QLKSSKMDLV
VAGTEAAVLM VESEADQLTE EVMLGAVVYG HEQAKVAIAA INELVRDAGK PAWDWQPPAR
NEPLIAKVAE FGLAKIEAAY QIRNKQARTH ACRAAYAEVK ISLAEAGVVF DNVDVDNLLF
ELEAKTVRGQ ILQGEPRIDG RDTRTVRPIE IRTGVLPRTH GSALFTRGET QALVVATLGT
DQDSQRIDAL AGDFRDSFLF HYNMPPFATG EVGRMGTTKR RETGHGRLAK RALVPLLPPK
DEFGYTIRVV SEITESNGSS SMASVCGGCL AMMDAGVPMK AHVAGIAMGL IKEGNRFAVL
TDILGDEDHL GDMDFKVAGT TAGVTALQMD IKIQGITKEI MQVALAQAKE ARLHILGKMV
EAMGTANTEV SNFAPRLYTM KINPEKIRDV IGKGGSVIRA LTEETGCQID IGEDGTITIA
STDADKAELA KKRIADITAE AEIGKVYEGP VVKILDFGAL INILPGKDGL LHISQIAHQR
VEKVTDFLTE GQVVKVKVLE TDEKGRIKLS MKALIERPEG MEFEERAPRR EGGFGDRGDR
GDRGPRRDRG GDRPERGERP ARAEQPATEE SGAPAAGQPQ QQQGQQQ
//
