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Database: UniProt
Entry: B1Y823
LinkDB: B1Y823
Original site: B1Y823 
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   29-OCT-2014, entry version 46.
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=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. Catalyzes the
CC       phosphorolysis of single-stranded polyribonucleotides processively
CC       in the 3'- to 5'-direction. {ECO:0000255|HAMAP-Rule:MF_01595}.
CC   -!- CATALYTIC ACTIVITY: RNA(n+1) + phosphate = RNA(n) + a nucleoside
CC       diphosphate. {ECO:0000255|HAMAP-Rule:MF_01595}.
CC   -!- COFACTOR: Magnesium. {ECO:0000255|HAMAP-Rule:MF_01595}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01595}.
CC   -!- SIMILARITY: Belongs to the polyribonucleotide
CC       nucleotidyltransferase family. {ECO:0000255|HAMAP-Rule:MF_01595}.
CC   -!- SIMILARITY: Contains 1 KH domain. {ECO:0000255|HAMAP-
CC       Rule:MF_01595}.
CC   -!- SIMILARITY: Contains 1 S1 motif domain. {ECO:0000255|HAMAP-
CC       Rule:MF_01595}.
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DR   EMBL; CP001013; ACB33765.1; -; Genomic_DNA.
DR   RefSeq; WP_012346527.1; NC_010524.1.
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; HGNFKSN; -.
DR   OrthoDB; EOG6WT8CC; -.
DR   BioCyc; LCHO395495:GHYL-1515-MONOMER; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-HAMAP.
DR   GO; GO:0000175; F:3'-5'-exoribonuclease activity; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0004654; F:polyribonucleotide nucleotidyltransferase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006402; P:mRNA catabolic process; IEA:UniProtKB-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   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; IPR004087; KH_dom.
DR   InterPro; IPR004088; KH_dom_type_1.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR012162; PNPase.
DR   InterPro; IPR027408; PNPase/RNase_PH_dom.
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; S1_dom.
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; 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   Complete proteome; Cytoplasm; Magnesium; Metal-binding;
KW   Nucleotidyltransferase; Reference proteome; RNA-binding; Transferase.
FT   CHAIN         1    767       Polyribonucleotide
FT                                nucleotidyltransferase.
FT                                /FTId=PRO_1000147928.
FT   DOMAIN      555    614       KH. {ECO:0000255|HAMAP-Rule:MF_01595}.
FT   DOMAIN      624    692       S1 motif. {ECO:0000255|HAMAP-
FT                                Rule:MF_01595}.
FT   METAL       488    488       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_01595}.
FT   METAL       494    494       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_01595}.
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
//
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