(data stored in ACNUC29543 zone)

SWISSPROT: PNP_SYNR3

ID   PNP_SYNR3               Reviewed;         719 AA.
AC   A5GRD7;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   08-MAY-2019, entry version 77.
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=SynRCC307_0543;
OS   Synechococcus sp. (strain RCC307).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=316278;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCC307;
RG   Genoscope;
RL   Submitted (MAY-2006) 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:
CC       Reaction=phosphate + RNA(n+1) = a ribonucleoside 5'-diphosphate +
CC         RNA(n); Xref=Rhea:RHEA:22096, Rhea:RHEA-COMP:11128, Rhea:RHEA-
CC         COMP:11129, ChEBI:CHEBI:43474, ChEBI:CHEBI:57930,
CC         ChEBI:CHEBI:83400; EC=2.7.7.8; Evidence={ECO:0000255|HAMAP-
CC         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
CC       nucleotidyltransferase family. {ECO:0000255|HAMAP-Rule:MF_01595}.
DR   EMBL; CT978603; CAK27446.1; -; Genomic_DNA.
DR   RefSeq; WP_011934961.1; NC_009482.1.
DR   SMR; A5GRD7; -.
DR   STRING; 316278.SynRCC307_0543; -.
DR   PRIDE; A5GRD7; -.
DR   EnsemblBacteria; CAK27446; CAK27446; SynRCC307_0543.
DR   KEGG; syr:SynRCC307_0543; -.
DR   eggNOG; ENOG4105C62; Bacteria.
DR   eggNOG; COG1185; LUCA.
DR   HOGENOM; HOG000218326; -.
DR   KO; K00962; -.
DR   OMA; RYMHNYN; -.
DR   OrthoDB; 122725at2; -.
DR   BioCyc; SSP316278:G1GJL-530-MONOMER; -.
DR   Proteomes; UP000001115; 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; 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;
DR   PRODOM; A5GRD7.
DR   SWISS-2DPAGE; A5GRD7.
KW   Complete proteome; Cytoplasm; Magnesium; Metal-binding;
KW   Nucleotidyltransferase; Reference proteome; RNA-binding; Transferase.
FT   CHAIN         1    719       Polyribonucleotide
FT                                nucleotidyltransferase.
FT                                /FTId=PRO_0000329902.
FT   DOMAIN      562    621       KH. {ECO:0000255|HAMAP-Rule:MF_01595}.
FT   DOMAIN      631    699       S1 motif. {ECO:0000255|HAMAP-
FT                                Rule:MF_01595}.
FT   METAL       495    495       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_01595}.
FT   METAL       501    501       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_01595}.
SQ   SEQUENCE   719 AA;  77871 MW;  AB89C0A1B73E63FB CRC64;
     MQGETRSISF DGREIRLTTR RYAPQAGGSV LIECGDTAVL VTATRANGRE GIDFLPLTCD
     YEERLYAAGR IPGSFMRRES RPPERATLAC RLIDRPIRPL FPSWMRDDLQ IVATVMSVDE
     RVPPDVLAVT GASLATLLAK IPFYGPMAAV RVGLLGDDFI LNPSYREIER SELDLVVAGT
     AEGVVMVEAG AQQLPEEDMI EAIDFGYEAV LELIRHQKET IAELGIEQVV PEKPAEDTTV
     PDYLAKQCTK DIGAVLSQFT LTKAERDSQL DSIKAKAAEA IAALKETDAV RAAVSSNGKL
     LGNSFKALTK SMMRAQIVKD GKRVDGRSLD QVRPISAAAG VLPKRVHGSG LFQRGLTQVL
     STATLGTPSD AQEMDDLNPS NEKHYLHHYN FPPYSVGETR PMRSPGRREI GHGALAERAL
     LPVLPPKESF PYVLRVVSEV LSSNGSTSMG SVCGSTLALM DAGVPIAAPV AGAAMGLIRE
     GSEVRVLTDI QGIEDFLGDM DFKVAGTEKG ITALQMDMKI TGLAMKTIGE AVTQARPARL
     HILEKMLEAL DKPRDTMSPH APRRLSFRID PELIGTVIGP GGRTIKGITE RTNTKIDIED
     TGIVTVASHD GAAAEEAQKI IEGLTRRVSE GEYFDGKVTR VIPIGAFVEI LPGKEGMIHI
     SQLSDQRVEK VEDVVNVGDE VRVRVREIDN RGRINLTLRG VPQDGSDPQP TVILPIGES
//

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