(data stored in ACNUC7421 zone)

HOGENOM: SHEDO_1_PE1010

ID   SHEDO_1_PE1010                       STANDARD;      PRT;   701 AA.
AC   SHEDO_1_PE1010; Q12QG9;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Polyribonucleotide nucleotidyltransferase; EC=2.7.7
DE   8;AltName: Full=Polynucleotide phosphorylase; Short=PNPase;
DE   (SHEDO_1.PE1010).
GN   Name=pnp; OrderedLocusNames=Sden_1019;
OS   SHEWANELLA DENITRIFICANS OS217.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=318161;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS SHEDO_1.PE1010.
CC       Shewanella denitrificans OS217, complete genome.
CC       annotated by Ensembl Genomes
CC   -!- ANNOTATIONS ORIGIN:PNP_SHEDO
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.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABE54307.1; Type=Erroneous initiation;
CC   -!- GENE_FAMILY: HOG000218326 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; Q12QG9; -.
DR   EMBL; CP000302; ABE54307.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; YP_562030.1; NC_007954.1.
DR   ProteinModelPortal; Q12QG9; -.
DR   SMR; Q12QG9; 616-691.
DR   STRING; Q12QG9; -.
DR   GeneID; 4016587; -.
DR   GenomeReviews; CP000302_GR; Sden_1019.
DR   KEGG; sdn:Sden_1019; -.
DR   NMPDR; fig|318161.14.peg.1000; -.
DR   eggNOG; COG1185; -.
DR   ProtClustDB; PRK11824; -.
DR   BioCyc; SDEN318161:SDEN_1019-MON; -.
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:EC.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006402; P:mRNA catabolic process; IEA:InterPro.
DR   GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR   HAMAP; MF_01595; PNPase; 1; -.
DR   InterPro; IPR001247; ExoRNase_PH_dom1.
DR   InterPro; IPR015847; ExoRNase_PH_dom2.
DR   InterPro; IPR004087; KH.
DR   InterPro; IPR004088; KH_type_1.
DR   InterPro; IPR018111; KH_type_1_subgr.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR016027; NA-bd_OB-fold-like.
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   Gene3D; G3DSA:2.40.50.140; OB_NA_bd_sub; 1.
DR   Gene3D; G3DSA:1.10.10.400; PNPase_PH_RNA-bd_bac/org-type; 1.
DR   PANTHER; PTHR11252; PNPase; 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.
DR   HOGENOMDNA; SHEDO_1.PE1010; -.
KW   polynucleotide phosphorylase/polyadenylase;
KW   Complete proteome; Cytoplasm; Nucleotidyltransferase; RNA-binding;
KW   Transferase.
SQ   SEQUENCE   701 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MGHVNPIVKS FEYGQHTVTL ETGVIARQAD AAVLASMGDT TVLVTVVGKK VADLSRDFFP
     LTVNYQEKTY AAGKIPGGFF KREGRPSEDE TLIARLIDRP IRPLFPNGFK NEVQVIITVV
     SVDPQIEPDI ISMIGTSAAL AISGIPFSGP LGAARVGYIN GEYLLNPTVD QLATSSLNLV
     VAGTKAAVLM VESEAKALAE EIMLGAVTYG HDQQQVVVDA IAEFKAEAGK PTWDWTAPVQ
     DQALVAKIKE LAEAGMTDAY QIEVKQDRYV QVGVVKAAAK AALVAENPDV DTREVDNLLG
     SLEKNVVRSR IIAGKPRIDG REPDMIRALN VLAGVLPRTH GSSLFTRGET QALVTCTLGT
     ERDAQKIDSI MGERTNRFML HYNFPPYSVG ETGMVGSPKR REIGHGKLAW RGMNAVMPTA
     EEFPYSIRVV SEITESNGSS SMASVCGTSL ALMDAGVPIK TSVAGIAMGL VKEGDDFVVL
     SDILGDEDHL GDMDFKVAGT RDGITALQMD IKIEGITKEI MDIALQQAYG ARVHILNVMD
     QAIGTHRGDI SAHAPRITTI KINPEKIRDV IGKGGAVIRA LTEETGTTIE LDDDGTVKIA
     SSNGEATKEA IRRIEEITAE VEVGRVYNGK VIRIVDFGAF INILPGKDGL VHISQISDER
     VANVSDHLEM NQDVKVKVME VDRQGRVRLS IKEAQEKVAA E
//

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