LOCUS       CDQ49483.1               172 aa    PRT              BCT 04-FEB-2016
DEFINITION  Vibrio anguillarum RNA pyrophosphohydrolase protein.
ACCESSION   LK021130-565
PROTEIN_ID  CDQ49483.1
SOURCE      Vibrio anguillarum
  ORGANISM  Vibrio anguillarum
            Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales;
            Vibrionaceae; Vibrio.
REFERENCE   1  (bases 1 to 3119695)
  AUTHORS   Holm K.
  JOURNAL   Submitted (26-MAR-2014) to the INSDC. Norstruct, Dept of Chemistry,
            University of Tromso, Science Park 3, NO-9037 Tromso, NORWAY.
REFERENCE   2
  AUTHORS   Holm K.O., Nilsson K., Hjerde E., Willassen N.P., Milton D.L.
  TITLE     Complete genome sequence of Vibrio anguillarum strain NB10, a
            virulent isolate from the Gulf of Bothnia
  JOURNAL   Stand Genomic Sci 10, 60-60(2015).
   PUBMED   26380645
FEATURES             Qualifiers
     source          /organism="Vibrio anguillarum"
                     /chromosome="1"
                     /host="Rainbow trout"
                     /strain="NB10"
                     /mol_type="genomic DNA"
                     /geo_loc_name="Sweden:Baltic Sea, Norrbyn Umeaa"
                     /isolation_source="clinical isolate, Rainbow trout"
                     /serovar="O1"
                     /db_xref="taxon:55601"
     protein         /transl_table=11
                     /gene="rppH"
                     /gene_synonym="nudH"
                     /gene_synonym="ygdP"
                     /locus_tag="VANGNB10_cI0568"
                     /old_locus_tag="TVA1986"
                     /function="Master regulator of 5'-dependent mRNA decay.
                     Accelerates the degradation of transcripts by removing
                     pyrophosphate from the 5'-end of triphosphorylated
                     RNA,leading to a more labile monophosphorylated state that
                     can stimulate subsequent ribonuclease cleavage.
                     Preferentially hydrolyzes diadenosine penta-phosphate with
                     ATP as one of the reaction products. Also able to
                     hydrolyze diadenosine hexa- and tetra-phosphate. Has no
                     activity on diadenosine tri-phosphate, ADP-ribose, NADH
                     and UDP-glucose. In the meningitis causing strain E.coli
                     K1, has been shown to play a role in HBMEC (human brain
                     microvascular endothelial cells) invasion in vitro."
                     /EC_number="3.6.1.-"
                     /note="user locus_tag: VANGcI0568"
                     /note="Similar to Escherichia coli (strain K12) rpph
                     recname: full=rna pyrophosphohydrolase ec=3.6.1.- altname:
                     full=(di)nucleoside polyphosphate hydrolase altname:
                     full=ap5a pyrophosphatase UniProt:P0A776 (EMBL:U00096)
                     (176 aa) fasta scores: E()=2.2e-56, 71.0% id in 176 aa"
BEGIN
        1 MIDGDGYRLN VGIVICNNHG QVFWAKRYGQ HSWQFPQGGI DDDETPEQAM FRELYEEVGL
       61 TKKDVKIIAT SRHWLRYKLP KRLVRWDSQP VCIGQKQKWF LLRLECDESR INMQRGSTPE
      121 FDGWRWVSYW YPVRQVVSFK RDVYRRAMKE FASFAMPFKE RNNKGKRKNK RG
//