Family Search for PF04167 (DUF402)

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PF04167 hits 27 sequences in PaperBLAST's database above the trusted cutoff. Showing hits to curated sequences only. Or see all hits or try another family.

NTDP_STAA8 / Q2G2M8 Nucleoside triphosphate/diphosphate phosphatase; Nucleoside diphosphatase; NDPase; EC 3.6.1.15; EC 3.6.1.6 from Staphylococcus aureus (strain NCTC 8325 / PS 47) (see paper)
NTDP_STAAN / Q7A4T2 Nucleoside triphosphate/diphosphate phosphatase; Nucleoside tri- and diphosphatase; Ntdp; EC 3.6.1.15; EC 3.6.1.6 from Staphylococcus aureus (strain N315) (see paper)
Q7A4T2 nucleoside diphosphate phosphatase (EC 3.6.1.6) from Staphylococcus aureus (see paper)
Aligns to 62:127 / 180 (36.7%), covers 98.5% of PF04167, 69.7 bits

• function: Has nucleoside phosphatase activity towards nucleoside triphosphates and nucleoside diphosphates (By similarity). Can hydrolyze nucleoside diphosphates (NDPs) and deoxynucleoside diphosphates (dNDPs), including ADP, GDP, UDP, CDP, IDP, TDP, dADP, dGDP and dCDP (PubMed:27422825).
  function: Plays an important role in S.aureus virulence (PubMed:27422825). Required for hemolysin production, nuclease production and colony spreading, and contributes to the expression of extracellular proteins and cell wall proteins (PubMed:27422825).
  catalytic activity: a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'- diphosphate + H(+) + phosphate (RHEA:23680)
  catalytic activity: a ribonucleoside 5'-diphosphate + H2O = a ribonucleoside 5'- phosphate + H(+) + phosphate (RHEA:36799)
  catalytic activity: a 2'-deoxyribonucleoside 5'-diphosphate + H2O = a 2'- deoxyribonucleoside 5'-phosphate + H(+) + phosphate (RHEA:64920)
  catalytic activity: ADP + H2O = AMP + H(+) + phosphate (RHEA:61436)
  catalytic activity: GDP + H2O = GMP + H(+) + phosphate (RHEA:22156)
  catalytic activity: H2O + UDP = H(+) + phosphate + UMP (RHEA:64876)
  catalytic activity: CDP + H2O = CMP + H(+) + phosphate (RHEA:64880)
  catalytic activity: H2O + IDP = H(+) + IMP + phosphate (RHEA:35207)
  catalytic activity: dADP + H2O = dAMP + H(+) + phosphate (RHEA:64928)
  catalytic activity: dGDP + H2O = dGMP + H(+) + phosphate (RHEA:64940)
  catalytic activity: dCDP + H2O = dCMP + H(+) + phosphate (RHEA:64952)
  cofactor: Mg(2+) Mn(2+) Co(2+) (Activity is highest with Mn(2+), followed by Co(2+) (PubMed:27422825). Has low activity with Mg(2+) at high magnesium concentrations (PubMed:27422825). The enzyme probably uses Mg(2+) under physiological conditions (By similarity). Cannot use Cu(2+), Ni(2+), Zn(2+) or Ca(2+) ions (PubMed:27422825).)
  disruption phenotype: Deletion mutant exhibits drastically decreased virulence in a silkworm infection model (PubMed:27422825). It has decreased hemolysin production, nuclease production and colony- spreading ability compared with the parent strain (PubMed:27422825). Deletion of the gene alters the expression of various genes, including the virulence regulatory genes agr, hla, sarZ and sarX, as well as metabolic genes involved in nucleotide metabolism, glycolysis and fermentation pathways (PubMed:27422825).
• function: Has nucleoside phosphatase activity towards nucleoside triphosphates and nucleoside diphosphates (PubMed:33955674). Can hydrolyze GTP, ATP, GDP and ADP (PubMed:33955674). GTP is the most preferred substrate, with the highest substrate affinity and catalytic efficiency (PubMed:33955674).
  catalytic activity: a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'- diphosphate + H(+) + phosphate (RHEA:23680)
  catalytic activity: a ribonucleoside 5'-diphosphate + H2O = a ribonucleoside 5'- phosphate + H(+) + phosphate (RHEA:36799)
  catalytic activity: GTP + H2O = GDP + H(+) + phosphate (RHEA:19669)
  catalytic activity: ATP + H2O = ADP + H(+) + phosphate (RHEA:13065)
  catalytic activity: GDP + H2O = GMP + H(+) + phosphate (RHEA:22156)
  catalytic activity: ADP + H2O = AMP + H(+) + phosphate (RHEA:61436)
  cofactor: Mg(2+) Mn(2+) Co(2+) (Activity is highest with Mn(2+), followed by Co(2+) and Mg(2+), but the enzyme probably uses Mg(2+) under physiological conditions (PubMed:33955674). Has low activity with Ca(2+) (PubMed:33955674). Cannot use Cu(2+) or Zn(2+) ions (PubMed:33955674).)
  subunit: Monomer in solution.

FAU1_THEKO / Q5JHN3 Probable ribonuclease FAU-1; RNA-binding protein FAU-1; EC 3.1.26.- from Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1) (Pyrococcus kodakaraensis (strain KOD1)) (see paper)
Aligns to 376:443 / 471 (14.4%), covers 100.0% of PF04167, 66.4 bits

• function: Probable RNase involved in rRNA stability through maturation and/or degradation of precursor rRNAs. Preferentially cleaves UA sequences in the 5' precursor region of 5S rRNA (PubMed:28978920). Binds to RNA in loop regions with AU-rich sequences (By similarity).
  disruption phenotype: Deletion mutant shows a delay of exponential phase, reduction of maximum cell number and significant changes in the nucleotide sequence lengths of its 5S, 16S, and 23S rRNAs in early exponential phase.

FAU1_PYRFU / Q8U4Q7 Probable ribonuclease FAU-1; FAU-1 protein; P.furiosus AU-binding; RNA-binding protein AU-1; RNA-binding protein FAU-1; EC 3.1.26.- from Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1) (see 2 papers)
Aligns to 374:441 / 469 (14.5%), covers 100.0% of PF04167, 59.5 bits

• function: Probable RNase involved in rRNA stability through maturation and/or degradation of precursor rRNAs. Preferentially cleaves UA sequences in the 5' precursor region of 5S rRNA (PubMed:28978920). Binds to RNA in loop regions with AU-rich sequences. Binds to the consensus sequence GGC(U/A)(U/A)U(U/C) in vitro (PubMed:12614195).
  subunit: Mainly homotrimer, but may form homohexamer, and homononamer.

FOMD_STRFR / D2SNF7 Cytidylyl-2-hydroxypropylphosphonate hydrolase; EC 3.6.1.- from Streptomyces fradiae (Streptomyces roseoflavus) (see paper)
Aligns to 78:147 / 207 (33.8%), covers 95.6% of PF04167, 42.4 bits

• function: Involved in fosfomycin biosynthesis (PubMed:30010320). Catalyzes the hydrolysis of cytidylyl (S)-2-hydroxypropylphosphonate ((S)-HPP-CMP) to give (S)-2-hydroxypropylphosphonate ((S)-HPP) and CMP (PubMed:30010320). Can also hydrolyze (R)-HPP-CMP and cytidylyl 2- hydroxyethylphosphonate (HEP-CMP), which is a biosynthetic intermediate before C-methylation, but the catalytic efficiency is much higher with (S)-HPP-CMP (PubMed:30010320).
  catalytic activity: cytidine 5'-({hydroxy[(S)-2- hydroxypropyl]phosphonoyl}phosphate) + H2O = (S)-2- hydroxypropylphosphonate + CMP + H(+) (RHEA:77231)
  cofactor: Mn(2+) Co(2+)

fomD / O83033 cytidylyl-2-hydroxypropylphosphonate hydrolase from Streptomyces wedmorensis (see paper)
FOMD_STRWE / O83033 Cytidylyl-2-hydroxypropylphosphonate hydrolase; EC 3.6.1.- from Streptomyces wedmorensis (see paper)
Aligns to 80:149 / 209 (33.5%), covers 95.6% of PF04167, 42.4 bits

• function: Involved in fosfomycin biosynthesis (PubMed:30010320). Catalyzes the hydrolysis of cytidylyl (S)-2-hydroxypropylphosphonate ((S)-HPP-CMP) to give (S)-2-hydroxypropylphosphonate ((S)-HPP) and CMP (PubMed:30010320). Can also hydrolyze (R)-HPP-CMP and cytidylyl 2- hydroxyethylphosphonate (HEP-CMP), which is a biosynthetic intermediate before C-methylation, but the catalytic efficiency is much higher with (S)-HPP-CMP (PubMed:30010320).
  catalytic activity: cytidine 5'-({hydroxy[(S)-2- hydroxypropyl]phosphonoyl}phosphate) + H2O = (S)-2- hydroxypropylphosphonate + CMP + H(+) (RHEA:77231)
  cofactor: Mn(2+) Co(2+)
  subunit: Monomer in solution.

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