The Open Protein Structure Annotation Network
PDB Keyword


    Table of contents
    1. 1. Topsan Members
    2. 2. Summary
    3. 3. References

    Live PFAM
    Name: Accession: PF02130 (PFAM live)
    # sequence matches: # architectures:
    # taxonomy ids: PDB:  1oz91tvi1xax1xm5

    Pfam ID: UPF0054 PDB: 1oz9_A
    Solved by: BSGC    
      Top FFAS hit in PDB: "1oz9A, Hypothetical protein AQ_1354" Top FFAS hit in Pfam: "PF11350, Protein of unknown function (DUF3152) "
      Top significant hit (PDB90): "1xaxA, structural genomics, unknown function ; nmr structure of hi0004, a putative essential gene product from haemophilus influenzae "
    CATH: CATH Domain E-value CATH Node
      1xaxA00 3.40E-39
      1tviA00 1.30E-37 3.40.390.30
    FUNFAM (eval=0 ): Putative metalloprotease C21orf57 homolog -like
    PUBSERVER: (view)
      Publications(s) found: 1859
      Publications(s) meeting filtering criteria: 21
    GeneSilico Metaserver
      PDBBLAST PDB: 1oz9_A SCOP : d.92.1.15
      FFAS PDB: 1xm5_A SCOP : d.92.1.15
      MGENTHREADER PDB: 1tvi_A SCOP : d.92.1.15
      PRC PDB: 1xm5_A SCOP : d.92.1.15
      SPARKS PDB: 1xm5_A SCOP : d.92.1.15
      BLASTP PDB: 1xm5_A SCOP : d.92.1.15
      HHBLITS PDB: 1xm5_A SCOP : d.92.1.15
      COMPASS PDB: 1xax_A
      CSBLAST PDB: 1oz9_A SCOP : d.92.1.15
      HHSEARCH PDB: 1xm5_A SCOP : d.92.1.15
    E.coli Annotations
    NCBI: 16128642 PORTECO PORAL: ybeY  GeneExpDB: b0659 

    Topsan Members

    Tag pages as 'PF02130' to appear in this list.

    Name Annotation Author(s)


    Based on the results in manuscripts PMID 20807199, PMID 20639334, PMID 21325267and structural and sequence conservations, it can be predicted to be a zinc-dependent RNA processing hydrolase, implicated in processing of 16S RNA, 23S RNA, 5S RNA and sRNAs in bacteria. They share a common fold with zincin-like metallopeptidases but lacks a conserved glutamate found in the latter and instead has an additional conserved histidine unique to this family. These domains are present in eukaryotes and bacteria. While predominantly appearing as single domain architectures, they tend to appear in combination with Hydrolyse_3 domains in Viridiplantae.




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