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The Open Protein Structure Annotation Network
PDB Keyword
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PF03671

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

    Pfam Family
    Name: Ufm1 Accession: PF03671 (PFAM live)
    Description
    Ubiquitin fold modifier 1 protein
    Comments
    This is a family of short ubiquitin-like proteins, that is like neither type-1 or type-2. It is a ubiquitin-fold modifier 1 (Ufm1) that is synthesised in a precursor form of 85 amino-acid residues. In humans the enzyme for Ufm1 is Uba5 and the conjugating enzyme is Ufc1. Prior to activation by Uba5 the extra two amino acids at the C-terminal region of the human pro-Ufm1 protein are removed to expose Gly whose residue is necessary for conjugation to target molecule(s). The mature Ufm1 is conjugated to yet unidentified endogenous proteins,[1]. While Ubiquitin and many Ubls possess the conserved C-terminal di-glycine that is adenylated by each specific E1 or E1-like enzyme, respectively, in an ATP-dependent manner, Ufm1(1-83) possesses a single glycine at its C-terminus, which is followed by a Ser-Cys dipeptide in the precursor form of Ufm1. The C-terminally processed Ufm1(1-83) is specifically activated by Uba5, an E1-like enzyme, and then transferred to its cognate Ufc1, an E2-like enzyme [2].

      

    Topsan Members

    Tag pages as 'PF03671' to appear in this list.

    Name Annotation Author(s)
    1l7y

    Summary

    Pfam family PFAM:PF03671 {Uncharacterized protein family (UPF0185) } with 65 members in NR database and additional 2 members in the metagenomic datasets is represented in Eukaryota. The first structural representative solved (PDB Id: TOPSAN:1l7y) was subject to FATCAT structural similarity search that indicated similarity to SCOP (v. 1.73) domain SCOP:d1c1yb_ classified as Beta-Grasp (ubiquitin-like) fold. Based on marginal prediction from FFAS confirmed by structural similarity one can argue that this family is remotely homologous to previously known structures from 'd1c1yb_' this fold. Based on sequence and structure analysis/ original paper one can hypothesize that this family is may interact with an unidentified activating enzyme in a new ubiquitin-like modification system

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