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Resolution: standard / high Figure 4.
Sequence architecture of RBR proteins. The detailed sequence architecture of the subfamilies
of RBR proteins is shown. The globular domains (such as cullin) and non-globular regions
(negative-charge clusters or proline-rich regions) are color-coded as shown in the
key. It should be noted that the typical sequence architecture is shown. There are
several exceptions: for example, PAUL proteins mostly contain three additional zinc
fingers, but a few representatives have only one. Similarly, dorfins have two predicted
hydrophobic helices with the exception of the protozoan members, which have only one
or none. The two sequences of the Fungi1 group are very diverse and have only the
RBR segment in common. Among the Plant1 representatives, one protein contains two
RRM domains instead of the usual two KH domains. Domain accession numbers: APC10,
PF03256; cullin, SM00182; DEXDc, SM00487; IBR, SM00647; RWD, SM00591; DUF1605, PF07717;
HA2, PF04408; HELICc, SM00490; KH, SM00322; RRM, SM 00360; ANK, SM002481; UBA, SM00165;
UBQ, SM00213; UIM, SM00726; and ZnF_RBZ, SM00547. The first two letters 'PF' and 'SM'
indicate the PFAM and SMART databases, respectively.
Eisenhaber et al. Genome Biology 2007 8:209 doi:10.1186/gb-2007-8-3-209 |