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Figure 1.
Figure 1. Amino acid sequence properties of M16B peptidase
family members. A: Domain structures of the M16 peptidase
family. The residues of the zinc-binding motif  HxxEHx  are
represented as vertical dotted lines. The glycine-rich region of
MPP
is indicated by a black filled box. The abbreviations of the
representative proteins are on the left side. IDE,
insulin-degrading enzyme; Ptr, pitrilysin;  MPP,
-subunit
of mitochondrial processing peptidase; Core1, core domain 1 of
cytochrome bc1 complex; RPP, rickettsial processing peptidase;
ppBH4, putative peptidase of Bacillus halodurans H4;
[74][alpha.gif] MPP, -subunit
of mitochondrial processing peptidase; Core 2, core domain 2 of
cytochrome bc1 complex; PreP, presequence peptidase; EuPtr,
eupitrilysin. B: Multiple sequence alignment of prokaryotic MPP
homologues retrieved at SSDB (http://www.genome.jp/kegg/ssdb/).
The UniProt accession numbers are Q5SIV0 (Thermus thermophilus
HB8), Q1IW66 (Deinococcus geothermalis), Q7ULM7 (Rhodopirellula
baltica), Q5P733 (Azoarcus sp. EbN1), Q479N3 (Dechloromonas
aromatica), A1WZF7 (Halorhodospira halophila), Q2JSQ8
(Cyanobacteria Yellowstone A-Prime), Q7NHF1 (Gloeobacter
violaceus), and Q7U7A2 (Synechococcus sp. WH8102). The secondary
structure elements of TTHA1264 are shown above each column.
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