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. 2016 Mar 3;291(18):9492–9500. doi: 10.1074/jbc.M116.714972

FIGURE 1.

FIGURE 1.

Phylogenetic analysis of the clan CD C11 peptidase family. A, unrooted neighbor joining tree of the C11 family from bacteria and archaeal species (Bact/Arch), Coccidia (Cocc), Chromerida (Chro), Chlorophyta (Chl), and Kinetoplastids (Kin; A, Trypanosoma; B, Leishmania/Endotrypanum/Crithidia; C, Bodonida). Clostripain (+)Uniprot ID P09870; PmC11(*)Uniprot ID, A7A9N3; and PNT1 (#)Uniprot ID, Q385B4 are marked. Key: 1, K2PE90 Trypanosoma cruzi. 2, A0A061IWY5 Trypanosoma rangeli. 3, F9W8X5 Trypanosoma congolense. 4, Tb927.11.6550 T. brucei. 5, G0UBL1 Trypanosoma vivax. 6, Q4QH06 Leishmania major. 7, AOFS01001278.1 2 2 2134 Endotrypanum monterogeii. 8, CfaC1 13 0800 Crithidia fasciculata. 9, BS39455 B. saltans. 10, EQ973215 Bacteroides fragilis. 11, GL883824 Paraprevotella xylaniphila. 12, AHHG01000029 Elizabethkingia anophelis. 13, P09870 C. histolyticum. 14, ADLW01000010 Dysgonomonas mossii. 15, AE010299 Methanosarcina acetivorans. 16, SNAP00000001341 Eimeria tenella. 17, B6ABJ5 Cryptosporidium muris. 18, MER037012 Cryptosporidium parvum. 19, Cvel 15101 Chromera velia. 20, A0A086LCT5 Toxoplasma gondii. 21, V4ZRY6 T. gondii. 22, F0VJH3 Neospora caninum. 23, U6G6U0 Eimeria praecox. 24, MER494436 Vitrella brassicaformis. 25, D8TW66 Volvox carteri. 26, A8I9P1 Chlamydomonas reinhardtii. 27, A0A0D2MVH2 Monoraphidium neglectum. 28, NC 018015 Thermococcus sp. CL1. 29, ABYK01000024 Arthrospira maxima. 30, DS990529 Aciduliprofundum boonei. 31, A7A9N3 P. merdae. 32, AJ437303 T. brucei MCA2 (outgroup). B, primary amino acid sequence alignment of PmC11 (from P. merdae), PNT1 (from T. brucei), and clostripain (from C. histolyticum) with identical residues highlighted in gray shading. The assigned secondary structure from the crystal structure of PmC11 (15) is mapped onto its sequence with the position of the PmC11 catalytic dyad and autocatalytic cleavage site (Lys147) highlighted by a red star and a red triangle, respectively. Connecting loops are colored gray/black, the main β-sheet is in orange, with other strands in olive, α-helices in blue, and the nonapeptide linker of clostripain underlined in red. Sequences around the catalytic site of clostripain, PmC11, and PNT1 are aligned where identical residues are highlighted in gray.