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Figure 2 | BMC Evolutionary Biology

Figure 2

From: Tic62: a protein family from metabolism to protein translocation

Figure 2

Multiple sequence alignment of the N-terminal domain of the Tic62-NAD(P)-related protein family. A multiple sequence alignment of the N-terminal domain (residues 87–334 in psTic62) of representative members of each of the six groups of Tic62-NAD(P)-related sequences was performed with ClustalX. Above the alignment the site of the GxxGxxG motif and the known secondary structure of the NP_568098 sequence from Arabidopsis [PDB:1XQ6] are displayed. α-helices and β-strands are represented by cylinders and arrows, respectively. The positions of the residues involved in the binding of NADP are marked with a triangle, and the identities of the residues from the crystal structure are indicated. The conserved residues between 1XQ6 and psTic62 are underlined. The sequence motifs that distinguish each group are shown in a box (see Results and Discussion). In the alignment the sequences are indicated with an abbreviation of the name of the organism followed by its identifying access code in the databases: ANAVA, A. variabilis ATCC 29413; ARATH, A. thaliana; CHLBS, C. phaeobacteroides BS1; CHLLI, C. limicola DSM 245; CHLPH, C. phaeobacteroides DSM 266; CHLRE, C. reinhardtii; CROWA, C. watsonii WH 8501; CYAME, C. merolae; GALSU, G. sulphuraria; GLOVI, G. violaceus PCC 7421; MEDTR, M. truncatula; NOSPU, N. punctiforme PCC 73102; NOSSP, Nostoc sp. PCC 7120; ORYSA, O. sativa; PHYPA, P. patens; PROAE, P. aestuarii DSM 271; PROMI, P. marinus str. MIT 9312; PROVI, P. vibrioformis DSM 265; SYNEL, S. elongatus PCC 6301; SYNSP, Synechocystis sp. PCC 6803; SYNWH, Synechococcus sp. WH 8102; TRIER, T. erythraeum IMS101. Note that the sequences from GALSU (GI and GIV), PHYPA (GII and GIII) and CHLRE (GIII and GIV) are incomplete sequences and lack part of the N- and C-terminal region. The representation of the alignment is the standard from the ClustalX program [43].

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