The Remorin C-terminal Anchor was shaped by convergent evolution among membrane binding domains

Figures & data

Figure 1. Diversity of RemCA domains across the plant kingdom and the identification of analogous membrane binding domains. (A) Natural diversity and conservation in the RemCA sequence illustrated by a sequence logo based on the alignment of 117 RemCA peptides from 26 plant species. (B) Analysis of bias in amino acid composition found in RemCA sequences. Frequencies are given as the average number of amino acids per 28 amino-acid long peptides in RemCA (Y-axis) or random 28- amino-acid long peptides extracted from the Uniprot database (Y-axis). (C) Two examples of membrane binding domains analogs of RemCA domain. The domains are shown in the context of the full-length protein structure (left) and superimposed with StREM1.3 RemCA model (right).

Table 1. RemCA analogous peptides identified by fold recognition searches showing a Pearson correlation coefficient for amino acid composition > 0.5

ρ^1	Structure^2	FATCAT score	Organism	Protein / domain
0.84	2kgjA	60.75	Escherichia coli	Parvulin domain of PpiD
0.80	2cfaA	67.51	Paramecium bursaria chlorella Virus 1	Flavin-dependant thymidylate synthase ThyX
0.78	1zk6A	60.27	Bacillus subtilis	PrsA PPIase
0.81	3aevA	71.21	Pyrococcus horikoshi	eIF2alpha-aDim2p-rRNA complex
0.79	3ct6A	66.73	Lactococcus lactis	DhaM
0.75	1r71A	64.02	Escherichia coli	DNA binding domain of KorB
0.73	1go3F	70.85	Methanococcus jannaschii	Archeal homolog of the eukaryotic RNA polimerase II RPB4/RPB7 complex
0.76	2ogiA	66.15	Streptococcus agalactiae	Putative metal dependent phosphohydrolase (sag1661)
0.72	1ku9A	66.99	Methanocaldococcus jannaschii	DNA-Binding Protein
0.72	1d2dA	93.43	Cricetulus griseus	EprS second repeated element
0.64	2ou3A	63.42	Nostoc punctiforme	tellurite resistance protein of cog3793
0.67	3mxzA	88.61	Arabidopsis thaliana	tubulin folding cofactor A
0.67	1bbhA	87.51	Allochromatium vinosum	Cytochrome C’
0.64	1x24A	69.58	Rattus norvegicus	Prl-1 (ptp4a)
0.67	1fjgT	64.43	Thermus thermophilus	30S Ribosomal subunit
0.64	2q1zA	69.36	Rhodobacter sphaeroides	SigE in complex with the anti-sigma ChrR
0.63	1s69A	66.94	Synechocystis SP.	cyanoglobin
0.62	2o08A	65.26	Bacillus halodurans	Putative HD superfamily hydrolase
0.66	2ztcA	64.71	Mycobacterium tuberculosis	MtRuvA Form II
0.61	1hbiA	67.34	Scapharca inaequivalvis	Dimeric hemoglobin
0.65	2v0oA	91.44	Homo sapiens	FCHO2 F-BAR domain
0.62	2ezkA	68.33	Enterobacteria phage Mu	Phage Mu transposase
0.65	1bvsA	70.27	Mycobacterium leprae	RuvA complexedto a holliday junction
0.59	3aq5A	67.63	Tetrahymena pyriformis	truncated hemoglobin
0.63	2rq7A	67.28	Thermosynechococcus elongatus – Spinacia oleracea	epsilon subunit chimera
0.62	1x59A	95.08	Homo sapiens	WHEP-TRS domain of human histidyl-tRNA synthetase
0.61	2aizP	64.17	Hemophilus influenzae	peptidoglycan associated lipoprotein
0.62	2h9dA	66.13	Pseudomonas aeruginosa	Isochorismate-Pyruvate Lyase
0.57	2dgzA	69.49	Homo sapiens	Werner syndrome ATP-dependent helicase
0.58	1aipC	70.84	Thermus thermophilus	EF-TU EF-TS complex
0.60	3mb2A	65.53	Chloroflexus aurantiacus	4-Oxalocrotonate Tautomerase
0.60	1cxzB	62.46	Homo sapiens	RhoA complexed with the effector domain of the protein kinase PKN/PRK1

¹Pearson correlation coefficient for amino acid composition;² PDB protein structure identifier.

DiNitto JP, Cronin TC, Lambright DG. Membrane recognition and targeting by lipid-binding domains. Sci STKE 2003; 2003:re16; http://dx.doi.org/10.1126/stke.2132003re16; PMID: 14679290

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