Multiple sequence alignment of the SWIRM domain

Copyright information:

Taken from "The SWIRM domain: a conserved module found in chromosomal proteins points to novel chromatin-modifying activities"

Genome Biology 2002;3(8):research0039.1-research0039.7.

Published online 24 Jul 2002

PMCID:PMC126233.

Copyright © 2002 Aravind and Iyer, licensee BioMed Central Ltd

Proteins are designated by their gene names followed by the species abbreviations and GenBank (gi) numbers. The coloring represents the conservation profile of amino-acid residues at 90% consensus distinguished by the following amino-acid classes: h, hydrophobic residues (LIYFMWACV (in the single-letter amino-acid code)), a, aromatic residues (FHYW) and l, aliphatic (LIAV) residues, all shaded yellow; c, charged (KERDH) residues (basic (KRH) residues and acidic (DE) residues) colored magenta; p, polar (STEDRKHNQC) residues colored blue; s, small (SACGDNPVT) residues colored green; u, tiny (GAS) residues shaded green (in positions that are always glycine, this is indicated with a G); b, big (LIYERFMWQ) residues shaded gray. The predicted secondary structure is shown above the alignment: H or h, α helix; E or e, β strand. Species abbreviations: At, ; Bna, ; Ce, ; Ddi, ; Dm, ; Ecu, ; Hs, ; Osa, ; Sc, ; Sp, ; Zm, . A subset of Rsc8p orthologs is represented in the automatically generated, uncurated PFAM-B entry 3680.