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Results: 5

1.
Figure 1

Figure 1. From: The cohesin complex: sequence homologies, interaction networks and shared motifs.

Structure of an SMC protein. (a) The five domains of SMC proteins. The amino-terminal domain includes a Walker A motif and the carboxy-terminal domain a DA-box (also known as a Walker B motif). (b) Proposed dimeric interaction of SMC molecules (see, for example, [8]).

Susan Jones, et al. Genome Biol. 2001;2(3):research0009.1-research0009.12.
2.
Figure 4

Figure 4. From: The cohesin complex: sequence homologies, interaction networks and shared motifs.

Sequence alignment of the conserved motif in Scc2, Chk1 and Pkh1, which includes the PROSITE serine/threonine (S/T) protein kinase motif. In the alignment the conserved residues of the motif identified using Teiresias are in red and additional conserved positions are in green. The residues that coincide with the S/T kinase motif are outlined with a box. The number before each motif indicates the position of the first residue within the complete sequence. The PROSITE S/T kinase motif is shown beneath the alignment. The alternative residues are shown in squared brackets; X denotes any residue; the active-site aspartic acid is in blue.

Susan Jones, et al. Genome Biol. 2001;2(3):research0009.1-research0009.12.
3.
Figure 5

Figure 5. From: The cohesin complex: sequence homologies, interaction networks and shared motifs.

Sequence alignments for three motifs shared by proteins in the cohesion network. (a) A motif shared by Scc2 and Trf4 in the network and a putative seryl-tRNA synthetase (YHH1) from yeast. (b) A motif shared by Scc1, Smc1 and a P-type ATPase from Plasmodium yoelii. (c) A motif shared by the cohesin loading factor Scc4 and SMC3. In each alignment the conserved residues of the motif identified using Teiresias are in red and additional conserved positions are in green. The number before each motif indicates the position of the first residue within the complete sequence.

Susan Jones, et al. Genome Biol. 2001;2(3):research0009.1-research0009.12.
4.
Figure 3

Figure 3. From: The cohesin complex: sequence homologies, interaction networks and shared motifs.

The cohesion interaction network. Lines connecting proteins indicate known or potential interactions as derived from two proteomic databases and the literature. Cohesin and the loading factors are in yellow; additional proteins involved in cohesion or interacting with cohesin or the loading factors are in blue; all other proteins in the network are in white. Proteins outlined with boxes are part of macromolecular complexes. Prp11 is part of a complex in the spliceosomal pathway, and Apc2 is part of the anaphase-promoting complex (APC). Tid3p and Spc24 are both part of the spindle-pole body. Solid black lines indicate proteins that form dimeric interactions. The cohesion network of 17 proteins includes all those labeled, excluding Apc2, Tid4, Tid1 and Rad51.

Susan Jones, et al. Genome Biol. 2001;2(3):research0009.1-research0009.12.
5.
Figure 2

Figure 2. From: The cohesin complex: sequence homologies, interaction networks and shared motifs.

Evolutionary tree for SMC proteins, created using PHYLIP [69,70]. Each of the five SMC families is highlighted and labeled. The names of the eukaryotic proteins present in the ancestral family are underlined. Bootstrap values from 100 bootstrap trials are shown on the primary branches of the tree. AQUAE, Aquifex aeolicus; ARATH, Arabidopsis thaliana; ARCFU, Archaeoglobus fulgidus; ASPN, Aspergillus niger; BACSU, Bacillus subtilis; CAEEL, Caenorhabditis elegans; CAUCR, Caulobacter crescentus; DROS, Drosophila; ECOLI, Escherichia coli; JAPPU, Japanese pufferfish; METJA, Methanococcus jannaschii; MUS,mouse; MYCGE, Mycoplasma genitalium; MYCHR, Mycoplasma hyorhinis; MYCPN, Mycoplasma pneumonia; PYRAB, Pyrococcus abyssii; PYRHO, Pyrococcus horikoshii; SCHP, Schizosaccharomyces pombe; SYNSP, Synechocystis sp.; THEMA, Thermotoga maritima; TREPA, Treponema pallidum; XENLA, XENO, Xenopus laevis; YEAST, Saccharomyces cerevisiae.

Susan Jones, et al. Genome Biol. 2001;2(3):research0009.1-research0009.12.

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