S100 Family: 2.60.120.200.14.1.1.1

Representative domain: 2w08A00

Classification Lineage (2.60.120.200.14.1.1.1)

CATH Code	Level Description	Links
2	Mainly Beta
2.60	Sandwich
2.60.120	Jelly Rolls
2.60.120.200		Gene3D
2.60.120.200.14
2.60.120.200.14.1
2.60.120.200.14.1.1
2.60.120.200.14.1.1.1

Summary of Non-Redundant Representatives


-	-	-	-	-	-	-	-	60

Non-Redundant Representatives (60)
Functional Families
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What is a Non-Redundant Representative?

CATH is a tree-like organisation of nodes that begins with the class node (i.e. the first branch-point of the tree) and ends with the domain nodes (i.e. the leaves of the tree). Each node below the class have a parent that they belong to, e.g. the parent of the H level (Homologous superfamily) is the T (Topology). Additionally, each node above the domains have child nodes that belong to them, e.g. the child nodes of a given H (Homologous superfamily) level are the S35 families (domains clustered at > 35% sequence identity).

S100 Count Entries in S100 Family 2.60.120.200.14.1.1.1 (60)

CATH code	Domain ID	Keywords
2.60.120.200.14.1.1.1.1	2w08A00	Homo sapiens, extracellular space, Serum amyloid P-component, chaperone-mediated protein complex assembly, unfolded protein binding, acute-phase response, protein folding
2.60.120.200.14.1.1.1.2	2w08B00	chaperone-mediated protein complex assembly, unfolded protein binding, acute-phase response, protein folding, Homo sapiens, Serum amyloid P-component, extracellular space
2.60.120.200.14.1.1.1.3	2w08C00	extracellular space, Serum amyloid P-component, Homo sapiens, acute-phase response, chaperone-mediated protein complex assembly, unfolded protein binding, protein folding
2.60.120.200.14.1.1.1.4	2w08D00	Serum amyloid P-component, extracellular space, Homo sapiens, acute-phase response, chaperone-mediated protein complex assembly, unfolded protein binding, protein folding
2.60.120.200.14.1.1.1.5	2w08E00	unfolded protein binding, chaperone-mediated protein complex assembly, acute-phase response, protein folding, Homo sapiens, extracellular space, Serum amyloid P-component
2.60.120.200.14.1.1.1.6	1sacA00	Serum amyloid P-component, extracellular space, Homo sapiens, protein folding, acute-phase response, unfolded protein binding, chaperone-mediated protein complex assembly
2.60.120.200.14.1.1.1.7	1sacB00	Homo sapiens, extracellular space, Serum amyloid P-component, protein folding, chaperone-mediated protein complex assembly, unfolded protein binding, acute-phase response
2.60.120.200.14.1.1.1.8	1sacC00	protein folding, acute-phase response, chaperone-mediated protein complex assembly, unfolded protein binding, extracellular space, Serum amyloid P-component, Homo sapiens
2.60.120.200.14.1.1.1.9	1sacD00	Homo sapiens, Serum amyloid P-component, extracellular space, unfolded protein binding, chaperone-mediated protein complex assembly, acute-phase response, protein folding
2.60.120.200.14.1.1.1.10	1sacE00	acute-phase response, unfolded protein binding, chaperone-mediated protein complex assembly, protein folding, Serum amyloid P-component, extracellular space, Homo sapiens
2.60.120.200.14.1.1.1.11	2a3yA00	Serum amyloid P-component, extracellular space, Homo sapiens, protein folding, acute-phase response, unfolded protein binding, chaperone-mediated protein complex assembly
2.60.120.200.14.1.1.1.12	2a3yB00	chaperone-mediated protein complex assembly, unfolded protein binding, acute-phase response, protein folding, Homo sapiens, Serum amyloid P-component, extracellular space
2.60.120.200.14.1.1.1.13	2a3yC00	chaperone-mediated protein complex assembly, unfolded protein binding, acute-phase response, protein folding, Homo sapiens, Serum amyloid P-component, extracellular space
2.60.120.200.14.1.1.1.14	2a3yD00	acute-phase response, unfolded protein binding, chaperone-mediated protein complex assembly, protein folding, extracellular space, Serum amyloid P-component, Homo sapiens
2.60.120.200.14.1.1.1.15	2a3yE00	protein folding, acute-phase response, chaperone-mediated protein complex assembly, unfolded protein binding, extracellular space, Serum amyloid P-component, Homo sapiens
2.60.120.200.14.1.1.1.16	1gykA00	acute-phase response, unfolded protein binding, chaperone-mediated protein complex assembly, protein folding, extracellular space, Serum amyloid P-component, Homo sapiens
2.60.120.200.14.1.1.1.17	1gykB00	Homo sapiens, extracellular space, Serum amyloid P-component, protein folding, unfolded protein binding, chaperone-mediated protein complex assembly, acute-phase response
2.60.120.200.14.1.1.1.18	1gykC00	acute-phase response, chaperone-mediated protein complex assembly, unfolded protein binding, protein folding, Serum amyloid P-component, extracellular space, Homo sapiens
2.60.120.200.14.1.1.1.19	1gykD00	protein folding, chaperone-mediated protein complex assembly, unfolded protein binding, acute-phase response, Homo sapiens, extracellular space, Serum amyloid P-component
2.60.120.200.14.1.1.1.20	1gykE00	Homo sapiens, Serum amyloid P-component, extracellular space, protein folding, chaperone-mediated protein complex assembly, unfolded protein binding, acute-phase response
2.60.120.200.14.1.1.1.21	2a3wA00	unfolded protein binding, chaperone-mediated protein complex assembly, acute-phase response, protein folding, Homo sapiens, Serum amyloid P-component, extracellular space
2.60.120.200.14.1.1.1.22	2a3wB00	acute-phase response, unfolded protein binding, chaperone-mediated protein complex assembly, protein folding, Serum amyloid P-component, extracellular space, Homo sapiens
2.60.120.200.14.1.1.1.23	2a3wC00	unfolded protein binding, chaperone-mediated protein complex assembly, acute-phase response, protein folding, Homo sapiens, Serum amyloid P-component, extracellular space
2.60.120.200.14.1.1.1.24	2a3wD00	acute-phase response, chaperone-mediated protein complex assembly, unfolded protein binding, protein folding, extracellular space, Serum amyloid P-component, Homo sapiens
2.60.120.200.14.1.1.1.25	2a3wE00	unfolded protein binding, chaperone-mediated protein complex assembly, acute-phase response, protein folding, Homo sapiens, Serum amyloid P-component, extracellular space
2.60.120.200.14.1.1.1.26	2a3wF00	unfolded protein binding, chaperone-mediated protein complex assembly, acute-phase response, protein folding, Homo sapiens, Serum amyloid P-component, extracellular space
2.60.120.200.14.1.1.1.27	2a3wG00	unfolded protein binding, chaperone-mediated protein complex assembly, acute-phase response, protein folding, Homo sapiens, Serum amyloid P-component, extracellular space
2.60.120.200.14.1.1.1.28	2a3wH00	acute-phase response, chaperone-mediated protein complex assembly, unfolded protein binding, protein folding, Serum amyloid P-component, extracellular space, Homo sapiens
2.60.120.200.14.1.1.1.29	2a3wI00	Homo sapiens, Serum amyloid P-component, extracellular space, unfolded protein binding, chaperone-mediated protein complex assembly, acute-phase response, protein folding
2.60.120.200.14.1.1.1.30	2a3wJ00	chaperone-mediated protein complex assembly, unfolded protein binding, acute-phase response, protein folding, Homo sapiens, Serum amyloid P-component, extracellular space
2.60.120.200.14.1.1.1.31	2a3wK00	Serum amyloid P-component, extracellular space, Homo sapiens, acute-phase response, unfolded protein binding, chaperone-mediated protein complex assembly, protein folding
2.60.120.200.14.1.1.1.32	2a3wL00	protein folding, unfolded protein binding, chaperone-mediated protein complex assembly, acute-phase response, Homo sapiens, Serum amyloid P-component, extracellular space
2.60.120.200.14.1.1.1.33	2a3wM00	Homo sapiens, extracellular space, Serum amyloid P-component, protein folding, unfolded protein binding, chaperone-mediated protein complex assembly, acute-phase response
2.60.120.200.14.1.1.1.34	2a3wN00	protein folding, unfolded protein binding, chaperone-mediated protein complex assembly, acute-phase response, Homo sapiens, Serum amyloid P-component, extracellular space
2.60.120.200.14.1.1.1.35	2a3wO00	Homo sapiens, Serum amyloid P-component, extracellular space, protein folding, chaperone-mediated protein complex assembly, unfolded protein binding, acute-phase response
2.60.120.200.14.1.1.1.36	2a3wP00	protein folding, acute-phase response, chaperone-mediated protein complex assembly, unfolded protein binding, Serum amyloid P-component, extracellular space, Homo sapiens
2.60.120.200.14.1.1.1.37	2a3wQ00	Homo sapiens, Serum amyloid P-component, extracellular space, protein folding, unfolded protein binding, chaperone-mediated protein complex assembly, acute-phase response
2.60.120.200.14.1.1.1.38	2a3wR00	unfolded protein binding, chaperone-mediated protein complex assembly, acute-phase response, protein folding, Homo sapiens, Serum amyloid P-component, extracellular space
2.60.120.200.14.1.1.1.39	2a3wS00	Homo sapiens, Serum amyloid P-component, extracellular space, protein folding, chaperone-mediated protein complex assembly, unfolded protein binding, acute-phase response
2.60.120.200.14.1.1.1.40	2a3wT00	Serum amyloid P-component, extracellular space, Homo sapiens, acute-phase response, chaperone-mediated protein complex assembly, unfolded protein binding, protein folding
2.60.120.200.14.1.1.1.41	1lgnA00	Homo sapiens, extracellular space, Serum amyloid P-component, protein folding, unfolded protein binding, chaperone-mediated protein complex assembly, acute-phase response
2.60.120.200.14.1.1.1.42	1lgnB00	protein folding, acute-phase response, chaperone-mediated protein complex assembly, unfolded protein binding, Serum amyloid P-component, extracellular space, Homo sapiens
2.60.120.200.14.1.1.1.43	1lgnC00	Serum amyloid P-component, extracellular space, Homo sapiens, acute-phase response, chaperone-mediated protein complex assembly, unfolded protein binding, protein folding
2.60.120.200.14.1.1.1.44	1lgnD00	Homo sapiens, extracellular space, Serum amyloid P-component, protein folding, chaperone-mediated protein complex assembly, unfolded protein binding, acute-phase response
2.60.120.200.14.1.1.1.45	1lgnE00	Homo sapiens, Serum amyloid P-component, extracellular space, unfolded protein binding, chaperone-mediated protein complex assembly, acute-phase response, protein folding
2.60.120.200.14.1.1.1.46	3d5oA00	Serum amyloid P-component, extracellular space, Homo sapiens, protein folding, acute-phase response, unfolded protein binding, chaperone-mediated protein complex assembly
2.60.120.200.14.1.1.1.47	3d5oB00	Serum amyloid P-component, extracellular space, Homo sapiens, acute-phase response, unfolded protein binding, chaperone-mediated protein complex assembly, protein folding
2.60.120.200.14.1.1.1.48	3d5oC00	Homo sapiens, Serum amyloid P-component, extracellular space, chaperone-mediated protein complex assembly, unfolded protein binding, acute-phase response, protein folding
2.60.120.200.14.1.1.1.49	3d5oD00	unfolded protein binding, chaperone-mediated protein complex assembly, acute-phase response, protein folding, Homo sapiens, Serum amyloid P-component, extracellular space
2.60.120.200.14.1.1.1.50	3d5oE00	extracellular space, Serum amyloid P-component, Homo sapiens, protein folding, acute-phase response, unfolded protein binding, chaperone-mediated protein complex assembly
2.60.120.200.14.1.1.1.51	2a3xA00	acute-phase response, chaperone-mediated protein complex assembly, unfolded protein binding, protein folding, extracellular space, Serum amyloid P-component, Homo sapiens
2.60.120.200.14.1.1.1.52	2a3xB00	unfolded protein binding, chaperone-mediated protein complex assembly, acute-phase response, protein folding, Homo sapiens, extracellular space, Serum amyloid P-component
2.60.120.200.14.1.1.1.53	2a3xC00	chaperone-mediated protein complex assembly, unfolded protein binding, acute-phase response, protein folding, Homo sapiens, extracellular space, Serum amyloid P-component
2.60.120.200.14.1.1.1.54	2a3xD00	Serum amyloid P-component, extracellular space, Homo sapiens, acute-phase response, chaperone-mediated protein complex assembly, unfolded protein binding, protein folding
2.60.120.200.14.1.1.1.55	2a3xE00	Homo sapiens, Serum amyloid P-component, extracellular space, protein folding, chaperone-mediated protein complex assembly, unfolded protein binding, acute-phase response
2.60.120.200.14.1.1.1.56	2a3xF00	protein folding, unfolded protein binding, chaperone-mediated protein complex assembly, acute-phase response, Homo sapiens, Serum amyloid P-component, extracellular space
2.60.120.200.14.1.1.1.57	2a3xG00	acute-phase response, unfolded protein binding, chaperone-mediated protein complex assembly, protein folding, Serum amyloid P-component, extracellular space, Homo sapiens
2.60.120.200.14.1.1.1.58	2a3xH00	extracellular space, Serum amyloid P-component, Homo sapiens, acute-phase response, chaperone-mediated protein complex assembly, unfolded protein binding, protein folding
2.60.120.200.14.1.1.1.59	2a3xI00	extracellular space, Serum amyloid P-component, Homo sapiens, acute-phase response, unfolded protein binding, chaperone-mediated protein complex assembly, protein folding
2.60.120.200.14.1.1.1.60	2a3xJ00	extracellular space, Serum amyloid P-component, Homo sapiens, acute-phase response, unfolded protein binding, chaperone-mediated protein complex assembly, protein folding

The information on Functional Families (FunFams) is currently being updated and will be released by the end of March 2012. The pages will include the following features:

Multiple alignments for each functional family
Representative structure for each functional with known catalytic and interface residues highlighted, along with conserved residues predicted by scorecons
Detailed functional information on diversity and conservation within Functional families
Multi-domain architectures

In the meantime, please find a summary of information on the FunFams and protein networks within this superfamily on the Gene3D pages:

http://gene3d.biochem.ucl.ac.uk/superfamily/?accession=2.60.120.200.14.1.1.1

What is a Non-Redundant Representative?

Why can't I have a multiple structural alignment of the whole superfamily?

The simple answer is that some of the larger superfamilies in CATH comprise relatives which are very structurally diverse, having different secondary structure embellishments. Attempting to provide a global alignment of all domains in the superfamily would result in poor quality alignments. As a result, structural alignments in CATH are generated by first clustering together the structures that have at least some recognisable structural similarity using a normalised RMSD score (SIMAX = RMSDxNumber of residues in the largest domain/number of aligned residues) less than a given cutoff.

What is an Close Structural Cluster?

A Close Structural Cluster describes a cluster of two or more CATH domains that have been grouped together due to their close structural similarity (SIMAX score < 5Å where SIMAX = RMSD x Number of residues in the larger domain/number of aligned residues).

What is a Distant Structural Cluster?

A Distant Structural Cluster describes a cluster of two or CATH domains that have been grouped together with a more relaxed structural similarity threshold to investigate more distant evolutionary similarities (SIMAX score < 5Å where SIMAX = RMSD x Number of residues in the larger domain/number of aligned residues).

What is a Structural Neighbour?

The term "structural neighbour" is used here to describe two CATH domains that share a degree of structural similarity. The SSAP algorithm is used to calculate this similarity and works by generating a structure-based pairwise alignment of the two domains then scoring this alignment using a RMSD score which has been normalised by the length of the larger domain divided by the number of aligned residues (SIMAX).

S100 Family: 2.60.120.200.14.1.1.1

Classification Lineage (2.60.120.200.14.1.1.1)

Summary of Non-Redundant Representatives

What is a Non-Redundant Representative?

S100 Count Entries in S100 Family 2.60.120.200.14.1.1.1 (60)

What is a Non-Redundant Representative?

Why can't I have a multiple structural alignment of the whole superfamily?

What is an Close Structural Cluster?

What is a Distant Structural Cluster?

What is a Structural Neighbour?

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