S100 Family: 3.90.230.10.1.1.1.1

Representative domain: 2gg2A00

Classification Lineage (3.90.230.10.1.1.1.1)

CATH Code	Level Description	Links
3	Alpha Beta
3.90	Alpha-Beta Complex
3.90.230	Creatine Amidinohydrolase
3.90.230.10	Creatinase/methionine aminopeptidase superfamily	Gene3D
3.90.230.10.1
3.90.230.10.1.1
3.90.230.10.1.1.1
3.90.230.10.1.1.1.1

Summary of Non-Redundant Representatives


-	-	-	-	-	-	-	-	24

Non-Redundant Representatives (24)
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 3.90.230.10.1.1.1.1 (24)

CATH code	Domain ID	Keywords
3.90.230.10.1.1.1.1.1	2gg2A00	Methionine aminopeptidase, Methionyl aminopeptidase., metalloaminopeptidase activity, Escherichia coli K-12, protein binding, ferrous iron binding, protein initiator methionine removal, methionyl aminopeptidase [EC:3.4.11.18]
3.90.230.10.1.1.1.1.2	2ggcA00	Escherichia coli K-12, protein binding, Methionine aminopeptidase, Methionyl aminopeptidase., metalloaminopeptidase activity, protein initiator methionine removal, methionyl aminopeptidase [EC:3.4.11.18], ferrous iron binding
3.90.230.10.1.1.1.1.3	2gg9A00	Escherichia coli K-12, protein binding, metalloaminopeptidase activity, Methionine aminopeptidase, Methionyl aminopeptidase., methionyl aminopeptidase [EC:3.4.11.18], protein initiator methionine removal, ferrous iron binding
3.90.230.10.1.1.1.1.4	2gg7A00	ferrous iron binding, methionyl aminopeptidase [EC:3.4.11.18], protein initiator methionine removal, metalloaminopeptidase activity, Methionine aminopeptidase, Methionyl aminopeptidase., protein binding, Escherichia coli K-12
3.90.230.10.1.1.1.1.5	2gg0A00	metalloaminopeptidase activity, Methionine aminopeptidase, Methionyl aminopeptidase., protein binding, Escherichia coli K-12, ferrous iron binding, methionyl aminopeptidase [EC:3.4.11.18], protein initiator methionine removal
3.90.230.10.1.1.1.1.6	2gg3A00	metalloaminopeptidase activity, Methionine aminopeptidase, Methionyl aminopeptidase., protein binding, Escherichia coli K-12, ferrous iron binding, methionyl aminopeptidase [EC:3.4.11.18], protein initiator methionine removal
3.90.230.10.1.1.1.1.7	1xnzA00	methionyl aminopeptidase [EC:3.4.11.18], Methionine aminopeptidase, Methionyl aminopeptidase., Escherichia coli O157:H7
3.90.230.10.1.1.1.1.8	2evcA00	Escherichia coli K-12, protein binding, Methionine aminopeptidase, Methionyl aminopeptidase., metalloaminopeptidase activity, protein initiator methionine removal, methionyl aminopeptidase [EC:3.4.11.18], ferrous iron binding
3.90.230.10.1.1.1.1.9	2p9aA00	Escherichia coli K-12, protein binding, metalloaminopeptidase activity, Methionine aminopeptidase, Methionyl aminopeptidase., methionyl aminopeptidase [EC:3.4.11.18], protein initiator methionine removal, ferrous iron binding
3.90.230.10.1.1.1.1.10	2q93A00	protein binding, Escherichia coli K-12, Methionine aminopeptidase, Methionyl aminopeptidase., metalloaminopeptidase activity, protein initiator methionine removal, methionyl aminopeptidase [EC:3.4.11.18], ferrous iron binding
3.90.230.10.1.1.1.1.11	2q96A00	ferrous iron binding, protein initiator methionine removal, methionyl aminopeptidase [EC:3.4.11.18], Methionine aminopeptidase, Methionyl aminopeptidase., metalloaminopeptidase activity, Escherichia coli K-12, protein binding
3.90.230.10.1.1.1.1.12	2q94A00	protein initiator methionine removal, methionyl aminopeptidase [EC:3.4.11.18], ferrous iron binding, Escherichia coli K-12, protein binding, Methionine aminopeptidase, Methionyl aminopeptidase., metalloaminopeptidase activity
3.90.230.10.1.1.1.1.13	2bb7A00	Escherichia coli O157:H7, Methionine aminopeptidase, Methionyl aminopeptidase., methionyl aminopeptidase [EC:3.4.11.18]
3.90.230.10.1.1.1.1.14	2evmA00	Escherichia coli K-12, protein binding, metalloaminopeptidase activity, Methionine aminopeptidase, Methionyl aminopeptidase., methionyl aminopeptidase [EC:3.4.11.18], protein initiator methionine removal, ferrous iron binding
3.90.230.10.1.1.1.1.15	2evoA00	ferrous iron binding, methionyl aminopeptidase [EC:3.4.11.18], protein initiator methionine removal, metalloaminopeptidase activity, Methionine aminopeptidase, Methionyl aminopeptidase., Escherichia coli K-12, protein binding
3.90.230.10.1.1.1.1.16	2evoB00	ferrous iron binding, protein initiator methionine removal, methionyl aminopeptidase [EC:3.4.11.18], Methionine aminopeptidase, Methionyl aminopeptidase., metalloaminopeptidase activity, protein binding, Escherichia coli K-12
3.90.230.10.1.1.1.1.17	2p98A00	protein initiator methionine removal, methionyl aminopeptidase [EC:3.4.11.18], ferrous iron binding, protein binding, Escherichia coli K-12, Methionine aminopeptidase, Methionyl aminopeptidase., metalloaminopeptidase activity
3.90.230.10.1.1.1.1.18	2q95A00	Escherichia coli K-12, protein binding, Methionine aminopeptidase, Methionyl aminopeptidase., metalloaminopeptidase activity, protein initiator methionine removal, methionyl aminopeptidase [EC:3.4.11.18], ferrous iron binding
3.90.230.10.1.1.1.1.19	2p99A00	protein binding, Escherichia coli K-12, Methionine aminopeptidase, Methionyl aminopeptidase., metalloaminopeptidase activity, protein initiator methionine removal, methionyl aminopeptidase [EC:3.4.11.18], ferrous iron binding
3.90.230.10.1.1.1.1.20	2gg8A00	ferrous iron binding, protein initiator methionine removal, methionyl aminopeptidase [EC:3.4.11.18], Methionine aminopeptidase, Methionyl aminopeptidase., metalloaminopeptidase activity, protein binding, Escherichia coli K-12
3.90.230.10.1.1.1.1.21	2q92A00	protein initiator methionine removal, methionyl aminopeptidase [EC:3.4.11.18], ferrous iron binding, Escherichia coli K-12, protein binding, Methionine aminopeptidase, Methionyl aminopeptidase., metalloaminopeptidase activity
3.90.230.10.1.1.1.1.22	2gg5A00	protein binding, Escherichia coli K-12, metalloaminopeptidase activity, Methionine aminopeptidase, Methionyl aminopeptidase., methionyl aminopeptidase [EC:3.4.11.18], protein initiator methionine removal, ferrous iron binding
3.90.230.10.1.1.1.1.23	2ggbA00	metalloaminopeptidase activity, Methionine aminopeptidase, Methionyl aminopeptidase., protein binding, Escherichia coli K-12, ferrous iron binding, methionyl aminopeptidase [EC:3.4.11.18], protein initiator methionine removal
3.90.230.10.1.1.1.1.24	1matA00	ferrous iron binding, methionyl aminopeptidase [EC:3.4.11.18], protein initiator methionine removal, metalloaminopeptidase activity, Methionine aminopeptidase, Methionyl aminopeptidase., protein binding, Escherichia coli K-12

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=3.90.230.10.1.1.1.1

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: 3.90.230.10.1.1.1.1

Classification Lineage (3.90.230.10.1.1.1.1)

Summary of Non-Redundant Representatives

What is a Non-Redundant Representative?

S100 Count Entries in S100 Family 3.90.230.10.1.1.1.1 (24)

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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