Fig. 2: Domain clusters.
From: ProtCID: a data resource for structural information on protein interactions

a (ACT)/(ACT) domain-level cluster containing 14 different chain Pfam architectures. First image shows all domain pairs; each subsequent image shows each chain architecture with the ACT domains in green and cyan. The non-domain segments are colored in light gray. This coloring schema applies to all protein–protein interface figures unless otherwise stated. b Three tRNA-synt_2d domain clusters occur in a family of tetrameric tRNA synthetases. The dimer of first cluster is colored in green and cyan, the dimer of cluster 2 is colored in green and purple, and the dimer of cluster 3 is colored in green and yellow. The colors of domains are same in tetramers. One hetero-tetramer (PDB: 1B70, stoichiometry A2B2, symmetry: C2) and one homo-tetramer (PDB: 2DU3 [https://doi.org/10.2210/pdb2DU3/pdb], stoichiometry A4, symmetry: D2) are shown. c (Ras)/(RA) is a diff-Pfam domain interface cluster with 8 crystal forms and 10 entries. All Ras domains are single chain domains from three UniProts (RASH_HUMAN, RAP1A_HUMAN and RAP1B_HUMAN). RA domains are in four different chain Pfam architectures from eight UniProts (AB1IP_MOUSE, AFAD_MOUSE, GNDS_RAT, GRB14_HUMAN, KRIT1_HUMAN, PLCE1_HUMAN, RAIN_HUMAN and RASF5_MOUSE). d Two intra-chain domain interface clusters of AMP-binding and AMP-binding_C with different domain/domain orientations. These two clusters have nine common UniProts (LUCI_PHOPY, Q8GN86_9BURK, LCFCS_THET8, ACS2A_HUMAN, 4CL2_TOBAC, MENE_BACSU, LGRA_BREPA, J9VFT1_CRYNH, E5XP76_9ACTN) and two common entries (PDB: 5IFI [https://doi.org/10.2210/pdb5IFI/pdb] and 5K85 [https://doi.org/10.2210/pdb5K85/pdb]). These two entries have one UniProt J9VFT1_CRYNH (Acetyl-coenzyme A synthetase from Cryptococcus neoformans), consisting of three monomers each. The chain A and B monomers are in the first conformation and the chain C monomers are in the second conformation. The AMP-binding_C domain of chain C monomer is colored in blue.