Protein superfamilies

large protein family of receptors that detect molecules outside the cell and activate internal signal transduction pathways and cellular responses

conserved part of a protein

homodimeric protein enzyme of 86 kilodaltons

The globins are a superfamily of heme-containing globular proteins, involved in binding and/or transporting oxygen. These proteins all incorporate the globin fold, a series of eight alpha helical segments. Two prominent members include myoglobin and hemoglobin. Both of these proteins reversibly bind oxygen via a heme prosthetic group. They are widely distributed in many organisms.

small structural protein motif found mostly in transcriptional genes

group of proteins that share a common evolutionary origin, reflected by similarity in their sequence

200px|thumb|The λ repressor of bacteriophage lambda employs two helix-turn-helix motifs (left; green) to bind [[DNA (right; blue and red). The λ repressor protein in this image is a dimer.]]

family of proteins involved in vesicle fusion

InterPro family

database that hierarchical categories protein structures based on structural and evolutionary relationships

protein structural motif found in proteins that bind nucleotides

InterPro Domain

proteins with structural motif that forms an α/β horseshoe fold

large protein superfamily of cell surface and soluble proteins

protein fold

InterPro Domain

group of proteins that share a common evolutionary origin, reflected by similarity in their structure

The lipocalins are a family of proteins which transport small hydrophobic molecules such as steroids, bilins, retinoids, and lipids, and most lipocalins are also able to bind to complexed iron (via siderophores or flavonoids) as well as heme. They share limited regions of sequence homology and a common tertiary structure architecture. This is an eight stranded antiparallel beta barrel with a repeated + 1 topology enclosing an internal ligand binding site.

In structural biology, a beta-propeller (β-propeller) is a type of all-β protein architecture characterized by 4 to 8 highly symmetrical blade-shaped beta sheets arranged toroidally around a central axis. Together the beta-sheets form a funnel-like active site.

cell surface receptors that bind tumor necrosis factor and trigger changes which influence the behavior of cells

InterPro Domain

protein motif that binds to specific sequences of DNA, in for example a Nuclear receptor

InterPro Family

InterPro Domain

protein domain

In molecular biology, the HMG-box (high-mobility group box) is a protein domain which is involved in DNA binding. The domain is composed of approximately 75 amino acid residues that collectively mediate the DNA-binding of chromatin-associated high-mobility group proteins. HMG-boxes are present in many transcription factors and chromatin-remodeling complexes, where they can mediate non-sequence or sequence-specific DNA binding.

type of protein fold

protein family

database of protein domains structures

protein structural domains, modules that function in the targeting of proteins to membranes

protein and genome structural and functional annotation database