Protein domains

group of eight neurotoxic proteins produced by Clostridium botulinum

conserved part of a protein

In molecular biology, luciferase is a generic term for the class of oxidative enzymes that produce bioluminescence, and is usually distinguished from a photoprotein. The name was first used by Raphaël Dubois who invented the words luciferin and luciferase, for the substrate and enzyme, respectively. Both words are derived from the Latin word lucifer, meaning "lightbearer", which in turn is derived from the Latin words for "light" (lux) and "to bring or carry" (ferre). Luciferases are widely used in biotechnology, for bioluminescence imaging microscopy and as reporter genes, for many of the sam

group of enzymes

Thaumatin (also known as talin) is a low-calorie sweetener and taste modifier. The protein is often used primarily for its flavor-modifying properties and not exclusively as a sweetener.

small structural protein motif found mostly in transcriptional genes

thumb|Image of CD4 co-receptor binding to MHC (Major Histocompatibility Complex) non-polymorphic region.

protein-coding gene in the species Homo sapiens

A homeobox is a DNA sequence, around 180 base pairs long, that regulates large-scale anatomical features in the early stages of embryonic development. Mutations in a homeobox may change large-scale anatomical features of the full-grown organism.

mammalian protein found in Homo sapiens

Motilin is a 22-amino acid polypeptide hormone in the motilin family that, in humans, is encoded by the MLN gene.

protein complex consisting of two chains of platelet-derived growth factor (PDGF) subunits

protein domain

The selectins (cluster of differentiation 62 or CD62) are a family of cell adhesion molecules (or CAMs). All selectins are single-chain transmembrane glycoproteins that share similar properties to C-type lectins due to a related amino terminus and calcium-dependent binding. Selectins bind to sugar moieties and so are considered to be a type of lectin, cell adhesion proteins that bind sugar polymers.

thumb|right|Trimeric Hemerythrin Protein Complex () Hemerythrin (also spelled haemerythrin; , ) is an oligomeric protein responsible for oxygen (O2) transport in the marine invertebrate phyla of priapulids, brachiopods, and in the annelid worm clades Magelona and Sipuncula. Myohemerythrin is a monomeric O2-binding protein found in the muscles of marine invertebrates. Hemerythrin and myohemerythrin are essentially colorless when deoxygenated, but turn a violet-pink in the oxygenated state.

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.]]

mammalian protein found in Homo sapiens

InterPro Family

mammalian protein found in Homo sapiens

exotoxin

Hemolysins or haemolysins are lipids and proteins that cause lysis of red blood cells by disrupting the cell membrane. Although the lytic activity of some microbe-derived hemolysins on red blood cells may be of great importance for nutrient acquisition, many hemolysins produced by pathogens do not cause significant destruction of red blood cells during infection. However, hemolysins are often capable of lysing red blood cells in vitro.

group of mitochondrial proteins involved in the respiratory chain

Monooxygenases are enzymes that incorporate one hydroxyl group (−OH) into substrates in many metabolic pathways. In this reaction, the two atoms of dioxygen are reduced to one hydroxyl group and one H2O molecule by the concomitant oxidation of NAD(P)H. One important subset of the monooxygenases, the cytochrome P450 omega hydroxylases, is used by cells to metabolize arachidonic acid (i.e. eicosatetraenoic acid) to the cell signaling molecules, 20-hydroxyeicosatetraenoic acid or to reduce or totally inactivate the activate signaling molecules for example by hydroxylating leukotriene B4 to 20-hyd

transcription regulator protein

class of enzymes

class of enzymes

InterPro Domain

Phospholamban, also known as PLN or PLB, is a micropeptide protein that in humans is encoded by the PLN gene. Phospholamban is a 52-amino acid integral membrane protein that regulates the calcium (Ca2+) pump in cardiac muscle cells.

thumb|Hypothetical model of the tetraspanin function

type of glutamate receptor

A bromodomain is an approximately 110 amino acid protein domain that recognizes acetylated lysine residues, such as those on the N-terminal tails of histones. Bromodomains, as the "readers" of lysine acetylation, are responsible in transducing the signal carried by acetylated lysine residues and translating it into various normal or abnormal phenotypes. Their affinity is higher for regions where multiple acetylation sites exist in proximity. This recognition is often a prerequisite for protein-histone association and chromatin remodeling. The domain itself adopts an all-α protein fold, a bundl

chemical compound

protein fold

enzymes involved in base excision repair

Chromodomains are evolutionarily conserved protein domains found across a wide variety of eukaryotic species. Some chromodomain-containing genes have multiple alternative splicing isoforms that omit the chromodomain entirely. They are prominent in chromatin-associated proteins, such as the Polycomb-group (PcG) proteins and Heterochromatin Protein 1 (HP1), where they function as methylated lysine readers involved in gene regulation and chromatin remodeling, facilitating both gene silencing and activation by modifying chromatin structure. Chromodomain-containing proteins also bind methylated his

InterPro Domain

class of transport proteins

Colipase, abbreviated CLPS, is a protein co-enzyme that counteracts the inhibitory effect of intestinal bile acid on the enzymatic activity of pancreatic lipase. It is secreted by the pancreas in an inactive form, procolipase, which is activated in the intestinal lumen by trypsin.

Rhodanese is a mitochondrial enzyme that detoxifies cyanide (CN−) by converting it to thiocyanate (SCN−, also known as "rhodanate"). In enzymatology, the common name is listed as thiosulfate sulfurtransferase (). The diagram on the right shows the crystallographically-determined structure of rhodanese.

class of enzymes

The enzyme cutinase (systematic name: cutin hydrolase, EC 3.1.1.74) is a member of the hydrolase family. It catalyzes the following reaction: R1COOR2 + H2O -> R1COOH + R2OH

Annexin is a common name for a group of cellular proteins. They are mostly found in eukaryotic organisms (animals, plants and fungi).

InterPro Domain

EF-Tu (elongation factor thermo unstable) is a prokaryotic elongation factor responsible for catalyzing the binding of an aminoacyl-tRNA (aa-tRNA) to the ribosome. It is a G-protein, and facilitates the selection and binding of an aa-tRNA to the A-site of the ribosome. As a reflection of its crucial role in translation, EF-Tu is one of the most abundant and highly conserved proteins in prokaryotes. It is found in eukaryotic mitochondria as TUFM.

Thrombospondins (TSPs) are a family of secreted glycoproteins with antiangiogenic functions. Due to their dynamic role within the extracellular matrix they are considered matricellular proteins. The first member of the family, thrombospondin 1 (THBS1), was discovered in 1971 by Nancy L. Baenziger.

class of enzymes

InterPro Domain

350px|thumb|Mevalonate pathway

class of enzymes

InterPro Domain

InterPro Domain

Synaptobrevins (synaptobrevin isotypes 1-2, also called VAMP1 and VAMP2) are small integral membrane proteins of secretory vesicles with molecular weight of 18 kilodalton (kDa) that are part of the vesicle-associated membrane protein (VAMP) family.

protein-coding gene in the species Homo sapiens

type of enzyme

protein toxins produced by insect species

InterPro Domain

class of enzymes

class of enzymes

InterPro Family