Protein Family Models

inosine-5'-monophosphate dehydrogenase catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the rate-limiting step in the de novo synthesis of guanine nucleotides

Date:

2024-01-12

ligand-gated ion channel (LIC or LGIC) is a member of a family of neurotransmitter receptors vital for communication throughout the nervous system

Date:

2023-12-19

Date:

2023-12-12

Date:

2023-12-12

This family appears to be the cytoplasmic domain of the calcium-activated chloride-channel, anoctamin, protein. It is responsible for creating the homodimeric architecture of the chloride-channel proteins. (from Pfam)

Date:

2023-12-12

Barttin is a family of mammalian proteins that are chloride ion channel beta-subunits crucial for renal Cl-re-absorption and inner ear K+ secretion. Bartter syndrome is a term covering a heterogeneous group of autosomal recessive salt-losing nephropathies that are caused by disturbed transepithelial sodium chloride re-absorption in the distal nephron. Mutations in the BCD proteins lead to sensorial deafness. (from Pfam)

Date:

2023-12-12

The CLCA family of calcium-activated chloride channels has been identified in many epithelial and endothelial cell types as well as in smooth muscle cells [1] and has four or five putative transmembrane regions. Additionally to their role as chloride channels some CLCA proteins function as adhesion molecules and may also have roles as tumour suppressors [2]. This protein cleaves itself into an N-terminal portion and a C-terminal portion. The N-terminus contains an HEXXHXXXGXXDE motif which is essential for proteolytic cleavage [3-4]. (from Pfam)

Date:

2023-12-12

Members of this family adopt an alpha-helical structure consisting of two four-helix bundles. They are predominantly found in prokaryotic orange carotenoid protein, and carotenoid binding proteins [1]. (from Pfam)

Date:

2023-12-12

This family contains prenylcysteine lyases (EC:1.8.3.5) that are approximately 500 residues long. Prenylcysteine lyase is a FAD-dependent thioether oxidase that degrades a variety of prenylcysteines, producing free cysteine, an isoprenoid aldehyde and hydrogen peroxide as products of the reaction [1]. It has been noted that this enzyme has considerable homology with ClP55, a 55 kDa protein that is associated with chloride ion pumps [2]. (from Pfam)

Date:

2023-12-12

This family consists of several mid-1-related chloride channels. mid-1-related chloride channel (MCLC) proteins function as a chloride channel when incorporated in the planar lipid bilayer [1]. (from Pfam)

Date:

2023-12-12

This family contains chlorite dismutase enzymes of bacterial and archaeal origin. This enzyme catalyses the disproportionation of chlorite into chloride and oxygen [1]. Note that many family members are hypothetical proteins. (from Pfam)

Date:

2023-12-12

This short domain lies at the very N-terminus of many serotonin and other transporter proteins, eg SNF, Pfam:PF00209. (from Pfam)

Date:

2023-12-12

The family carries eight putative transmembrane domains, and, although it has no similarity to other known channel proteins, it is clearly a calcium-activated ionic channel. It is expressed in various secretory epithelia, the retina and sensory neurons, and mediates receptor-activated chloride currents in diverse physiological processes [1]. (from Pfam)

Date:

2023-12-12

Peptidoglycan synthesis (PG) biosynthesis involves the formation of peptidoglycan precursor lipid II (undecaprenyl-pyrophosphate-linked N-acetyl glucosamine-N-acetyl muramic acid-pentapeptide) on the cytosolic face of the cell membrane. Lipid II is then translocated across the membrane and its glycopeptide moiety becomes incorporated into the growing cell wall mesh. MviN, renamed as MurJ, is a lipid II flippase essential for cell wall peptidoglycan synthesis [1, 2]. MurJ belongs to the MVF (mouse virulence factor) family of MOP superfamily transporters, which also includes the MATE (multidrug and toxic compound extrusion) transporter and eukaryotic OLF (oligosaccharidyl-lipid flippase) families. In addition to the canonical MOP transporter core consisting of 12 transmembrane helices (TMs), MurJ has two additional C-terminal TMs (13 and 14) of unknown function. Structural analysis indicates that the N lobe (TMs 1-6) and C lobe (TMs 7-14) are arranged in an inward-facing N-shape conformation, rather than the outward-facing V-shape conformation observed in all existing MATE transporter structures. Furthermore, a hydrophobic groove is formed by two C-terminal transmembrane helices, which leads into a large central cavity that is mostly cationic. Mutagenesis studies, revealed a solvent-exposed cavity that is essential for function. Mutation of conserved residues (Ser17, Arg18, Arg24, Arg52, and Arg255) at the proximal site failed to complement MurJ function, consistent with the idea that these residues are important for recognizing the diphosphate and/or sugar moieties of lipid II. It has also been suggested that the chloride . TRUNCATED at 1650 bytes (from Pfam)

Date:

2023-12-12

This family of ion channels contains 10 or 12 transmembrane helices. Each protein forms a single pore. It has been shown that some members of this family form homodimers. In terms of primary structure, they are unrelated to known cation channels or other types of anion channels. Three ClC subfamilies are found in animals. ClC-1 (Swiss:P35523) is involved in setting and restoring the resting membrane potential of skeletal muscle, while other channels play important parts in solute concentration mechanisms in the kidney [3]. These proteins contain two Pfam:PF00571 domains. (from Pfam)

Date:

2023-12-12

CBS domains are small intracellular modules that pair together to form a stable globular domain [2]. This family represents a single CBS domain. Pairs of these domains have been termed a Bateman domain [6]. CBS domains have been shown to bind ligands with an adenosyl group such as AMP, ATP and S-AdoMet [5]. CBS domains are found attached to a wide range of other protein domains suggesting that CBS domains may play a regulatory role making proteins sensitive to adenosyl carrying ligands. The region containing the CBS domains in Cystathionine-beta synthase is involved in regulation by S-AdoMet [4]. CBS domain pairs from AMPK bind AMP or ATP [5]. The CBS domains from IMPDH and the chloride channel CLC2 bind ATP [5]. (from Pfam)

Date:

2023-12-12

Human bestrophin is a chloride channel, while the Klebsiella pneumoniae homolog KpBest1 is a sodium channel.

Date:

2023-12-12

ClC family voltage-gated chloride channel protein containing a C-terminal CBS pair domain, catalyzes the selective flow of Cl(-) ions across the cellular membrane

Date:

2023-08-15

Members of this domain family are highly variable in architecture, and found in both prokaryotes and eukaryotes. Prokaryotic members include proteins with C-terminal sorting signals for processing by rhombosortases and myxosortases and eventual surface attachment. Eukaryotic member proteins include human calcium-activated chloride channel regulator 4.

Date:

2023-07-22

CLCAs, named for calcium-activated chloride channel bCLCA1, are proteins that resemble certain zinc-dependent metalloproteases in fold by lacking the signature HEXXH motifs. The CLCA_X family, described by this model, was identified based on weak similarities by Lenart, et al. as a notable CLCA-like family with a consistent architecture. The C-terminal half of the CLCA_X family was later described as the LPD1 domain (Large polyvalent protein-associated domain 1 - see PF18796) in a study of domains found within a variety of different architectures in larger proteins of phage and conjugative elements.

Date:

2023-07-14