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Search results 201 to 300 out of 1733 for Was

Category restricted to ProteinDomain (x)

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Categories

Category: ProteinDomain
Type Details Score
Protein Domain
Type: Family
Description: Islet cell autoantigen 69kDa (ICA69) or islet cell autoantigen 1 was identified with a group of type 1 diabetes-related islet autoantigens []. ICA69 is enriched in the Golgi complex, and its N-terminal half contains a BAR-domain []. ICA69 forms heteromeric BAR-domain complexes with another cytosolic lipid-binding protein, PICK1. Together they are key regulators of the formation and maturation of insulin granules [].
Protein Domain
Type: Family
Description: This entry represents serine/threonine-protein kinase 40 (STK40), also known as SINK-homologous inhibitory kinase (SHIK), which acts as a negative regulator of NF-kappa-B and p53-mediated gene transcription []. It It was identified as a protein related to SINK, a p65-interacting protein that inhibits p65 phosphorylation by the catalytic subunit of PKA, thereby inhibiting transcriptional competence of NF-kappaB.
Protein Domain
Type: Domain
Description: The RimM protein is essential for efficient processing of 16S rRNA []. It was shown to have affinity for free ribosomal 30S subunits but not for 30S subunits in the 70S ribosomes []. RimM contains a characteristic N-terminal domain and a PRC-barrel C-terminal domain, linked by an unstructured region []. The N-terminal domain folds into a closed β-barrel structure.
Protein Domain
Type: Family
Description: The DNA phosphorothioate modification system dnd (DNA instability during electrophoresis) recently has been shown to provide a modification essential to a restriction system. This protein family was detected by Partial Phylogenetic Profiling as linked to dnd, and its members usually are clustered with the dndABCDE genes.
Protein Domain
Type: Family
Description: This entry includes bacterial CYTH-domain containing proteins such as NeuTTM () from Nitrosomonas europaea []and CthTTM () from Clostridium thermocellum []They both have a high PPPase activity (though CthTM was less specific) but neither had any significant adenylyl cyclase activity [].CYTH domain proteins act on triphosphorylated substrates and require at least one divalent metal cation for catalysis [].
Protein Domain
Type: Family
Description: SPG5 (stationary phase protein 5) was identified as a protein required for survival at high temperature during stationary phase in Saccharomyces cerevisiae []. SPG5 is a positive regulator of the proteasome that is strongly induced in the stationary phase. It is critical for survival of cells that have ceased to proliferate due to nutrient limitation [].
Protein Domain
Type: Family
Description: This entry includes scytlidoglutamic peptidase (MEROPS identifier G01.001). The enzyme is active at acidic pH but is not inhibited by pepstatin, which led to it being considered a pepstatin-insensitive aspartic peptidase []. It was shown from the crystal structure that the active site residues are a glutamate (E) and glutamine (Q) [], and the name "eqolysin"was proposed for this family [].
Protein Domain
Type: Homologous_superfamily
Description: The ba3-type cytochrome c oxidase from Thermus thermophilus is known as a two subunit enzyme. From its crystal structure, it was discovered that an additional transmembrane helix, subunit IIa, spans the membrane. This subunit consists of 34 residues forming one helix across the membrane. The presence of this subunit seems to be important for the function of cytochrome c oxidases [].
Protein Domain
Type: Homologous_superfamily
Description: Hypothetical archaeal and bacterial proteins make up this superfamily. A few proteins are annotated as being potential metal-binding proteins, and in fact the members of this family have four highly conserved cysteine residues, but no further literature evidence was found in this regard. The structure of Clostridium perfringens protein CPE0013 has been solved ().
Protein Domain
Type: Family
Description: Hypothetical archaeal and bacterial proteins make up this family. A few proteins are annotated as being potential metal-binding proteins, and in fact the members of this family have four highly conserved cysteine residues, but no further literature evidence was found in this regard.
Protein Domain
Type: Family
Description: These sequences are derived from a number of hypothetical plant proteins. The region in question is approximately 270 amino acids long. Some members of this family are annotated as yeast pheromone receptor proteins AR781 but no literature was found to support this.
Protein Domain
Type: Domain
Description: The SUZ domain is a conserved RNA-binding domain found in eukaryotes and enriched in positively charged amino acids. It was first characterised in the Caenorhabditis elegans protein SZY-20 where it has been shown to bind RNA and allow their localization to the centrosome [].
Protein Domain
Type: Domain
Description: This domain is found in septin and tuftelin-interacting protein (STIP) and tuftelin-interacting protein 11 (TFIP11). STIP is essential for embryogenesis in Caenorhabditis elegans []. Tuftelin-interacting protein 11 is a component of the spliceosome involved in spliceosome disassembly []. TFIP11 was first identified in a yeast two-hybrid screening as a protein interacting with tuftelin, one of the presumed enamel matrix proteins [].
Protein Domain
Type: Domain
Description: This entry represents a reasonably well conserved core region of a family of phage tail proteins. The member from phage TP901-1 was characterised as a tail length tape measure protein in that a shortened form of the protein leads to phage with proportionately shorter tails [].
Protein Domain
Type: Family
Description: This family previously was designated pyruvate formate-lyase, but it now appears that members include the B12-independent glycerol dehydratase. This family includes the YbiW and PflD proteins of E. coli, described as isoforms of pyruvate-formate lyase found in a limited number additional species. PFL catalyses the reaction pyruvate + CoA ->acetyl-CoA + formate, which is a step in the fermentation of glucose.
Protein Domain
Type: Homologous_superfamily
Description: The RimM protein is essential for efficient processing of 16S rRNA []. It was shown to have affinity for free ribosomal 30S subunits but not for 30S subunits in the 70S ribosomes []. RimM contains a characteristic N-terminal domain and a PRC-barrel C-terminal domain, linked by an unstructured region []. The N-terminal domain folds into a closed β-barrel structure.
Protein Domain
Type: Family
Description: Neurensin-1 is a vesicular membrane protein expressed exclusively in brain that may play an important role in vesicular organelles transport and nerve signals []. Neurensin-2 is also expressed in neural cells, but with a different intracellular localisation: neurensin-1 was found mainly in neuritic processes, while neurensin-2 is found in cell bodies [].
Protein Domain
Type: Family
Description: Transmembrane (TMEM)-176A and 176B proteins are closely related to MS4A (membrane-spanning 4-domains subfamily A) proteins []. Their levels are significantly elevated in certain cancers [, ]. TMEM176B (LR8, Torid, Clast1) is broadly expressed, but was up regulated in antigen presenting cells in a rat model of allograft tolerance []. Their role in the immune system is unclear.
Protein Domain
Type: Family
Description: The proteins in this entry, which include YgiB, are functionally uncharacterised, however, transcription of ygiB is induced upon biofilm formation compared to planktonic growth in both exponential and stationary phase. Induction of expression was found to be dependent on the presence of the F plasmid []. Biofilm formation is impaired in mutants of ygiB [].
Protein Domain
Type: Family
Description: Members of this radical SAM protein family are HemZ, a protein involved in coproporphyrinogen III decarboxylation. Alternative names for this enzyme (EC ) include coproporphyrinogen dehydrogenase and oxygen-independent coproporphyrinogen III oxidase. The family is related to, but distinct from HemN, and in Bacillus subtilis was shown to be connected to peroxide stress and catalase formation [].
Protein Domain
Type: Family
Description: This entry represents putative lysis proteins from Bacteriophage MS2 and Bacteriophage BZ13.The bacteriophage MS2 lysin protein was identified as an overlapping cistron in the bacteriophage MS2 RNA []. This proteins induces the formation of specific membrane adhesion sites between the inner and outer membranes, apparently leading to host cell lysis. Lysis may be performed via activation of host murein hydrolases [, ].
Protein Domain
Type: Family
Description: Pescadillo (PES) protein was first identified as an essential protein for zebrafish embryonic development []. It is conserved from yeasts to humans. Pescadillo homologues are involved in embryonic development and ribosome biogenesis [, ]. It has been linked to chromosomal instability and cancer [, ].
Protein Domain
Type: Family
Description: Members of this are family are a B12-binding domain/radical SAM domain protein required for 3-methylhopanoid production []. Activity was confirmed by mutant phenotype by disrupting this gene in Methylococcus capsulatus strain Bath. This protein family should only occur in genomesthat encode a squalene-hopene cyclase.
Protein Domain
Type: Family
Description: Scara5 is a ferritin receptor that mediates non-transferrin iron delivery. It binds serum ferritin and then stimulates its endocytosis from the cell surface. It was identified as a cell type-specific alternatively mechanism of iron traffic during organogenesis []. It has been classified as belonging to class A scavenger receptors [].
Protein Domain
Type: Family
Description: Triadin was first identified from rabbit skeletal muscle sarcoplasmic reticulum as an abundant single transmembrane protein []. It binds to ryanodine receptor and calsequestrin in a Ca2+-dependent manner []. Later, several triadin isoforms produced by the alternative splicing of a single TRDN gene were identified [, ]. These isoforms have different localisations and binding partners [].
Protein Domain
Type: Repeat
Description: This putative domain is found at the N-terminal of a large number of bacterial proteins. Its adhesive function was described in Lactobacillus reuteri serine-rich repeat proteins []. Structure predictions show it is composed of a β-solenoid repeat related to Pectate lyase.
Protein Domain
Type: Domain
Description: This entry represents a domain found N-terminal to repeating stalk domains in bacterial surface proteins. The structure model of this domain consists out of seven β-strands within two β-sheets, similar to the RrgB pilus backbone, which was again described to correspond to the collagen binding domain. The position of this domain at the tip of bacterial surface proteins suggests an adhesive function.
Protein Domain
Type: Family
Description: Expression from a human cytomegalovirus early promoter (E1.7) has been shown to be activated in trans by the IE2 gene product. Although the IE1 gene product alone had no effect on this early viral promoter, maximal early promoter activity was detected when both IE1 and IE2 gene products were present []. The IE1 protein from cytomegalovirus is also known as UL123.
Protein Domain
Type: Family
Description: Phospholipase B (PLB) catalyses the hydrolytic cleavage of both acylester bonds of glycerophospholipids. This family of PLB enzymes has been identified in mammals, flies and nematodes but not in yeast [, ]. In Drosophila this protein was named LAMA for laminin ancestor since it is expressed in the neuronal and glial precursors that surround the lamina [].
Protein Domain
Type: Domain
Description: A conserved motif was identified in the LOC118487 protein was called the CHCH motif. Alignment of this protein with related members showed the presence of three subgroups of proteins, which are called the S (Small), N (N-terminal extended) and C (C-terminal extended) subgroups. All three sub-groups of proteins have in common that they contain a predicted conserved [coiled coil 1]-[helix 1]-[coiled coil 2]-[helix 2]domain (CHCH domain). Within each helix of the CHCH domain, there are two cysteines present in a C-X9-C motif. The N-group contains an additional double helix domain, and each helix contains the C-X9-C motif. This family contains a number of characterised proteins: Cox19 protein - a nuclear gene of Saccharomyces cerevisiae, codes for an 11kDa protein (Cox19p) required for expression of cytochrome oxidase. Because cox19 mutants are able to synthesise the mitochondrial and nuclear gene products of cytochrome oxidase, Cox19p probably functions post-translationally during assembly of the enzyme. Cox19p is present in the cytoplasm and mitochondria, where it exists as a soluble intermembrane protein. This dual location is similar to what was previously reported for Cox17p, a low molecular weight copper protein thought to be required for maturation of the CuA centre of subunit 2 of cytochrome oxidase. Cox19p have four conserved potential metal ligands, these are three cysteines and one histidine. Mrp10 - belongs to the class of yeast mitochondrial ribosomal proteins that are essential for translation []. Eukaryotic NADH-ubiquinone oxidoreductase 19kDa (NDUFA8) subunit []. The CHCH domain was previously called DUF657 [].
Protein Domain
Type: Family
Description: The UbiB family has five mammalian members (ADCK1-5), which are classified as atypical kinases. COQ8A (ADCK3) is an UbiB protein associated with ubiquinone (Coenzyme Q, CoQ) biosynthesis and ataxia []. Although COQ8A was predicted to be a protein kinase, it lacks canonical protein kinase activity [, ]. Instead, COQ8A has ATPase activity and interacts with lipid CoQ intermediates [].
Protein Domain
Type: Family
Description: This entry consist of uncharacterised proteins from bacteria, such as YqeY from Bacillus subtilis, and Aim41/YOR215C from yeast. Altered inheritance of mitochondria protein 41 (Aim41/YOR215C) is a protein of unknown function. It was detected in highly purified mitochondria in high-throughput studies, and null mutant displays reduced frequency of mitochondrial genome loss []. Aim41/YOR215C is not an essential gene.
Protein Domain
Type: Family
Description: Mitoguardin (Miga) was first identified in flies as a mitochondrial outer-membrane protein that promotes mitochondrial fusion. Later, the mammalian Miga homologues, Miga1 and Miga2, were identified. They are found to promote mitochondrial fusion by regulating mitochondrial phospholipid metabolism via MitoPLD [, ].
Protein Domain
Type: Family
Description: This entry represents the mRNA transport factor GFD1. GFD1 is a coiled-coiled protein of unknown function, which was identified as a high-copy suppressor of mutant alleles of ATP-dependent RNA helicase DBP5, which is involved in mRNA export from the nucleus. It may also play an important role in a late stage of NAB2-mRNA export [].
Protein Domain
Type: Family
Description: YggL from E.coli was recently characterised and it interacts with ribosome subunits 50S and 70S. It is a 50S-binding protein likely to be involved in particle assembly. It is a small protein extremely conserved in Gammaproteobacteria but also present in orders Burkholderiales and Neisseriales from Betaproteobacteria [].
Protein Domain
Type: Family
Description: This entry includes a group of RNA recognition motif domain containing proteins, including RBM27 and RBM26. The function of RBM27 is not clear.RBM26, also known as cutaneous T-cell lymphoma (CTCL) tumor antigen se70-2, was identified as a cutaneous lymphoma (CL)-associated antigen []. It contains two RNA recognition motifs (RRMs). The RRMs may play some functional roles in RNA-binding or protein-protein interactions.
Protein Domain
Type: Family
Description: This is a family of integral membrane proteins including Rdf complex subunits RnfA and RnfE []and Na+-translocating NADH:ubiquinone oxidoreductase (Na+-NQR) subunits NqrD and NqrE []. The Rnf complex is a ferredoxin:NAD+ oxidoreductase that appears to translocate different ions (protons or sodium) in different bacteria []. The similarity of RnfD to NADH-ubiquinone oxidoreductases was previously noted [].
Protein Domain
Type: Family
Description: This family of proteins are mitochondrial 18kDa proteins that are often misannotated as carbonic anhydrases. It was shown that knockdown of MTP18 protein results in a cytochrome c release from mitochondria and consequently leads to apoptosis []. Over expression studies suggest that MTP18 is required for mitochondrial fission [].
Protein Domain
Type: Family
Description: In infected cells, UL55 is associated with the nuclear matrix, and found adjacent to compartments containing the capsid protein ICP35. UL55 was not detected in assembled virions. It is thought that UL55 may play a role in virion assembly or maturation [].
Protein Domain
Type: Family
Description: Interleukin-1 receptor-associated kinase 1-binding protein 1 (IRAK1BP1, also known as SIMPL) was originally identified in a yeast two-hybrid screen system []. In mice, IRAK1BP1 inhibits inflammation by promoting nuclear translocation of NF-kappaB p50 []. In Haliotis diversicolor, IRAK1BP1 plays an important role in the adult abalone immune system and might be essential in embryo and larval development in abalone [].
Protein Domain
Type: Domain
Description: This entry represents lipid desaturase domains. The TMEM189 protein is a plasmanylethanolamine desaturase enzyme [, ]. It was previously described as the B domain or probable localisation domain of the transmembrane protein TMEM189 []which in some mammals is fused with Kua ubiquitin-conjugation E2 enzyme proteins []. The domain is also found on fatty acid saturase FAD4 in Arabidopsis [].
Protein Domain
Type: Family
Description: This protein was identified as being up-regulated during meiosis in Schizosaccharomyces pombe, where it is required for correct meiotic chromosome segregation []. This family of proteins is found in largely in plants and fungi. Proteins in this family are typically between 128 and 920 amino acids in length.
Protein Domain
Type: Family
Description: This entry represents archaeal phenylalanyl-tRNA ligase alpha chains. It was shown to act in a proposed pathway of tRNA(Cys) indirect aminoacylation, resulting in Cys biosynthesis from O-phosphoserine, in certain archaea. It charges tRNA(Cys) with O-phosphoserine. The pscS gene product converts the phosphoserine to Cys [].
Protein Domain
Type: Family
Description: This is a family of bacterial proteasome cofactors. The family member from Mycobacterium tuberculosis, protein Rv3780, was shown to form rings and cap proteasome core particles. It enhanced peptide and protein degradation by proteasomes in an adenosine triphosphate (ATP)-independent manner, promoting degradation of the heat shock protein repressor HspR [].
Protein Domain
Type: Family
Description: This entry represents bacterial members of the uncharacterised protein family UPF0761. It includes the E. coli gene product of yihY, and was previously thought to be a family of tRNA-processing ribonuclease BN proteins []. This has been shown to be incorrect [].
Protein Domain
Type: Homologous_superfamily
Description: All methionyl-tRNA synthetases (MetRS) display a highly conserved catalytic core with a Rossmann fold, the two halves of which are linked by a connectivepeptide (CP) []. In E. coli MetRS, a tightly bound zinc ion was shown to play a role in the folding of the CP region []. This entry represents the CP region.
Protein Domain
Type: Domain
Description: This entry represents the C-terminal domain of PSI proteins from Arabidopsis. This domain is found associated with DUF3475 ().PSI1 was identified as a gene that is co-expressed with the phytosulfokine (PSK) receptor genes PSKR1 and PSKR2 in Arabidopsis thaliana. PSI proteins are plant-specific and promote growth [].
Protein Domain
Type: Family
Description: Caleosins are a family of lipid-associated proteins that are ubiquitous in plants and true fungi. In plants, caleosinss are Ca(2+)-binding oil-body surface proteins []. Later, caleosin was identified as a putative peroxygenase, which is involved in oxylipin metabolism during biotic and abiotic stress responses in Arabidopsis []. The calcium binding domain is probably related to the calcium-binding EF-hands motif .
Protein Domain
Type: Domain
Description: This entry represents the C-terminal domain of bacterial proteins that bind plasminogen (PgbA and PgbB). This activity was identified in Helicobacter pylori where it is thought to contribute to the virulence of this bacterium. Both PgbA and PgbB are surface-exposed proteins that mediate binding to plasminogen such that it can be converted into plasmin in the presence of a plasminogen activator [].
Protein Domain
Type: Family
Description: This family consists of several leukocyte cell-derived chemotaxin 2 (LECT2) proteins. LECT2 is a liver-specific protein which is thought to be linked to hepatocyte growth although the exact function of this protein is unknown []. It contains an M23 metalloendopeptidase fold, but was found to be catalytically inactive as a metalloendopeptidase [].
Protein Domain
Type: Family
Description: This entry represents the centrosomal protein of 19kDa (CEP19, also known as C3orf34) from eukaryotes. It was identified by complementary proteomics methods []. It associates with the mother centriole in early interphase. It localises to spindle poles during mitosis, and to distinct foci oriented towards the midbody at telophase []. Its function is not clear.
Protein Domain
Type: Family
Description: This protein through the member sll1638 from Synechocystis sp. (strain PCC 6803), was shown to be part of the cyanobacteria photosystem II. It is homologous to (but quite diverged from) the chloroplast PsbQ protein, called oxygen-evolving enhancer protein 3 (OEE3). We designate this cyanobacteria protein PsbQ by homology.
Protein Domain
Type: Family
Description: Cytokine-like protein 1 (CYTL1) was identified as a secretory protein expressed in CD34+ haemopoietic cells []. CYTL1 seems to regulate chondrogenesis and is required for the maintenance of cartilage homeostasis [, ]. It may also work as a regulatory factor in embryo implantation []. This family of proteins, CYTL1, is found in vertebrates. Proteins have two conserved sequence motifs: PPTCYSR and DDC.
Protein Domain
Type: Domain
Description: This entry represents the N-terminal domain of the bacterial proteins (PgbA) that bind plasminogen. This activity was identified in In Helicobacter pylori where it is thought to contribute to the virulence of this bacterium. Both PgbA and PgbB are surface-exposed proteins that mediate binding to plasminogen such that it can be converted into plasmin in the presence of a Pg activator [].
Protein Domain
Type: Family
Description: RalR was originally thought to inhibit restriction modification []but instead is part of a toxin/antitoxin system and functions as a non-specific DNase []. Toxin RalR functions as a non-specific endonuclease that cleaves methylated and unmethylated DNA. The adjacent gene product, RalA (for RalR antitoxin), functions as an antitoxin for RalR.
Protein Domain
Type: Family
Description: Members of this protein family show essentially full-length homology, cyclically permuted, to YjhT from Escherichia coli. YjhT was shown to act as a mutarotase for sialic acid, and by this ability to be able to act as a virulence factor. Members of the YjhT family () and this cyclically-permuted family have multiple copies of the β-propeller-forming Kelch repeat.
Protein Domain
Type: Family
Description: This family consists of several Calicivirus VP2 proteins []. VP2 is a minor capsid protein encoded by all caliciviruses. It forms a large portal-like assembly at a unique three-fold axis of symmetry, following receptor engagement. This assembly-which was not detected in undecorated virions-is formed of twelve copies of VP2, arranged with their hydrophobic N terminus pointing away from the virion surface.
Protein Domain
Type: Family
Description: The general transcription termination factor CPSF1 is ubiquitously distributed among Archaea (aCPSF1). It was recently characterised as a ribonuclease essential for transcription termination to ensure programmed transcriptome and an optimal growth and physiology. It associates with archaeal RNAP and cleaves the transcript at the 3'-end, downstream the uridine-rich sequences recognised by its N-terminal KH-domain, a characteristic RNA binding domain [, ].
Protein Domain
Type: Family
Description: This entry represents 4-oxalocrotonate decarboxylase. This protein is characterised (indirectly) in Pseudomonas sp. (strain CF600) and was inactive except when co-expressed with DmpE, 2-oxopent-4-enoate hydratase, a homologous protein from the same operon []. Both of these enzymes are active in the degradation of catechol, a common intermediate in the degradation of aromatic compounds such as benzoate, toluene, phenol, dimethylphenol (dmp), salicylate, etc.
Protein Domain
Type: Family
Description: PimA, a member of a large family of acyl-CoA ligases, is found in a characteristic operon pimFABCDE for the metabolism of pimelate and related compounds. It is found, so far, in Bradyrhizobium japonicum and several strains of Rhodopseudomonas palustris. PimA from R. palustris was shown to be active as a CoA ligase for C(7) to C(14) dicarboxylates and fatty acids [].
Protein Domain
Type: Family
Description: ARHGEF10 is a Rho guanine nucleotide exchange factor that may play a role in developmental myelination of peripheral nerves []. It was found to regulate mitotic spindle formation and play a role in the regulation of the cell division cycle [].
Protein Domain
Type: Family
Description: This uncharacterised protein family was identified, by the method of partial phylogenetic profiling, as having a matching phylogenetic distribution to that of the photosynthetic reaction centre of the alpha-proteobacterial type. It is nearly always encoded near other photosynthesis-related genes, including puhA.
Protein Domain
Type: Family
Description: This protein family is restricted to a subset of endospore-forming bacteria, such as Bacillus subtilis, all of which are in the Firmicutes (low-GC Gram-positive) lineage. It is a minor SASP (small, acid-soluble spore protein) designated SspI. The gene in B. subtilis was previously designated ysfA.
Protein Domain
Type: Family
Description: This protein family is restricted to a subset of endospore-forming bacteria such as Bacillus subtilis, all of which are in the Firmicutes (low-GC Gram-positive) lineage. Although previously designated tlp (thioredoxin-like protein), the B. subtilis protein was shown to be a minor small acid-soluble spore protein SASP, unique to spores. The motif E[VIL]XDE near the C terminus probably represents at a germination protease cleavage site.
Protein Domain
Type: Domain
Description: This entry represents the AAA domain found in Strawberry notch protein.Strawberry notch proteins carry DExD/H-box groups and helicase C-terminal domains. These proteins promote the expression of diverse targets, potentially through interactions with transcriptional activator or repressor complexes []. Strawberry notch was first identified in Drosophila where functions downstream of Notch and regulates gene expression during development [, ].
Protein Domain
Type: Family
Description: This family describes mitochondrial transcription rescue factor 1 (MTRES1) which was previously known as C6orf203. MTRES1 has been shown to protect the cell from mitochondrial RNA loss during stress by associating with mitochondrial RNA polymerase POLRMT, and increasing mitochondrial transcription, without changing the stability of mitochondrial RNAs [].
Protein Domain
Type: Family
Description: L-threonine-O-3-phosphate decarboxylase (CobD) was shown to decarboxylate L-threonine O-3-phosphate to yield (R)-1-amino-2-propanol O-2-phosphate, which is the precursor for the linkage between the nucleotide loop and the corrin ring in the biosynthesis of cobalamin []. The molecule is a dimer where each subunit consists of a large and small domain []. This family contains pyridoxal phosphate-binding class II aminotransferases closely related to histidinol-phosphateaminotransferase (HisC).
Protein Domain
Type: Domain
Description: This entry represents a C-terminal domain associated with prokaryotic alpha-amylases. It adopts a secondary structure consisting of an eight-stranded antiparallel β-sheet containing a Greek key motif []. The function of this domain was studied in the Alpha-amylase from Geobacillus thermoleovorans (), showing this region plays an essential role raw starch binding [].
Protein Domain
Type: Family
Description: Cadherins are transmembrane proteins that mediate cell-cell adhesion in animals []. Cadherin-16 (CDH16) or kidney-specific (Kps) cadherin was first described as a kidney-specific adhesion molecule []and thereafter also found expressed in the thyroid gland. CDH16 colocalises with CDH1/E-cadherin on the basolateral plasma membrane of thyrocytes, and might play a role during thyroid development [].
Protein Domain
Type: Family
Description: This entry consists of ABC transporter permease proteins associated with urea transport and metabolism. They are encoded in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity [].
Protein Domain
Type: Family
Description: This entry consists of ABC transporter ATP-binding proteins associated with urea transport and metabolism. They are encoded in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity [].
Protein Domain
Type: Family
Description: This entry consists of ABC transporter ATP-binding proteins associated with urea transport and metabolism. They are encoded in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity [].
Protein Domain
Type: Domain
Description: This entry corresponds to the KH0 domain from the FMRP protein []. This is a divergent KH domain that was discovered through solving the structure of an N-terminal fragment of the FMRP protein []. KH0 does not have the canonical G-X-X-G motif between helices A and B []. It has been suggested that this domain may be involved in RNA binding [].
Protein Domain
Type: Domain
Description: The N-terminal domain of Gasdermins can bind membrane lipids, phosphoinositides and cardiolipin, and exhibits membrane-disrupting cytotoxicity. It was shown to be able to lyse phosphoinositide/cardiolipin-containing liposomes and form pores on membranes []. This entry represents the pore forming domain of gasdermin.
Protein Domain
Type: Family
Description: Nodulin-related protein 1 (NRP1) may play a role in the negative-feedback regulation of the abscisic acid (ABA) synthesis pathway. Overexpression of NRP1 enhanced susceptibility to heat stress and was accompanied of decreased accumulation of ABA after heat treatment []. The function of NRP2 is not clear.
Protein Domain
Type: Family
Description: Kiwellin was identified as a kiwi fruit allergenic protein. It can be processed into an N-terminal 4kDa peptide known as Kissper, which can form an anion-selective pore []. Its structure has been solved []. This entry also includes Kiwellin-like proteins from rice and other plants.
Protein Domain
Type: Family
Description: This entry represents regulatory subunit 6B (gene name PSMC4 or Rpt3) of the 26S proteasome, which is a component of the 19S proteasome cap []. PSMC4 is one of the ATPases that form a heterohexameric ring for unfolding ubiquitinated proteins targeted for degradation by the proteasome, and was initially identified as Tat-binding protein 7 [].
Protein Domain
Type: Repeat
Description: The thrombospondin repeat is a short aspartate rich repeat which binds tocalcium ions. The repeat was initially identified in thrombospondin proteins that contained 7 of these repeats []. The repeat lacks defined secondary structure [].This entry represents the type 3 thrombospondin repeat found in proteins of the thrombospondin family and related repeats present in other types of proteins.
Protein Domain
Type: Family
Description: Phylogenetically, the SLC23 family belongs to the nucleobase-ascorbate transporter (NAT) family, which consists of the Na(+)-dependent vitamin C transporters SVCT1 (SLC23A1) and SVCT2 (SLC23A2), as well as the orphan transporter SVCT3 (SLC23A3) []. The murine SLC23A3 gene was originally cloned from mouse yolk sac []. However, the function of SVCT3 remains unknown.
Protein Domain
Type: Homologous_superfamily
Description: The Epstein-Barr virus (strain GD1) nuclear antigen 1 (EBNA1) binds to and activates DNA replication from the latent origin of replication. The crystal structure of the DNA-binding and dimerization domains were solved [], and it was found that EBNA1 appears to bind DNA via two independent regions, the core and the flanking DNA-binding domains. This DNA-binding domain has a ferredoxin-like fold.
Protein Domain
Type: Homologous_superfamily
Description: This is the N-terminal domain of a family of virion proteins which contains a zinc finger domain. Its structure consists of a small β-hairpin with CxH motif and a short helix with CxxC motif. This protein was recently shown to inhibit cellular nucleocytoplasmic transport [].
Protein Domain
Type: Family
Description: This family includes the HopA1 effector protein from Pseudomonas syringae. Structurally this protein has an alpha + beta fold []. The effector protein HopA1 was shown to affect the EDS1 complex by binding EDS1 directly and activating the immune response signaling pathway.
Protein Domain
Type: Family
Description: This entry represents a protein family specific to the genus Plasmodium. The merozoite surface antigen 2 (MSA-2) may play a role in the merozoite attachment to the erythrocyte. This protein was proposed to be a candidate for a protective vaccine against malaria [, ].
Protein Domain
Type: Domain
Description: This domain was originally found in the C-terminal moiety of the Cp-7 lysin (lysozyme, ) encoded by Bacteriophage Cp-7 []. It is also found in the cell wall hydrolases of human and life-stock pathogens. CW_7 repeats make up a cell wall binding motif [].
Protein Domain
Type: Domain
Description: Myosin XVb, also called KIAA1783, was named based on its similarity with myosin XVa. It is a transcribed and unprocessed pseudogene whose predicted amino acid sequence contains mutated or deleted amino acid residues that are normally conserved and important for myosin function [].
Protein Domain
Type: Domain
Description: The function to find (FIIND) domain was initially discovered in two proteins, NLRP1 (aka NALP1, CARD7, NAC, DEFCAP) and CARD8 (aka TUCAN, Cardinal) []. NLRP1 is a member of the Nod-like receptor (NLR) protein superfamily and is involved in apoptosis and inflammation. To date, it is the only NLR protein known to have a FIIND domain. The FIIND domain is also present in the CARD8 protein where, like in NLRP1, it is followed by a C-terminal CARD domain. Both proteins are described to form an "inflammasome", a macro-molecular complex able to process caspase 1 and activate pro-IL1beta []. The FIIND domain is present in only a very small subset of the kingdom of life, comprising primates, rodents (mouse, rat), carnivores (dog) and a few more, such as horse. Publications describing the newly discovered NLRP1 protein failed to identify it as a separate domain; for example, it was taken as part of the adjacent leucine rich repeat domain (LRR) []. Upon discovery of CARD8 it was noted that the N-terminal region shared significant sequence identity with an undescribed region in NLRP1 []. Before getting its final name, FIIND [], this domain was termed NALP1-associated domain (NAD) []. This is a peptidase domain of the ZU5 superfamily that is predicted to be involved in autoproteolytic cleavage [].
Protein Domain
Type: Family
Description: Proteins in this entry are the IcmQ component of Dot/Icm secretion systems, as found in the obligate intracellular pathogens Legionella pneumophila and Coxiella burnetii. While this system resembles type IV secretion systems and has been called a form of type IV, the literature now seems to favor calling this the Dot/Icm system. This protein was shown to be essential for translocation [].
Protein Domain
Type: Family
Description: MOSMO, also known as Atthog (attenuator of hedgehog) in mouse, acts as a negative regulator of hedgehog (Hh) signaling, probably by promoting internalization and subsequent degradation of Smoothened (SMO). SMO is an oncoprotein that transduces the Hh signal across the membrane. In the absence of Atthog, SMO was stabilized at the cell surface and concentrated in the ciliary membrane [].
Protein Domain
Type: Family
Description: This family includes the RloB protein that is found within a bacterial restriction modification operon. It also includes the AbiLii protein that is found as part of a plasmid encoded phage abortive infection mechanism []. Deletion of part of the abiLii gene was sufficient to abolish phage resistance. Other proteins in this family are annotated as CRISPR Csm2 proteins.
Protein Domain
Type: Domain
Description: This entry represents the periplasmic core domain found in a variety of ABC transporters. The structure of this family has been solved for the MacB protein []. Some structural similarity was found to the periplasmic domain of the AcrB multidrug efflux transporter.
Protein Domain
Type: Domain
Description: CpG-methylation is a frequently occurring epigenetic modification of vertebrate genomes resulting in transcriptional repression. This domain is found at the C terminus of the methyl-CpG-binding domain (MBD) containing proteins MBD2 []and MBD3 []. The latter was shown to not bind directly to methyl-CpG DNA but rather interact with components of the NuRD/Mi2 complex [], an abundant deacetylase complex.
Protein Domain
Type: Domain
Description: This domain was first characterised as the C-terminal domain of Pab87 serine protease from Pyrococcus abyssi []. The domain is reported to play a crucial role in Pab87 octamerisation and active site compartmentalisation. Its up-and-down 8-stranded β-barrel 3D structure is reminiscent of the one found in lipocalins.
Protein Domain
Type: Homologous_superfamily
Description: This domain superfamily was determined from the crystal structure of a protein of unknown fuction from Bacillus subtilis. The domain is found in a family of proteins whose function is unknown; however it is found in the family represented by .
Protein Domain
Type: Domain
Description: This domain was determined from the crystal structure of a protein of unknown function from Rhizobium meliloti (Sinorhizobium meliloti). The domain is found in a family, which consists of several short bacterial proteins of around 100 residues in length. The function of this domain is unknown.
Protein Domain
Type: Homologous_superfamily
Description: This domain superfamily is found in a family of proteins with unknown function. YerB interacts with PcrA helicase. The interaction is not essential for cell viability or repair of UV-induced lesions []. The domain structure was determined from the crystal structure of the YerB protein from Bacillus subtilis.
Protein Domain
Type: Family
Description: This family includes the MJ0458 protein from Methanocaldococcus jannaschii (Methanococcus jannaschii), which was predicted to be related to aspartokinase and uridylate kinase []. MJ0458 has been characterised and renamed as MfnE. It functions as a 5-(aminomethyl)-3-furanmethanol phosphate kinase in the methanofuran biosynthetic pathway [].
Protein Domain
Type: Family
Description: The Tsx gene resides at the X-inactivation centre and once thought to encode a protein expressed in testis. However, this was disputed upon further analysis. ORF and immunostaining analysis concluded that Tsx may be non-coding. Tsx long transcript is abundantly expressed in meiotic germ cells, embryonic stem cells, and brain [].
Protein Domain
Type: Domain
Description: Thiosulphate:quinone oxidoreductase (TQO) catalyses one of the early steps in elemental sulphur oxidation. A novel TQO enzyme was purified from the thermo-acidophilic archaeon Acidianus ambivalens and shown to consist of a large subunit (DoxD) and a smaller subunit (DoxA). The DoxD- and DoxA-like two subunits are fused together in a single polypeptide in .
Protein Domain
Type: Family
Description: Beta-crystallins are the most abundant water-soluble proteins in the eye lens. Beta-crystallin B2 was first described as a structural protein of the ocular lens. Mutations in the beta-crystallin B2 gene (CRYBB2) are associated with congenital cataracts [, ]. However, beta-crystallin B2 is also expressed in several regions of the mammalian brain and has a role in hippocampal function and behavioral phenotypes in mice [].
Protein Domain
Type: Family
Description: This protein is has been characterised as both a phosphoserine phosphatase and a phosphoserine:homoserine phosphotransferase []. In Pseudomonas aeruginosa, where the characterisation was done, a second phosphoserine phosphatase (SerB) and a second homoserine kinase (thrB) are found, but in Fibrobacter succinogenes neither are present.