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In molecular biology mir-153 microRNA is a short RNA molecule. MicroRNAs function to regulate the expression levels of other genes by several mechanisms. | https://en.wikipedia.org/wiki/Mir-153_microRNA_precursor_family |
In molecular biology mir-190 microRNA is a short RNA molecule. MicroRNAs function is to regulate the expression levels of other genes by several mechanisms. | https://en.wikipedia.org/wiki/Mir-190_microRNA_precursor_family |
In molecular biology mir-198 microRNA is a short RNA molecule. MicroRNAs function to regulate the expression levels of other genes by several mechanisms. | https://en.wikipedia.org/wiki/Mir-198_microRNA_precursor_family |
In molecular biology mir-202 microRNA is a short RNA molecule. MicroRNAs function to regulate the expression levels of other genes by several mechanisms. The pre-miR-202 in the mouse genome is located fully within an exon, whereas in human it lies across a splice junction. This implies that human miR-202 is exposed to a negative regulation by splicing, whereas murine miR-202 is not. | https://en.wikipedia.org/wiki/Mir-202_microRNA_precursor_family |
In molecular biology mir-216 microRNA is a short RNA molecule. MicroRNAs function to regulate the expression levels of other genes by several mechanisms. | https://en.wikipedia.org/wiki/Mir-216_microRNA_precursor_family |
In molecular biology mir-23 microRNA is a short RNA molecule. MicroRNAs function to regulate the expression levels of other genes by several mechanisms. | https://en.wikipedia.org/wiki/Mir-23_microRNA_precursor_family |
In molecular biology mir-241 microRNA is a short RNA molecule. MicroRNAs function to regulate the expression levels of other genes by several mechanisms. | https://en.wikipedia.org/wiki/Mir-241_microRNA_precursor_family |
In molecular biology mir-275 microRNA is a short RNA molecule. MicroRNAs function to regulate the expression levels of other genes by several mechanisms. | https://en.wikipedia.org/wiki/Mir-275_microRNA_precursor_family |
In molecular biology mir-277 microRNA is a short RNA molecule. MicroRNAs function to regulate the expression levels of other genes by several mechanisms. | https://en.wikipedia.org/wiki/Mir-277_microRNA_precursor_family |
In molecular biology mir-278 microRNA is a short RNA molecule belonging to a class of molecules referred to as microRNAs. These function to regulate the expression levels of other genes by several mechanisms, primarily binding to their target at its 3'UTR. | https://en.wikipedia.org/wiki/Mir-278_microRNA_precursor_family |
In molecular biology mir-299 microRNA is a short RNA molecule. MicroRNAs function to regulate the expression levels of other genes by several mechanisms. | https://en.wikipedia.org/wiki/Mir-299_microRNA_precursor_family |
In molecular biology mir-301 microRNA is a short RNA molecule. MicroRNAs function to regulate the expression levels of other genes by several mechanisms. | https://en.wikipedia.org/wiki/Mir-301_microRNA_precursor_family |
In molecular biology mir-305 microRNA is a short RNA molecule. MicroRNAs function to regulate the expression levels of other genes by several mechanisms. | https://en.wikipedia.org/wiki/Mir-305_microRNA_precursor_family |
In molecular biology mir-322 microRNA is a short RNA molecule. MicroRNAs function to regulate the expression levels of other genes by several mechanisms. | https://en.wikipedia.org/wiki/Mir-322_microRNA_precursor_family |
In molecular biology mir-326 microRNA is a short RNA molecule. MicroRNAs function to regulate the expression levels of other genes by several mechanisms. | https://en.wikipedia.org/wiki/Mir-326_microRNA_precursor_family |
In molecular biology mir-330 microRNA is a short RNA molecule. MicroRNAs function to regulate the expression levels of other genes by several mechanisms. | https://en.wikipedia.org/wiki/Mir-330_microRNA_precursor_family |
In molecular biology mir-331 microRNA is a short RNA molecule. MicroRNAs function to regulate the expression levels of other genes by several mechanisms. | https://en.wikipedia.org/wiki/Mir-331_microRNA_precursor_family |
In molecular biology mir-345 microRNA is a short RNA molecule. MicroRNAs function to regulate the expression levels of other genes by several mechanisms. | https://en.wikipedia.org/wiki/Mir-345_microRNA_precursor_family |
In molecular biology mir-346 microRNA is a short RNA molecule. MicroRNAs function to regulate the expression levels of other genes by several mechanisms. | https://en.wikipedia.org/wiki/Mir-346_microRNA_precursor_family |
In molecular biology mir-350 microRNA is a short RNA molecule. MicroRNAs function to regulate the expression levels of other genes by several mechanisms. | https://en.wikipedia.org/wiki/Mir-350_microRNA_precursor_family |
In molecular biology mir-361 microRNA is a short RNA molecule. MicroRNAs function to regulate the expression levels of other genes by several mechanisms. For example, miR-361-5p might act as a suppressor in triple-negative breast cancer (TNBC) by targeting RQCD1 to inhibit the EGFR/PI3K/Akt signaling pathway. | https://en.wikipedia.org/wiki/Mir-361_microRNA_precursor_family |
In molecular biology mir-363 microRNA is a short RNA molecule. MicroRNAs function to regulate the expression levels of other genes by several mechanisms. | https://en.wikipedia.org/wiki/Mir-363_microRNA_precursor_family |
In molecular biology mir-365 microRNA is a short RNA molecule. MicroRNAs function to regulate the expression levels of other genes by several mechanisms. | https://en.wikipedia.org/wiki/Mir-365_microRNA_precursor_family |
In molecular biology mir-370 microRNA is a short RNA molecule. MicroRNAs function to regulate the expression levels of other genes by several mechanisms. This microRNA, mir-370-3p, has been shown to play a role in heart failure. The upregulation of mir-370-3p in the sinus node leads to downregulation of the pacemaker ion channel, HCN4, and thus downregulation of the corresponding ionic current, which causes sinus bradycardia. | https://en.wikipedia.org/wiki/Mir-370_microRNA_precursor_family |
In molecular biology mir-374 microRNA is a short RNA molecule. MicroRNAs function to regulate the expression levels of other genes by several mechanisms. | https://en.wikipedia.org/wiki/Mir-374_microRNA_precursor_family |
In molecular biology mir-383 microRNA is a short RNA molecule. MicroRNAs function to regulate the expression levels of other genes by several mechanisms. | https://en.wikipedia.org/wiki/Mir-383_microRNA_precursor_family |
In molecular biology mir-384 microRNA is a short RNA molecule. MicroRNAs function to regulate the expression levels of other genes by several mechanisms. | https://en.wikipedia.org/wiki/Mir-384_microRNA_precursor_family |
In molecular biology mir-390 microRNA is a short RNA molecule. MicroRNAs function to regulate the expression levels of other genes by several mechanisms. | https://en.wikipedia.org/wiki/Mir-390_microRNA_precursor_family |
In molecular biology mir-396 microRNA is a short RNA molecule. MicroRNAs function to regulate the expression levels of other genes by several mechanisms. | https://en.wikipedia.org/wiki/Mir-396_microRNA_precursor_family |
In molecular biology mir-397 microRNA is a short RNA molecule. MicroRNAs function to regulate the expression levels of other genes by several mechanisms. | https://en.wikipedia.org/wiki/Mir-397_microRNA_precursor_family |
In molecular biology mir-398 microRNA is a short RNA molecule. MicroRNAs function to regulate the expression levels of other genes by several mechanisms. | https://en.wikipedia.org/wiki/Mir-398_microRNA_precursor_family |
In molecular biology mir-430 microRNA is a short RNA molecule. MicroRNAs function to regulate the expression levels of other genes by several mechanisms. | https://en.wikipedia.org/wiki/Mir-430_microRNA_precursor_family |
In molecular biology mir-455 microRNA is a short RNA molecule. MicroRNAs function to regulate the expression levels of other genes by several mechanisms. | https://en.wikipedia.org/wiki/Mir-455_microRNA_precursor_family |
In molecular biology mir-5 microRNA is a short RNA molecule. MicroRNAs function to regulate the expression levels of other genes by several mechanisms. mir-5 has been implicated in regulation of VEGF in an experiment where a plasmid containing a cluster of mir-5, mir-10 and mir-7 was shown to down-regulate VEGF by 75%. mir-5 in chicken has been implicated in targeting genes involved in metabolism. | https://en.wikipedia.org/wiki/Mir-5_microRNA_precursor_family |
In molecular biology mir-535 microRNA is a short RNA molecule. MicroRNAs function to regulate the expression levels of other genes by several mechanisms. | https://en.wikipedia.org/wiki/Mir-535_microRNA_precursor_family |
In molecular biology mir-542 microRNA is a short RNA molecule. MicroRNAs function to regulate the expression levels of other genes by several mechanisms. | https://en.wikipedia.org/wiki/Mir-542_microRNA_precursor_family |
In molecular biology mir-589 microRNA is a short RNA molecule. MicroRNAs function to regulate the expression levels of other genes by several mechanisms. | https://en.wikipedia.org/wiki/Mir-589_microRNA_precursor_family |
In molecular biology mir-598 microRNA is a short RNA molecule. MicroRNAs function to regulate the expression levels of other genes by several mechanisms. | https://en.wikipedia.org/wiki/Mir-598_microRNA_precursor_family |
In molecular biology mir-625 microRNA is a short RNA molecule. MicroRNAs function to regulate the expression levels of other genes by several mechanisms. Many microRNAs play important roles in cancer development and progression. | https://en.wikipedia.org/wiki/Mir-625_microRNA_precursor_family |
In molecular biology mir-632 microRNA is a short RNA molecule. MicroRNAs function to regulate the expression levels of other genes by several mechanisms. | https://en.wikipedia.org/wiki/Mir-632_microRNA_precursor_family |
In molecular biology mir-636 microRNA is a short RNA molecule. MicroRNAs function to regulate the expression levels of other genes by several mechanisms. | https://en.wikipedia.org/wiki/Mir-636_microRNA_precursor_family |
In molecular biology mir-661 microRNA is a short RNA molecule. MicroRNAs function to regulate the expression levels of other genes by several mechanisms. | https://en.wikipedia.org/wiki/Mir-661_microRNA_precursor_family |
In molecular biology mir-663 microRNA is a short RNA molecule. MicroRNAs function to regulate the expression levels of other genes by several mechanisms. | https://en.wikipedia.org/wiki/Mir-663_microRNA_precursor_family |
In molecular biology mir-71 microRNA is a short RNA molecule. MicroRNAs function to regulate the expression levels of other genes by several mechanisms. | https://en.wikipedia.org/wiki/Mir-71_microRNA_precursor_family |
In molecular biology mir-711 microRNA is a short RNA molecule. MicroRNAs function to regulate the expression levels of other genes by several mechanisms. | https://en.wikipedia.org/wiki/Mir-711_microRNA_precursor_family |
In molecular biology mir-84 microRNA is a short RNA molecule. MicroRNAs function to regulate the expression levels of other genes by several mechanisms. | https://en.wikipedia.org/wiki/Mir-84_microRNA_precursor_family |
In molecular biology mir-885 microRNA is a short RNA molecule. MicroRNAs function to regulate the expression levels of other genes by several mechanisms. | https://en.wikipedia.org/wiki/Mir-885_microRNA_precursor_family |
In molecular biology short linear motifs (SLiMs), linear motifs or minimotifs are short stretches of protein sequence that mediate protein–protein interaction.The first definition was given by Tim Hunt: "The sequences of many proteins contain short, conserved motifs that are involved in recognition and targeting activities, often separate from other functional properties of the molecule in which they occur. These motifs are linear, in the sense that three-dimensional organization is not required to bring distant segments of the molecule together to make the recognizable unit. The conservation of these motifs varies: some are highly conserved while others, for example, allow substitutions that retain only a certain pattern of charge across the motif." | https://en.wikipedia.org/wiki/Short_linear_motif |
In molecular biology the B-box-type zinc finger domain is a short protein domain of around 40 amino acid residues in length. B-box zinc fingers can be divided into two groups, where types 1 and 2 B-box domains differ in their consensus sequence and in the spacing of the 7-8 zinc-binding residues. Several proteins contain both types 1 and 2 B-boxes, suggesting some level of cooperativity between these two domains. | https://en.wikipedia.org/wiki/B-box_zinc_finger |
In molecular biology the BED-type zinc finger domain is a protein domain which was named after the Drosophila proteins BEAF and DREF, is found in one or more copies in cellular regulatory factors and transposases from plants, animals and fungi. The BED finger is an about 50 to 60 amino acid residues domain that contains a characteristic motif with two highly conserved aromatic positions, as well as a shared pattern of cysteines and histidines that is predicted to form a zinc finger. As diverse BED fingers are able to bind DNA, it has been suggested that DNA-binding is the general function of this domain. Some proteins known to contain a BED domain include animal, plant and fungi AC1 and Hobo-like transposases; Caenorhabditis elegans Dpy-20 protein, a predicted cuticular gene transcriptional regulator; Drosophila BEAF (boundary element-associated factor), thought to be involved in chromatin insulation; Drosophila DREF, a transcriptional regulator for S-phase genes; and tobacco 3AF1 and tomato E4/E8-BP1, light- and ethylene-regulated DNA binding proteins that contain two BED fingers. Most genes in this family are believed to have evolved from the hAT family of DNA transposons. | https://en.wikipedia.org/wiki/BED_zinc_finger |
In molecular biology the Bacterial Microcompartment (BMC) domain is a protein domain found in a variety of shell proteins, including CsoS1A, CsoS1B and CsoS1C of Thiobacillus neapolitanus (Halothiobacillus neapolitanus) and their orthologs from other bacteria. These shell proteins form the polyhedral structure of the carboxysome and related structures that plays a metabolic role in bacteria. The BMC domain consists of about 90 amino acid residues, characterized by β-α-β motif connected by a β-hairpin. | https://en.wikipedia.org/wiki/BMC_domain |
The majority of the shell proteins consist of a single BMC domain in each subunit, forming a hexameric structure that assembles to form the flat facets of the polyhedral shell. To date, two shell proteins were found to consist a tandem BMC domains, of which forms a trimeric structure, giving a pseudo-hexameric appearance. == References == | https://en.wikipedia.org/wiki/BMC_domain |
In molecular biology the DHHC domain is a protein domain that acts as an enzyme, which adds a palmitoyl chemical group to proteins in order to anchor them to cell membranes. The DHHC domain was discovered in 1999 and named after a conserved sequence motif found in its protein sequence. Roth and colleagues showed that the yeast Akr1p protein could palmitoylate Yck2p in vitro and inferred that the DHHC domain defined a large family of palmitoyltransferases. | https://en.wikipedia.org/wiki/DHHC_domain |
In mammals twenty three members of this family have been identified and their substrate specificities investigated. Some members of the family such as ZDHHC3 and ZDHHC7 enhance palmitoylation of proteins such as PSD-95, SNAP-25, GAP43, Gαs. Others such as ZDHHC9 showed specificity only toward the H-Ras protein. However, a recent study questions the involvement of classical enzyme-substrate recognition and specificity in the palmitoylation reaction. Several members of the family have been implicated in human diseases. | https://en.wikipedia.org/wiki/DHHC_domain |
In molecular biology the DM domain is a protein domain first discovered in the doublesex proteins of Drosophila melanogaster and is also seen in C. elegans and mammalian proteins. In D. melanogaster the doublesex gene controls somatic sexual differentiation by producing alternatively spliced mRNAs encoding related sex-specific polypeptides. These proteins are believed to function as transcription factors on downstream sex-determination genes, especially on neuroblast differentiation and yolk protein genes transcription.The DM domain binds DNA as a dimer, allowing the recognition of pseudopalindromic sequences . The NMR analysis of the DSX DM domain revealed a novel zinc module containing 'intertwined' CCHC and HCCC zinc-binding sites. The recognition of the DNA requires the carboxy-terminal basic tail which contacts the minor groove of the target sequence. | https://en.wikipedia.org/wiki/DM_domain |
In molecular biology the FGGY carbohydrate kinase family is a family of evolutionarily related carbohydrate kinase enzymes. These enzymes include L-fuculokinase EC 2.7.1.51 (gene fucK); gluconokinase EC 2.7.1.12 (gene gntK); glycerol kinase EC 2.7.1.30 (gene glpK); xylulokinase EC 2.7.1.17 (gene xylB); D-ribulose kinase EC 2.7.1.47 (gene FGGY/YDR109c); and L-xylulose kinase EC 2.7.1.53 (gene lyxK). These enzymes are proteins of from 480 to 520 amino acid residues. | https://en.wikipedia.org/wiki/FGGY_carbohydrate_kinase_family |
These enzymes consist of two domains. The N-terminal and C-terminal domains both adopt a ribonuclease H-like fold and are structurally related to each other. == References == | https://en.wikipedia.org/wiki/FGGY_carbohydrate_kinase_family |
In molecular biology the FYVE zinc finger domain is named after the four cysteine-rich proteins: Fab 1 (yeast orthologue of PIKfyve), YOTB, Vac 1 (vesicle transport protein), and EEA1, in which it has been found. FYVE domains bind phosphatidylinositol 3-phosphate, in a way dependent on its metal ion coordination and basic amino acids. The FYVE domain inserts into cell membranes in a pH-dependent manner. The FYVE domain has been connected to vacuolar protein sorting and endosome function. | https://en.wikipedia.org/wiki/FYVE_domain |
In molecular biology the L-like lectin domain is a protein domain found in lectins which are similar to the leguminous plant lectins. Lectins are structurally diverse proteins that bind to specific carbohydrates. This family includes the VIP36 and ERGIC-53 lectins. Although proteins containing this domain were originally identified as a family of animal lectins, there are also yeast representatives.ERGIC-53 is a 53kDa protein, localised to the intermediate region between the endoplasmic reticulum and the Golgi apparatus (ER-Golgi-Intermediate Compartment, ERGIC). | https://en.wikipedia.org/wiki/L-type_lectin_domain |
It was identified as a calcium-dependent, mannose-specific lectin. Its dysfunction has been associated with combined factors V and VIII deficiency, suggesting an important and substrate-specific role for ERGIC-53 in the glycoprotein-secreting pathway.The L-like lectin domain has an overall globular shape composed of a beta-sandwich of two major twisted antiparallel beta-sheets. The beta-sandwich comprises a major concave beta-sheet and a minor convex beta-sheet, in a variation of the jelly roll fold. == References == | https://en.wikipedia.org/wiki/L-type_lectin_domain |
In molecular biology the LysM domain is a protein domain found in a wide variety of extracellular proteins and receptors. The LysM domain is named after the Lysin Motif which was the original name given to the sequence motif identified in bacterial proteins. The region was originally identified as a C-terminal repeat found in the Enterococcus hirae muramidase. The LysM domain is found in a wide range of microbial extracellular proteins, where the LysM domain is thought to provide an anchoring to extracellular polysaccharides such as peptidoglycan and chitin. | https://en.wikipedia.org/wiki/LysM_domain |
LysM domains are also found in plant receptors, including NFP, the receptor for Nod factor which is necessary for the root nodule symbiosis between legumes and symbiotic bacteria. The LysM domain is typically between 44 and 65 amino acid residues in length. The structure of the LysM domain showed that it is composed of a pair of antiparallel beta strands separated by a pair of short alpha helices. | https://en.wikipedia.org/wiki/LysM_domain |
In molecular biology the MIZ-type zinc finger domain is a zinc finger-containing protein with homology to the yeast protein, Nfi-1. Miz1 is a sequence specific DNA binding protein that can function as a positive-acting transcription factor. Miz1 binds to the homeobox protein Msx2, enhancing the specific DNA-binding ability of Msx2. Other proteins containing this domain include the human pias family (protein inhibitor of activated STAT protein). | https://en.wikipedia.org/wiki/MIZ_zinc_finger |
The name MIZ is derived from Msx-interacting-zinc finger. The crystal structure of S. cerevisiae sumo e3 ligase siz1 containing this domain has been solved. == References == | https://en.wikipedia.org/wiki/MIZ_zinc_finger |
In molecular biology the MYND-type zinc finger domain is a conserved protein domain. The MYND domain (myeloid, Nervy, and DEAF-1) is present in a large group of proteins that includes RP-8 (PDCD2), Nervy, and predicted proteins from Drosophila, mammals, Caenorhabditis elegans, yeast, and plants. The MYND domain consists of a cluster of cysteine and histidine residues, arranged with an invariant spacing to form a potential zinc-binding motif. | https://en.wikipedia.org/wiki/MYND_zinc_finger |
Mutating conserved cysteine residues in the DEAF-1 MYND domain does not abolish DNA binding, which suggests that the MYND domain might be involved in protein-protein interactions. Indeed, the MYND domain of ETO/MTG8 interacts directly with the N-CoR and SMRT co-repressors. Aberrant recruitment of co-repressor complexes and inappropriate transcriptional repression is believed to be a general mechanism of leukemogenesis caused by the t(8;21) translocations that fuse ETO with the acute myelogenous leukemia 1 (AML1) protein. | https://en.wikipedia.org/wiki/MYND_zinc_finger |
ETO has been shown to be a co-repressor recruited by the promyelocytic leukemia zinc finger (PLZF) protein. A divergent MYND domain present in the adenovirus E1A binding protein BS69 was also shown to interact with N-CoR and mediate transcriptional repression. The current evidence suggests that the MYND motif in mammalian proteins constitutes a protein-protein interaction domain that functions as a co-repressor-recruiting interface. | https://en.wikipedia.org/wiki/MYND_zinc_finger |
In molecular biology the PIN domain is a protein domain that is about 130 amino acids in length. PIN domains function as nuclease enzymes that cleave single stranded RNA in a sequence- or structure-dependent manner.PIN domains contain four nearly invariant acidic residues. Crystal structures show these residues clustered together in the putative active site. In eukaryotes PIN domains are found in proteins involved in nonsense mediated mRNA decay, in proteins such as SMG5 and SMG6, and in processing of 18S ribosomal RNA. | https://en.wikipedia.org/wiki/PIN_domain |
The majority of PIN-domain proteins found in prokaryotes are the toxic components of toxin-antitoxin operons. These loci provide a control mechanism that helps free-living prokaryotes cope with nutritional stress. == References == | https://en.wikipedia.org/wiki/PIN_domain |
In molecular biology the PLAT domain is a protein domain that is found in a variety of membrane or lipid associated proteins. It is called the PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology) domain. The known structure of pancreatic lipase shows this domain binds to procolipase Pfam PF01114, which mediates membrane association. This domain forms a beta-sandwich composed of two β-sheets of four β-strands each. | https://en.wikipedia.org/wiki/PLAT_domain |
In molecular biology the SPR domain is a protein domain found in the Sprouty (Spry) and Spred (Sprouty related EVH1 domain) proteins. These have been identified as inhibitors of the Ras/mitogen-activated protein kinase (MAPK) cascade, a pathway crucial for developmental processes initiated by activation of various receptor tyrosine kinases. These proteins share a conserved, C-terminal cysteine-rich region, the SPR domain. This domain has been defined as a novel cytosol to membrane translocation domain. It has been found to be a PtdIns(4,5)P2-binding domain that targets the proteins to a cellular localization that maximizes their inhibitory potential. It also mediates homodimer formation of these proteins.The SPR domain can occur in association with the WH1 domain (see InterPro: IPR000697) (located in the N-terminus) in the Spred proteins. | https://en.wikipedia.org/wiki/SPR_domain |
In molecular biology the SeqA protein is found in bacteria and archaea. The function of this protein is highly important in DNA replication. The protein negatively regulates the initiation of DNA replication at the origin of replication, in Escherichia coli, OriC. | https://en.wikipedia.org/wiki/SeqA_protein |
Additionally the protein plays a further role in sequestration. The importance of this protein is vital, without its help in DNA replication, cell division and other crucial processes could not occur. This protein domain is thought to be part of a much larger protein complex which includes other proteins such as SeqB. | https://en.wikipedia.org/wiki/SeqA_protein |
In molecular biology the ZZ-type zinc finger domain is a type of protein domain that was named because of its ability to bind two zinc ions. These domains contain 4-6 Cys residues that participate in zinc binding (plus additional Ser/His residues), including a Cys-X2-Cys motif found in other zinc finger domains. These zinc fingers are thought to be involved in protein-protein interactions. The structure of the ZZ domain shows that it belongs to the family of cross-brace zinc finger motifs that include the PHD, RING, and FYVE domains. | https://en.wikipedia.org/wiki/ZZ_zinc_finger |
ZZ-type zinc finger domains are found in: Transcription factors P300 and CBP. Plant proteins involved in light responses, such as Hrb1. E3 ubiquitin ligases MEX and MIB2 (EC). | https://en.wikipedia.org/wiki/ZZ_zinc_finger |
Dystrophin and its homologuesSingle copies of the ZZ zinc finger occur in the transcriptional adaptor/coactivator proteins P300, in cAMP response element-binding protein (CREB)-binding protein (CBP) and ADA2. CBP provides several binding sites for transcriptional coactivators. The site of interaction with the tumour suppressor protein p53 and the oncoprotein E1A with CBP/P300 is a Cys-rich region that incorporates two zinc-binding motifs: ZZ-type and TAZ2-type. | https://en.wikipedia.org/wiki/ZZ_zinc_finger |
The ZZ-type zinc finger of CBP contains two twisted anti-parallel beta-sheets and a short alpha-helix, and binds two zinc ions. One zinc ion is coordinated by four cysteine residues via 2 Cys-X2-Cys motifs, and the third zinc ion via a third Cys-X-Cys motif and a His-X-His motif. The first zinc cluster is strictly conserved, whereas the second zinc cluster displays variability in the position of the two His residues. | https://en.wikipedia.org/wiki/ZZ_zinc_finger |
In Arabidopsis thaliana (Mouse-ear cress), the hypersensitive to red and blue 1 (Hrb1) protein, which regulating both red and blue light responses, contains a ZZ-type zinc finger domain.ZZ-type zinc finger domains have also been identified in the testis-specific E3 ubiquitin ligase MEX that promotes death receptor-induced apoptosis. MEX has four putative zinc finger domains: one ZZ-type, one SWIM-type and two RING-type. The region containing the ZZ-type and RING-type zinc fingers is required for interaction with UbcH5a and MEX self-association, whereas the SWIM domain was critical for MEX ubiquitination. | https://en.wikipedia.org/wiki/ZZ_zinc_finger |
In addition, the Cys-rich domains of dystrophin, utrophin and an 87kDa post-synaptic protein contain a ZZ-type zinc finger with high sequence identity to P300/CBP ZZ-type zinc fingers. In dystrophin and utrophin, the ZZ-type zinc finger lies between a WW domain (flanked by and EF hand) and the C-terminal coiled-coil domain. Dystrophin is thought to act as a link between the actin cytoskeleton and the extracellular matrix, and perturbations of the dystrophin-associated complex, for example, between dystrophin and the transmembrane glycoprotein beta-dystroglycan, may lead to muscular dystrophy. | https://en.wikipedia.org/wiki/ZZ_zinc_finger |
Dystrophin and its autosomal homologue utrophin interact with beta-dystroglycan via their C-terminal regions, which are composed of a WW domain, an EF hand domain, and a ZZ-type zinc finger domain. The WW domain is the primary site of interaction between dystrophin or utrophin and dystroglycan, while the EF hand and ZZ-type zinc finger domains stabilise and strengthen this interaction. == References == | https://en.wikipedia.org/wiki/ZZ_zinc_finger |
In molecular biology the fructosamine kinase family is a family of enzymes. This family includes eukaryotic fructosamine-3-kinase enzymes which may initiate a process leading to the deglycation of fructoselysine and of glycated proteins and in the phosphorylation of 1-deoxy-1-morpholinofructose, fructoselysine, fructoseglycine, fructose and glycated lysozyme. The family also includes ketosamine-3-kinases (KT3K). Ketosamines derive from a non-enzymatic reaction between a sugar and a protein. | https://en.wikipedia.org/wiki/Fructosamine_kinase_family |
Ketosamine-3-kinases (KT3K) catalyse the phosphorylation of the ketosamine moiety of glycated proteins. The instability of a phosphorylated ketosamine leads to its degradation, and KT3K is thus thought to be involved in protein repair.The function of the prokaryotic members of this group has not been established. However, several lines of evidence indicate that they may function as fructosamine-3-kinases (FN3K). | https://en.wikipedia.org/wiki/Fructosamine_kinase_family |
First, they are similar to characterised FN3K from mouse and human. Second, the Escherichia coli members are found in close proximity on the genome to fructose-6-phosphate kinase (PfkB). Last, FN3K activity has been found in the blue-green algae Anacystis montana indicating such activity-directly demonstrated in eukaryotes-is nonetheless not confined to eukaryotes. == References == | https://en.wikipedia.org/wiki/Fructosamine_kinase_family |
In molecular biology the nematode Her-1 protein is a protein which adopts an all-helical structure with two subdomains: amino acids 19-80 comprise a left-handed three-helix bundle with an overhand connection between the second and third helices, whilst amino acids 81-164 comprise a left-handed anti-parallel four-helix bundle in which the first helix consists of four consecutive turns of 3-10-helix. Fourteen cysteines are conserved in all known HER-1 sequences and form seven disulphide bonds. The protein dictates male development in Caenorhabditis elegans, probably by playing a direct role in cell signalling during C. elegans sex determination. It also inhibits the function of tra-2a. == References == | https://en.wikipedia.org/wiki/Nematode_Her-1 |
In molecular biology the orange carotenoid N-terminal domain is a protein domain found predominantly at the N-terminus of the Orange carotenoid protein (OCP), and is involved in non-covalent binding of a carotenoid chromophore. It is unique for being present in soluble proteins, whereas the vast majority of domains capable of binding carotenoids are intrinsic membrane proteins. Thus far, it has exclusively been found in cyanobacteria, among which it is widespread. The domain also exists on its own, in uncharacterized cyanobacterial proteins referred to as "Red Carotenoid Protein" (RCP). | https://en.wikipedia.org/wiki/Orange_carotenoid_N-terminal_domain |
The domain adopts an alpha-helical structure consisting of two four-helix bundles.Orange carotenoid-binding proteins (OCP) were first identified in cyanobacterial species, where they occur associated with phycobilisome in the cellular thylakoid membrane. These proteins function in photoprotection, and are essential for non-photochemical quenching (NPQ). | https://en.wikipedia.org/wiki/Orange_carotenoid_N-terminal_domain |
In full-length OCP, the NPQ activity is regulated by photoactivation by strong blue-green light. OCP seems to act as a homodimer, and binds one molecule of 3'-hydroxyechinenone (a ketocarotenoid) and one chloride ion per subunit. The carotenoid binding site is lined with a striking number of methionine residues. | https://en.wikipedia.org/wiki/Orange_carotenoid_N-terminal_domain |
The N-terminal domain of OCP is usually accompanied by a C-terminal domain which belongs to the NTF2 superfamily and helps bind the carotenoid. OCP can be proteolytically cleaved into a red form (RCP), which lacks 15 residues from the N-terminus and approximately 150 residues from the C terminus. This domain is implicated in binding the phycobilisome complex, which thereby facilitates thermal dissipation (quenching) of excess absorbed light energy. | https://en.wikipedia.org/wiki/Orange_carotenoid_N-terminal_domain |
In molecular biology the protein SSI is a Subtilisin inhibitor-like which stands for Streptomyces subtilisin inhibitor. This is a protease inhibitor. These are often synthesised as part of a larger precursor protein, either as a prepropeptide. The function of this protein domain is to prevent access of the substrate to the active site. It is found only in bacteria. | https://en.wikipedia.org/wiki/SSI_protease_inhibitor |
In molecular biology the protein domain S-adenosylmethionine synthetase N terminal domain is found at the N-terminal of the enzyme. | https://en.wikipedia.org/wiki/S-Adenosylmethionine_synthetase_enzyme |
In molecular biology the protein domain, Siah interacting protein N-terminal domain is found at the N-terminal of the protein, Siah interacting protein (SIP). It has a helical hairpin structure with a hydrophobic core which is further stabilised by an arrangement of side chains contributed by the two amphipathic helices. The function of this domain remains to be fully elucidated, but it is known to be vital for interactions with Siah. It has also been hypothesised that SIP can dimerise through this N-terminal domain. | https://en.wikipedia.org/wiki/Siah_interacting_protein_N-terminal_domain |
In molecular biology the small pathogenicity island RNA X (alias RsaOR) gene is a bacterial non-coding RNA. It was discovered in a large-scale analysis of Staphylococcus aureus. SprX was shown to influence antibiotic resistance of the bacteria to Vancomycin and Teicoplanin glycopeptides, which are used to treat MRSA infections. In this study the authors identified a SprX target, stage V sporulation protein G (Spo VG). By reducing Spo VG expression levels, SprX affects S. aureus resistance to the glycopeptide antibiotics. Further work demonstrated its involvement in the regulation of pathogenicity factors. | https://en.wikipedia.org/wiki/SprX_small_RNA |
In molecular biology there are a number of neurogenic proteins referred to as mastermind-like proteins (MAMLs) of which this domain is the N-terminal region. Mastermind-like proteins act as critical transcriptional co-activators for Notch signaling.The N-terminal domain of MAML proteins, MAML1, MAML2, MAML3, is a polypeptide of up to 70 residues, numbers 15-67 of which adopt an elongated kinked helix that wraps around ANK and CSL forming one of the complexes in the build-up of the Notch transcriptional complex for recruiting general transcription factors. This N-terminal domain is responsible for its interaction with the ankyrin repeat region of the Notch proteins NOTCH1, NOTCH2, NOTCH3 and NOTCH4. It forms a DNA-binding complex with Notch proteins and RBPSUH/RBP-J kappa/CBF1, and also binds CREBBP/CBP and CDK8. | https://en.wikipedia.org/wiki/MamL-1_domain |
The C-terminal region is required for transcriptional activation. Notch receptors are cleaved upon ligand engagement and the intracellular domain of Notch shuttles to the nucleus. MAMLs form a functional DNA-binding complex with the cleaved Notch receptor and the transcription factor CSL, thereby regulating transcriptional events that are specific to the Notch pathway. | https://en.wikipedia.org/wiki/MamL-1_domain |
MAML proteins may also play roles as key transcriptional co-activators in other signal transduction pathways as well, including: muscle differentiation and myopathies (MEF2C), tumour suppressor pathway (p53) and colon carcinoma survival (beta-catenin). MAML proteins could mediate cross-talk among the various signaling pathways and the diverse activities of the MAML proteins converge to impact normal biological processes and human diseases, including cancers. == References == | https://en.wikipedia.org/wiki/MamL-1_domain |
In molecular biology this protein domain, refers to UbiD, which is found in prokaryotes, archaea and fungi, with two members in Archaeoglobus fulgidus. They are related to UbiD, a 3-octaprenyl-4-hydroxybenzoate carboxy-lyase from Escherichia coli that is involved in ubiquinone biosynthesis. The member from Helicobacter pylori has a C-terminal extension of just over 100 residues that is shared, in part, by the Aquifex aeolicus homologue. | https://en.wikipedia.org/wiki/UbiD_protein_domain |
In molecular biology, "formylglycine-generating enzyme" (sometimes annotated as formylglycine-generating sulfatase enzyme) is the name of the FGE protein domain, whether or not the protein is catalytically active. Both prokaryotic and eukaryotic homologs of FGE possess highly conserved active sites — including the catalytic cysteine residues required for enzymatic function. Activation of molecular oxygen is thought to be carried out by conserved residues close to the FGE catalytic site in aerobic organisms. The catalytic cysteine residues are involved in a thiol-cysteine exchange leading to the ultimate production of fGly. | https://en.wikipedia.org/wiki/Formylglycine-generating_enzyme |
In molecular biology, 2'-5'-oligoadenylate synthetase (2-5A synthetase) is an enzyme (EC 2.7.7.84) that reacts to interferon signal. It is an antiviral enzyme that counteracts viral attack by degrading RNAs, both viral and host. The enzyme uses ATP in 2'-specific nucleotidyl transfer reactions to synthesize 2'-5'-oligoadenylates, which activate latent ribonuclease (RNASEL), resulting in degradation of viral RNA and inhibition of virus replication.The C-terminal half of 2'-5'-oligoadenylate synthetase, also referred to as domain 2 of the enzyme, is largely alpha-helical and homologous to a tandem ubiquitin repeat. It carries the region of enzymatic activity between at the extreme C-terminal end. | https://en.wikipedia.org/wiki/2'-5'-oligoadenylate_synthase |
In molecular biology, ADF-H domain (actin-depolymerising factor homology domain) is an approximately 150 amino acid motif that is present in three phylogenetically distinct classes of eukaryotic actin-binding proteins. ADF/cofilins, which include ADF, cofilin, destrin, actophorin, coactosin, depactin and glia maturation factors (GMFs) beta and gamma. ADF/cofilins are small actin-binding proteins composed of a single ADF-H domain. They bind both actin-monomers and filaments and promote rapid filament turnover in cells by depolymerising/fragmenting actin filaments. | https://en.wikipedia.org/wiki/ADF-H_domain |
ADF/cofilins bind ADP-actin with higher affinity than ATP-actin and inhibit the spontaneous nucleotide exchange on actin monomers Twinfilins, which are actin monomer-binding proteins that are composed of two ADF-H domains Abp1/Drebrins, which are relatively large proteins composed of an N-terminal ADF-H domain followed by a variable region and a C-terminal SH3 domain. Abp1/Drebrins interact only with actin filaments and do not promote filament depolymerisation or fragmentation. | https://en.wikipedia.org/wiki/ADF-H_domain |
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