• Mini-RAG1 consists primarily of the catalytic center and the residues N-terminal to it, but it lacks a zinc finger region in RAG1 previously implicated in binding RAG2. (nih.gov)
  • The core domain and the first eight residues of the carboxyl-terminal domain of the enzyme, including the active-site nucleophile tyrosine-723, share significant structural similarity with the bacteriophage family of DNA integrases. (embl.de)
  • The method, named Predikin, identifies key conserved substrate-determining residues in the kinase catalytic domain that contact the substrate in the region of the phosphorylation site and so determine the sequence surrounding the phosphorylation site. (biomedcentral.com)
  • The second factor, termed peptide specificity, describes the interaction between amino acid residues in the catalytic domain of the protein kinase and the substrate residues that surround the phosphorylated residue. (biomedcentral.com)
  • Crystal structures of protein kinases with bound substrate peptides show that substrate residues at positions -3 to +3 relative to the phosphorylated serine, threonine or tyrosine residue adopt an extended conformation and bind to a pocket in the catalytic domain of the protein kinase [ 8 ]. (biomedcentral.com)
  • The heptapeptide sequence from -3 to +3 that best binds to the pocket is determined by the physicochemical nature of the residues in the catalytic domain that line the pocket and contact the substrate. (biomedcentral.com)
  • This C2 domain is about 116 amino-acid residues and is located between the two copies of the C1 domain in Protein Kinase C (that bind phorbol esters and diacylglycerol) (see PDOC00379) and the protein kinase catalytic domain (see PDOC00100). (bionity.com)
  • Bromodomains are proteins that contain modules of ~110 amino acids that recognize and bind acetylated lysine residues in histones and other proteins. (frontiersin.org)
  • The interactions with the amino acid residues responsible for the stabilizations of the inhibitors in the active site are addressed in detail. (nih.gov)
  • However, both proteins have similar biological functions and show 70% identity in amino acid sequence. (wikipedia.org)
  • On its N terminus it possesses catalytic domain, which shows the highest level of conservation between human and mouse proteins. (wikipedia.org)
  • The the Cysteine containing enzymatically active version of the domain is also found in the CDC25 class of protein phosphatases and a variety of proteins such as sulfide dehydrogenases and stress proteins such as Senesence specific protein 1 in plants, PspE and GlpE in bacteria and cyanide and arsenate resistance proteins. (embl.de)
  • There are 171652 RHOD domains in 136038 proteins in SMART's nrdb database. (embl.de)
  • Taxonomic distribution of proteins containing RHOD domain. (embl.de)
  • The complete taxonomic breakdown of all proteins with RHOD domain is also avaliable . (embl.de)
  • Click on the protein counts, or double click on taxonomic names to display all proteins containing RHOD domain in the selected taxonomic class. (embl.de)
  • There are 4321 TOPEUc domains in 4318 proteins in SMART's nrdb database. (embl.de)
  • 4 While proteins can be phosphorylated on nine amino acids, serine, threonine and tyrosine phosphorylation are by far the most predominant in eukaryotic cells. (ac.be)
  • 8 , 9 The protein is a member of a novel family of large proteins, which show sequence homology to the catalytic domain of phosphatidylinositol 3 kinase, 3 and are implicated in cell cycle regulation, signal transduction, and the response to DNA damage. (bmj.com)
  • The kinetic parameters of recombinant proteins showed that ZmHXK4-7 have high catalytic efficiency for Glc, fructose (Fru) and mannose (Man), ZmHXK7 has a lower Km for ATP, and together with ZmHXK8 they have lower sensitivity to inhibition by ADP, G6P and N-acetylglucosamine than ZmHXK4-6 and ZmHXK9. (biomedcentral.com)
  • A C2 domain is a protein structural domain involved in targeting proteins to cell membranes . (bionity.com)
  • Regions with significant homology [1] to the C2-domain have been found in many proteins. (bionity.com)
  • Additionally, BRDs contain several catalytic domains that enable them to act as methyltransferases, ATP-dependent re-modellers or histone acetyltransferases and helicases ( 8 ) Bromodomain and extra-terminal domain (BET) proteins are a family of transcriptional mediators that regulate gene expression ( 8 , 9 ). (frontiersin.org)
  • The expression of PCSK9 is also up-regulated by the sterol regulatory element binding proteins (SREBP's), a family of transcription factors that are responsible for the upregulation of genes involved in cholesterol and fatty acid metabolism, such as the LDLR gene. (nexelis.com)
  • The defining features of these enzymes are a unique catalytic triad, Ser-Glu-Asp (SED in single-letter notation), as well as the presence of an aspartic acid residue in the oxyanion hole. (expasy.org)
  • Using domain shuffling experiments, we present evidence showing that a central domain upstream of the conserved catalytic cysteine residue determines HopZ1 recognition specificity. (uea.ac.uk)
  • The latter enzyme, called Sc LPMO10D, and most of the enzymes found in this subclade are unique, not only because of variation in the catalytic domain, but also as their C-terminus contains a cell wall sorting signal (CWSS), which flags the LPMO for covalent anchoring to the cell wall. (nature.com)
  • The PTGS (COX) enzymes catalyze the conversion of arachidonic acid to prostaglandins in two steps. (wikipedia.org)
  • tRNA synthases are the enzymes that interpret the RNA code and attach specific aminoacids to the tRNAs that contain the cognate trinucleotide anticodons. (nih.gov)
  • The enzymes that dephosphorylate these three amino acids are classified into four groups on the basis of specific catalytic signatures/domain sequences and substrate preference. (ac.be)
  • Here, we cloned and functionally characterized putative catalytic enzymes to analyze their metabolic contribution during germination process. (biomedcentral.com)
  • The sequences of nine genes involved in phosphate metabolism were compared, and there were differences between serovars in the catalytic - ATP binding domain of the histidine kinase phoR. (usda.gov)
  • Analysis of the predicted PhoR amino acid sequences from additional Salmonella genomes indicated a conservation of sequences each within the Typhimurium, Give and Enteritidis serovars. (usda.gov)
  • The initial therapeutics were peptidomimetics, or compounds derived from the sequences of the amino acids of the MMP's endogenous ligands. (chemdiv.com)
  • The region of the rubella virus nonstructural open reading frame that contains the papain-like cysteine protease domain and its cleavage site was expressed with a Sindbis virus vector. (caltech.edu)
  • non-catalytic domains of eukaryotic dual-specificity MAPK-phosphatases. (embl.de)
  • The catalytic domain of this dual-specificity phosphatase has recently been mapped to the 180 most C-terminal amino acids. (embl.de)
  • An is propyl substituent α to the Zn 2+ -chelating hydroxamic acid moiety confers specificity by binding in the S10 subsite. (chemdiv.com)
  • This difference provides the principle basis for identification of inhibitors targeting the hemopexin domain with high selectivity and specificity. (suny.edu)
  • The regulation of PP2A is mainly accomplished by the identity of the regulatory B-type subunit, which determines substrate specificity, subcellular localization and catalytic activity of the PP2A holoenzyme. (ac.be)
  • Random and targeted mutagenesis identified three amino acids involved in HopZ1 allelic specificity. (uea.ac.uk)
  • Importantly, these compounds chelate the catalytic zinc ion in order to render the protease inactive. (chemdiv.com)
  • This study focused on the hemopexin domain of MMP-9, a nonproteolytic domain, which is essential for MMP-9 regulated tumor cell migration. (suny.edu)
  • Increased GCN2 activity in solid tumors enhances the production of amino acids and contributes to tumor cell survival in conditions of nutrient deprivation. (rndsystems.com)
  • We discuss the functional implications of these structures with respect to the underlying catalytic mechanism, substrate recognition and processing, and possible component interactions. (rcsb.org)
  • for example, the C2 domain in PTEN, brings the phosphatase domain into contact with the membrane where it can dephosphorylate its substrate, 3,4,5 tetraphospho-inositol , without removing it from the membrane - which would be energetically very costly. (bionity.com)
  • The RAG endonuclease consists of RAG1, which contains the active site for DNA cleavage, and RAG2, an accessory factor whose interaction with RAG1 is critical for catalytic function. (nih.gov)
  • Cleavage sites are serotype-specific, with the exception of BoNT/F5, which cleaves between amino acids 54 L and 55 E, four amino acids different from the standard BoNT/F cleavage site of 58 Q and 59 K 13 . (cdc.gov)
  • In the endoplasmic reticulum, it undergoes autocatalytic intramolecular cleavage to generate a 14 kDa pro- domain and a 60 kDa catalytic domain. (nexelis.com)
  • Figure 2) While metabolizing arachidonic acid primarily to PGG2, COX-2 also converts this fatty acid to small amounts of a racemic mixture of 15-Hydroxyicosatetraenoic acids (i.e., 15-HETEs) composed of ~22% 15(R)-HETE and ~78% 15(S)-HETE stereoisomers as well as a small amount of 11(R)-HETE. (wikipedia.org)
  • The conversion of arachidonic acid to PGG2 can be shown as a series of radical reactions analogous to polyunsaturated fatty acid autoxidation. (wikipedia.org)
  • Early inhibitors targeting MMP activity were designed to bind within the catalytic domain of these proteases. (chemdiv.com)
  • An in silico docking approach was employed to screen for novel small-molecule compound that bind to the hemopexin domain of MMP-9. (suny.edu)
  • Each subunit has a region called a motor domain (also known as its 'head') that can bind to the microtubule and to a molecule called ATP, which provides the energy required for the motor to step forward. (elifesciences.org)
  • It is composed of 8 β-sheets , forming a beta-sandwich motif, and co-ordinates 2 or 3 calcium ions, which bind in an indentation formed by the first and final loops of the domain, on the membrane binding face. (bionity.com)
  • In addition to this, phosphatidylinositol 3-kinase (PI3-kinase), an enzyme that phosphorylates phosphoinositides on the 3-hydroxyl group of the inositol ring, also uses a C2 domain to bind to the membrane (e.g. 1e8w PDB entry). (bionity.com)
  • The N-terminal C2a domain has been shown to bind phospholipids in a Ca2+-dependent manner (Fukuda, 1996 and Fukuda, 1997), while the role of the C2b domain remains unclear. (sdbonline.org)
  • A heat-stable aminopeptidase with similar biochemical properties to eukaryotic leucine aminopeptidase was purified to homogeneity from Escherichia coli K-12 by Vogt and named aminopeptidase I. The bacterial leucyi aminopeptidases range from 491 to 524 amino acids in length. (gla.ac.uk)
  • In response to amino acid deprivation or UV irradiation, GCN2 phosphorylates the alpha subunit of eukaryotic initiation factor 2 (eIF2a) at Ser51 and induces a delay in entry to S phase of the cell cycle. (rndsystems.com)
  • STK11/LKB1 encodes a 433 amino acid ubiquitously expressed protein with a central catalytic domain and regulatory N- and C-terminal domains. (medscape.com)
  • 4 - 7 The ATM gene encodes a nuclear phosphoprotein of approximately 350 kDa (3056 amino acids) and is ubiquitously expressed. (bmj.com)
  • The relationship of Cdc25 to the structurally well-characterized rhodanese spans the entire catalytic domain and served as template for a structural model for human Cdc25a, which is fundamentally different from previously suggested models for Cdc25 catalytic domain organization. (embl.de)
  • Protein Phosphatase 2A (PP2A) is a widely expressed family of protein phosphatases made of a core dimer, composed of a catalytic (C) subunit and a structural (A) subunit, in association with a third variable regulatory (B) subunit. (ac.be)
  • Structural analyses of several C2 domains have shown them to consist of similar ternary structures in which three Ca 2+ -binding loops are located at the end of an 8 stranded antiparallel beta sandwich. (bionity.com)
  • The crystal structures of human topoisomerase I comprising the core and carboxyl-terminal domains in covalent and noncovalent complexes with 22-base pair DNA duplexes reveal an enzyme that 'clamps' around essentially B-form DNA. (embl.de)
  • We also constructed, by homology modeling, a theoretical structure of the pUL105 N-terminal domain which indicates that the mutated conserved amino acids in this domain could be involved in ATP hydrolysis. (frontiersin.org)
  • Our rational design based the catalytic mechanism of the α -glucosidase reaction proved to be effective for producing mutants with improved the ratio of transglycosylation/hydrolysis of α -glucosidase, which provides an important theoretical basis for further research on the reaction mechanism of α -glucosidase. (researchsquare.com)
  • In recent years, nucleotide and amino acid sequence information has become available so that additional characterization of these viruses is possible, including further analysis of relationships among members of the genus. (cdc.gov)
  • The IDGF's have an eight-stranded alpha/beta barrel fold and are related to the glycosyl hydrolase family 18 (GH18) chitinases, but they have an amino acid substitution known to abolish chitinase catalytic activity. (nih.gov)
  • The ATM gene encodes a large protein that belongs to a family of kinases possessing a highly conserved C-terminal kinase domain related to the phosphatidylinositol 3-kinase domain. (bmj.com)
  • the membrane-binding domain consists of a series of amphipathic α helices with several hydrophobic amino acids exposed to a membrane monolayer. (wikipedia.org)
  • Analysis by circular dichroism spectroscopy showed that this fragment folds into a single stable domain made of mostly α‐helices with a melting point of 34.5°C. Size‐exclusion chromatography combined with multi‐angle light scattering indicated the formation of a dimer of the purified extracellular domain. (uni-wuerzburg.de)
  • By analyzing the single-molecule properties of engineered motors, we demonstrate that the non-catalytic domain has a key role in the motility mechanism by acting as a 'foothold' that allows Kar3 to bias translocation towards the minus end. (elifesciences.org)
  • The C2 domain is thought to be involved in calcium-dependent phospholipid binding [2] and in membrane targeting processes such as subcellular localisation. (bionity.com)
  • We assumed that substitution of Cys116 for His broke the original hydrogen-bond network and that this induced a significant effect of Tyr114 as a general acid catalyst, possibly due to the narrow space in the active site. (elsevierpure.com)
  • Alignment of E. coli PepA with bovine lens leucyi aminopeptidase reveals 44% sequence identity in the catalytic C-terminal domain, but only 18% identity in the N-terminal domain. (gla.ac.uk)
  • 60% sequence identity with only two amino acid substitutions in the active site of the enzyme. (cdc.gov)
  • C2 domains are also found in clostridial alpha toxins , where they are used to bring the catalytic phospholipase domain into contact with the plasma membrane , conferring the toxic activity on the protein. (bionity.com)
  • C2 domains are unique among membrane targeting domains in that they show wide range of lipid selectivity for the major components of cell membranes, including phosphatidylserine and phosphatidylcholine. (bionity.com)
  • Cullen, 1997), suggesting that an increase in intracellular IP4 levels leads to the release of the PH domain from the membrane. (sdbonline.org)
  • Fukuda, 1996), implying that release of the PH domain from the membrane is accompanied by activation of the catalytic domain. (sdbonline.org)
  • upon elevation of Ca2+ and IP4 concentrations, the PH domain binds to IP4 thereby stimulating catalytic activity, while at the same time the C2a domain takes over the role of membrane tether. (sdbonline.org)
  • They consist of a catalytic domain which interacts with the amino acid acceptor-T psi C helix of the tRNA, and a second domain which interacts with the rest of the tRNA structure. (nih.gov)
  • PCSK9 binds to the EGF domain of the LDLR and prevents LDLR from being sorted to the endosomes. (nexelis.com)
  • An inositol-1,3,4,5-tetrakisphosphate (IP4)-sensitive extended PH domain is essential for Gap1 activity, while Ca2+-sensitive C2 domains and a glutamine-rich region contribute equally to full activity in vivo. (sdbonline.org)
  • GCN2 contains an RWD domain (aa 21-134), a pseudo-kinase domain (aa 296-539), a catalytic domain (aa 590-1001), and a histidyl tRNA synthase-like domain (aa 1022-1493) followed by a C-terminal ribosome interacting region. (rndsystems.com)
  • Alternate splicing generates an isoform with a short deletion in the kinase domain and an isoform that is truncated at the N-terminal end of the kinase domain. (rndsystems.com)
  • Two adjacent acidic amino acids in this region (Asp-546 and Glu-547) are important for both the RAG1-RAG2 interaction and recombination activity, with Asp-546 of particular importance. (nih.gov)
  • The catalytic domain, which is responsible for enzyme activity, contains the highly conserved Zn 2+ binding region. (chemdiv.com)
  • The Gap1 catalytic domain alone is insufficient for in vivo activity of Gap1, indicating a requirement for the additional domains. (sdbonline.org)
  • Here we show that His-1272 is also necessary for protease activity, consistent with the active site of the enzyme being composed of a catalytic dyad consisting of Cys-1151 and His-1272. (caltech.edu)
  • The ability of Mini-RAG1 to interact with RAG2 depends on a predicted α-helix (amino acids 997-1008) near the RAG1 C terminus and a region of RAG1 from amino acids 479 to 559. (nih.gov)
  • The principal difference between PTP- NP-2 and PTP- NP is a 17-amino-acid insert near the N-terminus of PTP- NP that is absent in PTP- NP-2. (wikigenes.org)
  • This part codes N-terminal (366 amino acid) domain of the SCO6073 gene from S. coelicolor A3. (igem.org)
  • 3D structure of C2 domains has been reported [3] , the domain forms an eight-stranded beta sandwich constructed around a conserved 4-stranded motif, designated a C2 key [3] . (bionity.com)
  • First, hydrogen is abstracted from carbon 13 of arachidonic acid, and then two molecules of oxygen are added by the PTGS2 (COX-2), giving PGG2. (wikipedia.org)
  • Strains of Kentucky utilized amino acids as sole carbon and energy sources better than the Enteritidis and Kentucky strains. (usda.gov)
  • Both the cyclooxygenase and the peroxidase active sites are located in the catalytic domain, which accounts for approximately 80% of the protein. (wikipedia.org)
  • however they are considerably larger, with the mature catalytic domains containing approximately 375 amino acids. (expasy.org)
  • A third protease, α-secretase, cuts APP within the Aβ domain, thus precluding Aβ formation. (jneurosci.org)
  • By means of radiochemical amino acid sequencing, the site in the polyprotein cleaved by the nonstructural protease was found to follow Gly-1300 in the sequence Gly-1299-Gly-1300-Gly-1301. (caltech.edu)
  • It contains one GTPase binding domain (aa 75-105) plus a protein kinase catalytic region (aa 250-521). (rndsystems.com)
  • This region covers both the catalytic core and the DNA-binding domains. (embl.de)
  • The absence of endoperoxide-containing products derived from 10,10-difluoroarachidonic acid has been thought to indicate the importance of a C-10 carbocation in PGG2 synthesis. (wikipedia.org)
  • PTGS2 (COX-2), converts arachidonic acid (AA) to prostaglandin endoperoxide H2. (wikipedia.org)
  • and an alpha-helical C-terminal domain, the latter forming a deep cavity at the active site. (rcsb.org)