• residues 1-4, and 95-99 of each monomer), the turn encompassing residues 4-9, and the helix (residues 86-94 of each monomer). (proteopedia.org)
  • The interface between the core and terminal domains is composed primarily of small hydrophobic residues. (proteopedia.org)
  • Those which bind phosphorylated tyrosine residues may recruit multi-phosphorylated substrates for the adjacent active domains and are more conserved, while the other class have accumulated several variable amino acid substitutions and have a complete loss of tyrosine binding capability. (embl.de)
  • It is about 140 residues long and it has been suggested that this domain will be involved in tRNA recognition. (embl-heidelberg.de)
  • Catalytically active TR mART domains hallmark catalytic residues in the active site. (expasy.org)
  • domain causing residues 59 and 64 in Rac-1 to be displaced. (cellsignal.com)
  • The catalytic core domain contains three highly conserved residues Asp64, Asp116 and Glu152 (the DDE motif) that are essential for the catalytic activity of IN. (biomedcentral.com)
  • The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. (unl.edu)
  • Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). (unl.edu)
  • Pol δ is anchored to one of the three PCNA monomers through the C-terminal domain of the catalytic subunit. (nature.com)
  • Mammalian Pol δ consists of a catalytic subunit and three regulatory subunits (Fig. 1a ). (nature.com)
  • The catalytic subunit (p125) harbours the polymerase and exonuclease activities, and a metal-binding C-terminal domain (CTD). (nature.com)
  • This has been proposed by the ε subunit taking an extended conformation, with a terminal helix probing into the central architecture of the hexameric catalytic domain, preventing ATP hydrolysis. (tudelft.nl)
  • Tetramerization is mediated by assembly of the C-terminal tryptophan amphiphilic tetramerization (WAT) helices from each subunit as a superhelical assembly around a central lamellipodin-derived oligopeptide with a proline-rich attachment domain (PRAD) sequence that adopts a polyproline II helical conformation and runs antiparallel. (rcsb.org)
  • CnA also has 3 regulatory domains: a binding domain for its partner subunit CnB, a CaM-binding domain, and an autoinhibitory domain. (pancreapedia.org)
  • CnB, the regulatory subunit, contains 4 Ca 2+ -binding EF hand motifs that regulate (through a conformational change) the catalytic function of Cn. (pancreapedia.org)
  • Following the sIII strand the sequence meets the 'S-shaped double loop' that is of primary importance for the peptide structure and catalytic activity (see further) as it extends to the cleft side "bulge", continuing to the only antiparallel β-strand sIV, which is prime importance for binding peptidic substrates or inhibitors by forming main chain hydrogen bond. (wikipedia.org)
  • This arrangement allows PCNA to thread and stabilize the DNA exiting the catalytic cleft and recruit FEN1 to one unoccupied monomer in a toolbelt fashion. (nature.com)
  • The catalytic reaction takes place in the cleft formed at the junction of the two domains. (anl.gov)
  • BacA has a C-terminal catalytic glycosyl hydrolase family 25 (GH25) domain and an N-terminal peptidoglycan-binding domain comprised of three alpha helices which is similar to a domain found in matrixins. (nih.gov)
  • The DxDxT catalytic motif is present in all HAD-like domains, along with a characteristic and conserved sequence of α-helices and β-sheets [3]. (aocs.org)
  • UvrB/uvrC motif, GIY-YIG catalytic domain, Helix-hairpin-helix domain, UvrC Helix-hairpin-helix N-terminal [Interproscan]. (ntu.edu.sg)
  • UvrB/uvrC motif, GIY-YIG catalytic. (ntu.edu.sg)
  • The position of helix αC and the lack of a conserved arginine within an equivalent HRD motif suggested that the NleH2 kinase domain's active conformation might not require phosphorylation. (northwestern.edu)
  • In this study, we performed mutagenic analyses of the C-terminal region of the catalytic core domain of HIV-1 IN in order to delineate the critical amino acid(s) and/or motif(s) required for the induction of the lethal phenotype in the yeast strain HP16, and to further elucidate the molecular mechanism which causes this phenotype. (biomedcentral.com)
  • Surprisingly, the TH1 helix maintains its conformation in the crystal of the full-length toxin even at pH 5. (rcsb.org)
  • Structurally, all known receptor PTPases, are made up of a variable length extracellular domain, followed by a transmembrane region and a C-terminal catalytic cytoplasmic domain. (embl.de)
  • 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)
  • In X-ray crystallographic studies, we have determined the structures of the catalytic portions of the enzyme in complex with statin molecules. (nih.gov)
  • These studies show that the HMG-like moiety of statin molecules occupy the HMG binding site of the enzyme, with the hydrophobic groups of the statins occupying a binding site exposed by movement of flexible helices in the enzyme catalytic domain. (nih.gov)
  • The chloride-binding functions to activate the enzyme, which acts by a two-step mechanism involving a catalytic nucleophile base (usually an Asp) and a catalytic proton donor (usually a Glu) that are responsible for the formation of the beta-linked glycosyl-enzyme intermediate. (embl.de)
  • The regulatory influence of the rhodopsin domain on the enzyme activity is only partially understood and holds the key for a deeper understanding of intra-molecular signaling pathways. (elifesciences.org)
  • The enzyme is fully functional and reveals possible determinants of interdomain flexibility at a hinge region following the pivot helix. (anl.gov)
  • The enzyme retains the preference for NADP(+) cofactor from the parent E. coli domain II, although there are subtle differences in catalytic activity. (anl.gov)
  • The receptor makes a single pass through the cell membrane and contains an intracellular kinase catalytic region divided by a hydrophilic insert. (creation.com)
  • This has led to the development of a range of ERK1/2 inhibitors (ERKi) that either inhibit kinase catalytic activity (catERKi) or additionally prevent the activating pT-E-pY dual phosphorylation of ERK1/2 by MEK1/2 (dual-mechanism or dmERKi). (babraham.ac.uk)
  • However, recent studies have suggested that BRAFi/MEKi and ERK1/2i resistance can arise through activation of a parallel signalling pathway leading to activation of ERK5, an unusual protein kinase that contains both a kinase domain and a transcriptional transactivation domain. (babraham.ac.uk)
  • We demonstrate that neither catalytic nor receptor-binding domains change their structure upon this acidification, while the T-domain undergoes a conformational change that results in the unfolding of the TH2-3 helices. (rcsb.org)
  • On C-terminal part of the CAT Domain the hB α-helix, known as the "active-site helix" encompasses part of the "zinc-binding consensus sequence" HEXXHXXGXXH that is characteristic of the Metzincin superfamily. (wikipedia.org)
  • In bacterial RNA polymerase (RNAP), the bridge helix and switch regions form an intricate network with the catalytic active centre and the main channel. (houstonmethodist.org)
  • From N- to C-terminus, 206K harbors methyltransferase (MT), cysteine proteinase (PRO), helicase (HEL or 42K) and RNA-dependent RNA polymerase (POL or 66K) domains. (datexis.com)
  • Furthermore, we propose a model for the ubiquinol-binding site which identifies a hydrophobic pocket, between helices II and III, leading from a proposed membrane-binding domain to the catalytic domain. (silverchair.com)
  • There are 37989 PTPc domains in 29134 proteins in SMART's nrdb database. (embl.de)
  • Taxonomic distribution of proteins containing PTPc domain. (embl.de)
  • The complete taxonomic breakdown of all proteins with PTPc domain is also avaliable . (embl.de)
  • Click on the protein counts, or double click on taxonomic names to display all proteins containing PTPc domain in the selected taxonomic class. (embl.de)
  • There are 26085 Arg_tRNA_synt_N domains in 26083 proteins in SMART's nrdb database. (embl-heidelberg.de)
  • Taxonomic distribution of proteins containing Arg_tRNA_synt_N domain. (embl-heidelberg.de)
  • The complete taxonomic breakdown of all proteins with Arg_tRNA_synt_N domain is also avaliable . (embl-heidelberg.de)
  • Click on the protein counts, or double click on taxonomic names to display all proteins containing Arg_tRNA_synt_N domain in the selected taxonomic class. (embl-heidelberg.de)
  • There are 4203 Aamy_C domains in 4158 proteins in SMART's nrdb database. (embl.de)
  • Percentage points are related to the number of proteins with Aamy_C domain which could be assigned to a KEGG orthologous group, and not all proteins containing Aamy_C domain. (embl.de)
  • The HAD domain-containing proteins catalyze hydrolase or phosphohydrolase reactions. (aocs.org)
  • Of the three tail spikes, two have protein domains associated with the pectate lyase family of proteins (Tsp2) and P22 tail spike family (Tsp3) with the prospect that these enable Salmonella O antigen degradation. (biomedcentral.com)
  • Tail spike proteins of Vi01 and SboM-AG3 are predicted to contain conserved right-handed parallel β-helical structures but the internal protein domains are varied allowing different host specificities. (biomedcentral.com)
  • The conserved Asp25-Thr26-Gly27 catalytic triad, is situated at the interface of the core domains from the two monomers. (proteopedia.org)
  • The mART domain adopts a mixed α/β-fold with a characteristic β-sandwich structure. (expasy.org)
  • Despite the similarity of the catalytic domains of MMPs, this entry will focus only on the structural features of MMP-1 catalytic domain. (wikipedia.org)
  • Most of the 10 exons coding the intracellular portion correspond to specific structural elements, such as α-helices or β-sheets. (creation.com)
  • A structural model based on AlphaFold2 prediction and verified by crosslinking-MS indicates an interaction of the long SAM-key helix with protrusion I, a subdomain located between the two ATPase lobes that is critical for control of enzymatic activity. (dlr.de)
  • Of course it might be that the glycine can not stabilize any structure, which should be present at this residue.We do not have any structural data for this point, but predictions suggest a position either in a helix or at the edge of a sheet structure. (tu-muenchen.de)
  • IN is a 32 kDa protein with three distinct structural domains, the N-terminal zinc-binding domain, the central catalytic core domain and the C-terminal domain. (biomedcentral.com)
  • Some enzymatically inactive mART domains, for example, the N-terminal domains of C2 and VIP2 toxins, have acquired a new, protein-binding function. (expasy.org)
  • Enzymatically active nsp15 forms a hexamer through a dimer of trimers (point group 32), whose assembly is facilitated by the oligomerization domain. (insidecorona.net)
  • a Domain organization of the four subunits of human Pol δ and amino acid sequence of PCNA-interacting (PIP-box) motifs. (nature.com)
  • Although all alpha-amylases possess the same catalytic function, they can vary with respect to sequence. (embl.de)
  • The PAP activities of the lipins depend on a conserved C-terminus domain with sequence homology to the haloacid dehalogenase or HAD-like domain [1]. (aocs.org)
  • Primary sequence and domain structure of CnA. (pancreapedia.org)
  • Using multiple sequence alignment and structure prediction, we identify an evolutionarily conserved domain that is modeled to contain a SAM-like fold with one long, protruding helix, which we term SAM-key. (dlr.de)
  • The dataset with sequence identity from 40% to 80% sequence identity only contain structures in connection with aromatic hydroxylation namely Tryptophan and Tyrosin from chicken and rat though the structure gained from the rat also contains the tetramerisation domain we also find in our reference structure . (tu-muenchen.de)
  • BirA, a member of the group II biotin-protein ligase family, contains an N-terminal helix-turn-helix DNA-binding domain, a catalytic core that catalyzes biotinyl 5′ adenylate (bio-5′-AMP) synthesis, and a C-terminal domain that plays a role in DNA binding, dimerization, and catalytic function. (watson-int.cn)
  • It has two domains, one that binds protective antigen and another that has ADP-ribosyltransferase activity [ 5 ]. (expasy.org)
  • Mutation of the interaction interface phenocopies the domain deletion with a lack of DNA-stimulated ATPase activation and a nucleosome-remodeling defect, thereby confirming a role of the SAM-key helix in regulating ATPase activity. (dlr.de)
  • Our data thereby demonstrate a central role of the SAM-key domain in mediating the activation of Fun30 catalytic activity, thus highlighting the importance of allosteric activation for this class of enzymes. (dlr.de)
  • If the mutation would have occurred rather near the catalytic site, our judgment would have been different with respect to the strong affinity of glutamic acid to ions, which plays a major role in PheOH-activity. (tu-muenchen.de)
  • CTD C-terminal domain, OB oligonucleotide binding domain, PDE phosphodiesterase domain. (nature.com)
  • The helix of the terminal domain packs against several beta-strands of the core domain. (proteopedia.org)
  • This entry represents the alpha-amylase C-terminal domain. (embl.de)
  • CnAβ also has two splice variants which differ in their C-terminal domain (30). (pancreapedia.org)
  • N terminal domain, Helix-turn-helix domain of resolvase, N-terminal catalytic domain, HTH domain [InterProScan]. (ntu.edu.sg)
  • The crystal structure of a C-terminal domain of enterohemorrhagic Escherichia coli type III effector NleH2 has been determined to 2.6 Å resolution. (northwestern.edu)
  • The structure resembles those of protein kinases featuring the catalytic, activation, and glycine-rich loop motifs and ATP-binding site. (northwestern.edu)
  • This domain is quite crucial in dimer formation and stabilization of an active PR. (proteopedia.org)
  • This domain is quite useful in dimer stabilization, as well as the catalytic site stability. (proteopedia.org)
  • The catalytic domains within a dimer are asymmetrically linked to the WAT/PRAD. (rcsb.org)
  • As the overall change of size and the change in polarity from rather negative to positive and regarding the fact, that arginine is a rather seldom used amino acid (mostly appearing in the catalytic domain for phosphorylated substrates), we would say, that this is rather a disease causing mutation. (tu-muenchen.de)
  • The catalytic domain (CAT) of MMP-1 starts with the F100 (non-truncated CAT) as the first amino-acid of the N-terminal loop of the CAT domain. (wikipedia.org)
  • The first published x-ray structure of the CAT domain was representative of the truncated form of this domain, where the first 7 amino-acids are not present. (wikipedia.org)
  • It consists 99 amino acids, which forming 10 β-strand and 1 α-helix. (proteopedia.org)
  • PTPase domains consist of about 300 amino acids. (embl.de)
  • The catalytic domain of this dual-specificity phosphatase has recently been mapped to the 180 most C-terminal amino acids. (embl.de)
  • This domain is found at the amino terminus of Arginyl tRNA synthetase, also called additional domain 1 (Add-1). (embl-heidelberg.de)
  • or RhoGEF domain consists of an ~ 150 amino acid region that induces Rho family GTPases to displace GDP. (cellsignal.com)
  • The others all are connected or part of the ACT-domain which is known to be controlled by amino-acid concentration, which relates to our target protein. (tu-muenchen.de)
  • XopAI uses an altered mART domain to bind its own N-terminal peptide containing a conserved Arg residue [ 8 ]. (expasy.org)
  • Some of the receptor PTPases contain fibronectin type III (FN-III) repeats, immunoglobulin-like domains, MAM domains or carbonic anhydrase-like domains in their extracellular region. (embl.de)
  • Extracellularly the receptor is made up of five immunoglobulin-like domains. (creation.com)
  • domain is composed of a unique, extended bundle of α-helices. (cellsignal.com)
  • This bundle is composed mainly of the CR1, CR2, and CR3 regions that each form separate α−helices which pack together. (cellsignal.com)
  • The bacterial enzymes are hexameric, arranged with 32 symmetry, and each polypeptide consists of an N-terminal substrate-binding segment (domain I) followed by a C-terminal cofactor-binding segment (domain II). (anl.gov)
  • We tracked the catalytic reaction of RGC and the free GC domain independently by UV-light induced release of GTP from the photolabile NPE-GTP substrate. (elifesciences.org)
  • The catalytic core sits on top of PCNA in an open configuration while the regulatory subunits project laterally. (nature.com)
  • Each domain core is formed mainly by perpendicular packing of a five-stranded mixed β-sheet against a three-stranded antiparallel β-sheet. (expasy.org)
  • The profile we developed covers the entire TR mART core domain. (expasy.org)
  • Our study identified three HIV-1 IN mutants, V165A, A179P and KR186,7AA, located in the C-terminal region of the catalytic core domain of IN that do not induce the lethal phenotype in yeast. (biomedcentral.com)
  • Overall, this study demonstrates that three mutations located in the C-terminal region of the catalytic core domain of HIV-1 IN inhibit the IN-induced lethal phenotype in yeast by inhibiting the binding of IN to the host chromatin. (biomedcentral.com)
  • These results demonstrate that the C-terminal region of the catalytic core domain of HIV-1 IN is important for binding to host chromatin and is crucial for both viral replication and the promotion of the IN-induced lethal phenotype in yeast. (biomedcentral.com)
  • GH5-7 displayed a substrate preference toward galactomannan by showing 10-times higher catalytic efficiency than to linear β-mannan. (megazyme.com)
  • domain appears to greatly increase catalytic efficiency in many cases. (cellsignal.com)
  • This entry represents the PTPase domain found in several tyrosine-specific protein phosphatases (PTPases). (embl.de)
  • These structures show that a nsp15 monomer consist of three conserved domains, the N-terminal oligomerization domain, the middle domain, and the catalytic NendoU domain. (insidecorona.net)
  • The overall results imply that the membrane interactions of the T-domain are critical in ensuring the proper conformational changes required for the preparation of the diphtheria toxin for the cellular entry. (rcsb.org)
  • This partial folding of the catalytic loop is most likely stabilized through intra IN domain domain interactions and interactions with vDNA ALK inhibitor which contribute in the helix 4 elongation. (sykpathway.com)
  • MMP-1 has an archetypal structure consisting of a pre-domain, a pro-domain, a catalytic domain, a linker region and a hemopexin-like domain. (wikipedia.org)
  • In the absence of substrate, the two domains move apart as rigid bodies, as shown by the apo structure of glutamate dehydrogenase from Clostridium symbiosum. (anl.gov)
  • It is predicted to be two positions N-terminal of a helix structure. (tu-muenchen.de)
  • In this paper, we review experimental studies that have contributed to our current understanding of its structure, with particular reference to the catalytic site. (silverchair.com)
  • The second class shows a release of evolutionary constraint for the sites around the catalytic centre, which emphasises a difference in function from the first group. (embl.de)
  • is inclusive of papers focused on stucture, function, and properties of enzymes as well as catalytic and inhibition mechanisms of enzymes, mechanisms of drug action, and related advances on enzymes. (mdpi.com)
  • domains (RhoGEFs) also play a role in these events by acting as primary Rho GTPase activators. (cellsignal.com)
  • The proteases involved are of different origins and types: (i) present as precursor in plasma, (ii) secreted into the plasma by activated platelets or other blood cells, or (iii) intracellularly activated and cleaving cytosolic receptor domains. (frontiersin.org)
  • In the resulting arrangement, the tetramerization domain is largely shielded by the catalytic domains, which may contribute to the stability of the human BChE (HuBChE) tetramer. (rcsb.org)
  • domain of Tiam-1 to Rac-1 the switch I region within the GTP binding pocket of Rac-1 is shifted and binds within a groove formed by the CR1 and CR3 regions within Tiam-1. (cellsignal.com)
  • A second loop precedes large "amphipathic α-helix" (hA) that longitudinally spans protein site. (wikipedia.org)
  • The α-helix hB finishes abruptly at Gly225 where the last loop of the domain starts. (wikipedia.org)
  • This domain includes a mostly solvent exposed loop (residue 33-43) preceding the beta hairpin containing the flaps (residue 44-63). (proteopedia.org)
  • Functional diversity between PTPases is endowed by regulatory domains and subunits. (embl.de)
  • In previous works, we established that the PRO domain is a key regulator of TYMV replication. (datexis.com)
  • The PRO domain is also essential for the recruitment of 66K to the membrane replication sites. (datexis.com)
  • Two short α-helices form the inhibitory domain and block the catalytic center under basal low Ca 2+ conditions. (pancreapedia.org)
  • the CaM binding α helix is contained within the this DR. (right panel) X-ray crystallography of CaM (blue) demonstrates binding to the α helix of CnA (colored yellow). (pancreapedia.org)
  • Distinct signature sequences in the nucleotide-binding domain have been linked to the binding of NAD(+) versus NADP(+), but they are not unambiguous predictors of cofactor preference. (anl.gov)
  • Note the regulatory domains that bind CnB and CaM as well as the autoinhibitory domain (AI). (pancreapedia.org)