• The N-terminal domain of APOBEC-1 like proteins is the catalytic domain, while the C-terminal domain is a pseudocatalyitc domain. (embl.de)
  • Englbrecht CC, Schoof H, Bohm S (2004) Conservation, diversification and expansion of C2H2 zinc finger proteins in the Arabidopsis thaliana genome. (springer.com)
  • Proteins containing this domain are listed below. (embl.de)
  • There are 13548 MAM domains in 5639 proteins in SMART's nrdb database. (embl.de)
  • Taxonomic distribution of proteins containing MAM domain. (embl.de)
  • The complete taxonomic breakdown of all proteins with MAM domain is also avaliable . (embl.de)
  • Click on the protein counts, or double click on taxonomic names to display all proteins containing MAM domain in the selected taxonomic class. (embl.de)
  • There are 308772 RING domains in 276130 proteins in SMART's nrdb database. (embl-heidelberg.de)
  • MMP9 (matrix metallopeptidase 9, GELB, CLG4B) is a matrix metalloproteinase, a family of zinc and calcium-dependent endopeptidases that degrade extracellular matrix proteins. (thermofisher.com)
  • Several mammalian proteins involved in chromatin and DNA modification contain CXXC zinc finger domains. (cipsm.de)
  • The MARCKS domain regulates the nuclear localizations of type IV DGKs while the PDZ-binding and ankyrin domains regulate interactions with several proteins. (nih.gov)
  • Among the established custom DNA binding domains, Cas9 is most easily scaled to facilitate genome-scale perturbations 3 , 4 due to its simplicity of programming relative to zinc finger proteins and transcription activator-like effectors (TALEs). (cdc.gov)
  • This domain occurred 337 times on human genes ( 772 proteins). (umbc.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)
  • The means by which the activity of the catalytic subunit of CSN (CSN5) is regulated is not fully understood and thus new tools are required to study its activity. (gla.ac.uk)
  • It consists of 2 catalytic (C) trimers held together by 3 dimers of regulatory (R) subunit which is itself composed of an effector binding domain and a Zinc binding domain. (europa.eu)
  • 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)
  • 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)
  • In contrast, the CXXC domain of Dnmt1 selectively binds DNA substrates containing unmethylated CpG sites. (cipsm.de)
  • The propeptide domain contains a cysteine residue that binds zinc in the active site to form the cysteine switch. (periobasics.com)
  • In its binding with sulfhydryl groups, lead may interfere with the activity of zinc metalloenzymes, as zinc binds to a sulfhydryl group at the active site. (cdc.gov)
  • Lead also binds to metallothionein, a sulfhydryl-rich protein, but does not appear to displace cadmium or zinc. (cdc.gov)
  • This work demonstrated that, while ACE is a single polypeptide chain, it is composed of two homologous catalytic domains, each of which is independently catalytic. (cedars-sinai.edu)
  • Its primary structure comprises several domain motifs. (wikipedia.org)
  • a Domain organization of the four subunits of human Pol δ and amino acid sequence of PCNA-interacting (PIP-box) motifs. (nature.com)
  • Zinc finger (Znf) domains are relatively small protein motifs which contain multiple finger-like protrusions that make tandem contacts with their target molecule. (embl-heidelberg.de)
  • Zinc-binding motifs are stable structures, and they rarely undergo conformational changes upon binding their target. (embl-heidelberg.de)
  • It contains a catalytic domain, a central coiled-coil domain, and a C-terminal region containing a Rho-binding domain (RBD), a zinc finger, and a pleckstrin homology (PH) domain, in addition to other motifs. (umbc.edu)
  • It ligates the catalytic zinc to maintain the enzyme in an inactive state. (wikipedia.org)
  • The catalytic domain, which is responsible for enzyme activity, contains the highly conserved Zn 2+ binding region. (chemdiv.com)
  • Angiotensin-converting enzyme (ACE) is a zinc metalloprotease best known for its role in blood pressure regulation. (rcsb.org)
  • This domain is found at the N terminus of the Apolipoprotein B mRNA editing enzyme. (embl.de)
  • This indicates that these domain-domain interactions are critical for structure and function of the enzyme. (embl.de)
  • The aim of the project was to characterize intrachain and interchain interactions involved in the regulatory behaviour of a model allosteric enzyme of known 3-dimensional structure: aspartate carbamoyltransferase (ATCase) of Escherichia coli, a protein consisting of distinct catalytic and regulatory subunits. (europa.eu)
  • In order to investigate the interchain contacts involved in the cooperative interactions between the catalytic sites, a series of modified forms of the enzyme was prepared by site directed mutagenesis. (europa.eu)
  • The results obtained show that the R1-C4 interaction is essential for the establishment of the enzyme conformation having low affinity for aspartate (T state), and consequently for the existence of cooperactivity between the catalytic sites. (europa.eu)
  • Modulation of the renin-angiotensin system (RAS), and particularly inhibition of angiotensin-converting enzyme (ACE), a zinc metallopeptidase, has long been a prime strategy in the treatment of hypertension. (scienceopen.com)
  • Angiotensin converting enzyme 2 (ACE-2), also known as ACEH (ACE homolog), is an integral membrane protein and a zinc metalloprotease of the ACE family. (bio-techne.com)
  • We show that cdHDAC7 has an additional class IIa HDAC-specific zinc binding motif adjacent to the active site which is likely to participate in substrate recognition and protein-protein interaction and may provide a site for modulation of activity. (rcsb.org)
  • The catalytic zinc is coordinated by three histidines from the conserved HEXXHXXGXXH binding motif. (wikipedia.org)
  • In order to determine the acyltransferases responsible for the modification of Spike, researchers have individually depleted the 23 conserved zinc-finger domains with a DHHC motif in their catalytic sites (ZDHHCs) by RNA interference in Hela cells. (news-medical.net)
  • The 3D structure of the zinc ligation system is unique to the RING domain and is referred to as the 'cross-brace' motif. (embl-heidelberg.de)
  • All five members of this family (SMYD1-5) contain a conserved catalytic SET domain and a zinc-finger MYND motif. (thesgc.org)
  • This suggests the involvement of these subsites in conferring C-domain-selective BPPb binding, in agreement with the mutagenesis results where unique residues governing differences in active site exposure, lid structure and dynamics between the two domains were the major drivers for C-domain-selective BPPb binding. (rcsb.org)
  • Mere disruption of BPPb interactions with unique S 2 and S 4 subsite residues, which synergistically assist in BPPb binding, was insufficient to abolish C-domain selectivity. (rcsb.org)
  • The combination of unique S 9 -S 4 and S 2 ' subsite C-domain residues was required for the favourable entry, orientation and thus, selective binding of the peptide. (rcsb.org)
  • Two non-consecutive sets of zinc-binding residues form two separate metal-binding sites. (nih.gov)
  • The human MMP9 proenzyme consists of five domains. (wikipedia.org)
  • The MAM domain consists of approximately 170 amino acids. (embl.de)
  • These PTPases have an extracellular region which consists of a MAM domain followed by an Ig-like domain and four fibronectin-type III domains. (embl.de)
  • It consists at least of a catalytic light chain and a multidomain heavy chain which has 2 LDL receptor class A domains, a MAM domain, a SRCR domain and a CUB domain. (embl.de)
  • Structurally, MMP8 consists of several domains: a prodomain that is cleaved upon activation, a catalytic domain containing the zinc-binding site, a short hinge region and a hemopexinlike domain. (reliatech.de)
  • The predicted human ACE-2 protein sequence consists of 805 amino acids, including a N-terminal signal peptide, a single catalytic domain, a C-terminal membrane anchor, and a short cytoplasmic tail. (bio-techne.com)
  • Matrix metallopeptidase 9 (MMP-9), also known as 92 kDa type IV collagenase, 92 kDa gelatinase or gelatinase B (GELB), is a matrixin, a class of enzymes that belong to the zinc-metalloproteinases family involved in the degradation of the extracellular matrix. (wikipedia.org)
  • These enzymes share common functional domains and activation mechanisms as they depend on Ca 2+ and Zn 2+ ions and are active at neutral pH. (periobasics.com)
  • Matrix metalloproteases (MMPs) are a family of zinc-dependent endopeptidases that collectively have the capacity to degrade virtually every component of the extracellular matrix (ECM). (chemdiv.com)
  • Matrix metalloproteinase are a family of zinc dependent endopeptidases that are capable of degrading most components of the extra cellular matrix (ECM) [ 7 - 9 ]. (biomedcentral.com)
  • Matrix metalloproteinases (MMPs) are a family of zinc and calcium dependent endopeptidases with the combined ability to degrade all the components of the extracellular matrix. (reliatech.de)
  • The characteristic domain structure of MMPs includes 4 domains. (chemdiv.com)
  • Matrix metalloproteinases (MMPs) are a family of zinc-dependent proteinases that are capable of cleaving all extra cellular matrix (ECM) substrates. (biomedcentral.com)
  • Tissue inhibitors of matrix metallo-proteinases (TIMPs) are known to have the ability to inhibit the catalytic activity of MMPs. (biomedcentral.com)
  • The structural organization of all MMPs presents a prepeptide sequence that directs their secretion in the extracellular environment and a propeptide domain that maintains them in their zymogenic form. (periobasics.com)
  • Other MMPs, known as membrane-type MMPs (MT-MMP), are linked to the plasma membrane either by a transmembrane domain or by a glycosyl-phosphatidyl inositol linkage, attached to the hemopexin domain. (periobasics.com)
  • Four of the MT-MMPs contain hydrophobic transmembrane domains (MMP-14, MMP-15, MMP-16, MMP-24), followed by a cytoplasmic domain. (periobasics.com)
  • In humans the MMP9 gene encodes for a signal peptide, a propeptide, a catalytic domain with inserted three repeats of fibronectin type II domain followed by a C-terminal hemopexin-like domain. (wikipedia.org)
  • Serine/Threonine Kinases (STKs), Citron Rho-interacting kinase (CRIK) subfamily, catalytic (c) domain. (umbc.edu)
  • The CRIK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. (umbc.edu)
  • MMP9 has a gelatin-binding domain consisting of three fibronectin type II units, a catalytic domain containing the zinc-binding site, a proline-rich type V collagen-homologous domain and a hemopexin-like domain. (thermofisher.com)
  • The catalytic core sits on top of PCNA in an open configuration while the regulatory subunits project laterally. (nature.com)
  • In both subunits, the MAM domain is located after the catalytic domain. (embl.de)
  • Here, we characterize the structure and enzymatic activity of the catalytic domain of human HDAC7 (cdHDAC7). (rcsb.org)
  • Early inhibitors targeting MMP activity were designed to bind within the catalytic domain of these proteases. (chemdiv.com)
  • The Gap1 catalytic domain alone is insufficient for in vivo activity of Gap1, indicating a requirement for the additional domains. (sdbonline.org)
  • 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)
  • CSN5 contains a JAMM domain with a Zn2+ atom facilitating its catalytic activity. (gla.ac.uk)
  • The synthesis of several activity-based probes for CSN5 was attempted, each containing a zinc-binding group (ZBG) for attachment onto the catalytic site, a NEDD8 peptide to enable selectivity to CSN5 and a biotin tag for subsequent biochemical assays. (gla.ac.uk)
  • The Bernstein Laboratory studies how ACE and other components of the renin-angiotensin system affect blood pressure.One of the major products of ACE catalytic activity is the peptide angiotensin II, one of the central regulators of blood pressure. (cedars-sinai.edu)
  • We show that the CXXC domain of Tet1 has no DNA binding activity and is dispensable for catalytic activity in vivo. (cipsm.de)
  • Interestingly, neither wild type nor ΔCXXC Dnmt1 re-methylated imprinted CpG sites of the H19a promoter in dnmt1−/− ESCs, arguing against a role of the CXXC domain in restraining Dnmt1 methyltransferase activity on unmethylated CpG sites. (cipsm.de)
  • Biochemical and activity-based probe analyses identify a non-canonical zinc finger domain as the E3 active site, which utilizes the strictly conserved Cys4462, not involved in zinc coordination, as the reactive nucleophile. (biorxiv.org)
  • Here we present a novel activity of recombinant ADAM12-S and its domain deletion mutants on S-carboxymethylated transferrin (Cm-Tf). (ox.ac.uk)
  • Kinetic analysis revealed that the noncatalytic C-terminal domains are important regulators of Cm-Tf activity and that ADAM12-PC consisting of the pro domain and catalytic domain is the most active on this substrate. (ox.ac.uk)
  • This cell surface glycoprotein contains a zinc-metalloprotease domain capable of degrading a variety of polypeptides. (embl.de)
  • We present the BPPb N-domain structure in comparison with the previously reported BPPb C-domain structure and highlight key differences in peptide interactions with the S 4 to S 9 subsites. (rcsb.org)
  • This emphasizes the need to consider factors other than direct protein-inhibitor interactions to guide the design of domain-selective ACE inhibitors, especially in the case of larger peptides. (rcsb.org)
  • In receptor tyrosine phosphatase mu-like molecules the MAM domain is important for homophilic cell-cell interactions. (embl.de)
  • The domain has been shown to play a role in homodimerization of protein-tyrosine phosphatase mu [ ( PUBMED:7782276 ) ] and appears to help determine the specificity of these interactions. (embl.de)
  • No pairwise interactions are available for this conserved domain. (umbc.edu)
  • Apart from the catalytic domain in the middle of the molecule, all Gap1 family members share two N-terminal C2 domains and a C-terminal extended PH domain. (sdbonline.org)
  • Species diversity in the structure of zonadhesin, a sperm-specific membrane protein containing multiple cell adhesion molecule-like domains. (embl.de)
  • Three zinc-binding groups were considered including hydroxamic acid, imidazole and a precursor of a potent small molecule CSN5 inhibitor, CSN5i-3. (gla.ac.uk)
  • A dinuclear metal center composed of one iron and one zinc molecule each lies next to a β sandwich on the active site ( Figure 2 ). (pancreapedia.org)
  • We compared the structure and function of the CXXC domains in the DNA methyltransferase Dnmt1 and the methylcytosine dioxygenase Tet1. (cipsm.de)
  • 1.Brown MA, Sims RJ 3rd, Gottlieb PD, Tucker PW (2006) Identification and characterization of Smyd2: a split SET/MYND domain-containing histone H3 lysine 36-specific methyltransferase that interacts with the Sin3 histone deacetylase complex . (thesgc.org)
  • However, the physiological relevance of any of these domains for Gap1 in vivo function has not been established. (sdbonline.org)
  • Surprisingly, a Dnmt1 mutant construct lacking the CXXC domain formed covalent complexes with cytosine bases both in vitro and in vivo and rescued DNA methylation patterns in dnmt1−/− embryonic stem cells (ESCs) just as efficiently as wild type Dnmt1. (cipsm.de)
  • Human ADAM12 (a disintegrin and metalloproteinase) is a multidomain zinc metalloproteinase expressed at high levels during development and in human tumors. (ox.ac.uk)
  • 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)
  • The spacing of the cysteines in such a domain is C-x(2)-C-x(9 to 39)-C-x(1 to 3)-H-x(2 to 3)-C-x(2)-C-x(4 to 48)-C-x(2)-C. Metal ligand pairs one and three co-ordinate to bind one zinc ion, whilst pairs two and four bind the second. (embl-heidelberg.de)
  • CnB resembles CaM in that both bind to an extended α helix on their respective CnA domains. (pancreapedia.org)
  • Note the regulatory domains that bind CnB and CaM as well as the autoinhibitory domain (AI). (pancreapedia.org)
  • Here, we used site-directed mutagenesis, an ACE chimera and X-ray crystallography to unveil the molecular basis for C-domain-selective ACE inhibition by the bradykinin-potentiating peptide b (BPPb), naturally present in Brazilian pit viper venom. (rcsb.org)
  • In a separate approach, a peptide of the NEDD8 C-terminal tail was synthesised and successfully biotinylated, however conjugation to the zinc-binding groups hydroxamic acid and imidazole were unsuccessful due to the low solubility of the peptide. (gla.ac.uk)
  • Collectrin lacks a catalytic domain, which indicates that there is more to ACE-like function than simple peptide hydrolysis. (scienceopen.com)
  • Site directed mutagenesis was used to check the catalytic role of residue C his 134, which is in a position to interact with the carbonyl group of CP, and was a candidate for bearing a group whose deprotonation is involved in catalytic efficiency. (europa.eu)
  • The results establish that C his 134 is indeed the residue interacting with the carbonyl group of CP but that it is not directly involved in the catalytic mechanism. (europa.eu)
  • The 1.9Å crystal structure of the human CA VI catalytic domain reveals a prototypical mammalian CA fold, and a novel dimeric arrangement as compared to previously-reported CA structures. (ox.ac.uk)
  • It is classified as a type IV DAG kinase (DGK), containing myristoylated alanine-rich protein kinase C substrate (MARCKS), PDZ-binding, and ankyrin domains, in addition to C1 and catalytic domains that are present in all DGKs. (nih.gov)
  • DAG kinase iota contains two copies of the C1 domain. (nih.gov)
  • Catalytic domain of the Protein Serine/Threonine Kinase, Citron Rho-interacting kinase. (umbc.edu)
  • Oxidoreductase FAD-binding domain, Oxidoreductase NAD-binding domain, 2Fe-2S iron-sulfur cluster binding domain [Interproscan]. (ntu.edu.sg)
  • Binding of CaM along with Ca 2+ binding to CnB induces displacement of the inhibitory domain, thus exposing the catalytic domain. (pancreapedia.org)
  • Depletion of intracellular zinc by N,N,N′,N′ -tetrakis(2-pyridylmethyl) ethylenediamine (TPEN) induces p53-mediated protein synthesis-dependent apoptosis of mouse cortical neurons. (molcells.org)
  • The crystal structures of human cdHDAC7 and its complexes with two hydroxamate inhibitors are the first structures of the catalytic domain of class IIa HDACs and demonstrate significant differences with previously reported class I and class IIb-like HDAC structures. (rcsb.org)
  • Three type II fibronectin repeats are inserted in the catalytic domain, although these domains are omitted in most crystallographic structures of MMP9 in complex with inhibitors. (wikipedia.org)
  • Their binding properties depend on the amino acid sequence of the finger domains and of the linker between fingers, as well as on the higher-order structures and the number of fingers. (embl-heidelberg.de)
  • The hemopexin domain is important to facilitate the cleavage of triple helical interstitial collagens. (wikipedia.org)
  • They have yielded positive results from their combined strategy of adjusting the binding affinity of the zinc finger array and slowing the catalytic rate of the Fok1 cleavage domain. (explorebiotech.com)
  • Here, we identified a C 2 H 2 -type zinc finger transcription factor from Arabidopsis , ZAT10, as a substrate of MPKs. (springer.com)
  • Here, we examined the requirement for poly(ADP-ribose) polymerase (PARP)-1 as an upstream regulator of p53 in zinc depletion-induced neuronal apoptosis. (molcells.org)
  • LysR substrate binding domain, Bacterial regulatory helix-turn-helix protein [Interproscan]. (ntu.edu.sg)
  • So, all MMP's may be regarded as derivatives of a 4-domain prototype structure, formed either by addition or deletion of regulatory domains. (periobasics.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)
  • While current generation ACE inhibitors target both ACE domains, domain-selective ACE inhibitors may be clinically advantageous, either reducing side effects or having utility in new indications. (rcsb.org)
  • Among the tissue inhibitors of metalloproteinases (TIMP) examined, the N-terminal domain of TIMP-3 (N-TIMP-3) inhibits ADAM12-S and ADAM12-PC with low nanomolar Ki(app) values while TIMP-2 inhibits them with a slightly lower affinity (9-44 nM). (ox.ac.uk)
  • Cas9 nuclease can be converted into an RNA-guided DNA binding protein (dCas9) via inactivation of its two catalytic domains 12 , 13 and then fused to transcription activation domains. (cdc.gov)
  • MMP-2 and MMP-9 (also known as gelatinases based on their substrate preference) contain fibronectin-like domain repeats which aid in substrate binding. (periobasics.com)
  • MMP-7 or matrilysins is smallest in size and lacks the hemopexin domain, yet it displays specificity in substrate degradation. (periobasics.com)
  • The propeptide domain is characterized by a conserved PRCGVPD sequence. (wikipedia.org)
  • ACE2 is a type I integral membrane protein with its active site domain exposed to the extracellular surface of endothelial cells and the renal tubular epithelium. (scienceopen.com)
  • SET and MYND domain-containing protein 2 (SMYD2) is a member of the SMYD family of protein methyltransferases. (thesgc.org)
  • Glycosyl hydrolases family 2, Beta galactosidase small chain, Domain of unknown function(DUF4981) [Interproscan]. (ntu.edu.sg)
  • 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)
  • ADAM12 exists as two splice variants: a classical type 1 membrane-anchored form (ADAM12-L) and a secreted splice variant (ADAM12-S) consisting of pro, catalytic, disintegrin, cysteine-rich, and EGF domains. (ox.ac.uk)
  • the E-value for the APOBEC_N domain shown below is 3.6e-38. (embl.de)
  • APOBEC-3 like members contain two copies of this domain. (embl.de)
  • Lead interferes with the synthesis of heme, resulting in accumulation of ALA in tissues and elevated excretion of ALA in urine, elevation of zinc protoporphyrin in erythrocyte, reductions in blood hemoglobin, and in a hypochromic, normocytic anemia at higher levels of exposure. (cdc.gov)