• Proteins
  • Although proteins of the PARP family are related through their PARP catalytic domain, they do not resemble each other outside of that region, but rather, they contain unique domains that distinguish them from each other and hint at their discrete functions. (ebi.ac.uk)
  • centre
  • 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. (ebi.ac.uk)
  • The polypeptide has a highly conserved modular organisation consisting of an N-terminal DNA-binding domain, a central regulating segment, and a C-terminal or F region accommodating the catalytic centre. (ebi.ac.uk)
  • motifs
  • The methyltransferases or methylases are classified into three groups (Groups α, β, and γ) based on the sequential order of certain 9 motifs and the Target Recognition Domain (TRD). (wikipedia.org)
  • Motifs IV-VIII play a role in the catalytic activity, while motifs 1-III and X play a role in binding of the cofactor. (wikipedia.org)
  • Its primary structure comprises several domain motifs. (wikipedia.org)
  • membrane-bindin
  • Exon 2 contains the junction of the membrane-binding domain and the catalytic domain of b5R, which shows that there are two forms of b5R: a soluble form and a membrane-bound form. (wikipedia.org)
  • The NH2-terminal structure of the membrane-binding domain is CH3(CH2)12-CO-Gly-Ala-Gln-Leu-Ser-Thr-Leu-Gly-His-Met-Val-Leu-Phe-Pro-Val-Trp-Phe-Leu-Tyr-Ser-Leu-Leu-Met-Lys. (wikipedia.org)
  • activity
  • This domain catalyses a demethylase activity with a preference for 3-methylthymidine. (ebi.ac.uk)
  • 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)
  • consists
  • The alpha-hd domain is about 130 amino acids in length and consists of an up-up-down-up-down-down motif of helices. (ebi.ac.uk)
  • cleft
  • The Structure of Shikimate dehydrogenase is characterized by two domains, two alpha helices and two beta sheets with a large cleft separating the domains of the monomer. (wikipedia.org)
  • amino acids
  • 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)
  • A carboxy-terminal region of one hundred and fifty-nine amino acids, the focal adhesion targeting domain (FAT), has been shown to be responsible for targeting FAK to focal adhesions. (wikipedia.org)
  • cytochrome
  • Cytochrome b5 reductase is involved in the transfer of reducing equivalents from the physiological electron donor, NADH, via an FAD domain to the small molecules of cytochrome b5. (wikipedia.org)
  • alpha
  • However, unlike the typical cytidine deaminases, APOBEC3G contains a unique alpha helix between two beta sheets in the catalytic domain that could be a cofactor binding site. (wikipedia.org)
  • This domain is composed of four alpha helices arranged in a bundle. (wikipedia.org)
  • site
  • The N- and C-terminal domains, although structurally related by a 2-fold axis, have only limited sequence homology except the vicinity of the active site. (ebi.ac.uk)
  • APOBEC3G has a symmetric structure, resulting in 2 homologous catalytic domains, the N-terminal (CD1) and C-terminal (CD2) domains, each of which contains a Zn2+ coordination site. (wikipedia.org)
  • mainly
  • The PH domain functions mainly in the interaction of PDPK1 with phosphatidylinositol (3,4)-bisphosphate and phosphatidylinositol (3,4,5)-trisphosphate which is important in localization and activation of some of membrane associated PDPK1's substrates including AKT. (wikipedia.org)
  • histone
  • Nucleosome formation is dependent on the positive charges of the H4 histones and the negative charge on the surface of H2A histone fold domains. (wikipedia.org)
  • inactive
  • Inactive single domain phosphatases can still specifically bind substrates, and protect again dephosphorylation, while the inactive domains of tandem phosphatases can be further subdivided into two classes. (ebi.ac.uk)
  • role
  • The Catalytic Domain of MMP-1 is composed of five highly twisted β-strands (sI-sV), three α-helix (hA-hC) and a total of eight loops, enclosing a total of five metal ions, three Ca2+ and two Zn2+, one of which with catalytic role. (wikipedia.org)