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  • 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)
  • homology
  • 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)
  • Poly(ADP-ribose) polymerases: homology, structural domains and functions. (ebi.ac.uk)
  • orientation
  • The activation of PDPK1's main effector, AKT, is believed to require a proper orientation of the kinase and PH domains of PDPK1 and AKT at the membrane. (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)
  • subunit
  • The function of the amino-terminal domain is less clear, but it has been shown to interact with the beta-1 integrin subunit in vitro and is thought to be involved in the transduction of signals from ECM-integrin clusters. (wikipedia.org)
  • functions
  • The N-terminal SH2 domain of this protein functions as a positive regulator of transformation whereas the C-terminal SH3 domain functions as a negative regulator of transformation. (wikipedia.org)
  • capable
  • a translocation domain that is capable of translocating the protease or protease fragment from within an endosome, across the endosomal membrane and into the cytosol of the nociceptive sensory afferent. (patentsencyclopedia.com)