Modomics - A Database of RNA Modifications

ID Card:

Full name: alkB homolog 4, lysine demethylase
Synonym: FLJ20013
GI: 74734701
UniProt: Q9NXW9
Alpha Fold Predicted Structure: AF-Q9NXW9-F1



Protein sequence:

MAAAAAETPEVLRECGCKGIRTCLICERQRGSDPPWELPPAKTYRFIYCSDTGWAVGTEESDFEGWAFPFPGVMLIEDFVTREEEAELVRLMDRDPWKLSQSGRRKQDYGPKVNFRKQKLKTEGFCGLPSFSREVVRRMGLYPGLEGFRPVEQCNLDYCPERGSAIDPHLDDAWLWGERLVSLNLLSPTVLSMCREAPGSLLLCSAPSAAPEALVDSVIAPSRSVLCQEVEVAIPLPARSLLVLTGAARHQWKHAIHRRHIEARRVCVTFRELSAEFGPGGRQQELGQELLRIALSFQGRPV

Comments:

Alpha-ketoglutarate-Dependent Dioxygenase AlkB Homolog4 is a member of the superfamily of alpha-ketoglutarate and Fe(II)-dependent dioxygenase, and is located in the nucleus and cytoplasm (Li al. 2013 ). It is involved in both DNA and protein dmethylation. Specifically, it demethylates DNA N(6)-methyladenosine (m6A), therby having a role in Pylycom silencing (Li al. 2013 ).

S-adenosyl-methionine-dependent-methyltransferases are a highly versatile class of enzymes that is involved in the transfer of methyl groups to different biomolecules such as DNA, proteins and small-metabolites (Struck al. 2012 ). Of note, SAM methylates Lys84 (K84me1) in actin. K84me1 maintain actomyosine dynamics and supports the normal cleavage furrow ingression during cytokinesis and cell migration (Li al. 2013 ).

Non-muscle myosin II (NMII) generates the contractile force that is required for furrow regression, specifically by sliding along F-actin filaments. ALKBH4 demethylates K84me1 contributing to the maintenance of actomyosin dynamics, supporting normal cleavage furrow regression during cytokinesis and cell migration (Li al. 2013 ).





Alpha Fold Predicted Structure:






Clear Selection and Reset Camera

Protein sequence:

M A A A A A E T P E V L R E C G C K G I R T C L I C E R Q R G S D P P W E L P P A K T Y R F I Y C S D T G W A V G T E E S D F E G W A F P F P G V M L I E D F V T R E E E A E L V R L M D R D P W K L S Q S G R R K Q D Y G P K V N F R K Q K L K T E G F C G L P S F S R E V V R R M G L Y P G L E G F R P V E Q C N L D Y C P E R G S A I D P H L D D A W L W G E R L V S L N L L S P T V L S M C R E A P G S L L L C S A P S A A P E A L V D S V I A P S R S V L C Q E V E V A I P L P A R S L L V L T G A A R H Q W K H A I H R R H I E A R R V C V T F R E L S A E F G P G G R Q Q E L G Q E L L R I A L S F Q G R P V
50100150200250300SequenceGHTBSN

Secondary Structure Alphabet

  • G: 3-turn helix (310helix)
  • H: α-helix
  • I: 𝝅-helix (5 - turn helix)
  • T: Hydrogen Bonded Turn
  • B: β-sheet
  • S: Bend
  • C: Coil (residues not present in any of the above conformations)
  • N: Not assigned

Download PDB Structures & DSSP Secondary Structures:

Alpha Fold Pdb Files   AF-Q9NXW9-F1.pdb  
Alpha Fold Pdbx/mmCIF Files   AF-Q9NXW9-F1.cif  
DSSP Secondary Structures   Q9NXW9.dssp  





Diseases connected to this enzyme:

Publications: