Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
A [auth B]F_UNCLASSIFIEDe2pv0B3 A: a/b three-layered sandwichesX: Rossmann-likeH: Rossmann-relatedT: S-adenosyl-L-methionine-dependent methyltransferasesF: F_UNCLASSIFIEDECOD (1.6)
A [auth B]PF17980e2pv0B1 A: few secondary structure elementsX: RING/U-box-likeH: RING/U-box-likeT: FYVE/PHD zinc fingerF: PF17980ECOD (1.6)
A [auth B]PF21255e2pv0B2 A: few secondary structure elementsX: RING/U-box-likeH: RING/U-box-likeT: FYVE/PHD zinc fingerF: PF21255ECOD (1.6)
B [auth A]F_UNCLASSIFIEDe2pv0A6 A: a/b three-layered sandwichesX: Rossmann-likeH: Rossmann-relatedT: S-adenosyl-L-methionine-dependent methyltransferasesF: F_UNCLASSIFIEDECOD (1.6)
B [auth A]PF17980e2pv0A5 A: few secondary structure elementsX: RING/U-box-likeH: RING/U-box-likeT: FYVE/PHD zinc fingerF: PF17980ECOD (1.6)
B [auth A]PF21255e2pv0A4 A: few secondary structure elementsX: RING/U-box-likeH: RING/U-box-likeT: FYVE/PHD zinc fingerF: PF21255ECOD (1.6)
CF_UNCLASSIFIEDe2pv0C6 A: a/b three-layered sandwichesX: Rossmann-likeH: Rossmann-relatedT: S-adenosyl-L-methionine-dependent methyltransferasesF: F_UNCLASSIFIEDECOD (1.6)
CPF17980e2pv0C5 A: few secondary structure elementsX: RING/U-box-likeH: RING/U-box-likeT: FYVE/PHD zinc fingerF: PF17980ECOD (1.6)
CPF21255e2pv0C4 A: few secondary structure elementsX: RING/U-box-likeH: RING/U-box-likeT: FYVE/PHD zinc fingerF: PF21255ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

ChainDomainClassArchitectureTopologyHomologyProvenance Source (Version)
A [auth B]3.40.50.150 Alpha Beta 3-Layer(aba) Sandwich Rossmann fold Vaccinia Virus protein VP39CATH (4.3.0)
B [auth A]3.40.50.150 Alpha Beta 3-Layer(aba) Sandwich Rossmann fold Vaccinia Virus protein VP39CATH (4.3.0)
C3.40.50.150 Alpha Beta 3-Layer(aba) Sandwich Rossmann fold Vaccinia Virus protein VP39CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
A [auth B],
B [auth A],
C
PF21255DNMT3, ADD PHD zinc finger (ADDz_Dnmt3b)DNMT3, ADD PHD zinc fingerDNMT3s are de novo DNA methyltransferases responsible for the establishment of DNA methylation patterns in mammalian genomes [1-4]. The ATRX-DNMT3-DNMT3L (ADD) domain contains two parts, a C2-C2-like zinc finger (Pfam:PF17980) and a PHD-like zinc fin ...DNMT3s are de novo DNA methyltransferases responsible for the establishment of DNA methylation patterns in mammalian genomes [1-4]. The ATRX-DNMT3-DNMT3L (ADD) domain contains two parts, a C2-C2-like zinc finger (Pfam:PF17980) and a PHD-like zinc finger, represented in this entry. In this domain, the conserved His residue observed in classical PHD zinc fingers is replaced by a cysteine.
Domain
A [auth B],
B [auth A],
C
PF17980Cysteine rich ADD domain in DNMT3 (ADD_DNMT3)Cysteine rich ADD domain in DNMT3This is a cysteine-rich domain termed ADD (ATRX-DNMT3-DNMT3L, AD-DATRX) found in DNMT3A proteins. The ADD domains of the DNMT3 family have a decisive role in blocking DNMT activity in the areas of the genome with chromatin containing methylated H3K4. ...This is a cysteine-rich domain termed ADD (ATRX-DNMT3-DNMT3L, AD-DATRX) found in DNMT3A proteins. The ADD domains of the DNMT3 family have a decisive role in blocking DNMT activity in the areas of the genome with chromatin containing methylated H3K4. Furthermore, the ADD domain of DNMMT3A (ADD-3A) competes with the chromodomain (CD) of heterochromatin protein 1 alpha (HP1alpha, CDHP1alpha) for binding to the H3 tail. The DNA methyltransferase (DNMT) 3 family members DNMT3A and DNMT3B and the DNMT3-like non-enzymatic regulatory factor DNMT3L, are involved in de-novo establishment of DNA methylation patterns in early mammalian development [1,2].
Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
A [auth B],
B [auth A],
C
DNA (cytosine-5)-methyltransferase 3-like