Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
APF02373,PF02375e5fwjA1 A: beta sandwichesX: jelly-rollH: Double-stranded beta-helix (From Topology)T: Double-stranded beta-helixF: PF02373,PF02375ECOD (1.6)
APF02928e5fwjA3 A: few secondary structure elementsX: Glucocorticoid receptor-likeH: LIM domain-likeT: LIM domain-likeF: PF02928ECOD (1.6)
BPF02373,PF02375e5fwjB3 A: beta sandwichesX: jelly-rollH: Double-stranded beta-helix (From Topology)T: Double-stranded beta-helixF: PF02373,PF02375ECOD (1.6)
BPF02928e5fwjB1 A: few secondary structure elementsX: Glucocorticoid receptor-likeH: LIM domain-likeT: LIM domain-likeF: PF02928ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

ChainDomainClassArchitectureTopologyHomologyProvenance Source (Version)
A2.60.120.650 Mainly Beta Sandwich Jelly Rolls CupinCATH (4.3.0)
B2.60.120.650 Mainly Beta Sandwich Jelly Rolls CupinCATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
A, B
PF21323Lysine-specific demethylase 5, C-terminal helical domain (KDM5_C-hel)Lysine-specific demethylase 5, C-terminal helical domainThis is the C-terminal helical domain from Lysine-specific demethylase 5 subfamily (KDM5), which is localised between the Jumonji C (JmjC) domain and the C5HC2 zinc finger motif (Pfam:PF02928) [1-5].Domain
A, B
PF02928C5HC2 zinc finger (zf-C5HC2)C5HC2 zinc fingerPredicted zinc finger with eight potential zinc ligand binding residues. This domain is found in Jumonji [1]. This domain may have a DNA binding function.Domain
A, B
PF02373JmjC domain, hydroxylase (JmjC)JmjC domain, hydroxylaseThe JmjC domain belongs to the Cupin superfamily [3]. JmjC-domain proteins may be protein hydroxylases that catalyse a novel histone modification [4]. This is confirmed to be a hydroxylase: the human JmjC protein named Tyw5p unexpectedly acts in the ...The JmjC domain belongs to the Cupin superfamily [3]. JmjC-domain proteins may be protein hydroxylases that catalyse a novel histone modification [4]. This is confirmed to be a hydroxylase: the human JmjC protein named Tyw5p unexpectedly acts in the biosynthesis of a hypermodified nucleoside, hydroxy-wybutosine, in tRNA-Phe by catalysing hydroxylation [5].
Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
A, B
HISTONE DEMETHYLASE JARID1C