| Primary Identifier | IPR004087 | Type | Domain |
| Short Name | KH_dom |
| description | The K homology (KH) domain was first identified in the human heterogeneous nuclear ribonucleoprotein (hnRNP) K. An evolutionarily conserved sequence of around 70 amino acids, the KH domain is present in a wide variety of nucleic acid-binding proteins. The KH domain binds RNA, and can function in RNA recognition []. It is found in multiple copies in several proteins, where they can function cooperatively or independently. For example, in the AU-rich element RNA-binding protein KSRP, which has 4 KH domains, KH domains 3 and 4 behave as independent binding modules to interact with different regions of the AU-rich RNA targets []. The solution structure of the first KH domain of FMR1 []and of the C-terminal KH domain of hnRNP K []determined by nuclear magnetic resonance(NMR) revealed a β-α-α-β-β-α structure. Proteins containing KH domains include:Bacterial and organelle PNPases [].Archaeal and eukaryotic exosome subunits [].Eukaryotic and prokaryotic RS3 ribosomal proteins [].Vertebrate Fragile X messenger ribonucleoprotein 1 (FMR1) [].Vigilin, which has 14 KH domains [].AU-rich element RNA-binding protein KSRP.hnRNP K, which contains 3 KH domains.Human onconeural ventral antigen-1 (NOVA-1) [].According to structural analyses [, , ], the KH domain can be separated in two groups - type 1 and type 2. |
