| Type: | Domain | Name: | K Homology domain |
| 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 beta-alpha-alpha-beta-beta-alpha structure. Proteins containing KH domains include:Bacterial and organelle PNPases [].Archaeal and eukaryotic exosome subunits [].Eukaryotic and prokaryotic RS3 ribosomal proteins [].Vertebrate fragile X mental retardation protein 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. | Short Name: | KH_dom |
| DB identifier | Type | Name |
|---|---|---|
| IPR009019 | Domain | K homology domain, prokaryotic type |
| IPR015946 | Domain | K homology domain-like, alpha/beta |
| IPR012162 | Family | Polyribonucleotide nucleotidyltransferase |
| IPR005704 | Family | Ribosomal protein S3, bacterial |
| IPR005703 | Family | Ribosomal protein S3, eukaryotic/archaeal |
| IPR017705 | Family | Ribonuclease Y |
| IPR019975 | Family | KH-domain/beta-lactamase-domain protein, archaea |
| IPR019964 | Family | KH domain protein, archaea |
