LIS - Legume Information System
Information about legume traits for crop improvement
GlycineMine
v5.1.0.3
Glycine data from LIS
v5.1.0.3
Glycine data from LIS
| Type | 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 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. |
| Short Name | KH_dom |
