InterPro : IPR009019

Name  K homology domain, prokaryotic type Short Name  KH_prok-type
Type  Domain Description  The K homology domain is a common RNA-binding motif present in one or multiple copies in both prokaryotic and eukaryotic regulatory proteins. The KH motifs may act cooperatively to bind RNA in the case of multiple motifs, or independently in the case of single KH motif proteins. Prokaryotic (pKH) and eukaryotic (eKH) KH domains share a KH-motif, but have different topologies. The pKH domain has been found in a number of proteins, including the N-terminal domain of the S3 ribosomal protein [], the C-terminal domain of Era GTPase []and the two C-terminal domains of the NusA transcription factor []. The structure of the pKH domain consists of a two-layer alpha/beta fold in the arrangement alpha/beta(2)/alpha/beta.
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Sequence Features

GO Displayer

Proteins

InterPro protein domain ID --> Contigs

 

Other

0 Child Features

2 Contains

Id Name Short Name Type
IPR004044 K Homology domain, type 2 KH_dom_type_2 Domain
IPR004087 K Homology domain KH_dom Domain

7 Found In

Id Name Short Name Type
IPR005703 Ribosomal protein S3, eukaryotic/archaeal Ribosomal_S3_euk/arc Family
IPR005704 Ribosomal protein S3, bacterial Ribosomal_S3_bac Family
IPR010213 Transcription termination factor NusA Tscrpt_termination_fac_NusA Domain
IPR005662 GTP-binding protein Era GTP-bd_Era Family
IPR019975 KH-domain/beta-lactamase-domain protein, archaea KH-dom/beta-lactamase-dom_arc Family
IPR020627 Uncharacterised protein family UPF0109 UPF0109 Family
IPR010212 NusA protein, KH domain-containing, archaeal NusA_KH-contain_arc Family

0 Parent Features

3 Publications

First Author Title Year Journal Volume Pages
Wimberly BT Structure of the 30S ribosomal subunit. 2000 Nature 407 327-39
Chen X Crystal structure of ERA: a GTPase-dependent cell cycle regulator containing an RNA binding motif. 1999 Proc Natl Acad Sci U S A 96 8396-401
Worbs M An extended RNA binding surface through arrayed S1 and KH domains in transcription factor NusA. 2001 Mol Cell 7 1177-89



To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)