InterPro : IPR013083

Name  Zinc finger, RING/FYVE/PHD-type Short Name  Znf_RING/FYVE/PHD
Type  Domain Description  Zinc finger (Znf) domains are relatively small protein motifs which contain multiple finger-like protrusions that make tandem contacts with their target molecule. Some of these domains bind zinc, but many do not; instead binding other metals such as iron, or no metal at all. For example, some family members form salt bridges to stabilise the finger-like folds. They were first identified as a DNA-binding motif in transcription factor TFIIIA from Xenopus laevis(African clawed frog), however they are now recognised to bind DNA, RNA, protein and/or lipid substrates [, , , , ]. Their binding properties depend on the amino acid sequence of the finger domains and of the linker between fingers, as well as on the higher-order structures and the number of fingers. Znf domains are often found in clusters, where fingers can have different binding specificities. There are many superfamilies of Znf motifs, varying in both sequence and structure. They display considerable versatility in binding modes, even between members of the same class (e.g. some bind DNA, others protein), suggesting that Znf motifs are stable scaffolds that have evolved specialised functions. For example, Znf-containing proteins function in gene transcription, translation, mRNA trafficking, cytoskeleton organisation, epithelial development, cell adhesion, protein folding, chromatin remodelling and zinc sensing, to name but a few []. Zinc-binding motifs are stable structures, and they rarely undergo conformational changes upon binding their target. This entry represents RING-, PHD-, and FYVE-type zinc finger domains, which share a common dimetal (zinc)-bound alpha/beta structural fold, as well as the non-zinc-containing U-box domain, which is similar to the RING zinc finger only lacking the metal ion-binding residues (U-box associated with multi-ubiquitination).
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Sequence Features

GO Displayer

Proteins

InterPro protein domain ID --> Contigs

 

Other

5 Child Features

Id Name Short Name Type
IPR003613 U box domain Ubox_domain Domain
IPR001841 Zinc finger, RING-type Znf_RING Domain
IPR018957 Zinc finger, C3HC4 RING-type Znf_C3HC4_RING-type Domain
IPR011011 Zinc finger, FYVE/PHD-type Znf_FYVE_PHD Domain
IPR022723 RDM domain, Ret finger protein-like RDM_domain_RFPL Domain

3 Contains

Id Name Short Name Type
IPR017907 Zinc finger, RING-type, conserved site Znf_RING_CS Conserved_site
IPR019786 Zinc finger, PHD-type, conserved site Zinc_finger_PHD-type_CS Conserved_site
IPR017455 Zinc finger, FYVE-related Znf_FYVE-rel Domain

8 Found In

Id Name Short Name Type
IPR004575 Cdk-activating kinase assemblyfactor MAT1/Tfb3 MAT1/Tfb3 Family
IPR002853 Transcription factor TFIIE, alpha subunit TFIIE_asu Family
IPR016818 Nitric oxide synthase-interacting Nitric_oxide_synth-interacting Family
IPR004580 DNA repair protein, Rad18 Rad18 Family
IPR017335 E3 ubiquitin ligase, RNF8 E3_Ub_ligase_RNF8 Family
IPR016398 E3 ubiquitin-protein ligase p28 E3_ubiquitin-prot_ligase_p28 Family
IPR012227 TNF receptor-associated factor TRAF TNF_rcpt--assoc_TRAF Family
IPR001237 43kDa postsynaptic protein Postsynaptic Family

0 Parent Features

6 Publications

First Author Title Year Journal Volume Pages
Matthews JM Zinc fingers--folds for many occasions. 2002 IUBMB Life 54 351-5
Gamsjaeger R Sticky fingers: zinc-fingers as protein-recognition motifs. 2007 Trends Biochem Sci 32 63-70
Hall TM Multiple modes of RNA recognition by zinc finger proteins. 2005 Curr Opin Struct Biol 15 367-73
Brown RS Zinc finger proteins: getting a grip on RNA. 2005 Curr Opin Struct Biol 15 94-8
Klug A Zinc finger peptides for the regulation of gene expression. 1999 J Mol Biol 293 215-8
Laity JH Zinc finger proteins: new insights into structural and functional diversity. 2001 Curr Opin Struct Biol 11 39-46



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)