InterPro results for type:repeat

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HEAT, type 2 (IPR021133) The HEAT repeat is a tandemly repeated, 37-47 amino acid long module occurring in a number of cytoplasmic proteins, including the four name-giving proteins huntingtin, elongation ...

FG-GAP repeat (IPR013517) This region contains the extracellular repeat that is found in up to seven copies in alpha integrins. This repeat has been predicted to fold into a beta propeller structure. The r...

Stress-induced protein, KGG, repeat (IPR019626) This repeat contains a highly conserved, characteristic sequence motif, KGG, that is recognised by plants and lower eukaryotes. Further downstream from this motif is a Walker A, n...

Spectrin/alpha-actinin (IPR018159) Spectrin repeats are found in several proteins involved in cytoskeletal structure. These include spectrin alpha and beta subunits, alpha-actinin and dystrophin. The spectrin repea...

Zinc metalloproteinase 18-residue repeat (IPR026471) This entry represents a short (18-amino acid) tandem repeat that occurs variable numbers of times in zinc metalloproteinase C (zmpC) homologues in various species of Streptococcus...

Putative TPR-like repeat (IPR031545) This entry represents a TPR-like repeats found in a group of eukaryotic proteins. Many sequences are annotated as being signal recognition proteins...

BspA type Leucine rich repeat region (IPR026906) This entry represents a leucine rich repeat. A leucine-rich repeat (LRR) is a protein structural motif that forms an alpha/beta horseshoe fold. Leucine-rich repeats are frequently...

Pyrrolo-quinoline quinone beta-propeller repeat (IPR018391) Pyrrolo-quinoline quinone (PQQ) is a redox coenzyme, which serves as a cofactor for a number of enzymes (quinoproteins) and particularly for some bacterial dehydrogenases. A numbe...

Fibronectin-binding repeat, SSURE (IPR021021) Streptococcal surface repeat domain - SSURE - is a protein fragment found to bind to extracellular matrix protein fibronectin but not to collagen or submaxillary mucin in Streptoc...

RHS repeat (IPR031325) RHS (rearrangement hotspot) proteins contain extended repeat regions. These repeats often appear to be involved in ligand binding. Note that the signature in this entry does not f...