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Links from Protein

Items: 16

1.

kelch repeat protein

Date:
2024-08-14
Family Accession:
NF025330.5
Method:
HMM
2.

kelch repeat-containing protein

Date:
2024-08-14
Family Accession:
NF024810.5
Method:
HMM
3.

kelch repeat-containing protein

Date:
2024-08-14
Family Accession:
NF024807.5
Method:
HMM
4.

kelch repeat protein

The kelch motif was initially discovered in Kelch (Swiss:Q04652). In this protein there are six copies of the motif. It has been shown that Swiss:Q04652 is related to Galactose Oxidase [1] for which a structure has been solved [2]. The kelch motif forms a beta sheet. Several of these sheets associate to form a beta propeller structure as found in Pfam:PF00064, Pfam:PF00400 and Pfam:PF00415. [1]. 8126718. Drosophila kelch motif is derived from a common enzyme fold. Bork P, Doolittle RF;. J Mol Biol 1994;236:1277-1282. [2]. 2002850. Novel thioether bond revealed by a 1.7 A crystal structure of galactose oxidase. Ito N, Phillips SE, Stevens C, Ogel ZB, McPherson MJ, Keen JN, Yadav KD, Knowles PF;. Nature 1991;350:87-90. [3]. 15475350. Crystal structure of the Kelch domain of human Keap1. Li X, Zhang D, Hannink M, Beamer LJ;. J Biol Chem 2004;279:54750-54758. (from Pfam)

GO Terms:
Molecular Function:
protein binding (GO:0005515)
Date:
2024-10-16
Family Accession:
NF019272.5
Method:
HMM
5.

kelch repeat protein

The kelch motif was initially discovered in Kelch (Swiss:Q04652). In this protein there are six copies of the motif. It has been shown that Swiss:Q04652 is related to Galactose Oxidase [1] for which a structure has been solved [2]. The kelch motif forms a beta sheet. Several of these sheets associate to form a beta propeller structure as found in Pfam:PF00064, Pfam:PF00400 and Pfam:PF00415. [1]. 8126718. Drosophila kelch motif is derived from a common enzyme fold. Bork P, Doolittle RF;. J Mol Biol 1994;236:1277-1282. [2]. 2002850. Novel thioether bond revealed by a 1.7 A crystal structure of galactose oxidase. Ito N, Phillips SE, Stevens C, Ogel ZB, McPherson MJ, Keen JN, Yadav KD, Knowles PF;. Nature 1991;350:87-90. [3]. 15475350. Crystal structure of the Kelch domain of human Keap1. Li X, Zhang D, Hannink M, Beamer LJ;. J Biol Chem 2004;279:54750-54758. (from Pfam)

GO Terms:
Molecular Function:
protein binding (GO:0005515)
Date:
2024-10-16
Family Accession:
NF013507.5
Method:
HMM
6.
new record, indexing in progress
Family Accession:
7.
new record, indexing in progress
Family Accession:
8.
new record, indexing in progress
Family Accession:
9.
new record, indexing in progress
Family Accession:
10.
new record, indexing in progress
Family Accession:
11.
new record, indexing in progress
Family Accession:
12.
new record, indexing in progress
Family Accession:
13.
new record, indexing in progress
Family Accession:
14.

N-acetylneuraminate epimerase

N-acetylneuraminate epimerase converts alpha-N-acetylneuranimic acid (Neu5Ac) to the beta-anomer, accelerating the equilibrium between the alpha- and beta-anomers

Date:
2019-07-30
Family Accession:
11487115
Method:
Sparcle
15.

N-acetylneuraminate epimerase

Date:
2020-10-26
Family Accession:
NF010730.0
Method:
HMM
16.

YjhT family mutarotase

Members of this protein family contain multiple copies of the beta-propeller-forming Kelch repeat. All are full-length homologs to YjhT of Escherichia coli, which has been identified as a mutarotase for sialic acid. This protein improves bacterial ability to obtain host sialic acid, and thus serves as a virulence factor. Some bacteria carry what appears to be a cyclically permuted homolog of this protein.

Date:
2019-09-10
Family Accession:
TIGR03547.1
Method:
HMM
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