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serine aminopeptidase domain-containing protein
This domain is found in bacteria and eukaryotes and is approximately 110 amino acids in length. It is found in association with Pfam:PF00561. The majority of the members in this family carry the exopeptidase active-site residues of Ser-122, Asp-239 and His-269 as in UniProtKB:Q7ZWC2. (from Pfam)
alpha/beta fold hydrolase
This family contains alpha/beta hydrolase enzymes of diverse specificity. (from Pfam)
alpha/beta hydrolase
This is a family of putative bacterial peptidases and hydrolases that bear similarity to a tripeptidyl aminopeptidase isolated from Streptomyces lividans (Swiss:Q54410). A member of this family (Swiss:Q6E3K7) is thought to be involved in the C-terminal processing of propionicin F, a bacteriocidin characterised from Propionibacterium freudenreichii [1]. [1]. 15574930. Molecular and genetic characterization of propionicin F, a bacteriocin from Propionibacterium freudenreichii. Brede DA, Faye T, Johnsborg O, Odegard I, Nes IF, Holo H;. Appl Environ Microbiol 2004;70:7303-7310. (from Pfam)
Ndr family
This family consists of proteins from different gene families: Ndr1/RTP/Drg1, Ndr2, and Ndr3. Their similarity was previously noted [1]. The precise molecular and cellular function of members of this family is still unknown. Yet, they are known to be involved in cellular differentiation events. The Ndr1 group was the first to be discovered. Their expression is repressed by the proto-oncogenes N-myc and c-myc, and in line with this observation, Ndr1 protein expression is down-regulated in neoplastic cells, and is reactivated when differentiation is induced by chemicals such as retinoic acid. Ndr2 and Ndr3 expression is not under the control of N-myc or c-myc. Ndr1 expression is also activated by several chemicals: tunicamycin and homocysteine induce Ndr1 in human umbilical endothelial cells; nickel induces Ndr1 in several cell types. Members of this family are found in wide variety of multicellular eukaryotes, including an Ndr1 type protein in Helianthus annuus (sunflower), known as Sf21 Swiss:O23969. Interestingly, the highest scoring matches in the noise are all alpha/beta hydrolases Pfam:PF00561, suggesting that this family may have an enzymatic function (Bateman A pers. obs.). [1]. 10581191. Identification of new genes ndr2 and ndr3 which are related to Ndr1/RTP/Drg1 but show distinct tissue specificity and response to N-myc. Okuda T, Kondoh H;. Biochem Biophys Res Commun 1999;266:208-215. (from Pfam)
This catalytic domain is found in a very wide range of enzymes. [1]. 1409539. The alpha/beta hydrolase fold. Ollis DL, Cheah E, Cygler M, Dijkstra B, Frolow F, Franken SM, Harel M, Remington SJ, Silman I, Schrag J, Sussman JL, Verschueren KHG, Goldman A;. Protein Eng 1992;5:197-211. (from Pfam)
pyrimidine utilization protein D
This protein is observed in operons extremely similar to that characterized in E. coli K-12 [1] responsible for the import and catabolism of pyrimidines, primarily uracil. This protein is a member of the hydrolase, alpha/beta fold family defined by PF00067.
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