Protein Family Models

This entry represents the alpha helical AAA+ lid domain that is found to the C-terminus of AAA domains. (from Pfam)

Date:

2025-01-31

This domain is found in the FtsH family of proteins. FtsH is the only membrane-bound ATP-dependent protease universally conserved in prokaryotes ([1]). It only efficiently degrades proteins that have a low thermodynamic stability - e.g. it lacks robust unfoldase activity. This feature may be key and implies that this could be a criterion for degrading a protein. In Oenococcus oeni FtsH is involved in protection against environmental stress ([2]), and shows increased expression under heat or osmotic stress. These two lines of evidence suggest that it is a fundamental prokaryotic self-protection mechanism that checks if proteins are correctly folded (personal obs: Yeats C). The precise function of this N-terminal region is unclear. [1]. 12667449. Lack of a robust unfoldase activity confers a unique level of substrate specificity to the universal AAA protease FtsH. Herman C, Prakash S, Lu CZ, Matouschek A, Gross CA;. Mol Cell 2003;11:659-669. [2]. 12732516. The ftsH gene of the wine bacterium Oenococcus oeni is involved in protection against environmental stress. Bourdineaud JP, Nehme B, Tesse S, Lonvaud-Funel A;. Appl Environ Microbiol 2003;69:2512-2520. (from Pfam)

Date:

2025-02-02

This Pfam entry includes some of the AAA proteins not detected by the Pfam:PF00004 model. [1]. 7646486. A 200-amino acid ATPase module in search of a basic function. Confalonieri F, Duguet M;. Bioessays 1995;17:639-650. A large extension of the family. [2]. 9927482. AAA+: A class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes. Neuwald AF, Aravind L, Spouge JL, Koonin EV;. Genome Res 1999;9:27-43. (from Pfam)

Date:

2025-02-03

This family consists of the C-terminal region of several eukaryotic and archaeal RuvB-like 1 (Pontin or TIP49a) and RuvB-like 2 (Reptin or TIP49b) proteins. The N-terminal domain contains the Pfam:PF00004 domain. In zebrafish, the liebeskummer (lik) mutation, causes development of hyperplastic embryonic hearts. lik encodes Reptin, a component of a DNA-stimulated ATPase complex. Beta-catenin and Pontin, a DNA-stimulated ATPase that is often part of complexes with Reptin, are in the same genetic pathways. The Reptin/Pontin ratio serves to regulate heart growth during development, at least in part via the beta-catenin pathway [1]. TBP-interacting protein 49 (TIP49) was originally identified as a TBP-binding protein, and two related proteins are encoded by individual genes, tip49a and b. Although the function of this gene family has not been elucidated, they are supposed to play a critical role in nuclear events because they interact with various kinds of nuclear factors and have DNA helicase activities.TIP49a has been suggested to act as an autoantigen in some patients with autoimmune diseases [2]. [1]. 12464178. Reptin and pontin antagonistically regulate heart growth in zebrafish embryos. Rottbauer W, Saurin AJ, Lickert H, Shen X, Burns CG, Wo ZG, Kemler R, Kingston R, Wu C, Fishman M;. Cell 2002;111:661-672. [2]. 10902922. Chromosome mapping and expression of human tip49 family genes. Makino Y, Kanemaki M, Koga A, Osano K, Matsu-Ura T, Kurokawa Y, Kishimoto T, Tamura T;. DNA Seq 2000;11:145-148. (from Pfam)

Date:

2025-02-03

Date:

2025-02-01

AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes [2]. [1]. 7646486. A 200-amino acid ATPase module in search of a basic function. Confalonieri F, Duguet M;. Bioessays 1995;17:639-650. A large extension of the family. [2]. 9927482. AAA+: A class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes. Neuwald AF, Aravind L, Spouge JL, Koonin EV;. Genome Res 1999;9:27-43. (from Pfam)

Date:

2025-02-01