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:

2024-08-14

This is the C-terminal domain of ClpB protein, referred to as the D2-small domain, and is a mixed alpha-beta structure. Compared with the D1-small domain (included in AAA, Pfam:PF00004) it lacks the long coiled-coil insertion, and instead of helix C4 contains a beta-strand (e3) that is part of a three stranded beta-pleated sheet. In Thermophilus the whole protein forms a hexamer with the D1-small and D2-small domains located on the outside of the hexamer, with the long coiled-coil being exposed on the surface. The D2-small domain is essential for oligomerisation, forming a tight interface with the D2-large domain of a neighbouring subunit and thereby providing enough binding energy to stabilise the functional assembly [1]. The domain is associated with two Clp_N, Pfam:PF02861, at the N-terminus as well as AAA, Pfam:PF00004 and AAA_2, Pfam:PF07724. [1]. 14567920. The structure of ClpB: a molecular chaperone that rescues. proteins from an aggregated state.. Lee S, Sowa ME, Watanabe YH, Sigler PB, Chiu W, Yoshida M, Tsai. FT;. Cell. 2003;115:229-240. (from Pfam)

Date:

2024-08-14

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:

2024-08-14

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:

2024-08-14

This family consists of several bacterial TniB NTP-binding proteins. TniB is a probable ATP-binding protein [1] which is involved in Tn5053 mercury resistance transposition [2]. This entry represents a P-loop domain. [1]. 8195081. Transposon Tn5090 of plasmid R751, which carries an integron, is. related to Tn7, Mu, and the retroelements.. Radstrom P, Skold O, Swedberg G, Flensburg J, Roy PH, Sundstrom. L;. J Bacteriol 1994;176:3257-3268.. [2]. 8594337. Four genes, two ends, and a res region are involved in. transposition of Tn5053: a paradigm for a novel family of. transposons carrying either a mer operon or an integron.. Kholodii GY, Mindlin SZ, Bass IA, Yurieva OV, Minakhina SV,. Nikiforov VG;. Mol Microbiol 1995;17:1189-1200. (from Pfam)

Date:

2024-08-14

Date:

2024-08-14

Date:

2024-08-14

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:

2024-08-14