Protein Family Models for Protein (Select 2552852012) - Protein Family Models

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Select item 4284891.

AAA lid domain

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

Family Accession:: NF036834.5
Method:: HMM

Select item 4226602.

AAA family ATPase

GO Terms:

Molecular Function:: ATP hydrolysis activity (GO:0016887)

Date:: 2024-08-14

Family Accession:: NF024793.5
Method:: HMM

Select item 4209123.

C-terminal, D2-small domain, of ClpB protein

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

Family Accession:: NF021915.5
Method:: HMM

Select item 4172994.

AAA family ATPase

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)

GO Terms:

Molecular Function:: ATP binding (GO:0005524)

Molecular Function:: ATP hydrolysis activity (GO:0016887)

Date:: 2024-08-14

Family Accession:: NF019344.5
Method:: HMM

Select item 4169355.

AAA family ATPase

GO Terms:

Molecular Function:: ATP binding (GO:0005524)

Molecular Function:: ATP hydrolysis activity (GO:0016887)

Date:: 2024-08-14

Family Accession:: NF019348.5
Method:: HMM

Select item 4126316.

UvrB/UvrC motif-containing protein

GO Terms:

Molecular Function:: protein binding (GO:0005515)

Date:: 2024-08-14

Family Accession:: NF014232.5
Method:: HMM

Select item 4118797.

sigma 54-interacting transcriptional regulator

GO Terms:

Molecular Function:: ATP binding (GO:0005524)

Biological Process:: regulation of DNA-templated transcription (GO:0006355)

Molecular Function:: transcription factor binding (GO:0008134)

Date:: 2024-08-14

Family Accession:: NF012385.5
Method:: HMM

Select item 4116218.

AAA family ATPase

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)

GO Terms:

Molecular Function:: ATP binding (GO:0005524)

Molecular Function:: ATP hydrolysis activity (GO:0016887)

Date:: 2024-08-14

Family Accession:: NF012234.5
Method:: HMM

Select item 4038929.