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Links from Protein

Items: 1 to 20 of 37

1.

magnesium chelatase domain-containing protein

Date:
2023-12-12
Family Accession:
NF024931.4
Method:
HMM
2.

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:
2024-04-03
Family Accession:
NF019348.4
Method:
HMM
3.

S16 family serine protease

The Lon serine proteases must hydrolyse ATP to degrade protein substrates. In Escherichia coli, these proteases are involved in turnover of intracellular proteins, including abnormal proteins following heat-shock. The active site for protease activity resides in a C-terminal domain. The Lon proteases are classified as family S16 in Merops. [1]. 12208506. Domain structure and ATP-induced conformational changes in. Escherichia coli protease Lon revealed by limited proteolysis. and autolysis.. Vasilyeva OV, Kolygo KB, Leonova YF, Potapenko NA, Ovchinnikova. TV;. FEBS Lett 2002;526:66-70. (from Pfam)

GO Terms:
Molecular Function:
ATP-dependent peptidase activity (GO:0004176)
Molecular Function:
serine-type endopeptidase activity (GO:0004252)
Biological Process:
proteolysis (GO:0006508)
Date:
2024-04-03
Family Accession:
NF017200.4
Method:
HMM
4.

LON peptidase substrate-binding domain-containing protein

This domain has been shown to be part of the PUA superfamily [2]. This domain represents a general protein and polypeptide interaction domain for the ATP-dependent serine peptidase, LON, Peptidase_S16, Pfam:PF05362. ATP-dependent Lon proteases are conserved in all living organisms and catalyse rapid turnover of short-lived regulatory proteins and many damaged or denatured proteins. [1]. 16199667. Crystal structure of the N-terminal domain of E. coli Lon. protease.. Li M, Rasulova F, Melnikov EE, Rotanova TV, Gustchina A, Maurizi. MR, Wlodawer A;. Protein Sci. 2005;14:2895-2900.. [2]. 19191354. Structural genomics reveals EVE as a new ASCH/PUA-related. domain.. Bertonati C, Punta M, Fischer M, Yachdav G, Forouhar F, Zhou W,. Kuzin AP, Seetharaman J, Abashidze M, Ramelot TA, Kennedy MA,. Cort JR, Belachew A, Hunt JF, Tong L, Montelione GT, Rost B;. Proteins. 2009;75:760-773.. [3]. 20834233. Crystal structure of Lon protease: molecular architecture of. gated entry to a sequestered degradation chamber.. Cha SS, An YJ, Lee CR, Lee HS, Kim YG, Kim SJ, Kwon KK, De. Donatis GM, Lee JH, Maurizi MR, Kang SG;. EMBO J. 2010;29:3520-3530. (from Pfam)

Date:
2024-04-03
Family Accession:
NF014269.4
Method:
HMM
5.

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:
2024-04-03
Family Accession:
NF012234.4
Method:
HMM
6.
new record, indexing in progress
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new record, indexing in progress
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new record, indexing in progress
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new record, indexing in progress
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new record, indexing in progress
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new record, indexing in progress
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new record, indexing in progress
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new record, indexing in progress
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new record, indexing in progress
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new record, indexing in progress
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new record, indexing in progress
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new record, indexing in progress
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new record, indexing in progress
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new record, indexing in progress
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20.
new record, indexing in progress
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