Protein Family Models for Protein (Select 489319482) - Protein Family Models

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Select item 4303011.

tRNA modifying enzyme MnmG/GidA C-terminal helical domain

Date:: 2024-08-14

Family Accession:: NF045129.2
Method:: HMM

Select item 4227022.

tRNA modifying enzyme MnmG/GidA C-terminal helical bundle

The GidA associated domain is a domain that has been identified at the C-terminus of protein GidA. It consists of several helices, last three being rather short and forming small bundle and are represented in this entry. GidA is a tRNA modification enzyme found in bacteria and mitochondrial. Based on mutational analysis the C-terminal helices have been suggested to be implicated in binding of the D-stem of tRNA [2] and, specifically this domain, to be responsible for the interaction with protein MnmE [1]. Structures of GidA in complex with either tRNA or MnmE are missing. Reported to bind to Pfam family MnmE, Pfam:PF12631. [1]. 18565343. Crystal structures of the conserved tRNA-modifying enzyme GidA:. implications for its interaction with MnmE and substrate.. Meyer S, Scrima A, Versees W, Wittinghofer A;. J Mol Biol. 2008;380:532-547.. [2]. 19446527. Conserved cysteine residues of GidA are essential for biogenesis. of 5-carboxymethylaminomethyluridine at tRNA anticodon.. Osawa T, Ito K, Inanaga H, Nureki O, Tomita K, Numata T;. Structure. 2009;17:713-724.. [3]. 19801413. Structure-function analysis of Escherichia coli MnmG (GidA), a. highly conserved tRNA-modifying enzyme.. Shi R, Villarroya M, Ruiz-Partida R, Li Y, Proteau A, Prado S,. Moukadiri I, Benitez-Paez A, Lomas R, Wagner J, Matte A,. Velazquez-Campoy A, Armengod ME, Cygler M;. J Bacteriol. 2009;191:7614-7619. (from Pfam)

Date:: 2024-08-14

Family Accession:: NF025300.5
Method:: HMM

Select item 4120293.

FAD-dependent oxidoreductase

Date:: 2024-08-14

Family Accession:: NF013314.5
Method:: HMM

Select item 4111764.

FAD-binding protein

This family includes members that bind FAD. This family includes the flavoprotein subunits from succinate and fumarate dehydrogenase, aspartate oxidase and the alpha subunit of adenylylsulphate reductase. [1]. 8061609. Structure of glutathione reductase from Escherichia coli at 1.86. A resolution: comparison with the enzyme from human. erythrocytes.. Mittl PR, Schulz GE. Protein Sci 1994;3:799-809. (from Pfam)

Date:: 2024-08-14

Family Accession:: NF013086.5
Method:: HMM

Select item 4073145.

new record, indexing in progress

Family Accession:

Select item 4013096.

new record, indexing in progress

Family Accession:

Select item 3895807.

new record, indexing in progress

Family Accession:

Select item 3883478.

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Family Accession:

Select item 3638449.

new record, indexing in progress

Family Accession:

Select item 34733810.

new record, indexing in progress

Family Accession:

Select item 34694111.

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Family Accession:

Select item 32585412.

new record, indexing in progress

Family Accession:

Select item 31588313.

new record, indexing in progress

Family Accession:

Select item 31561614.

new record, indexing in progress

Family Accession:

Select item 9239815.

tRNA uridine-5-carboxymethylaminomethyl modification enzyme MnmG/GidA

tRNA uridine-5-carboxymethylaminomethyl modification enzyme MnmG/GidA such as tRNA uridine-5-carboxymethylaminomethyl(34) synthesis enzyme MnmG, which is involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34

Date:: 2024-07-19

Family Accession:: 11418560
Method:: Sparcle

Select item 6204216.

new record, indexing in progress

Family Accession:

Select item 6192917.

new record, indexing in progress

Family Accession:

Select item 4692518.

new record, indexing in progress

Family Accession:

Select item 4671119.

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Family Accession:

Select item 3137520.

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Family Accession:

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