Protein Family Models for Protein (Select 495684936) - Protein Family Models

Select item 4126981.

tRNA synthetases class I (C) catalytic domain

This family includes only cysteinyl tRNA synthetases. (from Pfam)

Date:: 2024-08-14

Family Accession:: NF013565.5
Method:: HMM

Select item 4109862.

Other tRNA synthetase sub-families are too dissimilar to be included. Paper describing PDB structure 1a8h. [1]. 10673435. The 2.0 A crystal structure of Thermus thermophilus methionyl-tRNA synthetase reveals two RNA-binding modules. Sugiura I, Nureki O, Ugaji-Yoshikawa Y, Kuwabara S, Shimada A, Tateno M, Lorber B, Giege R, Moras D, Yokoyama S, Konno M;. Structure. 2000;8:197-208. Paper describing PDB structure 1f4l. [2]. 11243794. How methionyl-tRNA synthetase creates its amino acid recognition pocket upon L-methionine binding. Serre L, Verdon G, Choinowski T, Hervouet N, Risler JL, Zelwer C;. J Mol Biol. 2001;306:863-876. Paper describing PDB structure 1ffy. [3]. 10446055. Insights into editing from an ile-tRNA synthetase structure with tRNAile and mupirocin. Silvian LF, Wang J, Steitz TA;. Science. 1999;285:1074-1077. Paper describing PDB structure 1gax. [4]. 11114335. Structural basis for double-sieve discrimination of L-valine from L-isoleucine and L-threonine by the complex of tRNA(Val) and valyl-tRNA synthetase. Fukai S, Nureki O, Sekine S, Shimada A, Tao J, Vassylyev DG, Yokoyama S;. Cell 2000;103:793-803. Paper describing PDB structure 1h3n. [5]. 10811626. The 2 A crystal structure of leucyl-tRNA synthetase and its complex with a leucyl-adenylate analogue. Cusack S, Yaremchuk A, Tukalo M;. EMBO J. 2000;19:2351-2361. (from Pfam)

GO Terms:

Molecular Function:: nucleotide binding (GO:0000166)

Molecular Function:: aminoacyl-tRNA ligase activity (GO:0004812)

Molecular Function:: ATP binding (GO:0005524)

Biological Process:: tRNA aminoacylation for protein translation (GO:0006418)

Date:: 2024-10-16

Family Accession:: NF012361.5
Method:: HMM

Select item 3891823.

new record, indexing in progress

Family Accession:

Select item 3890664.

new record, indexing in progress

Family Accession:

Select item 3484305.

new record, indexing in progress

Family Accession:

Select item 3469506.

new record, indexing in progress

Family Accession:

Select item 1473407.

cysteine--1-D-myo-inosityl 2-amino-2-deoxy-alpha-D-glucopyranoside ligase

Members of this protein family are MshC, l-cysteine:1-D-myo-inosityl 2-amino-2-deoxy-alpha-D-glucopyranoside ligase, an enzyme that uses ATP to ligate a Cys residue to a mycothiol precursor molecule, in the second to last step in mycothiol biosynthesis. This enzyme shows considerable homology to Cys--tRNA ligases, and many instances are misannotated as such. Mycothiol is found in Mycobacterium tuberculosis, Corynebacterium glutamicum, Streptomyces coelicolor, and various other members of the Actinobacteria. Mycothiol is an analog to glutathione.

Gene:: mshC

GO Terms:

Biological Process:: mycothiol biosynthetic process (GO:0010125)

Molecular Function:: cysteine-glucosaminylinositol ligase activity (GO:0035446)

Date:: 2024-05-30

Family Accession:: TIGR03447.1
Method:: HMM

Select item 603188.

cysteine--1-D-myo-inosityl 2-amino-2-deoxy-alpha-D-glucopyranoside ligase

cysteine--1-D-myo-inosityl 2-amino-2-deoxy-alpha-D-glucopyranoside ligase catalyzes the ATP-dependent condensation of 1-O-(2-amino-2-deoxy-alpha-D-glucopyranosyl)-1D-myo-inositol (GlcN-Ins) and L-cysteine to form L-Cys-GlcN-Ins

Date:: 2019-07-02

Family Accession:: 11485899
Method:: Sparcle

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