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Links from Protein

Items: 14

1.

class I tRNA ligase family protein

This family includes methionyl tRNA synthetases. (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:
2024-08-14

Family Accession:
NF020892.5
Method:
HMM

2.

DALR domain-containing protein

This DALR domain is found in cysteinyl-tRNA-synthetases [1]. [1]. 10447505. Evolution of aminoacyl-tRNA synthetases--analysis of unique. domain architectures and phylogenetic trees reveals a complex. history of horizontal gene transfer events.. Wolf YI, Aravind L, Grishin NV, Koonin EV;. Genome Res 1999;9:689-710. (from Pfam)

GO Terms:
Molecular Function:
nucleotide binding (GO:0000166)
Molecular Function:
cysteine-tRNA ligase activity (GO:0004817)
Molecular Function:
ATP binding (GO:0005524)
Cellular Component:
cytoplasm (GO:0005737)
Biological Process:
cysteinyl-tRNA aminoacylation (GO:0006423)
Date:
2024-08-14

Family Accession:
NF020752.5
Method:
HMM

3.

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

4.

class I tRNA ligase family protein

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:
2024-08-14

Family Accession:
NF012361.5
Method:
HMM

5.
new record, indexing in progress
Family Accession:
6.
new record, indexing in progress
Family Accession:
7.
new record, indexing in progress
Family Accession:
8.
new record, indexing in progress
Family Accession:
9.
new record, indexing in progress
Family Accession:
10.
new record, indexing in progress
Family Accession:
11.
new record, indexing in progress
Family Accession:
12.
new record, indexing in progress
Family Accession:
13.

cysteine--tRNA ligase

cysteine--tRNA ligase catalyzes the attachment of cysteine to tRNA(Cys)

Date:
2024-04-09

Family Accession:
11415459
Method:
Sparcle

14.

cysteine--tRNA ligase

Cysteine--tRNA ligase charges a cysteine by linking its carboxyl group to the alpha-phosphate of ATP and then transfers the aminoacyl-adenylate to its tRNA. This HMM finds the cysteinyl-tRNA synthetase from most but not from all species. Many archaea instead and a few bacteria rely on the SepRS/SepCysS pathway, first ligating phosphoserine to tRNA(Cys), then replacing the phosphate with sulfide.

Gene:
cysS
GO Terms:
Molecular Function:
cysteine-tRNA ligase activity (GO:0004817)
Molecular Function:
ATP binding (GO:0005524)
Cellular Component:
cytoplasm (GO:0005737)
Biological Process:
cysteinyl-tRNA aminoacylation (GO:0006423)
Date:
2024-05-30

Family Accession:
TIGR00435.1
Method:
HMM

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