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Links from Protein

Items: 8

1.

Sua5 family C-terminal domain-containing protein

This domain can be found in the C terminus of threonylcarbamoyl-AMP synthases, including Sua5 from Saccharomyces cerevisiae and YwlC from Bacillus subtilis. Threonylcarbamoyl-AMP synthase is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t6A37) in tRNAs that read codons beginning with adenine [1,2]. This domain adopts the Rossmann fold and may be involved in GTP and/or tRNA binding based on structural similarity with both GTP and tRNA binding proteins [3]. [1]. 19287007. The universal YrdC/Sua5 family is required for the formation of threonylcarbamoyladenosine in tRNA. El Yacoubi B, Lyons B, Cruz Y, Reddy R, Nordin B, Agnelli F, Williamson JR, Schimmel P, Swairjo MA, de Crecy-Lagard V;. Nucleic Acids Res. 2009;37:2894-2909. [2]. 23072323. Mechanism of N6-threonylcarbamoyladenonsine (t(6)A) biosynthesis: isolation and characterization of the intermediate threonylcarbamoyl-AMP. Lauhon CT;. Biochemistry. 2012;51:8950-8963. [3]. 18004774. X-ray crystal structure of a hypothetical Sua5 protein from Sulfolobus tokodaii strain 7. Agari Y, Sato S, Wakamatsu T, Bessho Y, Ebihara A, Yokoyama S, Kuramitsu S, Shinkai A;. Proteins. 2008;70:1108-1111. (from Pfam)

Date:
2024-10-16
Family Accession:
NF015446.5
Method:
HMM
2.

Sua5/YciO/YrdC/YwlC family protein

This domain has been shown to bind preferentially to dsRNA [1]. The domain is found in SUA5 Swiss:P32579 as well as HypF and YrdC Swiss:P45748. It has also been shown to be required for telomere recombniation in yeast. [1]. 11206077. The structure of the yrdC gene product from Escherichia coli reveals a new fold and suggests a role in RNA binding. Teplova M, Tereshko V, Sanishvili R, Joachimiak A, Bushueva T, Anderson WF, Egli M;. Protein Sci 2000;9:2557-2566. [2]. 19287007. The universal YrdC/Sua5 family is required for the formation of threonylcarbamoyladenosine in tRNA. El Yacoubi B, Lyons B, Cruz Y, Reddy R, Nordin B, Agnelli F, Williamson JR, Schimmel P, Swairjo MA, de Crecy-Lagard V;. Nucleic Acids Res. 2009;37:2894-2909. [3]. 19884342. The Sua5 protein is essential for normal translational regulation in yeast. Lin CA, Ellis SR, True HL;. Mol Cell Biol. 2010;30:354-363. [4]. 20309016. Sua5p is required for telomere recombination in Saccharomyces cerevisiae. Meng FL, Chen XF, Hu Y, Tang HB, Dang W, Zhou JQ;. Cell Res. 2010;20:495-498. (from Pfam)

GO Terms:
Molecular Function:
double-stranded RNA binding (GO:0003725)
Date:
2024-10-16
Family Accession:
NF013468.5
Method:
HMM
3.
new record, indexing in progress
Family Accession:
4.
new record, indexing in progress
Family Accession:
5.
new record, indexing in progress
Family Accession:
6.
new record, indexing in progress
Family Accession:
7.

L-threonylcarbamoyladenylate synthase

L-threonylcarbamoyladenylate synthase catalyzes the conversion of L-threonine, HCO(3)(-)/CO(2) and ATP to give threonylcarbamoyl-AMP (TC-AMP) as the acyladenylate intermediate, with the release of diphosphate, and is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine

Date:
2024-09-18
Family Accession:
10000243
Method:
Sparcle
8.

L-threonylcarbamoyladenylate synthase

Has paralogs, but YrdC called a tRNA modification protein. Ref 2 authors say probably heteromultimeric complex. Paralogs may mean its does the final binding to the tRNA.

GO Terms:
Molecular Function:
double-stranded RNA binding (GO:0003725)
Biological Process:
tRNA modification (GO:0006400)
Molecular Function:
L-threonylcarbamoyladenylate synthase (GO:0061710)
Date:
2024-05-16
Family Accession:
TIGR00057.1
Method:
HMM
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