Protein Family Models

This domain is found in some members of the GatB and aspartyl tRNA synthetases. (from Pfam)

Date:

2023-12-12

This family contains OB-fold domains that bind to nucleic acids [4]. The family includes the anti-codon binding domain of lysyl, aspartyl, and asparaginyl -tRNA synthetases (See Pfam:PF00152). Aminoacyl-tRNA synthetases catalyse the addition of an amino acid to the appropriate tRNA molecule EC:6.1.1.-. This family also includes part of RecG helicase involved in DNA repair. Replication factor A is a hetero-trimeric complex, that contains a subunit in this family [2,3]. This domain is also found at the C-terminus of bacterial DNA polymerase III alpha chain. [1]. 2047877. Class II aminoacyl transfer RNA synthetases: crystal structure. of yeast aspartyl-tRNA synthetase complexed with tRNA(Asp).. Ruff M, Krishnaswamy S, Boeglin M, Poterszman A, Mitschler A,. Podjarny A, Rees B, Thierry JC, Moras D;. Science 1991;252:1682-1689.. [2]. 7760808. Rpa4, a homolog of the 34-kilodalton subunit of the replication. protein A complex.. Keshav KF, Chen C, Dutta A;. Mol Cell Biol 1995;15:3119-3128.. [3]. 8990123. Structure of the single-stranded-DNA-binding domain of. replication protein A bound to DNA.. Bochkarev A, Pfuetzner RA, Edwards AM, Frappier L;. Nature 1997;385:176-181.. [4]. 10829230. Protein fold recognition using sequence profiles and its. application in structural genomics.. Koonin EV, Wolf YI, Aravind L;. Adv Protein Chem 2000;54:245-275. (from Pfam)

Date:

2024-04-03

Members of this family contain a domain found in class II ligases of amino acids to tRNA for protein translation, but also in related proteins such as the EF-P-lysine lysyltransferase EpmA.

Date:

2023-12-12

aspartate--tRNA ligase attaches aspartate to the 3' OH group of ribose of tRNA(Asp)

Date:

2022-07-29

Catalyzes a two-step reaction, first charging an aspartate molecule by linking its carboxyl group to the alpha-phosphate of ATP, followed by transfer of the aminoacyl-adenylate to its tRNA; contains discriminating and non-discriminating subtypes

Gene:

aspS

Date:

2021-07-21

Asparate--tRNA ligases in this family may be discriminating (6.1.1.12) or nondiscriminating (6.1.1.23). In a multiple sequence alignment of representative asparaginyl-tRNA synthetases (asnS), archaeal/eukaryotic type aspartyl-tRNA synthetases (aspS_arch), and bacterial type aspartyl-tRNA synthetases (aspS_bact), there is a striking similarity between asnS and aspS_arch in gap pattern and in sequence, and a striking divergence of aspS_bact. Consequently, a separate model was built for each of the three groups. This HMM, aspS_bact, represents aspartyl-tRNA synthetases from the Bacteria and from mitochondria. In some species, this enzyme aminoacylates tRNA for both Asp and Asn; Asp-tRNA(asn) is subsequently transamidated to Asn-tRNA(asn). This model generates very low scores for the archaeal type of aspS and for asnS; scores between the trusted and noise cutoffs represent fragmentary sequences.

Gene:

aspS

Date:

2023-06-23