Protein Family Models

This is the N-terminal domain found in archeal type-2 serine-tRNA ligase (SerRS) (EC:6.1.1.11). The SerRS N-terminal domain interacts with the extra-arm stem and the outer corner of tRNA specific to Selenocysteine (tRNA-Sec) [1, 2]. [1]. 23649835. Tertiary structure of bacterial selenocysteine tRNA.. Itoh Y, Sekine S, Suetsugu S, Yokoyama S;. Nucleic Acids Res. 2013;41:6729-6738.. [2]. 16675947. Structure of the unusual seryl-tRNA synthetase reveals a. distinct zinc-dependent mode of substrate recognition.. Bilokapic S, Maier T, Ahel D, Gruic-Sovulj I, Soll D,. Weygand-Durasevic I, Ban N;. EMBO J. 2006;25:2498-2509. (from Pfam)

Date:

2024-04-03

This HMM finds multiple types of aminoacyl--tRNA ligase, such as those for Thr, Pro, His, and Ser in Escherichia coli. Because equivalog-level HMMs exist to identify full-length members of the tRNA ligase families, any protein receiving annotation from this HMM is most likely to be either a partial sequence or a tRNA ligase-related protein involved in some process other than protein translation on the ribosome.

Date:

2024-04-03

Catalyzes a two-step reaction, first charging a serine molecule by linking its carboxyl group to the alpha-phosphate of ATP, followed by transfer of the aminoacyl-adenylate to its tRNA

Date:

2020-10-26

The seryl-tRNA synthetases from a few of the Archaea, represented by this model, are very different from the set of mutually more closely related seryl-tRNA synthetases from Eubacteria, Eukaryotes, and other Archaea. Although distantly homologous, the present set differs enough not to be recognized by the pfam HMM tRNA-synt_2b that recognizes the remainder of seryl-tRNA synthetases among oither class II amino-acyl tRNA synthetases.

Gene:

serS

Date:

2021-04-27