Protein Family Models

MOSC (molybdenum cofactor sulfurase C-terminal) domain-containing protein similar to Bacillus subtilis uncharacterized protein YflK

Date:

2024-08-09

The MOSC (MOCO sulfurase C-terminal) domain is a superfamily of beta-strand-rich domains identified in the molybdenum cofactor sulfurase and several other proteins from both prokaryotes and eukaryotes. These MOSC domains contain an absolutely conserved cysteine and occur either as stand-alone forms such as Swiss:P32157, or fused to other domains such as NifS-like catalytic domain in Molybdenum cofactor sulfurase. The MOSC domain is predicted to be a sulfur-carrier domain that receives sulfur abstracted by the pyridoxal phosphate-dependent NifS-like enzymes, on its conserved cysteine, and delivers it for the formation of diverse sulfur-metal clusters. [1]. 11886751. MOSC domains: ancient, predicted sulfur-carrier domains, present in diverse metal--sulfur cluster biosynthesis proteins including Molybdenum cofactor sulfurases. Anantharaman V, Aravind L;. FEMS Microbiol Lett 2002;207:55-61. (from Pfam)

Date:

2024-10-16

This small triple helical domain has been predicted to assume a topology similar to helix-turn-helix domains. These domains are found at the C-terminus of proteins related to Swiss:P32157 [1,2]. See figure 2. [1]. 11886751. MOSC domains: ancient, predicted sulfur-carrier domains, present in diverse metal--sulfur cluster biosynthesis proteins including Molybdenum cofactor sulfurases. Anantharaman V, Aravind L;. FEMS Microbiol Lett 2002;207:55-61. [2]. 29459651. Crystal structure of the hydroxylaminopurine resistance protein, YiiM, and its putative molybdenum cofactor-binding catalytic site. Namgung B, Kim JH, Song WS, Yoon SI;. Sci Rep. 2018;8:3304. (from Pfam)

Date:

2024-10-16