Protein Family Models

The TOBE domain [1] (Transport-associated OB) always occurs as a dimer as the C-terminal strand of each domain is supplied by the partner. Probably involved in the recognition of small ligands such as molybdenum (eg Swiss:P46930) and sulfate (Swiss:P16676). Found in ABC transporters immediately after the ATPase domain. [1]. 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:

2024-10-16

Date:

2024-08-14

molybdenum-dependent DNA-binding transcriptional regulator represses the modABCD operon and activates the moaABCD and napFDAGHBC operons

Date:

2017-02-03

Represses the modABCD operon and activates the moaABCD and napFDAGHBC operons

Gene:

modE

Date:

2021-10-15

This model describes a multigene family of molybdenum-pterin binding proteins of about 70 amino acids in Clostridium pasteurianum, as a tandemly-repeated domain C-terminal to an unrelated domain in ModE, a molybdate transport gene repressor of E. coli, and in single or tandemly paired domains in several related proteins.

Date:

2024-06-12

ModE is a molybdate-activated repressor of the molybdate transport operon in E. coli. It consists of the domain represented by this HMM and two tandem copies of mop-like domain, where Mop proteins are a family of 68-residue molybdenum-pterin binding proteins of Clostridium pasteurianum. This HMM also represents the full length of a pair of archaeal proteins that lack Mop-like domains. PSI-BLAST analysis shows similarity to helix-turn-helix regulatory proteins.

Date:

2019-09-10