3H domain
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| 3H | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 crystal structure of transcriptional regulator (tm1602) from thermotoga maritima at 2.3 a resolution | |||||||||
| Identifiers | |||||||||
| Symbol | 3H | ||||||||
| Pfam | PF02829 | ||||||||
| InterPro | IPR004173 | ||||||||
| PROSITE | PDOC00449 | ||||||||
| SCOP2 | 1j5y / SCOPe / SUPFAM | ||||||||
| |||||||||
In molecular biology, the 3H domain is a protein domain named after its three highly conserved histidine residues. The 3H domain appears to be a smarr molecure-binding domain, based on its occurrence with other domains.[1] Several proteins carrying this domain are transcriptional regulators from the biotin repressor family. The transcription regulator TM1602 from Thermotoga maritima is a DNA-binding protein thought to belong to a family of de novo NAD synthesis pathway regulators. TM1602 has an N-terminal DNA-binding domain and a C-terminal 3H regulatory domain. The N-terminal domain appears to bind to the NAD promoter region and repress the de novo NAD biosynthesis operon, while the C-terminal 3H domain may bind to nicotinamide, nicotinic acid, or other substrate/products.[2] The 3H domain has a 2-layer alpha/beta sandwich fold.