Summary: Archaeal transcriptional regulator TrmB
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Archaeal transcriptional regulator TrmB Provide feedback
TrmB is an alpha-glucoside sensing transcriptional regulator. The protein is the transcriptional repressor for gene cluster encoding trehalose/maltose ABC transporter in T.litoralis and P.furiosus . TrmB has lost its DNA binding domain but retained its sugar recognition site. A nonreducing glucosyl residue is shared by all substrates bound to TrmB which suggests that its a common recognition motif .
Krug M, Lee SJ, Diederichs K, Boos W, Welte W; , J Biol Chem. 2006;281:10976-10982.: Crystal structure of the sugar binding domain of the archaeal transcriptional regulator TrmB. PUBMED:16473881 EPMC:16473881
This tab holds annotation information from the InterPro database.
InterPro entry IPR021586
TrmB is an alpha-glucoside sensing transcriptional regulator. The protein is the transcriptional repressor for a gene cluster encoding trehalose/maltose ABC transporter in Thermococcus litoralis and Pyrococcus furiosus [PUBMED:16473881]. A nonreducing glucosyl residue is shared by all substrates bound to TrmB which suggests that its a common recognition motif [PUBMED:16473881].
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Curation and family details
|Number in seed:||25|
|Number in full:||219|
|Average length of the domain:||172.40 aa|
|Average identity of full alignment:||16 %|
|Average coverage of the sequence by the domain:||56.20 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 11927849 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||5|
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For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Regulator_TrmB domain has been found. There are 2 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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