Conserved Protein Domain Family
SH3_18

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pfam18354: SH3_18 
CarS bacterial SH3 domain
This is an SH3 domain found in antirepressor proteins such as CarS from Myxococcus xanthus. CarS antirepressor recognizes and neutralizes its cognate repressors to turn on a photo-inducible promoter. CarS physically interacts with the MerR-type winged-helix DNA-binding domain of these repressors leading to activation of carB operon. Structural studies of CarS from M. Xanthus reveals a beta-barrel fold akin to that in SH3 domains. However, it diverges from the typical SH3 domain fold in the lengths and conformations of the connecting loops. Functional analysis reveal that SH3 domain-like fold in the antirepressor CasS, mimics operator DNA in sequestering the repressor DNA recognition helix to activate transcription.
Statistics
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PSSM-Id: 497175
Aligned: 2 rows
Threshold Bit Score: 155.488
Created: 19-Feb-2025
Updated: 28-Apr-2025
Structure
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Aligned Rows:
PubMed ReferencesClick to see Conserved Features Help

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
KFE64192      16 MIQDPSLIVFEDVNGAPVKMGEAVKIVETSEDGSIGRRFLGRTGTVVGLVYDDPEVQYPRDPLVRVRVEGLGEDLFFVGE 95 
WP_014396682   1 MKHDPSLILTEDVDGAPVRMGAAVMIVRTEADDSVSERFLGRVGVVVALVFDDPPMQYPRDPLIQVRVAGLGEDLFFARE 80  Corallococcus c...
KFE64192      96 LEPAP 100
WP_014396682  81 IVEVP 85  Corallococcus coralloides
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